UniProtKB - P12497 (POL_HV1N5)
Gag-Pol polyprotein
gag-pol
Functioni
Miscellaneous
Catalytic activityi
- a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)PROSITE-ProRule annotationEC:2.7.7.49PROSITE-ProRule annotation EC:2.7.7.7PROSITE-ProRule annotation
- Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.PROSITE-ProRule annotation EC:3.4.23.16
- Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.By similarity EC:3.1.26.13
- 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.By similarity EC:3.1.13.2
Cofactori
Protein has several cofactor binding sites:- Mg2+By similarityNote: Binds 2 magnesium ions for reverse transcriptase polymerase activity.By similarity
- Mg2+By similarityNote: Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding.By similarity
- Mg2+By similarityNote: Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions.By similarity
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 221 – 222 | Cis/trans isomerization of proline peptide bond; by human PPIA/CYPABy similarity | 2 | |
Active sitei | 513 | For protease activity; shared with dimeric partnerPROSITE-ProRule annotation | 1 | |
Metal bindingi | 697 | Magnesium; catalytic; for reverse transcriptase activityBy similarity | 1 | |
Metal bindingi | 772 | Magnesium; catalytic; for reverse transcriptase activityBy similarity | 1 | |
Metal bindingi | 773 | Magnesium; catalytic; for reverse transcriptase activityBy similarity | 1 | |
Sitei | 988 | Essential for RT p66/p51 heterodimerizationBy similarity | 1 | |
Sitei | 1001 | Essential for RT p66/p51 heterodimerizationBy similarity | 1 | |
Metal bindingi | 1030 | Magnesium; catalytic; for RNase H activityBy similarity | 1 | |
Metal bindingi | 1065 | Magnesium; catalytic; for RNase H activityBy similarity | 1 | |
Metal bindingi | 1085 | Magnesium; catalytic; for RNase H activityBy similarity | 1 | |
Metal bindingi | 1136 | Magnesium; catalytic; for RNase H activityBy similarity | 1 | |
Metal bindingi | 1211 | Magnesium; catalytic; for integrase activity | 1 | |
Metal bindingi | 1263 | Magnesium; catalytic; for integrase activity | 1 | |
Metal bindingi | 1299 | Magnesium; catalytic; for integrase activityBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 390 – 407 | CCHC-type 1PROSITE-ProRule annotationAdd BLAST | 18 | |
Zinc fingeri | 411 – 428 | CCHC-type 2PROSITE-ProRule annotationAdd BLAST | 18 | |
Zinc fingeri | 1150 – 1191 | Integrase-typePROSITE-ProRule annotationAdd BLAST | 42 | |
DNA bindingi | 1370 – 1417 | Integrase-typePROSITE-ProRule annotationAdd BLAST | 48 |
GO - Molecular functioni
- aspartic-type endopeptidase activity Source: UniProtKB-KW
- DNA binding Source: UniProtKB-KW
- DNA-directed DNA polymerase activity Source: UniProtKB-KW
- exoribonuclease H activity Source: UniProtKB-EC
- identical protein binding Source: IntAct
- lipid binding Source: UniProtKB-KW
- phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
- RNA binding Source: UniProtKB-KW
- RNA-directed DNA polymerase activity Source: UniProtKB-KW
- RNA-DNA hybrid ribonuclease activity Source: InterPro
- structural molecule activity Source: InterPro
- zinc ion binding Source: InterPro
GO - Biological processi
- DNA integration Source: UniProtKB-KW
- DNA recombination Source: UniProtKB-KW
- establishment of integrated proviral latency Source: UniProtKB-KW
- induction by virus of host cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB-KW
- suppression by virus of host gene expression Source: UniProtKB-KW
- viral entry into host cell Source: UniProtKB-KW
- viral genome integration into host DNA Source: UniProtKB-KW
- viral penetration into host nucleus Source: UniProtKB-KW
Keywordsi
Names & Taxonomyi
Protein namesi | Recommended name: Gag-Pol polyproteinAlternative name(s): Pr160Gag-Pol Cleaved into the following 11 chains: Alternative name(s): p2 Alternative name(s): PR Retropepsin Reverse transcriptase/ribonuclease H (EC:2.7.7.49, EC:2.7.7.7, EC:3.1.26.13) Alternative name(s): Exoribonuclease H (EC:3.1.13.2) p66 RT |
Gene namesi | Name:gag-pol |
Organismi | Human immunodeficiency virus type 1 group M subtype B (isolate NY5) (HIV-1) |
Taxonomic identifieri | 11698 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Pararnavirae › Artverviricota › Revtraviricetes › Ortervirales › Retroviridae › Orthoretrovirinae › Lentivirus › |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] |
Subcellular locationi
- Host cell membrane ; Lipid-anchor 1 Publication
- host multivesicular body 1 Publication Note: These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly.1 Publication
- Virion membrane ; Lipid-anchor Curated
- Host nucleus By similarity
- Host cytoplasm By similarity
- Virion Curated
- Virion Curated
- Virion Curated
- Host nucleus Curated
- Host cytoplasm Curated Note: Nuclear at initial phase, cytoplasmic at assembly.Curated
GO - Cellular componenti
- host cell nucleus Source: UniProtKB-SubCell
- host cell plasma membrane Source: UniProtKB-SubCell
- host multivesicular body Source: UniProtKB-SubCell
- viral nucleocapsid Source: UniProtKB-KW
- virion membrane Source: UniProtKB-SubCell
