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Protein

Gag polyprotein

Gene

gag

Organism
Equine infectious anemia virus (strain Wyoming) (EIAV)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Matrix protein p15 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane.By similarity
Capsid protein p26 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex.By similarity
Nucleocapsid protein p11 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).By similarity
p9 plays a role in budding of the assembled particle by interacting with PDCD6IP/AIP1.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri381 – 398CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri400 – 417CCHC-type 2PROSITE-ProRule annotationAdd BLAST18

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Viral budding, Viral budding via the host ESCRT complexes, Virus exit from host cell

Keywords - Ligandi

Metal-binding, Viral nucleoprotein, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Gag polyprotein
Cleaved into the following 5 chains:
Gene namesi
Name:gag
OrganismiEquine infectious anemia virus (strain Wyoming) (EIAV)
Taxonomic identifieri11672 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusEquine lentivirus group
Virus hostiEquus asinus (Donkey) (Equus africanus asinus) [TaxID: 9793]
Equus caballus (Horse) [TaxID: 9796]

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_00000387801 – 124Matrix protein p15Add BLAST124
ChainiPRO_0000038781125 – 354Capsid protein p26Add BLAST230
PeptideiPRO_0000272315355 – 359p1Sequence analysis5
ChainiPRO_0000038782360 – 435Nucleocapsid protein p11Add BLAST76
ChainiPRO_0000038783436 – 486p9Add BLAST51

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi322 ↔ 342

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP69732.

Interactioni

Subunit structurei

p9 interacts with human PDCD6IP/AIP1.By similarity

Structurei

Secondary structure

1486
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 16Combined sources10
Beta strandi20 – 22Combined sources3
Beta strandi27 – 29Combined sources3
Turni45 – 47Combined sources3
Helixi53 – 64Combined sources12
Helixi71 – 86Combined sources16
Beta strandi92 – 95Combined sources4
Helixi98 – 108Combined sources11
Helixi146 – 152Combined sources7
Turni153 – 157Combined sources5
Helixi159 – 168Combined sources10
Turni169 – 171Combined sources3
Helixi174 – 183Combined sources10
Helixi188 – 208Combined sources21
Beta strandi220 – 222Combined sources3
Helixi228 – 231Combined sources4
Turni232 – 235Combined sources4
Helixi238 – 242Combined sources5
Helixi244 – 246Combined sources3
Helixi247 – 269Combined sources23
Helixi274 – 276Combined sources3
Helixi285 – 297Combined sources13
Helixi305 – 316Combined sources12
Helixi320 – 325Combined sources6
Turni326 – 328Combined sources3
Helixi335 – 341Combined sources7
Turni342 – 344Combined sources3
Beta strandi383 – 386Combined sources4
Turni393 – 395Combined sources3
Helixi410 – 413Combined sources4
Beta strandi463 – 465Combined sources3
Helixi466 – 470Combined sources5
Turni471 – 476Combined sources6
Helixi477 – 479Combined sources3
Turni480 – 482Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EIAX-ray2.70A140-346[»]
1HEKX-ray2.80A/B1-124[»]
2BL6NMR-A381-417[»]
2EIAX-ray2.70A/B141-346[»]
2K84NMR-A457-486[»]
2R03X-ray2.59B456-463[»]
4ZUTX-ray2.60C21-32[»]
4ZUUX-ray2.20C172-180[»]
4ZUWX-ray2.60C21-32[»]
ProteinModelPortaliP69732.
SMRiP69732.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69732.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi457 – 461LYPX(n)L motif5

Domaini

Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. p9 contains one L domain: a LYPX(n)L motif, which interacts with PDCD6IP/AIP1 (By similarity).By similarity

Sequence similaritiesi

Contains 2 CCHC-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri381 – 398CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri400 – 417CCHC-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.
4.10.60.10. 1 hit.
InterProiIPR014834. Gag_p15.
IPR000721. Gag_p24.
IPR012344. Matrix_HIV/RSV.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF08723. Gag_p15. 1 hit.
PF00607. Gag_p24. 1 hit.
PF00098. zf-CCHC. 2 hits.
[Graphical view]
SMARTiSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50158. ZF_CCHC. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P69732-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDPLTWSKA LKKLEKVTVQ GSQKLTTGNC NWALSLVDLF HDTNFVKEKD
60 70 80 90 100
WQLRDVIPLL EDVTQTLSGQ EREAFERTWW AISAVKMGLQ INNVVDGKAS
110 120 130 140 150
FQLLRAKYEK KTANKKQSEP SEEYPIMIDG AGNRNFRPLT PRGYTTWVNT
160 170 180 190 200
IQTNGLLNEA SQNLFGILSV DCTSEEMNAF LDVVPGQAGQ KQILLDAIDK
210 220 230 240 250
IADDWDNRHP LPNAPLVAPP QGPIPMTARF IRGLGVPRER QMEPAFDQFR
260 270 280 290 300
QTYRQWIIEA MSEGIKVMIG KPKAQNIRQG AKEPYPEFVD RLLSQIKSEG
310 320 330 340 350
HPQEISKFLT DTLTIQNANE ECRNAMRHLR PEDTLEEKMY ACRDIGTTKQ
360 370 380 390 400
KMMLLAKALQ TGLAGPFKGG ALKGGPLKAA QTCYNCGKPG HLSSQCRAPK
410 420 430 440 450
VCFKCKQPGH FSKQCRSVPK NGKQGAQGRP QKQTFPIQQK SQHNKSVVQE
460 470 480
TPQTQNLYPD LSEIKKEYNV KEKDQVEDLN LDSLWE
Length:486
Mass (Da):54,809
Last modified:July 21, 1986 - v1
Checksum:i97137FA5933D1DDA
GO

Sequence databases

PIRiA03949. FOLJEV.

Cross-referencesi

Sequence databases

PIRiA03949. FOLJEV.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EIAX-ray2.70A140-346[»]
1HEKX-ray2.80A/B1-124[»]
2BL6NMR-A381-417[»]
2EIAX-ray2.70A/B141-346[»]
2K84NMR-A457-486[»]
2R03X-ray2.59B456-463[»]
4ZUTX-ray2.60C21-32[»]
4ZUUX-ray2.20C172-180[»]
4ZUWX-ray2.60C21-32[»]
ProteinModelPortaliP69732.
SMRiP69732.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP69732.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP69732.

Family and domain databases

Gene3Di1.10.1200.30. 1 hit.
1.10.150.90. 1 hit.
1.10.375.10. 1 hit.
4.10.60.10. 1 hit.
InterProiIPR014834. Gag_p15.
IPR000721. Gag_p24.
IPR012344. Matrix_HIV/RSV.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF08723. Gag_p15. 1 hit.
PF00607. Gag_p24. 1 hit.
PF00098. zf-CCHC. 2 hits.
[Graphical view]
SMARTiSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50158. ZF_CCHC. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGAG_EIAVY
AccessioniPrimary (citable) accession number: P69732
Secondary accession number(s): P03351
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Caution

The original EMBL accession numbers (M11337 and M14855) assigned to this isolate (isolate Wyoming) have been made secondary to M16575 which is from a different isolate (clone 1365).Curated

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.