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Protein

Gag-Pro-Pol polyprotein

Gene

gag-pro-pol

Organism
Rous sarcoma virus (strain Schmidt-Ruppin B) (RSV-SRB)
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)DescriptionActionsGraphical viewLength
Active sitei614For protease activity; shared with dimeric partnerPROSITE-ProRule annotation1
Metal bindingi815Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi890Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi891Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi1158Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi1192Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi1213Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi1272Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi1344Magnesium; catalytic; for integrase activity1
Metal bindingi1401Magnesium; catalytic; for integrase activity1
Metal bindingi1437Magnesium; catalytic; for integrase activity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri533 – 550CCHC-typePROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1280 – 1321Integrase-typePROSITE-ProRule annotationAdd BLAST42
DNA bindingi1502 – 1550Integrase-typePROSITE-ProRule annotationAdd BLAST49

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, 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, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Gag-Pro-Pol polyprotein
Cleaved into the following 12 chains:
Integrase (EC:2.7.7.-By similarity, EC:3.1.-.-By similarity)
Short name:
IN
Alternative name(s):
pp32
Gene namesi
Name:gag-pro-pol
OrganismiRous sarcoma virus (strain Schmidt-Ruppin B) (RSV-SRB)
Taxonomic identifieri269447 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeAlpharetrovirus
Virus hostiGallus gallus (Chicken) [TaxID: 9031]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1344D → N: Complete loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003970581 – 155Matrix protein p19By similarityAdd BLAST155
ChainiPRO_0000397059156 – 166p2ABy similarityAdd BLAST11
ChainiPRO_0000397060167 – 177p2BBy similarityAdd BLAST11
ChainiPRO_0000397061178 – 239p10By similarityAdd BLAST62
ChainiPRO_0000397062240 – 479Capsid protein p27By similarityAdd BLAST240
ChainiPRO_0000397063480 – 488p3By similarity9
ChainiPRO_0000397064489 – 577Nucleocapsid protein p12By similarityAdd BLAST89
ChainiPRO_0000397065578 – 708Protease p15By similarityAdd BLAST131
ChainiPRO_0000397066709 – 1567Reverse transcriptase beta-subunitBy similarityAdd BLAST859
ChainiPRO_0000040984709 – 1280Reverse transcriptase alpha-subunitBy similarityAdd BLAST572
ChainiPRO_00000409851281 – 1567IntegraseBy similarityAdd BLAST287
ChainiPRO_00003970671568 – 1603p4By similarityAdd BLAST36

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei155 – 156Cleavage; by viral protease p15By similarity2
Sitei166 – 167Cleavage; by viral protease p15By similarity2
Sitei177 – 178Cleavage; by viral protease p15By similarity2
Sitei239 – 240Cleavage; by viral protease p15By similarity2
Sitei479 – 480Cleavage; by viral protease p15By similarity2
Sitei488 – 489Cleavage; by viral protease p15By similarity2
Sitei577 – 578Cleavage; by viral protease p15By similarity2
Sitei708 – 709Cleavage; by viral protease p15By similarity2
Sitei1280 – 1281Cleavage; by viral protease p15By similarity2
Sitei1567 – 1568Cleavage; by viral protease p15By similarity2

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

Structurei

Secondary structure

11603
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1340 – 1347Combined sources8
Helixi1349 – 1351Combined sources3
Beta strandi1356 – 1362Combined sources7
Turni1363 – 1365Combined sources3
Beta strandi1368 – 1375Combined sources8
Helixi1378 – 1392Combined sources15
Beta strandi1396 – 1399Combined sources4
Helixi1404 – 1407Combined sources4
Helixi1409 – 1418Combined sources10
Beta strandi1421 – 1423Combined sources3
Beta strandi1428 – 1432Combined sources5
Helixi1434 – 1453Combined sources20
Beta strandi1457 – 1459Combined sources3
Helixi1462 – 1477Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A5VX-ray1.90A1332-1487[»]
1A5WX-ray2.00A1332-1487[»]
1A5XX-ray1.90A1332-1487[»]
1ASUX-ray1.70A1332-1487[»]
1ASVX-ray2.20A1332-1487[»]
1ASWX-ray1.80A1332-1487[»]
1CXQX-ray1.02A1333-1487[»]
1CXUX-ray1.42A1333-1487[»]
1CZ9X-ray1.20A1333-1487[»]
1CZBX-ray1.06A1333-1487[»]
1VSDX-ray1.70A1335-1479[»]
1VSEX-ray2.20A1335-1479[»]
1VSFX-ray2.05A1335-1479[»]
1VSHX-ray1.95A1335-1479[»]
1VSIX-ray2.20A1335-1479[»]
1VSJX-ray2.10A1335-1479[»]
1VSKX-ray2.20A1334-1479[»]
1VSLX-ray2.20A1334-1479[»]
1VSMX-ray2.15A1334-1479[»]
3O4NX-ray1.80A/B1333-1479[»]
3O4QX-ray1.55A1333-1479[»]
ProteinModelPortaliO92956.
SMRiO92956.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO92956.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini609 – 690Peptidase A2PROSITE-ProRule annotationAdd BLAST82
Domaini750 – 938Reverse transcriptasePROSITE-ProRule annotationAdd BLAST189
Domaini1163 – 1280RNase HPROSITE-ProRule annotationAdd BLAST118
Domaini1333 – 1496Integrase catalyticPROSITE-ProRule annotationAdd BLAST164

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi172 – 175PPXY motifBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi171 – 174Poly-Pro4

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 1 CCHC-type zinc finger.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)DescriptionActionsGraphical viewLength
Zinc fingeri533 – 550CCHC-typePROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1280 – 1321Integrase-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