Keywords - Cellular componenti
Capsid protein, Host cell membrane, Host cytoplasm, Host endosome, Host membrane, Host nucleus, Membrane, VirionPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 9 | S → A: Loss of ability to fuse with target cell membranes and infect host cell. 1 Publication | 1 | |
Mutagenesisi | 67 | S → A: Loss of ability to fuse with target cell membranes and infect host cell. 1 Publication | 1 | |
Mutagenesisi | 72 | S → A: Loss of ability to fuse with target cell membranes and infect host cell. 1 Publication | 1 | |
Mutagenesisi | 77 | S → A: Loss of ability to fuse with target cell membranes and infect host cell. 1 Publication | 1 |
Keywords - Diseasei
AIDSChemistry databases
DrugBanki | DB03118, (2Z)-1-(5-Chloro-1H-indol-3-yl)-3-hydroxy-3-(1H-tetrazol-5-yl)-2-propen-1-one DB02086, (3,4-Dihydroxy-Phenyl)-Triphenyl-Arsonium DB07575, 2,4-DIAMINO-1,5-DIPHENYL-3-HYDROXYPENTANE DB02994, Cacodylic acid DB08027, CAP-1 DB03676, Cystein-S-Yl Cacodylate DB08231, Myristic acid DB03963, S-(Dimethylarsenic)Cysteine |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed; by hostBy similarity | |||
ChainiPRO_0000261276 | 2 – 1435 | Gag-Pol polyproteinAdd BLAST | 1434 | |
ChainiPRO_0000042394 | 2 – 132 | Matrix protein p17By similarityAdd BLAST | 131 | |
ChainiPRO_0000042395 | 133 – 363 | Capsid protein p24By similarityAdd BLAST | 231 | |
PeptideiPRO_0000042396 | 364 – 377 | Spacer peptide 1By similarityAdd BLAST | 14 | |
ChainiPRO_0000042397 | 378 – 432 | Nucleocapsid protein p7By similarityAdd BLAST | 55 | |
PeptideiPRO_0000246725 | 433 – 440 | Transframe peptideSequence analysis | 8 | |
ChainiPRO_0000042398 | 441 – 488 | p6-polSequence analysisAdd BLAST | 48 | |
ChainiPRO_0000038660 | 489 – 587 | ProteaseBy similarityAdd BLAST | 99 | |
ChainiPRO_0000042399 | 588 – 1147 | Reverse transcriptase/ribonuclease HBy similarityAdd BLAST | 560 | |
ChainiPRO_0000042400 | 588 – 1027 | p51 RTBy similarityAdd BLAST | 440 | |
ChainiPRO_0000042401 | 1028 – 1147 | p15By similarityAdd BLAST | 120 | |
ChainiPRO_0000042402 | 1148 – 1435 | IntegraseBy similarityAdd BLAST | 288 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 2 | N-myristoyl glycine; by hostBy similarity | 1 | |
Modified residuei | 132 | Phosphotyrosine; by hostBy similarity | 1 | |
Modified residuei | 148 | Phosphoserine; by host MAPK11 Publication | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 132 – 133 | Cleavage; by viral proteaseBy similarity | 2 | |
Sitei | 363 – 364 | Cleavage; by viral proteaseBy similarity | 2 | |
Sitei | 377 – 378 | Cleavage; by viral proteaseBy similarity | 2 | |
Sitei | 432 – 433 | Cleavage; by viral proteaseSequence analysis | 2 | |
Sitei | 440 – 441 | Cleavage; by viral proteaseBy similarity | 2 | |
Sitei | 488 – 489 | Cleavage; by viral proteaseBy similarity | 2 | |
Sitei | 587 – 588 | Cleavage; by viral proteaseBy similarity | 2 | |
Sitei | 1027 – 1028 | Cleavage; by viral protease; partialBy similarity | 2 | |
Sitei | 1147 – 1148 | Cleavage; by viral proteaseBy similarity | 2 |
Keywords - PTMi
Lipoprotein, Myristate, PhosphoproteinPTM databases
iPTMneti | P12497 |
Interactioni
Subunit structurei
Homotrimer; further assembles as hexamers of trimers (By similarity). Matrix protein p17:
Interacts with gp41 (via C-terminus) (PubMed:8918455).
Interacts with host CALM1; this interaction induces a conformational change in the Matrix protein, triggering exposure of the myristate group (PubMed:21799007).
Interacts with host AP3D1; this interaction allows the polyprotein trafficking to multivesicular bodies during virus assembly (PubMed:15766529). Part of the pre-integration complex (PIC) which is composed of viral genome, matrix protein, Vpr and integrase (By similarity).
By similarity3 PublicationsHomodimer; the homodimer further multimerizes as homohexamers or homopentamers (PubMed:24066695).
Interacts with human PPIA/CYPA; This interaction stabilizes the capsid (PubMed:8980234).
Interacts with human NUP153 (PubMed:24130490).
Interacts with host PDZD8; this interaction stabilizes the capsid (By similarity).
Interacts with monkey TRIM5; this interaction destabilizes the capsid (By similarity).
By similarity3 PublicationsHeterodimer of p66 RT and p51 RT (RT p66/p51) (By similarity). Heterodimerization of RT is essential for DNA polymerase activity (By similarity). The overall folding of the subdomains is similar in p66 RT and p51 RT but the spatial arrangements of the subdomains are dramatically different (By similarity).
By similarityHomotetramer; may further associate as a homohexadecamer (By similarity). Part of the pre-integration complex (PIC) which is composed of viral genome, matrix protein, Vpr and integrase (By similarity).
Interacts with human SMARCB1/INI1 and human PSIP1/LEDGF isoform 1 (By similarity).
Interacts with human KPNA3; this interaction might play a role in nuclear import of the pre-integration complex (By similarity).
Interacts with human NUP153; this interaction might play a role in nuclear import of the pre-integration complex (PubMed:19369352).
