ID Q77YG5_FOAMV Unreviewed; 811 AA.
AC Q77YG5;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Gag polyprotein {ECO:0000256|ARBA:ARBA00019628};
GN Name=gag {ECO:0000313|EMBL:AAC82577.1};
OS Human spumaretrovirus (SFVcpz(hu)) (Human foamy virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Spumaretrovirinae; Spumavirus;
OC Simian foamy virus.
OX NCBI_TaxID=11963 {ECO:0000313|EMBL:AAC82577.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AAC82577.1}
RP NUCLEOTIDE SEQUENCE.
RA Petropoulos C.J.;
RT "Appendix 2: Retroviral taxonomy, protein structure, sequences, and genetic
RT maps.";
RL (In) Coffin, J.M. (eds.);
RL RETROVIRUSES, pp.757-0, Cold Spring Harbor Laboratory Press, Cold Spring
RL Harbor, New York, NY, USA (1997).
RN [2] {ECO:0000313|EMBL:AAC82577.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Chappey C.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in capsid formation and genome binding. Shortly
CC after infection, interaction between incoming particle-associated Gag
CC proteins and host dynein allows centrosomal targeting of the viral
CC genome (associated to Gag), prior to nucleus translocation and
CC integration into host genome. {ECO:0000256|ARBA:ARBA00025354}.
CC -!- SUBUNIT: The protease is a homodimer, whose active site consists of two
CC apposed aspartic acid residues. {ECO:0000256|PROSITE-ProRule:PRU00863}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Host nucleus
CC {ECO:0000256|ARBA:ARBA00004147}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
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DR EMBL; AF033816; AAC82577.1; -; Genomic_RNA.
DR MEROPS; A09.001; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044163; C:host cytoskeleton; IEA:InterPro.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019076; P:viral release from host cell; IEA:InterPro.
DR Gene3D; 1.20.5.1500; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR InterPro; IPR049099; Gag_C.
DR InterPro; IPR049101; Gag_central.
DR InterPro; IPR004957; Gag_N.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR001641; Spumavirus_A9.
DR Pfam; PF20672; Gag_FV_central; 1.
DR Pfam; PF20673; Gag_spuma_C; 1.
DR Pfam; PF03276; Gag_spuma_N; 1.
DR Pfam; PF03539; Spuma_A9PTase; 1.
DR PRINTS; PR00920; SPUMVIRPTASE.
DR PROSITE; PS51531; FV_PR; 1.
PE 4: Predicted;
KW Aspartyl protease {ECO:0000256|PROSITE-ProRule:PRU00863};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Cytoplasmic inwards viral transport {ECO:0000256|ARBA:ARBA00023120};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00863};
KW Microtubular inwards viral transport {ECO:0000256|ARBA:ARBA00022952};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU00863};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Viral nucleoprotein {ECO:0000256|ARBA:ARBA00023086};
KW Virion {ECO:0000256|ARBA:ARBA00022844};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT DOMAIN 635..774
FT /note="Peptidase A9"
FT /evidence="ECO:0000259|PROSITE:PS51531"
FT REGION 175..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 655
FT /note="For protease activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00863"
SQ SEQUENCE 811 AA; 89614 MW; 99C661CDFAF31065 CRC64;
MASGSNVEEY ELDVEALVVI LRDRNIPRNP LHGEVIGLRL TEGWWGQIER FQMVRLILQD
DDNEPLQRPR YEVIQRAVNP HTMFMISGPL AELQLAFQDL DLPEGPLRFG PLANGHYVQG
DPYSSSYRPV TMAETAQMTR DELEDVLNTQ SEIEIQMINL LELYEVETRA LRRQLAERSS
TGQGGISPGA PRSRPPVSSF SGLPSLPSIP GIHPRAPSPP RATSTPGNIP WSLGDDSPPS
SSFPGPSQPR VSFHPGNPFV EEEGHRPRSQ SRERRREILP APVPSAPPMI QYIPVPPPPP
IGTVIPIQHI RSVTGEPPRN PREIPIWLGR NAPAIDGVFP VTTPDLRCRI INAILGGNIG
LSLTPGDCLT WDSAVATLFI RTHGTFPMHQ LGNVIKGIVD QEGVATAYTL GMMLSGQNYQ
LVSGIIRGYL PGQAVVTALQ QRLDQEIDNQ TRAETFIQHL NAVYEILGLN ARGQSIRASV
TPQPRPSRGR GRGQNTSRPS QGPANSGRGR QRPASGQSNR GSSTQNQNQD NLNQGGYNLR
PRTYQPQRYG GGRGRRWNDN TNNQESRPSD QGSQTPRPNQ AGSGVRGNQS QTPRPAAGRG
GRGNHNRNQR SSGAGDSRAV NTVTQSATSS TDESSSAVTA ASGRIKGTKL LAHWDSGATI
TCIPESFLED EQPIKKTLIK TIHGEKQQNV YYVTFKVKGR KVEAEVIASP YEYILLSPTD
VPWLTQQPLQ LTILVPLQEY QEKILSKTAL PEDQKQQLKT LFVKYDNLWQ HWENQVGHRK
IRPHNIATGD YPPRPQKQYP INPKAKPVYK L
//
