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Protein

Gag-Pro polyprotein

Gene

gag-pro

Organism
Rous sarcoma virus (strain Prague C) (RSV-PrC)
Status
Reviewed-Annotation score: Annotation score: 4 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei614For protease activity; shared with dimeric partnerPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri507 – 524CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri533 – 550CCHC-type 2PROSITE-ProRule annotationAdd BLAST18

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.23.B10. 5464.

Protein family/group databases

MEROPSiA02.015.

Names & Taxonomyi

Protein namesi
Recommended name:
Gag-Pro polyprotein
Cleaved into the following 8 chains:
Gene namesi
Name:gag-pro
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, Viral matrix protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000261131 – 155Matrix protein p19Add BLAST155
ChainiPRO_0000026114156 – 166p2AAdd BLAST11
ChainiPRO_0000026115167 – 177p2BAdd BLAST11
ChainiPRO_0000026116178 – 239p10Add BLAST62
ChainiPRO_0000026117240 – 479Capsid protein p27Add BLAST240
ChainiPRO_0000026118480 – 488p39
ChainiPRO_0000026119489 – 577Nucleocapsid protein p12Add BLAST89
ChainiPRO_0000026120578 – 701Protease p15Add BLAST124

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins.1 Publication

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

Interactioni

Subunit structurei

The protease is active as a homodimer.

Protein-protein interaction databases

MINTiMINT-6616346.

Structurei

Secondary structure

1701
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 16Combined sources15
Turni17 – 19Combined sources3
Helixi25 – 31Combined sources7
Helixi33 – 35Combined sources3
Helixi42 – 46Combined sources5
Turni48 – 51Combined sources4
Helixi52 – 60Combined sources9
Turni61 – 63Combined sources3
Beta strandi67 – 71Combined sources5
Helixi72 – 86Combined sources15
Helixi222 – 230Combined sources9
Beta strandi234 – 236Combined sources3
Beta strandi241 – 243Combined sources3
Beta strandi245 – 250Combined sources6
Helixi255 – 268Combined sources14
Helixi273 – 282Combined sources10
Helixi289 – 299Combined sources11
Helixi302 – 325Combined sources24
Beta strandi334 – 337Combined sources4
Helixi342 – 345Combined sources4
Turni350 – 354Combined sources5
Helixi356 – 362Combined sources7
Helixi365 – 385Combined sources21
Helixi392 – 394Combined sources3
Helixi403 – 415Combined sources13
Beta strandi417 – 419Combined sources3
Helixi421 – 423Combined sources3
Helixi424 – 435Combined sources12
Helixi438 – 444Combined sources7
Helixi454 – 462Combined sources9
Beta strandi579 – 581Combined sources3
Beta strandi584 – 586Combined sources3
Beta strandi589 – 596Combined sources8
Beta strandi605 – 613Combined sources9
Beta strandi621 – 623Combined sources3
Turni624 – 626Combined sources3
Beta strandi633 – 635Combined sources3
Beta strandi650 – 655Combined sources6
Beta strandi657 – 662Combined sources6
Beta strandi672 – 674Combined sources3
Beta strandi677 – 680Combined sources4
Beta strandi682 – 686Combined sources5
Helixi688 – 693Combined sources6
Beta strandi697 – 699Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A6SNMR-A2-87[»]
1BAIX-ray2.40A/B578-701[»]
1EM9X-ray2.05A/B240-393[»]
1EOQNMR-A394-488[»]
1P7NX-ray2.60A215-386[»]
2IHXNMR-A503-563[»]
2RSPX-ray2.00A/B578-701[»]
2X8Qelectron microscopy18.30A240-465[»]
3G0VX-ray2.00A389-465[»]
3G1GX-ray2.01A/B390-476[»]
3G1IX-ray2.10A/B389-465[»]
3G21X-ray0.90A389-465[»]
3G26X-ray1.55A389-465[»]
3G28X-ray1.64A389-465[»]
3G29X-ray2.50A/B389-465[»]
5A9Eelectron microscopy7.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R84-577[»]
ProteinModelPortaliP03322.
SMRiP03322.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03322.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini609 – 690Peptidase A2PROSITE-ProRule annotationAdd BLAST82