By similarity1 PublicationBinary interactionsi
Hide detailsCapsid protein p24 (PRO_0000042395)
With | #Exp. | IntAct |
---|---|---|
itself | 3 | EBI-2369107,EBI-2369107 |
Integrase (PRO_0000042402)
With | #Exp. | IntAct |
---|---|---|
PSIP1 - isoform 1 [O75475-1] from Homo sapiens. | 3 | EBI-10131955,EBI-5279836 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
IntActi | P12497, 5 interactors |
Chemistry databases
BindingDBi | P12497 |
Structurei
Secondary structure
3D structure databases
BMRBi | P12497 |
SMRi | P12497 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P12497 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 508 – 577 | Peptidase A2PROSITE-ProRule annotationAdd BLAST | 70 | |
Domaini | 631 – 821 | Reverse transcriptasePROSITE-ProRule annotationAdd BLAST | 191 | |
Domaini | 1021 – 1144 | RNase HPROSITE-ProRule annotationAdd BLAST | 124 | |
Domaini | 1201 – 1351 | Integrase catalyticPROSITE-ProRule annotationAdd BLAST | 151 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 7 – 31 | Interaction with Gp411 PublicationAdd BLAST | 25 | |
Regioni | 8 – 43 | Interaction with host CALM1By similarityAdd BLAST | 36 | |
Regioni | 12 – 19 | Interaction with host AP3D11 Publication | 8 | |
Regioni | 14 – 33 | Interaction with membrane phosphatidylinositol 4,5-bisphosphate and RNA1 PublicationAdd BLAST | 20 | |
Regioni | 73 – 77 | Interaction with membrane phosphatidylinositol 4,5-bisphosphate1 Publication | 5 | |
Regioni | 189 – 227 | Interaction with human PPIA/CYPA and NUP1533 PublicationsAdd BLAST | 39 | |
Regioni | 277 – 363 | Dimerization/Multimerization of capsid protein p24By similarityAdd BLAST | 87 | |
Regioni | 489 – 493 | Dimerization of proteaseBy similarity | 5 | |
Regioni | 537 – 543 | Dimerization of proteaseBy similarity | 7 | |
Regioni | 576 – 588 | Dimerization of proteaseBy similarityAdd BLAST | 13 | |
Regioni | 814 – 822 | RT 'primer grip'By similarity | 9 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 16 – 22 | Nuclear export signalBy similarity | 7 | |
Motifi | 26 – 32 | Nuclear localization signalBy similarity | 7 | |
Motifi | 985 – 1001 | Tryptophan repeat motifBy similarityAdd BLAST | 17 |
Domaini
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 390 – 407 | CCHC-type 1PROSITE-ProRule annotationAdd BLAST | 18 | |
Zinc fingeri | 411 – 428 | CCHC-type 2PROSITE-ProRule annotationAdd BLAST | 18 | |
Zinc fingeri | 1150 – 1191 | Integrase-typePROSITE-ProRule annotationAdd BLAST | 42 |
Keywords - Domaini
Repeat, Zinc-fingerFamily and domain databases
CDDi | cd05482, HIV_retropepsin_like, 1 hit |
DisProti | DP00410 |
Gene3Di | 1.10.10.200, 1 hit 1.10.1200.30, 1 hit 1.10.150.90, 1 hit 1.10.375.10, 1 hit 2.30.30.10, 1 hit 2.40.70.10, 1 hit 3.30.420.10, 2 hits 3.30.70.270, 3 hits |
InterProi | View protein in InterPro IPR001969, Aspartic_peptidase_AS IPR043502, DNA/RNA_pol_sf IPR000721, Gag_p24 IPR017856, Integrase-like_N IPR036862, Integrase_C_dom_sf_retrovir IPR001037, Integrase_C_retrovir IPR001584, Integrase_cat-core IPR003308, Integrase_Zn-bd_dom_N IPR000071, Lentvrl_matrix_N IPR012344, Matrix_HIV/RSV_N IPR001995, Peptidase_A2_cat IPR021109, Peptidase_aspartic_dom_sf IPR034170, Retropepsin-like_cat_dom IPR018061, Retropepsins IPR008916, Retrov_capsid_C IPR008919, Retrov_capsid_N IPR010999, Retrovr_matrix IPR043128, Rev_trsase/Diguanyl_cyclase IPR012337, RNaseH-like_sf IPR002156, RNaseH_domain IPR036397, RNaseH_sf IPR000477, RT_dom IPR010659, RVT_connect IPR010661, RVT_thumb IPR001878, Znf_CCHC IPR036875, Znf_CCHC_sf |
Pfami | View protein in Pfam PF00540, Gag_p17, 1 hit PF00607, Gag_p24, 1 hit PF00552, IN_DBD_C, 1 hit PF02022, Integrase_Zn, 1 hit PF00075, RNase_H, 1 hit PF00665, rve, 1 hit PF00077, RVP, 1 hit PF00078, RVT_1, 1 hit PF06815, RVT_connect, 1 hit PF06817, RVT_thumb, 1 hit PF00098, zf-CCHC, 2 hits |
PRINTSi | PR00234, HIV1MATRIX |
SMARTi | View protein in SMART SM00343, ZnF_C2HC, 2 hits |
