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Protein

Gag-Pro-Pol polyprotein

Gene

gag-pro-pol

Organism
Rous sarcoma virus (strain Prague C) (RSV-PrC)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Capsid protein p27 forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex.By similarity
The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell.PROSITE-ProRule annotation

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).PROSITE-ProRule annotation
Endonucleolytic cleavage to 5'-phosphomonoester.PROSITE-ProRule annotation

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: Binds 8 Mg2+ ions per integrase homotetramer.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei614 – 6141For protease activity; shared with dimeric partnerPROSITE-ProRule annotation
Metal bindingi815 – 8151Magnesium; catalytic; for reverse transcriptase activityBy similarity
Metal bindingi890 – 8901Magnesium; catalytic; for reverse transcriptase activityBy similarity
Metal bindingi891 – 8911Magnesium; catalytic; for reverse transcriptase activityBy similarity
Metal bindingi1158 – 11581Magnesium; catalytic; for RNase H activityBy similarity
Metal bindingi1192 – 11921Magnesium; catalytic; for RNase H activityBy similarity
Metal bindingi1213 – 12131Magnesium; catalytic; for RNase H activityBy similarity
Metal bindingi1272 – 12721Magnesium; catalytic; for RNase H activityBy similarity
Metal bindingi1344 – 13441Magnesium; catalytic; for integrase activityBy similarity
Metal bindingi1401 – 14011Magnesium; catalytic; for integrase activityBy similarity
Metal bindingi1437 – 14371Magnesium; catalytic; for integrase activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri507 – 52418CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri533 – 55018CCHC-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1280 – 132142Integrase-typePROSITE-ProRule annotationAdd
BLAST
DNA bindingi1502 – 155049Integrase-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed DNA polymerase, Transferase

Keywords - Biological processi

DNA integration, DNA recombination, Viral genome integration, Virus entry into host cell

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding, RNA-binding, Viral nucleoprotein, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Gag-Pro-Pol polyprotein
Cleaved into the following 12 chains:
Integrase (EC:2.7.7.-1 Publication, EC:3.1.-.-1 Publication)
Short name:
IN
Alternative name(s):
pp32
Gene namesi
Name:gag-pro-pol
OrganismiRous sarcoma virus (strain Prague C) (RSV-PrC)
Taxonomic identifieri11888 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeAlpharetrovirus
Virus hostiGallus gallus (Chicken) [TaxID: 9031]
Proteomesi
  • UP000007183 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Virion

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2750.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 155155Matrix protein p19PRO_5000053588Add
BLAST
Chaini156 – 16611p2APRO_0000397068Add
BLAST
Chaini167 – 17711p2BPRO_0000397069Add
BLAST
Chaini178 – 23962p10PRO_5000053589Add
BLAST
Chaini240 – 479240Capsid protein p27PRO_5000053590Add
BLAST
Chaini480 – 4889p3PRO_0000397070
Chaini489 – 57789Nucleocapsid protein p12PRO_5000053591Add
BLAST
Chaini578 – 708131Protease p15PRO_5000053592Add
BLAST
Chaini709 – 1567859Reverse transcriptase beta-subunitPRO_0000397071Add
BLAST
Chaini709 – 1280572Reverse transcriptase alpha-subunitPRO_0000040986Add
BLAST
Chaini1281 – 1567287IntegrasePRO_0000040987Add
BLAST
Chaini1568 – 160336p4PRO_0000397072Add
BLAST

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei155 – 1562Cleavage; by viral protease p15
Sitei166 – 1672Cleavage; by viral protease p15
Sitei177 – 1782Cleavage; by viral protease p15
Sitei239 – 2402Cleavage; by viral protease p15
Sitei479 – 4802Cleavage; by viral protease p15
Sitei488 – 4892Cleavage; by viral protease p15
Sitei577 – 5782Cleavage; by viral protease p15
Sitei708 – 7092Cleavage; by viral protease p15
Sitei1280 – 12812Cleavage; by viral protease p15
Sitei1567 – 15682Cleavage; by viral protease p15

Miscellaneous databases

PMAP-CutDBO92805.

Interactioni

Subunit structurei

The protease is active as a homodimer (By similarity). The integrase forms a homotetramer. Reverse transcriptase is a heterodimer of alpha and beta subunits. Three forms of RT exist: alpha-alpha (alpha-Pol), beta-beta (beta-Pol), and alpha-beta, with the major form being the heterodimer. Both the polymerase and RNase H active sites are located in the alpha subunit of heterodimeric RT alpha-beta.By similarity1 Publication

Protein-protein interaction databases

MINTiMINT-214692.

