ID K7QJ84_9POLY Unreviewed; 699 AA.
AC K7QJ84;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Large T antigen {ECO:0000256|ARBA:ARBA00018805};
OS Macaca fascicularis polyomavirus 1.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Alphapolyomavirus;
OC Alphapolyomavirus macacae.
OX NCBI_TaxID=1236398 {ECO:0000313|EMBL:AFU25608.1, ECO:0000313|Proteomes:UP000102806};
RN [1] {ECO:0000313|EMBL:AFU25608.1, ECO:0000313|Proteomes:UP000102806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2085 {ECO:0000313|EMBL:AFU25608.1};
RX PubMed=23818846;
RA Scuda N., Madinda N.F., Akoua-Koffi C., Adjogoua E.V., Wevers D.,
RA Hofmann J., Cameron K.N., Leendertz S.A., Couacy-Hymann E., Robbins M.,
RA Boesch C., Jarvis M.A., Moens U., Mugisha L., Calvignac-Spencer S.,
RA Leendertz F.H., Ehlers B.;
RT "Novel Polyomaviruses of Nonhuman Primates: Genetic and Serological
RT Predictors for the Existence of Multiple Unknown Polyomaviruses within the
RT Human Population.";
RL PLoS Pathog. 9:E1003429-E1003429(2013).
CC -!- SUBUNIT: Forms homohexamers in the presence of ATP. Interacts with host
CC HDAC1. Interacts (via LXCXE domain) with host RB1; the interaction
CC induces the aberrant dissociation of RB1-E2F1 complex thereby
CC disrupting RB1's activity. Interacts (via LXCXE domain) with host pRB-
CC related proteins RBL1 and RBL2. Interacts (via C-terminus) with host
CC TOP1 and POLA1 allowing DNA replication. Interacts with host
CC preinitiation complex components TBP, TFIIA and TFIID to regulate
CC transcription initiation. {ECO:0000256|ARBA:ARBA00026077}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; JX159986; AFU25608.1; -; Genomic_DNA.
DR RefSeq; YP_007195262.1; NC_019851.1.
DR GeneID; 14258149; -.
DR KEGG; vg:14258149; -.
DR OrthoDB; 14669at10239; -.
DR Proteomes; UP000102806; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR014015; Helicase_SF3_DNA-vir.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR016392; Lg_T_Ag_polyomavir.
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 Pfam; PF06431; Polyoma_lg_T_C; 1.
DR Pfam; PF02217; T_Ag_DNA_bind; 1.
DR PIRSF; PIRSF003368; Large_T_antigen_polyomaV; 1.
DR SMART; SM00382; AAA; 1.
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 12..86
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 205..325
FT /note="T-ag OBD"
FT /evidence="ECO:0000259|PROSITE:PS51287"
FT DOMAIN 332..424
FT /note="T-ag D1-type"
FT /evidence="ECO:0000259|PROSITE:PS51341"
FT DOMAIN 465..665
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51206"
FT DNA_BIND 205..325
FT /note="T-ag OBD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00620"
FT REGION 130..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 699 AA; 80194 MW; CC699E0D5788109A CRC64;
MDQILSQEER YELMDLLQIT RAAWGNLSLM KKAYKTVSKL YHPDKGGDST KMQRLNELFQ
RVQVTLLEIR SDSGTSSSQG YYSESPSFMR TPFAYCPEEN QDADSSGSWG KWWRDYVNKE
CCNDLFCTET MSSSSDEENG PPPPPPPTEE EDEIEEVPET PHTSTQSQSQ SQSQSFEETP
SSQNSFTCTP PKRRKSDEKK PEDFPVCLYA FLSHAIYSNK TMNSFLIYTT LEKSRQLYKT
VEKSKIKVDF KASFSYKDEE GEGSLLFLIT LGKHRVSAVK HFCVSQCTLS FIHCKGVVKP
LELYKALGKP PFKLLEENKP GVSMFDFQEE KEQSVNWQEI CNFASEAKIS DVLLLLGIYI
DFAVEPGKCS KCEKKQHKFH YNYHKAHHAN ACLFLESRAQ KNICQQAVDQ VLAARRLKLV
ECTRLELLEE RFLQLFEEME DFLHGEIEIL RWMSGVAWYT ILLDNSWDVF QNILQLITTS
QPKKRNVLFK GPINSGKTTL ASAFMHFFDG KALNINCPAD KLSFELGVAI DQFCVLLDDV
KGQITLNKHL QPGQGISNLD NLRDHLDGTI KVNLEKKHIN KRSQIFPPVI MTMNEYLLPP
TVGVRFALHL HFKPKAYLKQ SLEKSDLVAR RILNSGYTIL LLLLWYNPVD SFTPKVQEKV
VQWKETLERY VSITQFGNIQ QNIIDGKDPL DGIVIEEQM
//