SUPFAMi | SSF46919, SSF46919, 1 hit SSF47836, SSF47836, 1 hit SSF47943, SSF47943, 1 hit SSF50122, SSF50122, 1 hit SSF50630, SSF50630, 1 hit SSF53098, SSF53098, 2 hits SSF56672, SSF56672, 1 hit SSF57756, SSF57756, 1 hit |
PROSITEi | View protein in PROSITE PS50175, ASP_PROT_RETROV, 1 hit PS00141, ASP_PROTEASE, 1 hit PS50994, INTEGRASE, 1 hit PS51027, INTEGRASE_DBD, 1 hit PS50879, RNASE_H, 1 hit PS50878, RT_POL, 1 hit PS50158, ZF_CCHC, 2 hits PS50876, ZF_INTEGRASE, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsiribosomal frameshifting. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MGARASVLSG GELDKWEKIR LRPGGKKQYK LKHIVWASRE LERFAVNPGL
60 70 80 90 100
LETSEGCRQI LGQLQPSLQT GSEELRSLYN TIAVLYCVHQ RIDVKDTKEA
110 120 130 140 150
LDKIEEEQNK SKKKAQQAAA DTGNNSQVSQ NYPIVQNLQG QMVHQAISPR
160 170 180 190 200
TLNAWVKVVE EKAFSPEVIP MFSALSEGAT PQDLNTMLNT VGGHQAAMQM
210 220 230 240 250
LKETINEEAA EWDRLHPVHA GPIAPGQMRE PRGSDIAGTT STLQEQIGWM
260 270 280 290 300
THNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF
310 320 330 340 350
YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPG ATLEEMMTAC
360 370 380 390 400
QGVGGPGHKA RVLAEAMSQV TNPATIMIQK GNFRNQRKTV KCFNCGKEGH
410 420 430 440 450
IAKNCRAPRK KGCWKCGKEG HQMKDCTERQ ANFLREDLAF PQGKAREFSS
460 470 480 490 500
EQTRANSPTR RELQVWGRDN NSLSEAGADR QGTVSFSFPQ ITLWQRPLVT
510 520 530 540 550
IKIGGQLKEA LLDTGADDTV LEEMNLPGRW KPKMIGGIGG FIKVRQYDQI
560 570 580 590 600
LIEICGHKAI GTVLVGPTPV NIIGRNLLTQ IGCTLNFPIS PIETVPVKLK
610 620 630 640 650
PGMDGPKVKQ WPLTEEKIKA LVEICTEMEK EGKISKIGPE NPYNTPVFAI
660 670 680 690 700
KKKDSTKWRK LVDFRELNKR TQDFWEVQLG IPHPAGLKQK KSVTVLDVGD
710 720 730 740 750
AYFSVPLDKD FRKYTAFTIP SINNETPGIR YQYNVLPQGW KGSPAIFQCS
760 770 780 790 800
MTKILEPFRK QNPDIVIYQY MDDLYVGSDL EIGQHRTKIE ELRQHLLRWG
810 820 830 840 850
FTTPDKKHQK EPPFLWMGYE LHPDKWTVQP IVLPEKDSWT VNDIQKLVGK
860 870 880 890 900
LNWASQIYAG IKVRQLCKLL RGTKALTEVV PLTEEAELEL AENREILKEP
910 920 930 940 950
VHGVYYDPSK DLIAEIQKQG QGQWTYQIYQ EPFKNLKTGK YARMKGAHTN
960 970 980 990 1000
DVKQLTEAVQ KIATESIVIW GKTPKFKLPI QKETWEAWWT EYWQATWIPE
1010 1020 1030 1040 1050
WEFVNTPPLV KLWYQLEKEP IIGAETFYVD GAANRETKLG KAGYVTDRGR
1060 1070 1080 1090 1100
QKVVPLTDTT NQKTELQAIH LALQDSGLEV NIVTDSQYAL GIIQAQPDKS
1110 1120 1130 1140 1150
ESELVSQIIE QLIKKEKVYL AWVPAHKGIG GNEQVDGLVS AGIRKVLFLD
1160 1170 1180 1190 1200
GIDKAQEEHE KYHSNWRAMA SDFNLPPVVA KEIVASCDKC QLKGEAMHGQ
1210 1220 1230 1240 1250
VDCSPGIWQL DCTHLEGKVI LVAVHVASGY IEAEVIPAET GQETAYFLLK
1260 1270 1280 1290 1300
LAGRWPVKTV HTDNGSNFTS TTVKAACWWA GIKQEFGIPY NPQSQGVIES
1310 1320 1330 1340 1350
MNKELKKIIG QVRDQAEHLK TAVQMAVFIH NFKRKGGIGG YSAGERIVDI
1360 1370 1380 1390 1400
IATDIQTKEL QKQITKIQNF RVYYRDSRDP VWKGPAKLLW KGEGAVVIQD
1410 1420 1430
NSDIKVVPRR KAKIIRDYGK QMAGDDCVAS RQDED
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M19921 Genomic RNA Translation: AAA44988.2 Sequence problems. |
Keywords - Coding sequence diversityi
Ribosomal frameshiftingSimilar proteinsi
Cross-referencesi
Web resourcesi
HIV drug resistance mutations |
hivdb HIV drug resistance database |
BioAfrica: HIV bioinformatics in Africa |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M19921 Genomic RNA Translation: AAA44988.2 Sequence problems. |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1A43 | X-ray | 2.60 | A | 278-363 | [»] | |
1A8O | X-ray | 1.70 | A | 284-352 | [»] | |
1AFV | X-ray | 3.70 | A/B | 133-283 | [»] | |
1AK4 | X-ray | 2.36 | C/D | 133-277 | [»] | |
1AUM | X-ray | 3.00 | A | 283-352 | [»] | |
1B92 | X-ray | 2.02 | A | 1197-1359 | [»] | |
1B9D | X-ray | 1.70 | A | 1197-1359 | [»] | |
1B9F | X-ray | 1.70 | A | 1197-1359 | [»] | |
1BAJ | X-ray | 2.60 | A | 278-377 | [»] | |
1BHL | X-ray | 2.20 | A | 1204-1354 | [»] | |
1BI4 | X-ray | 2.50 | A/B/C | 1197-1356 | [»] | |
1BIS | X-ray | 1.95 | A/B | 1194-1356 | [»] | |
1BIU | X-ray | 2.50 | A/B/C | 1194-1359 | [»] | |
1BIZ | X-ray | 1.95 | A/B | 1197-1359 | [»] | |
