ID K7QJJ5_9POLY Unreviewed; 673 AA.
AC K7QJJ5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Large T antigen {ECO:0000256|ARBA:ARBA00018805};
OS Alphapolyomavirus sextipanos.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Alphapolyomavirus.
OX NCBI_TaxID=1891738 {ECO:0000313|EMBL:AFU25590.1, ECO:0000313|Proteomes:UP000107907};
RN [1] {ECO:0000313|EMBL:AFU25590.1, ECO:0000313|Proteomes:UP000107907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5743 {ECO:0000313|EMBL:AFU25590.1};
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; JX159982; AFU25590.1; -; Genomic_DNA.
DR RefSeq; YP_007195289.1; NC_019857.1.
DR GeneID; 14258187; -.
DR KEGG; vg:14258187; -.
DR OrthoDB; 14669at10239; -.
DR Proteomes; UP000107907; 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: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 178..299
FT /note="T-ag OBD"
FT /evidence="ECO:0000259|PROSITE:PS51287"
FT DOMAIN 306..398
FT /note="T-ag D1-type"
FT /evidence="ECO:0000259|PROSITE:PS51341"
FT DOMAIN 439..599
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51206"
FT DNA_BIND 178..299
FT /note="T-ag OBD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00620"
FT REGION 131..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 76915 MW; 6A25A32347E7BE22 CRC64;
MDQVLSIEEK NELMDLLQIS RAAWGNLSLM KKAYKSASKL YHPDKGGDPQ KMQRLNELFQ
KLQVALLEIR SDCGSSSSQG YYSESSFYFT ETPFSHCQPT DEEGGSWGKW WRQFVNKECC
DDLFCSETMA SSESDEENTS APLSAEDPEP EPEASQNSFT CTPPKRKKTE PNTPEDFPNC
LYSFLSHAIY SNKTTNSFLI YTTVEKGKQL FKNVDKSKIK VDFKAIFSYK EEGILEGSLL
FFITLGRHRV SAIKHFCVSQ CTLSFIHCKG VTKPLELYKA LGKPPFRLIE ENKPGVSMFD
FEEEKEQSVN WQELCNYALE AKIGDVLLLL GIYLDFAVEP GTCAKCEKKS HKFHYNYHSK
HHANARLFLE SRSQKAICQQ AIDQVLAARR LKLVECTRME LLEERFLQLF DEMEDFLHGE
IEILRWMAGV AWFTILIDNS WDVFQQVLQL ITTNQPKHRN VLFKGPINSG KTTVASAFLH
FLNGKALNIN CPADKLSFEL GCAMDQFVVL LDDVKGQITL NKHLQPGQGI NNLDNLRDHL
DGTIKVNLEK KHVNKVSQIF PPAIMTMNEY LLPPTIGARF ALHIHFKNRA FLRQSLEKSD
LIPRRILNSG YTILLLLLWY NPVASFTPAV QDKVVQWKET LEKYVSITQF GKIQQNILDG
NDPLHGIVIE EQI
//