Chemistry

BindingDBiP03354.

Structurei

Secondary structure

1
1603
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1339 – 13479Combined sources
Helixi1349 – 13513Combined sources
Beta strandi1356 – 13627Combined sources
Turni1363 – 13653Combined sources
Beta strandi1368 – 13758Combined sources
Helixi1378 – 139215Combined sources
Beta strandi1396 – 14005Combined sources
Helixi1404 – 14074Combined sources
Helixi1409 – 141810Combined sources
Beta strandi1421 – 14244Combined sources
Helixi1430 – 14334Combined sources
Helixi1435 – 145319Combined sources
Beta strandi1457 – 14593Combined sources
Helixi1462 – 14643Combined sources
Helixi1465 – 147814Combined sources
Helixi1488 – 14936Combined sources
Beta strandi1503 – 15075Combined sources
Beta strandi1509 – 15113Combined sources
Beta strandi1513 – 152210Combined sources
Beta strandi1524 – 15318Combined sources
Turni1532 – 15343Combined sources
Beta strandi1537 – 15415Combined sources
Helixi1542 – 15443Combined sources
Beta strandi1545 – 15473Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BAIX-ray2.4A/B578-701[»]
1C0MX-ray2.53A/B/C/D1329-1566[»]
1C1AX-ray3.10A/B1329-1566[»]
3TIRX-ray4.10A240-465[»]
4FW1X-ray1.86A/B1329-1550[»]
4FW2X-ray2.65A/B1281-1550[»]
5EJKX-ray3.80A/B/C/D/E/F/G/H1281-1550[»]
ProteinModelPortaliP03354.
SMRiP03354. Positions 2-87, 214-469, 503-552, 578-701, 1329-1550.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03354.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini609 – 69082Peptidase A2PROSITE-ProRule annotationAdd
BLAST
Domaini750 – 938189Reverse transcriptasePROSITE-ProRule annotationAdd
BLAST
Domaini1149 – 1280132RNase HPROSITE-ProRule annotationAdd
BLAST
Domaini1333 – 1496164Integrase catalyticPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi172 – 1754PPXY motifBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi171 – 1744Poly-Pro

Domaini

Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. P2B contains one L domain: a PPXY motif which probably binds to the WW domains of HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases (By similarity).By similarity
Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity).By similarity

Sequence similaritiesi

Contains 2 CCHC-type zinc fingers.PROSITE-ProRule annotation
Contains 1 integrase catalytic domain.PROSITE-ProRule annotation
Contains 1 integrase-type DNA-binding domain.PROSITE-ProRule annotation
Contains 1 integrase-type zinc finger.PROSITE-ProRule annotation
Contains 1 peptidase A2 domain.PROSITE-ProRule annotation
Contains 1 reverse transcriptase domain.PROSITE-ProRule annotation
Contains 1 RNase H domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri507 – 52418CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri533 – 55018CCHC-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1280 – 132142Integrase-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Family and domain databases

Gene3Di1.10.10.200. 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.
4.10.60.10. 1 hit.
InterProiIPR001969. Aspartic_peptidase_AS.
IPR004028. Gag_M.
IPR000721. Gag_p24.
IPR001037. Integrase_C_retrovir.
IPR001584. Integrase_cat-core.
IPR017856. Integrase_Zn-bd_dom-like_N.
IPR003308. Integrase_Zn-bd_dom_N.
IPR012344. Matrix_HIV/RSV.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR018061. Retropepsins.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR010661. RVT_thumb.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00607. Gag_p24. 1 hit.
PF00552. IN_DBD_C. 1 hit.
PF02022. Integrase_Zn. 1 hit.
PF02813. Retro_M. 1 hit.
PF00665. rve. 1 hit.
PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
PF06817. RVT_thumb. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]
ProDomiPD002871. Gag_M. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF46919. SSF46919. 1 hit.
SSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF50122. SSF50122. 1 hit.
SSF50630. SSF50630. 1 hit.
SSF53098. SSF53098. 2 hits.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50175. 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. 1 hit.
PS50876. ZF_INTEGRASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by ribosomal frameshifting. AlignAdd to basket

