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Database: UniProt
Entry: Q9WG03_BFPYV
LinkDB: Q9WG03_BFPYV
Original site: Q9WG03_BFPYV 
ID   Q9WG03_BFPYV            Unreviewed;       587 AA.
AC   Q9WG03;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Large T antigen {ECO:0000256|ARBA:ARBA00018805};
OS   Budgerigar fledgling disease virus (BFPyV) (Aves polyomavirus 1).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Sepolyvirales; Polyomaviridae; Gammapolyomavirus.
OX   NCBI_TaxID=1891747 {ECO:0000313|EMBL:AAD30961.1, ECO:0000313|Proteomes:UP000180851};
OH   NCBI_TaxID=9224; Psittacidae (parrots).
RN   [1] {ECO:0000313|EMBL:AAD30961.1, ECO:0000313|Proteomes:UP000180851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lafferty S.L., Fudge A.M., Schmidt R.E., Wilson V.G., Phalen D.N.;
RT   "Avian polyomavirus infection and disease in a green aracaris (Pteroglossus
RT   viridis).";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; AF118150; AAD30961.1; -; Genomic_DNA.
DR   Proteomes; UP000180851; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0039576; P:disruption by virus of host JAK-STAT cascade via inhibition of JAK1 activity; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0039645; P:perturbation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 3.40.1310.20; -; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 1.20.1050.70; Large T antigen, SV40, domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.10.510; Zinc finger, large T-antigen D1 domain; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR014015; Helicase_SF3_DNA-vir.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR010932; Lg_T_Ag_Polyomavir_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003133; T_Ag_DNA-bd.
DR   InterPro; IPR017910; Znf_lg_T-Ag_D1-typ.
DR   InterPro; IPR037102; Znf_lg_T-Ag_D1_dom_sf.
DR   PANTHER; PTHR24074; CO-CHAPERONE PROTEIN DJLA; 1.
DR   PANTHER; PTHR24074:SF58; LD30543P; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF06431; Polyoma_lg_T_C; 1.
DR   Pfam; PF02217; T_Ag_DNA_bind; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF55464; Origin of replication-binding domain, RBD-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51206; SF3_HELICASE_1; 1.
DR   PROSITE; PS51287; T_AG_OBD; 1.
DR   PROSITE; PS51341; ZF_LTAG_D1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00620}; Early protein {ECO:0000256|ARBA:ARBA00022518};
KW   G1/S host cell cycle checkpoint dysregulation by virus
KW   {ECO:0000256|ARBA:ARBA00023309};
KW   Host nucleus {ECO:0000256|ARBA:ARBA00022562};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Inhibition of host innate immune response by virus
KW   {ECO:0000256|ARBA:ARBA00022632};
KW   Inhibition of host interferon signaling pathway by virus
KW   {ECO:0000256|ARBA:ARBA00022830};
KW   Inhibition of host JAK1 by virus {ECO:0000256|ARBA:ARBA00023318};
KW   Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00022830};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Modulation of host cell cycle by virus {ECO:0000256|ARBA:ARBA00022504};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00671}.
FT   DOMAIN          6..82
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          102..219
FT                   /note="T-ag OBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51287"
FT   DOMAIN          221..319
FT                   /note="T-ag D1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51341"
FT   DOMAIN          360..520
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51206"
FT   DNA_BIND        102..219
FT                   /note="T-ag OBD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00620"
FT   REGION          58..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   587 AA;  67105 MW;  59CCBC02BBCCC567 CRC64;
     MASLRRLTEL LGLPVTATAA DIKTAYRRTA LKYHPDKGGD EEKMKELNTL MEEFRETEGL
     RADETLEDSD PEPEESGYAT FENVSVPDID GAFFKLMKLK KCMQTYFSVN ERRKQQSCPD
     CHLLITSITK MPQLKAHLYE HFGIKGHMLA HWTGIALLVL QLEKPTRIST VHNFCKKYCT
     ISICSVRGIK KNCVHALITT LLDVPGLDPE ECSIDMNVVD EKQFMHAMLY DYAVQIDCTD
     ALLLLAIYKR LAQPTDKCPE CQKDKDTVKR KRSTHIDDHP RHQHNASLFL HIKDQKRLCQ
     CAVDAELAEK RFRSATMTRD ERLKERFRTV LRNIQELLDG ETEAIDDFVT AILLFNMLFP
     DVDVIVDILQ TMVKNPPKRR YYIFKGPVNT GKTTVAAAIL ALCTGASLNV NGTPDRLQFE
     LGCAIDQFMV LFEDVKGTPE PDTNLPSGFG MVNLDNLRDH LEGSVPVNLE RKHQNKVSQI
     FPPGIITMNN YVLPHTIQAR ARTLVNFKHI KVYAKALRNN ISVLEQRLIT KPETLLAYLL
     IRPESEKEIS ADLRAEFLTV IENLKFEVDE RFFQYNNRLH EGLCVHE
//
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