1BL3 | X-ray | 2.00 | A/B/C | 1197-1356 | [»] | |
1GWP | NMR | - | A | 133-283 | [»] | |
1HIW | X-ray | 2.30 | A/B/C/Q/R/S | 1-132 | [»] | |
1HYV | X-ray | 1.70 | A | 1194-1359 | [»] | |
1HYZ | X-ray | 2.30 | A | 1194-1359 | [»] | |
1ITG | X-ray | 2.30 | A | 1194-1359 | [»] | |
1K6Y | X-ray | 2.40 | A/B/C/D | 1148-1359 | [»] | |
1M9D | X-ray | 1.90 | C/D | 133-278 | [»] | |
1QS4 | X-ray | 2.10 | A/B/C | 1203-1356 | [»] | |
1UPH | NMR | - | A | 2-132 | [»] | |
1WJB | NMR | - | A/B | 1148-1202 | [»] | |
1WJD | NMR | - | A/B | 1148-1202 | [»] | |
1WKN | model | - | A/B | 1148-1417 | [»] | |
1ZA9 | model | - | A/D/H/K | 1148-1194 | [»] | |
B/E/I/L | 1197-1356 | [»] | ||||
C/F/J/M | 1367-1417 | [»] | ||||
2B4J | X-ray | 2.02 | A/B | 1197-1359 | [»] | |
2GOL | X-ray | 2.20 | A | 2-131 | [»] | |
B/D | 133-277 | [»] | ||||
2GON | X-ray | 1.90 | A/B/C/D | 133-278 | [»] | |
2H3F | NMR | - | A | 2-132 | [»] | |
2H3I | NMR | - | A | 2-132 | [»] | |
2H3Q | NMR | - | A | 2-132 | [»] | |
2H3V | NMR | - | A | 2-132 | [»] | |
2H3Z | NMR | - | A | 2-132 | [»] | |
2HMX | NMR | - | A | 1-132 | [»] | |
2HVP | X-ray | 3.00 | A | 489-587 | [»] | |
2ITG | X-ray | 2.60 | A | 1197-1359 | [»] | |
2JPR | NMR | - | A | 133-277 | [»] | |
2JYG | NMR | - | A | 280-363 | [»] | |
2JYL | NMR | - | A | 280-363 | [»] | |
2LF4 | NMR | - | A | 133-363 | [»] | |
2LYA | NMR | - | A | 2-132 | [»] | |
2LYB | NMR | - | A | 2-132 | [»] | |
2M3Z | NMR | - | A | 378-432 | [»] | |
2M8L | NMR | - | A/B | 133-363 | [»] | |
2M8N | NMR | - | A | 133-363 | [»] | |
2M8P | NMR | - | A | 133-363 | [»] | |
2ONT | X-ray | 2.40 | A | 278-352 | [»] | |
2PWM | X-ray | 1.90 | A/B/C/D/E/F/G/H | 133-278 | [»] | |
2PWO | X-ray | 1.45 | A/B/C/D | 133-278 | [»] | |
2PXR | X-ray | 1.50 | C | 133-278 | [»] | |
2X2D | X-ray | 1.95 | D/E | 133-278 | [»] | |
2XDE | X-ray | 1.40 | A/B | 133-278 | [»] | |
2XV6 | X-ray | 1.89 | A/C | 278-352 | [»] | |
2XXM | X-ray | 1.65 | A | 278-352 | [»] | |
3AV9 | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
3AVA | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
3AVB | X-ray | 1.85 | A/B | 1197-1359 | [»] | |
3AVC | X-ray | 1.77 | A/B | 1197-1359 | [»] | |
3AVF | X-ray | 1.70 | A/B | 1197-1356 | [»] | |
3AVG | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
3AVH | X-ray | 1.88 | A/B | 1197-1359 | [»] | |
3AVJ | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
3AVK | X-ray | 1.75 | A/B | 1197-1359 | [»] | |
3AVL | X-ray | 1.88 | A/B | 1197-1359 | [»] | |
3AVM | X-ray | 1.88 | A/B | 1197-1359 | [»] | |
3AVN | X-ray | 2.10 | A/B | 1197-1359 | [»] | |
3DIK | electron microscopy | 9.00 | A | 133-351 | [»] | |
3DPH | X-ray | 2.01 | A/B | 278-363 | [»] | |
3DS0 | X-ray | 1.60 | A | 278-363 | [»] | |
3DS1 | X-ray | 1.60 | A | 278-363 | [»] | |
3DS2 | X-ray | 1.20 | A/B | 278-363 | [»] | |
3DS3 | X-ray | 2.70 | A/B | 278-363 | [»] | |
3DS4 | X-ray | 1.12 | A/B | 278-363 | [»] | |
3DS5 | X-ray | 2.40 | A/B/C/D | 278-363 | [»] | |
3DTJ | X-ray | 4.00 | A/B/C/D | 278-363 | [»] | |
3GV2 | X-ray | 7.00 | A/B/C/D/E/F | 133-355 | [»] | |
3H47 | X-ray | 1.90 | A | 133-363 | [»] | |
3H4E | X-ray | 2.70 | A/B/C/D/E/F/G/H/I/J/K/L | 133-363 | [»] | |
3L3U | X-ray | 1.40 | A/B | 1197-1359 | [»] | |
3L3V | X-ray | 2.00 | A/B | 1197-1359 | [»] | |
3LPT | X-ray | 2.00 | A | 1197-1359 | [»] | |
3LPU | X-ray | 1.95 | A | 1197-1359 | [»] | |
3LRY | X-ray | 1.98 | A/B | 278-363 | [»] | |
3MGE | X-ray | 1.90 | A | 133-363 | [»] | |
3NF6 | X-ray | 1.90 | A/B | 1197-1359 | [»] | |
3NF7 | X-ray | 1.80 | A/B | 1197-1359 | [»] | |
3NF8 | X-ray | 1.90 | A/B | 1197-1359 | [»] | |
3NF9 | X-ray | 1.95 | A/B | 1197-1359 | [»] | |
3NFA | X-ray | 1.95 | A/B | 1197-1359 | [»] | |
3P05 | X-ray | 2.50 | A/B/C/D/E | 133-363 | [»] | |
3P0A | X-ray | 5.95 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T | 133-363 | [»] | |
3S85 | X-ray | 2.80 | A/B/C/D/E/F/G/H/I/J/K/L | 489-587 | [»] | |
