ID   GAG_FIVT2               Reviewed;         449 AA.
AC   P31821;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   23-FEB-2022, entry version 90.
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 (isolate TM2) (FIV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=31676;
OH   NCBI_TaxID=9681; Felidae (cat family).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1649349; DOI=10.1128/jvi.65.8.4539-4542.1991;
RA   Kiyomasu T., Miyazawa T., Furuya T., Shibata R., Sakai H., Sakuragi J.I.,
RA   Fukasawa M., Maki N., Hasegawa A., Mikami T., Adachi A.;
RT   "Identification of feline immunodeficiency virus rev gene activity.";
RL   J. Virol. 65:4539-4542(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1312825; DOI=10.1007/bf01317136;
RA   Maki N., Miyazawa T., Fukasawa M., Hasegawa A., Hayami M., Miki K.,
RA   Mikami T.;
RT   "Molecular characterization and heterogeneity of feline immunodeficiency
RT   virus isolates.";
RL   Arch. Virol. 123:29-45(1992).
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; M59418; AAA43072.1; -; Genomic_RNA.
DR   PIR; A45557; A45557.
DR   SMR; P31821; -.
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_0000038790"
FT   CHAIN           136..357
FT                   /note="Capsid protein p24"
FT                   /id="PRO_0000038791"
FT   PEPTIDE         358..366
FT                   /note="p1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000272317"
FT   CHAIN           367..449
FT                   /note="Nucleocapsid protein p13"
FT                   /id="PRO_0000038792"
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          117..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           437..440
FT                   /note="PTAP/PSAP motif"
SQ   SEQUENCE   449 AA;  49255 MW;  CF6235A3590FBF67 CRC64;
     MGNGQGRDWK MAIKRCSNVA VGVGSKSKRF GEGNFRWAIR MANVTTGREP GDIPETLEQL
     RSIICDLQDR REHYGSSKEI DMAITTLKVF AVAGILNMTV STATAAENMY AQMGLDTRPS
     VKESGGKEEG PPQAYPIQTV NGAPQYVALD PKMVSIFMEK AREGLGGEEV QLWFTAFSAN
     LTSTDMATLI MSAPGCAADK EILDETLKQM TAEYDRTHPP DGPRPLPYFT AAEIMGIGLT
     QEQQAEPRFA PARMQCRAWY LEALGKLAAI KAKSPRAVQL KQGAKEDYSS FIDRLFAQID
     QEQNTAEVKL YLKQSLSIAN ANPDCKRAMS HLKPESTLEE KLRACQEVGS PGYKMQLLAE
     ALTRVQTVQT KGPRLVCFNC KKPGHLARQC KEAKRCNNCG KPGHLAANCW QGGRKTSGNE
     KVGRAAAPVN QVQQIVPSAP PMEEKLLDL