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: O92956-1) [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 RAMVLGKSGE LKTWGLVLGA LKAAREEQVT SEQAKFWLGL
110 120 130 140 150
GGGRVSPPGP ECIEKPATER RIDKGEEVGE TTVQRDAKMA PEETATPKTV
160 170 180 190 200
GTSCYHCGTA IGCNCATASA PPPPYVGSGL YPSLAGVGEQ QGQGGDTPRG
210 220 230 240 250
AEQPRAEPGH AGLAPGPALT DWARIREELA STGPPVVAMP VVIKTEGPAW
260 270 280 290 300
TPLEPKLITR LADTVRTKGL RSPITMAEVE ALMSSPLLPH DVTNLMRVIL
310 320 330 340 350
GPAPYALWMD AWGVQLQTVI AAATRDPRHP ANGQGRGERT NLDRLKGLAD
360 370 380 390 400
GMVGNPQGQA ALLRPGELVA ITASALQAFR EVARLAEPAG PWADITQGPS
410 420 430 440 450
ESFVDFANRL IKAVEGSDLP PSARAPVIID CFRQKSQPDI QQLIRAAPST
460 470 480 490 500
LTTPGEIIKY VLDRQKIAPL TDQGIAAAMS SAIQPLVMAV VNRERDGQTG
510 520 530 540 550
SGGRARRLCY TCGSPGHYQA QCPKKRKSGN SRERCQLCDG MGHNAKQCRR
560 570 580 590 600
RDSNQGQRPG RGLSSGPWPV SEQPAVSLAM TMEHKDRPLV RVILTNTGSH
610 620 630 640 650
PVKQRSVYIT ALLDSGADIT IISEEDWPTD WPVVDTANPQ IHGIGGGIPM
660 670 680 690 700
RKSRDMIELG VINRDGSLER PLLLFPAVAM VRGSILGRDC LQGLGLRLTN
710 720 730 740 750
LVGRATVLTV 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 PSLRMLHYMD DLLLAASSHD
910 920 930 940 950
GLEAAGEEVI NTLERAGFTI SPDKIQREPG VQYLGYKLGS TYVAPVGLVA
960 970 980 990 1000
EPRIATLWDV QKLVGSLQWL RPALGIPPRL MGPFYEQLRG SDPNEAREWN
1010 1020 1030 1040 1050
LDMKMAWREI VQLSTTAALE RWDPALPLEG AVVRCEQGAI GVLGQGLSTH
1060 1070 1080 1090 1100
PRPCLWLFST QPTKAFTAWL EVLTLLITKL RASAVRTFGK EVDILLLPAC
1110 1120 1130 1140 1150
FREDLPLPEG ILLALRGFAG 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 TLHIGPRALS
1310 1320 1330 1340 1350
KACNISMQQA REVVQTCPHC NSAPALEAGV NPRGLGPLQI WQTDFTLEPR
1360 1370 1380 1390 1400
MAPRSWLAVT VDTASSAIVV TQHGRVTSVA AQHHWATAIA VLGRPKAIKT
1410 1420 1430 1440 1450
DNGSCFTSKS TREWLARWGI AHTTGIPGNS QGQAMVERAN RLLKDKIRVL
1460 1470 1480 1490 1500
AEGDGFMKRI PASKQGELLA KAMYALNHFE RGENTKTPVQ KHWRPTVLTE
1510 1520 1530 1540 1550
GPPVKIRIET GEWEKGWNVL VWGRGYAAVK NRDTDKVIWV PSRKVKPDIT
1560 1570 1580 1590 1600
QKDEVTKKDE ASPLFAGSSD WIPWGDEQEG LQEEAASNKQ EGPGEDTLAA

NES
Note: Produced by -1 ribosomal frameshifting.
Length:1,603
Mass (Da):173,990
Last modified:August 10, 2010 - v2
Checksum:i3BEFAA397C54CDE7
GO
Isoform Gag-Pro polyprotein (identifier: O92954-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry O92954.
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):74,753
GO

Sequence cautioni

The sequence AAC08988 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1376V → A (PubMed:8805516).Curated1
Sequence conflicti1441R → K (PubMed:8805516).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF052428 Genomic DNA. Translation: AAC08988.1. Different initiation.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF052428 Genomic DNA. Translation: AAC08988.1. Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A5VX-ray1.90A1332-1487[»]
1A5WX-ray2.00A1332-1487[»]
1A5XX-ray1.90A1332-1487[»]
1ASUX-ray1.70A1332-1487[»]
1ASVX-ray2.20A1332-1487[»]
1ASWX-ray1.80A1332-1487[»]
1CXQX-ray1.02A1333-1487[»]
1CXUX-ray1.42A1333-1487[»]
1CZ9X-ray1.20A1333-1487[»]
1CZBX-ray1.06A1333-1487[»]
1VSDX-ray1.70A1335-1479[»]
1VSEX-ray2.20A1335-1479[»]
1VSFX-ray2.05A1335-1479[»]
1VSHX-ray1.95A1335-1479[»]
1VSIX-ray2.20A1335-1479[»]
1VSJX-ray2.10A1335-1479[»]
1VSKX-ray2.20A1334-1479[»]
1VSLX-ray2.20A1334-1479[»]
1VSMX-ray2.15A1334-1479[»]
3O4NX-ray1.80A/B1333-1479[»]
3O4QX-ray1.55A1333-1479[»]
ProteinModelPortaliO92956.
SMRiO92956.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO92956.

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_RSVSB
AccessioniPrimary (citable) accession number: O92956
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: August 10, 2010
Last modified: November 30, 2016
This is version 101 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, 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.