3WNE | X-ray | 1.70 | A/B | 1203-1359 | [»] | |
3WNF | X-ray | 1.45 | A/B | 1203-1359 | [»] | |
3WNG | X-ray | 1.75 | A/B | 1203-1359 | [»] | |
3WNH | X-ray | 1.50 | A/B | 1203-1359 | [»] | |
3ZCM | X-ray | 1.80 | A/B | 1203-1359 | [»] | |
3ZSO | X-ray | 1.75 | A/B | 1203-1359 | [»] | |
3ZSQ | X-ray | 1.70 | A/B | 1203-1359 | [»] | |
3ZSR | X-ray | 1.70 | A/B | 1203-1359 | [»] | |
3ZSV | X-ray | 1.75 | A/B | 1203-1359 | [»] | |
3ZSW | X-ray | 1.80 | A/B | 1203-1359 | [»] | |
3ZSX | X-ray | 1.95 | A/B | 1203-1359 | [»] | |
3ZSY | X-ray | 2.20 | A/B | 1203-1359 | [»] | |
3ZSZ | X-ray | 2.00 | A/B | 1203-1359 | [»] | |
3ZT0 | X-ray | 1.95 | A/B | 1203-1359 | [»] | |
3ZT1 | X-ray | 1.75 | A/B | 1203-1359 | [»] | |
3ZT2 | X-ray | 1.70 | A/B | 1203-1359 | [»] | |
3ZT3 | X-ray | 1.95 | A/B | 1203-1359 | [»] | |
3ZT4 | X-ray | 2.20 | A/B | 1203-1359 | [»] | |
4AH9 | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
4AHR | X-ray | 1.90 | A/B | 1197-1359 | [»] | |
4AHS | X-ray | 1.75 | A/B | 1197-1359 | [»] | |
4AHT | X-ray | 1.80 | A/B | 1197-1359 | [»] | |
4AHU | X-ray | 1.90 | A/B | 1197-1359 | [»] | |
4AHV | X-ray | 1.80 | A/B | 1197-1359 | [»] | |
4CE9 | X-ray | 2.10 | A/B | 1197-1359 | [»] | |
4CEA | X-ray | 1.80 | A/B | 1197-1359 | [»] | |
4CEB | X-ray | 1.75 | A/B | 1197-1359 | [»] | |
4CEC | X-ray | 1.75 | A/B | 1197-1359 | [»] | |
4CED | X-ray | 1.75 | A/B | 1197-1359 | [»] | |
4CEE | X-ray | 1.80 | A/B | 1197-1359 | [»] | |
4CEF | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
4CEO | X-ray | 1.90 | A/B | 1197-1359 | [»] | |
4CEQ | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
4CER | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
4CES | X-ray | 1.85 | A/B | 1197-1359 | [»] | |
4CEZ | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
4CF0 | X-ray | 1.85 | A/B | 1197-1359 | [»] | |
4CF1 | X-ray | 1.95 | A/B | 1197-1359 | [»] | |
4CF2 | X-ray | 1.95 | A/B | 1197-1359 | [»] | |
4CF8 | X-ray | 1.65 | A/B | 1197-1359 | [»] | |
4CF9 | X-ray | 2.10 | A/B | 1197-1359 | [»] | |
4CFA | X-ray | 2.05 | A/B | 1197-1359 | [»] | |
4CFB | X-ray | 1.95 | A/B | 1197-1359 | [»] | |
4CFC | X-ray | 1.90 | A/B | 1197-1359 | [»] | |
4CFD | X-ray | 2.15 | A/B | 1197-1359 | [»] | |
4CGD | X-ray | 2.00 | A/B | 1197-1359 | [»] | |
4CGF | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
4CGG | X-ray | 1.75 | A/B | 1197-1359 | [»] | |
4CGH | X-ray | 1.76 | A/B | 1197-1359 | [»] | |
4CGI | X-ray | 2.07 | A/B | 1197-1359 | [»] | |
4CGJ | X-ray | 2.15 | A/B | 1197-1359 | [»] | |
4CHN | X-ray | 2.00 | A/B | 1197-1359 | [»] | |
4CHO | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
4CHP | X-ray | 1.90 | A/B | 1197-1359 | [»] | |
4CHQ | X-ray | 1.95 | A/B | 1197-1359 | [»] | |
4CHY | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
4CHZ | X-ray | 1.80 | A/B | 1197-1359 | [»] | |
4CIE | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
4CIF | X-ray | 1.80 | A/B | 1197-1359 | [»] | |
4CIG | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
4CJ3 | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
4CJ4 | X-ray | 1.80 | A/B | 1197-1359 | [»] | |
4CJ5 | X-ray | 1.95 | A/B | 1197-1359 | [»] | |
4CJE | X-ray | 1.90 | A/B | 1197-1359 | [»] | |
4CJF | X-ray | 1.90 | A/B | 1197-1359 | [»] | |
4CJK | X-ray | 1.75 | A/B | 1197-1359 | [»] | |
4CJL | X-ray | 1.77 | A | 1197-1359 | [»] | |
4CJP | X-ray | 2.00 | A/B | 1197-1359 | [»] | |
4CJQ | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
4CJR | X-ray | 1.80 | A/B | 1197-1359 | [»] | |
4CJS | X-ray | 1.80 | A/B | 1197-1359 | [»] | |
4CJT | X-ray | 1.71 | A/B | 1197-1359 | [»] | |
4CJU | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
4CJV | X-ray | 1.95 | A/B | 1197-1359 | [»] | |
4CJW | X-ray | 1.95 | A/B | 1197-1359 | [»] | |
4CK1 | X-ray | 1.75 | A/B | 1197-1359 | [»] | |
4CK2 | X-ray | 1.85 | A/B | 1197-1359 | [»] | |
4CK3 | X-ray | 1.79 | A/B | 1197-1359 | [»] | |