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi172 – 175PPXY motif4

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

Sequence similaritiesi

Contains 2 CCHC-type zinc fingers.PROSITE-ProRule annotation
Contains 1 peptidase A2 domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri507 – 524CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri533 – 550CCHC-type 2PROSITE-ProRule annotationAdd BLAST18

Keywords - Domaini

Repeat, Zinc-finger

Family and domain databases

Gene3Di1.10.1200.30. 1 hit.
1.10.150.90. 1 hit.
1.10.375.10. 1 hit.
2.40.70.10. 1 hit.
4.10.60.10. 1 hit.
InterProiIPR001969. Aspartic_peptidase_AS.
IPR004028. Gag_M.
IPR000721. Gag_p24.
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.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00607. Gag_p24. 1 hit.
PF02813. Retro_M. 1 hit.
PF00077. RVP. 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]
SUPFAMiSSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF50630. SSF50630. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50158. ZF_CCHC. 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 polyprotein (identifier: P03322-1) [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

L
Note: Produced by conventional translation.
Length:701
Mass (Da):74,527
Last modified:July 21, 1986 - v1
Checksum:i5FD365D9CFEF37F1
GO
Isoform Gag-Pro-Pol polyprotein (identifier: P03354-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P03354.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by -1 ribosomal frameshifting.
Length:1,603
Mass (Da):173,881
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti505A → S AA sequence (Ref. 2) Curated1
Sequence conflicti536Q → E AA sequence (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02342 Genomic RNA. Translation: AAB59932.1.
V01197 Genomic DNA. Translation: CAA24512.1.
PIRiA90834. FOFV1R.
RefSeqiNP_056887.1. NC_001407.1.

Genome annotation databases

GeneIDi1491923.
KEGGivg:1491923.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02342 Genomic RNA. Translation: AAB59932.1.
V01197 Genomic DNA. Translation: CAA24512.1.
PIRiA90834. FOFV1R.
RefSeqiNP_056887.1. NC_001407.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A6SNMR-A2-87[»]
1BAIX-ray2.40A/B578-701[»]
1EM9X-ray2.05A/B240-393[»]
1EOQNMR-A394-488[»]
1P7NX-ray2.60A215-386[»]
2IHXNMR-A503-563[»]
2RSPX-ray2.00A/B578-701[»]
2X8Qelectron microscopy18.30A240-465[»]
3G0VX-ray2.00A389-465[»]
3G1GX-ray2.01A/B390-476[»]
3G1IX-ray2.10A/B389-465[»]
3G21X-ray0.90A389-465[»]
3G26X-ray1.55A389-465[»]
3G28X-ray1.64A389-465[»]
3G29X-ray2.50A/B389-465[»]
5A9Eelectron microscopy7.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R84-577[»]
ProteinModelPortaliP03322.
SMRiP03322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-6616346.

Protein family/group databases

MEROPSiA02.015.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1491923.
KEGGivg:1491923.

Enzyme and pathway databases

BRENDAi3.4.23.B10. 5464.

Miscellaneous databases

EvolutionaryTraceiP03322.

Family and domain databases

Gene3Di1.10.1200.30. 1 hit.
1.10.150.90. 1 hit.
1.10.375.10. 1 hit.
2.40.70.10. 1 hit.
4.10.60.10. 1 hit.
InterProiIPR001969. Aspartic_peptidase_AS.
IPR004028. Gag_M.
IPR000721. Gag_p24.
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.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00607. Gag_p24. 1 hit.
PF02813. Retro_M. 1 hit.
PF00077. RVP. 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]
SUPFAMiSSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF50630. SSF50630. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGAG_RSVP
AccessioniPrimary (citable) accession number: P03322
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

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.