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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//