4COC | X-ray | 1.59 | A/B/C | 278-363 | [»] | |
4COP | X-ray | 1.85 | A/B | 278-363 | [»] | |
4DGA | X-ray | 1.90 | C/D | 133-277 | [»] | |
4DGE | X-ray | 2.20 | C/D | 133-277 | [»] | |
4DMN | X-ray | 2.45 | A | 1197-1359 | [»] | |
4E1M | X-ray | 1.90 | A | 1197-1359 | [»] | |
4E1N | X-ray | 2.00 | A | 1197-1359 | [»] | |
4E91 | X-ray | 1.70 | A/B | 133-278 | [»] | |
4E92 | X-ray | 1.80 | A/B | 133-278 | [»] | |
4GVM | X-ray | 2.16 | A | 1197-1359 | [»] | |
4GW6 | X-ray | 2.65 | A | 1197-1359 | [»] | |
4ID1 | X-ray | 1.87 | A | 1197-1359 | [»] | |
4IPY | X-ray | 1.64 | A/B/C/D | 278-363 | [»] | |
4JLH | X-ray | 2.09 | A | 1197-1359 | [»] | |
4JMU | X-ray | 2.00 | A | 1-111 | [»] | |
4LH4 | X-ray | 1.80 | A | 1197-1359 | [»] | |
4LH5 | X-ray | 2.19 | A | 1197-1359 | [»] | |
4LQW | X-ray | 1.95 | C/D | 133-278 | [»] | |
4NX4 | X-ray | 1.50 | C | 133-278 | [»] | |
4O0J | X-ray | 2.05 | A | 1197-1359 | [»] | |
4O55 | X-ray | 2.24 | A | 1197-1359 | [»] | |
4O5B | X-ray | 2.37 | A | 1197-1359 | [»] | |
4OVL | X-ray | 1.70 | A/B | 1197-1359 | [»] | |
4PHV | X-ray | 2.10 | A/B | 489-587 | [»] | |
4QNB | X-ray | 2.00 | A | 133-363 | [»] | |
4WYM | X-ray | 2.60 | A/B/C/D/E/F/G/H/I/J/K/L | 133-363 | [»] | |
4Y1C | X-ray | 2.30 | A/B | 1197-1359 | [»] | |
4Y1D | X-ray | 1.93 | A/B | 1197-1359 | [»] | |
4ZHR | X-ray | 2.60 | A | 588-1147 | [»] | |
B | 588-1015 | [»] | ||||
5HVP | X-ray | 2.00 | A/B | 489-587 | [»] | |
5JL4 | X-ray | 1.76 | A/B | 1197-1359 | [»] | |
5KGW | X-ray | 2.34 | A | 1197-1359 | [»] | |
5KGX | X-ray | 2.67 | A | 1197-1359 | [»] | |
5KRS | X-ray | 1.70 | A | 1204-1354 | [»] | |
5KRT | X-ray | 1.65 | A | 1204-1354 | [»] | |
5TEO | X-ray | 2.05 | A/B | 278-377 | [»] | |
5U1C | electron microscopy | 3.90 | A/B/C/D | 1132-1136 | [»] | |
A/B/C/D | 1148-1435 | [»] | ||||
5VCK | X-ray | 1.80 | A/B | 489-587 | [»] | |
5VEA | X-ray | 2.00 | A | 489-587 | [»] | |
5VJ3 | X-ray | 2.00 | A | 489-587 | [»] | |
5XN0 | X-ray | 2.60 | A/C | 588-1142 | [»] | |
B/D | 588-1015 | [»] | ||||
5XN1 | X-ray | 2.45 | A/C | 588-1142 | [»] | |
B/D | 588-1015 | [»] | ||||
5XN2 | X-ray | 2.38 | A/C | 588-1142 | [»] | |
B/D | 588-1015 | [»] | ||||
6ES8 | X-ray | 1.90 | A | 133-351 | [»] | |
6IK9 | X-ray | 2.44 | B/D | 588-1015 | [»] | |
6IKA | X-ray | 2.60 | B/D | 588-1015 | [»] | |
6JCF | X-ray | 2.15 | A | 1198-1359 | [»] | |
6JCG | X-ray | 2.50 | A | 1198-1359 | [»] | |
6KDJ | X-ray | 2.51 | B/D | 588-1015 | [»] | |
6KDK | X-ray | 2.56 | B/D | 588-1015 | [»] | |
6KDM | X-ray | 2.32 | B/D | 588-1015 | [»] | |
6KDN | X-ray | 2.30 | B/D | 588-1015 | [»] | |
6KDO | X-ray | 2.57 | B/D | 588-1015 | [»] | |
6MCR | X-ray | 1.48 | A | 489-587 | [»] | |
6MCS | X-ray | 1.52 | A | 489-587 | [»] | |
6OOS | X-ray | 1.90 | A/B/C/D | 489-587 | [»] | |
6OOT | X-ray | 1.82 | A/B | 489-587 | [»] | |
6OOU | X-ray | 2.13 | A/B | 489-587 | [»] | |
6OPW | X-ray | 2.10 | A/B | 489-587 | [»] | |
6OPY | X-ray | 2.13 | A/B | 489-587 | [»] | |
6OPZ | X-ray | 2.20 | A/B | 489-587 | [»] | |
6OXO | X-ray | 2.00 | A/B | 489-587 | [»] | |
6OXP | X-ray | 1.97 | A/B | 489-587 | [»] | |
6OXQ | X-ray | 1.89 | A/B | 489-587 | [»] | |
6OXR | X-ray | 2.04 | A/B | 489-587 | [»] | |
6OXS | X-ray | 1.99 | A/B | 489-587 | [»] | |
6OXT | X-ray | 1.86 | A/B | 489-587 | [»] | |
6OXU | X-ray | 1.86 | A/B | 489-587 | [»] | |
6OXV | X-ray | 1.99 | A/B | 489-587 | [»] | |
6OXW | X-ray | 1.98 | A/B | 489-587 | [»] | |
6OXX | X-ray | 1.96 | A/B | 489-587 | [»] | |
6OXY | X-ray | 1.96 | A/B | 489-587 | [»] | |
6OXZ | X-ray | 1.96 | A/B | 489-587 | [»] | |
6OY0 | X-ray | 2.00 | A/B | 489-587 | [»] | |
6OY1 | X-ray | 2.00 | A/B | 489-587 | [»] | |
6OY2 | X-ray | 1.99 | A/B | 489-587 | [»] | |
6OYD | X-ray | 1.46 | A | 489-587 | [»] | |
6OYR | X-ray | 1.54 | A | 489-587 | [»] | |
6PJB | X-ray | 1.98 | A/B | 489-587 | [»] | |
6PJC | X-ray | 1.97 | A/B/C/D | 489-587 | [»] | |
6PJD | X-ray | 1.89 | A/B | 489-587 | [»] | |