Note: Translation results in the formation of the Gag-Pro. Ribosomal frameshifting at the gag-pro/pol genes boundary produces the Gag-Pro-Pol polyprotein.
Isoform Gag-Pro-Pol polyprotein (identifier: P03354-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEAVIKVISS ACKTYCGKTS PSKKEIGAML SLLQKEGLLM SPSDLYSPGS
60 70 80 90 100
WDPITAALSQ RAMILGKSGE LKTWGLVLGA LKAAREEQVT SEQAKFWLGL
110 120 130 140 150
GGGRVSPPGP ECIEKPATER RIDKGEEVGE TTVQRDAKMA PEETATPKTV
160 170 180 190 200
GTSCYHCGTA IGCNCATASA PPPPYVGSGL YPSLAGVGEQ QGQGGDTPPG
210 220 230 240 250
AEQSRAEPGH AGQAPGPALT DWARVREELA STGPPVVAMP VVIKTEGPAW
260 270 280 290 300
TPLEPKLITR LADTVRTKGL RSPITMAEVE ALMSSPLLPH DVTNLMRVIL
310 320 330 340 350
GPAPYALWMD AWGVQLQTVI AAATRDPRHP ANGQGRGERT NLNRLKGLAD
360 370 380 390 400
GMVGNPQGQA ALLRPGELVA ITASALQAFR EVARLAEPAG PWADIMQGPS
410 420 430 440 450
ESFVDFANRL IKAVEGSDLP PSARAPVIID CFRQKSQPDI QQLIRTAPST
460 470 480 490 500
LTTPGEIIKY VLDRQKTAPL TDQGIAAAMS SAIQPLIMAV VNRERDGQTG
510 520 530 540 550
SGGRARGLCY TCGSPGHYQA QCPKKRKSGN SRERCQLCNG MGHNAKQCRK
560 570 580 590 600
RDGNQGQRPG KGLSSGPWPG PEPPAVSLAM TMEHKDRPLV RVILTNTGSH
610 620 630 640 650
PVKQRSVYIT ALLDSGADIT IISEEDWPTD WPVMEAANPQ IHGIGGGIPM
660 670 680 690 700
RKSRDMIELG VINRDGSLER PLLLFPAVAM VRGSILGRDC LQGLGLRLTN
710 720 730 740 750
LIGRATVLTV ALHLAIPLKW KPDHTPVWID QWPLPEGKLV ALTQLVEKEL
760 770 780 790 800
QLGHIEPSLS CWNTPVFVIR KASGSYRLLH DLRAVNAKLV PFGAVQQGAP
810 820 830 840 850
VLSALPRGWP LMVLDLKDCF FSIPLAEQDR EAFAFTLPSV NNQAPARRFQ
860 870 880 890 900
WKVLPQGMTC SPTICQLVVG QVLEPLRLKH PSLCMLHYMD DLLLAASSHD
910 920 930 940 950
GLEAAGEEVI STLERAGFTI SPDKVQREPG VQYLGYKLGS TYVAPVGLVA
960 970 980 990 1000
EPRIATLWDV QKLVGSLQWL RPALGIPPRL MGPFYEQLRG SDPNEAREWN
1010 1020 1030 1040 1050
LDMKMAWREI VRLSTTAALE RWDPALPLEG AVARCEQGAI GVLGQGLSTH
1060 1070 1080 1090 1100
PRPCLWLFST QPTKAFTAWL EVLTLLITKL RASAVRTFGK EVDILLLPAC
1110 1120 1130 1140 1150
FREDLPLPEG ILLALKGFAG KIRSSDTPSI FDIARPLHVS LKVRVTDHPV
1160 1170 1180 1190 1200
PGPTVFTDAS SSTHKGVVVW REGPRWEIKE IADLGASVQQ LEARAVAMAL
1210 1220 1230 1240 1250
LLWPTTPTNV VTDSAFVAKM LLKMGQEGVP STAAAFILED ALSQRSAMAA
1260 1270 1280 1290 1300
VLHVRSHSEV PGFFTEGNDV ADSQATFQAY PLREAKDLHT ALHIGPRALS
1310 1320 1330 1340 1350
KACNISMQQA REVVQTCPHC NSAPALEAGV NPRGLGPLQI WQTDFTLEPR
1360 1370 1380 1390 1400
MAPRSWLAVT VDTASSAIVV TQHGRVTSVA VQHHWATAIA VLGRPKAIKT
1410 1420 1430 1440 1450
DNGSCFTSKS TREWLARWGI AHTTGIPGNS QGQAMVERAN RLLKDRIRVL
1460 1470 1480 1490 1500
AEGDGFMKRI PTSKQGELLA KAMYALNHFE RGENTKTPIQ KHWRPTVLTE
1510 1520 1530 1540 1550
GPPVKIRIET GEWEKGWNVL VWGRGYAAVK NRDTDKVIWV PSRKVKPDIT
1560 1570 1580 1590 1600
QKDEVTKKDE ASPLFAGISD WIPWEDEQEG LQGETASNKQ ERPGEDTLAA

