GAG_FIVSD
ID GAG_FIVSD Reviewed; 450 AA.
AC P19027;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 23-FEB-2022, entry version 95.
DE RecName: Full=Gag polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p15;
DE Short=MA;
DE Contains:
DE RecName: Full=Capsid protein p24;
DE Short=CA;
DE Contains:
DE RecName: Full=p1;
DE Contains:
DE RecName: Full=Nucleocapsid protein p13;
DE Short=NC;
GN Name=gag;
OS Feline immunodeficiency virus (strain San Diego) (FIV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11675;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate PPR;
RX PubMed=1697907; DOI=10.1128/jvi.64.10.4605-4613.1990;
RA Phillips T.R., Talbott R.L., Lamont C., Muir S., Lovelace K.M., Elder J.H.;
RT "Comparison of two host cell range variants of feline immunodeficiency
RT virus.";
RL J. Virol. 64:4605-4613(1990).
CC -!- FUNCTION: Matrix protein p15 forms the outer shell of the core of the
CC virus, lining the inner surface of the viral membrane. {ECO:0000250}.
CC -!- FUNCTION: Capsid protein p24 forms the conical core of the virus that
CC encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.
CC -!- FUNCTION: Nucleocapsid protein p13 encapsulates and protects viral
CC dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc
CC fingers (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p13]: Virion {ECO:0000305}.
CC -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC essential for viral particle budding. They recruit proteins of the host
CC ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC ESCRT-associated proteins. Nucleocapsid protein p13 contains one L
CC domain: a PTAP/PSAP motif, which interacts with the UEV domain of
CC TSG101 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the feline lentivirus group gag polyprotein
CC family. {ECO:0000305}.
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DR EMBL; M36968; AAA43075.1; -; Genomic_RNA.
DR SMR; P19027; -.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.90; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR012344; Matrix_HIV/RSV_N.
DR InterPro; IPR008916; Retrov_capsid_C.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF00098; zf-CCHC; 2.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 3: Inferred from homology;
KW Capsid protein; Host-virus interaction; Metal-binding; Repeat;
KW Viral budding; Viral budding via the host ESCRT complexes;
KW Viral matrix protein; Viral nucleoprotein; Viral release from host cell;
KW Virion; Virion maturation; Zinc; Zinc-finger.
FT CHAIN 1..135
FT /note="Matrix protein p15"
FT /id="PRO_0000038787"
FT CHAIN 136..357
FT /note="Capsid protein p24"
FT /id="PRO_0000038788"
FT PEPTIDE 358..366
FT /note="p1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000272323"
FT CHAIN 367..450
FT /note="Nucleocapsid protein p13"
FT /id="PRO_0000038789"
FT ZN_FING 375..392
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 394..411
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 116..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 438..441
FT /note="PTAP/PSAP motif"
SQ SEQUENCE 450 AA; 49134 MW; 8DA3959AE7F11818 CRC64;
MGNGQGRDWK MAIKRCSNVA VGVGGKSKKF GEGNFRWAIR MANVSTGREP GDIPETLDQL
RLVICDLQER REKFGSSKEI DMAITTLKVF AVVGLLNMTV STAAAAENMY TQMGLDTRPS
TKEAGGKEEG PPQAYPIQTV NGAPQYVALD PKMVSIFMEK AREGLGGEEV QLWFTAFSAN
LTPTDMATLI MAAPGCAADK EILDESLKQL TAEYDRTNPP DGPRPLPYFT AAEIMGIGLT
QEQQAEARFA PARMQCRAWY LEALGKLAAI KAKSPRAVQL RQGAKEDYSS FIDRLFAQID
QEQNTAEVKL YLKQSLSIAN ANAECKKAMS HLKPESTLEE KLRACQEIGS PGYKMQLLAE
ALTKVQVVQS KGSGPVCFNC KKPGHLARQC RDVKKCNKCG KPGHLAAKCW QGGKRNSGNW
KAGRAAAPVN QVQQTVMPSA PPMEEKLLDL