6PJE | X-ray | 1.92 | A/B | 489-587 | [»] | |
6PJF | X-ray | 1.94 | A/B | 489-587 | [»] | |
6PJG | X-ray | 1.80 | A/B | 489-587 | [»] | |
6PJH | X-ray | 1.85 | A/B | 489-587 | [»] | |
6PJI | X-ray | 1.90 | A/B | 489-587 | [»] | |
6PJK | X-ray | 2.00 | A/B | 489-587 | [»] | |
6PJL | X-ray | 1.99 | A/B | 489-587 | [»] | |
6PJM | X-ray | 1.93 | A/B | 489-587 | [»] | |
6PJN | X-ray | 1.98 | A/B | 489-587 | [»] | |
6PJO | X-ray | 1.95 | A/B | 489-587 | [»] | |
6PUT | electron microscopy | 2.90 | A/B/C/D | 1148-1435 | [»] | |
6PUW | electron microscopy | 2.90 | A/B/C/D | 1148-1435 | [»] | |
6PUY | electron microscopy | 2.80 | A/B/C/D | 1148-1435 | [»] | |
6PUZ | electron microscopy | 2.80 | A/B/C/D | 1148-1435 | [»] | |
6U8Q | electron microscopy | 4.67 | A/B/C/D/I/J/K/L/M/N/O/P | 1148-1435 | [»] | |
6UM8 | X-ray | 2.33 | A/B | 1204-1359 | [»] | |
6V3K | electron microscopy | 3.40 | A/B/C/D | 1148-1435 | [»] | |
6VDK | electron microscopy | 4.50 | A/B/C/D/I/J/M/P | 1148-1435 | [»] | |
9HVP | X-ray | 2.80 | A/B | 489-587 | [»] | |
BMRBi | P12497 | |||||
SMRi | P12497 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P12497, 5 interactors |
Chemistry databases
BindingDBi | P12497 |
DrugBanki | DB03118, (2Z)-1-(5-Chloro-1H-indol-3-yl)-3-hydroxy-3-(1H-tetrazol-5-yl)-2-propen-1-one DB02086, (3,4-Dihydroxy-Phenyl)-Triphenyl-Arsonium DB07575, 2,4-DIAMINO-1,5-DIPHENYL-3-HYDROXYPENTANE DB02994, Cacodylic acid DB08027, CAP-1 DB03676, Cystein-S-Yl Cacodylate DB08231, Myristic acid DB03963, S-(Dimethylarsenic)Cysteine |
PTM databases
iPTMneti | P12497 |
Protocols and materials databases
ABCDi | P12497, 25 sequenced antibodies |
Miscellaneous databases
EvolutionaryTracei | P12497 |
PROi | PR:P12497 |
Family and domain databases
CDDi | cd05482, HIV_retropepsin_like, 1 hit |
DisProti | DP00410 |
Gene3Di | 1.10.10.200, 1 hit 1.10.1200.30, 1 hit 1.10.150.90, 1 hit 1.10.375.10, 1 hit 2.30.30.10, 1 hit 2.40.70.10, 1 hit 3.30.420.10, 2 hits 3.30.70.270, 3 hits |
InterProi | View protein in InterPro IPR001969, Aspartic_peptidase_AS IPR043502, DNA/RNA_pol_sf IPR000721, Gag_p24 IPR017856, Integrase-like_N IPR036862, Integrase_C_dom_sf_retrovir IPR001037, Integrase_C_retrovir IPR001584, Integrase_cat-core IPR003308, Integrase_Zn-bd_dom_N IPR000071, Lentvrl_matrix_N IPR012344, Matrix_HIV/RSV_N IPR001995, Peptidase_A2_cat IPR021109, Peptidase_aspartic_dom_sf IPR034170, Retropepsin-like_cat_dom IPR018061, Retropepsins IPR008916, Retrov_capsid_C IPR008919, Retrov_capsid_N IPR010999, Retrovr_matrix IPR043128, Rev_trsase/Diguanyl_cyclase IPR012337, RNaseH-like_sf IPR002156, RNaseH_domain IPR036397, RNaseH_sf IPR000477, RT_dom IPR010659, RVT_connect IPR010661, RVT_thumb IPR001878, Znf_CCHC IPR036875, Znf_CCHC_sf |
Pfami | View protein in Pfam PF00540, Gag_p17, 1 hit PF00607, Gag_p24, 1 hit PF00552, IN_DBD_C, 1 hit PF02022, Integrase_Zn, 1 hit PF00075, RNase_H, 1 hit PF00665, rve, 1 hit PF00077, RVP, 1 hit PF00078, RVT_1, 1 hit PF06815, RVT_connect, 1 hit PF06817, RVT_thumb, 1 hit PF00098, zf-CCHC, 2 hits |
PRINTSi | PR00234, HIV1MATRIX |
SMARTi | View protein in SMART SM00343, ZnF_C2HC, 2 hits |
SUPFAMi | SSF46919, SSF46919, 1 hit SSF47836, SSF47836, 1 hit SSF47943, SSF47943, 1 hit SSF50122, SSF50122, 1 hit SSF50630, SSF50630, 1 hit SSF53098, SSF53098, 2 hits SSF56672, SSF56672, 1 hit SSF57756, SSF57756, 1 hit |
PROSITEi | View protein in PROSITE PS50175, ASP_PROT_RETROV, 1 hit PS00141, ASP_PROTEASE, 1 hit PS50994, INTEGRASE, 1 hit PS51027, INTEGRASE_DBD, 1 hit PS50879, RNASE_H, 1 hit PS50878, RT_POL, 1 hit PS50158, ZF_CCHC, 2 hits PS50876, ZF_INTEGRASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | POL_HV1N5 | |
Accessioni | P12497Primary (citable) accession number: P12497 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1989 |
Last sequence update: | July 27, 2011 | |
Last modified: | December 2, 2020 | |
This is version 224 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references