NES
Note: Produced by -1 ribosomal frameshifting.
Length:1,603
Mass (Da):173,881
Last modified:August 10, 2010 - v2
Checksum:i01AF800FDF929CB6
GO
Isoform Gag-Pro polyprotein (identifier: P03322-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P03322.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by conventional translation.
Length:701
Mass (Da):74,527
GO

Sequence cautioni

The sequence AAB59933 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti756 – 7561E → V in CAA48535 (PubMed:8387633).Curated
Sequence conflicti1206 – 12061T → A in CAA48535 (PubMed:8387633).Curated
Sequence conflicti1274 – 12741Q → K in CAA48535 (PubMed:8387633).Curated
Sequence conflicti1381 – 13811V → A in CAA48535 (PubMed:8387633).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti722 – 7221P → S.
Natural varianti724 – 7241H → R.
Natural varianti884 – 8841C → R.
Natural varianti907 – 9071E → K.
Natural varianti955 – 9551A → T.
Natural varianti1012 – 10121R → Q.
Natural varianti1182 – 11821A → V.
Natural varianti1243 – 12431S → G.
Natural varianti1575 – 15751E → G.
Natural varianti1577 – 15771E → K.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01197 Genomic DNA. No translation available.
J02342 Genomic RNA. Translation: AAB59933.1. Different initiation.
X68524 Genomic DNA. Translation: CAA48535.1.
AF033808 Genomic RNA. Translation: AAC82561.1.
PIRiA03955. GNFV1R.
RefSeqiNP_056886.1. NC_001407.1.

Genome annotation databases

GeneIDi2193432.
KEGGivg:2193432.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01197 Genomic DNA. No translation available.
J02342 Genomic RNA. Translation: AAB59933.1. Different initiation.
X68524 Genomic DNA. Translation: CAA48535.1.
AF033808 Genomic RNA. Translation: AAC82561.1.
PIRiA03955. GNFV1R.
RefSeqiNP_056886.1. NC_001407.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BAIX-ray2.4A/B578-701[»]
1C0MX-ray2.53A/B/C/D1329-1566[»]
1C1AX-ray3.10A/B1329-1566[»]
3TIRX-ray4.10A240-465[»]
4FW1X-ray1.86A/B1329-1550[»]
4FW2X-ray2.65A/B1281-1550[»]
5EJKX-ray3.80A/B/C/D/E/F/G/H1281-1550[»]
ProteinModelPortaliP03354.
SMRiP03354. Positions 2-87, 214-469, 503-552, 578-701, 1329-1550.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-214692.

Chemistry

BindingDBiP03354.
ChEMBLiCHEMBL2750.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2193432.
KEGGivg:2193432.

Miscellaneous databases

EvolutionaryTraceiP03354.
PMAP-CutDBO92805.

Family and domain databases

Gene3Di1.10.10.200. 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.
4.10.60.10. 1 hit.
InterProiIPR001969. Aspartic_peptidase_AS.
IPR004028. Gag_M.
IPR000721. Gag_p24.
IPR001037. Integrase_C_retrovir.
IPR001584. Integrase_cat-core.
IPR017856. Integrase_Zn-bd_dom-like_N.
IPR003308. Integrase_Zn-bd_dom_N.
IPR012344. Matrix_HIV/RSV.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR018061. Retropepsins.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR010661. RVT_thumb.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00607. Gag_p24. 1 hit.
PF00552. IN_DBD_C. 1 hit.
PF02022. Integrase_Zn. 1 hit.
PF02813. Retro_M. 1 hit.
PF00665. rve. 1 hit.
PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
PF06817. RVT_thumb. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]
ProDomiPD002871. Gag_M. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF46919. SSF46919. 1 hit.
SSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF50122. SSF50122. 1 hit.
SSF50630. SSF50630. 1 hit.
SSF53098. SSF53098. 2 hits.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50175. 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. 1 hit.
PS50876. ZF_INTEGRASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOL_RSVP
AccessioniPrimary (citable) accession number: P03354
Secondary accession number(s): O92805, Q07462, Q64983
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 10, 2010
Last modified: May 11, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

The reverse transcriptase is an error-prone enzyme that lacks a proof-reading function. High mutations rate is a direct consequence of this characteristic. RT also displays frequent template switching leading to high recombination rate. Recombination mostly occurs between homologous regions of the two copackaged RNA genomes. If these two RNA molecules derive from different viral strains, reverse transcription will give rise to highly recombinated proviral DNAs.

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.