ID Q91NP9_POVJC Unreviewed; 688 AA.
AC Q91NP9;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Large T antigen {ECO:0000256|ARBA:ARBA00018805};
OS JC polyomavirus (JCPyV) (JCV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Betapolyomavirus;
OC Betapolyomavirus secuhominis.
OX NCBI_TaxID=10632 {ECO:0000313|EMBL:AAK70236.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AAK70236.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=125B {ECO:0000313|EMBL:AAK70236.1};
RA Stoner G.L., Jobes D.V., Ryschkewitsch C.F., Fernandez Cobo M.;
RT "Evolutionary analysis of the human polyomavirus JC.";
RL Submitted (JUN-2000) 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; AF281599; AAK70236.1; -; Genomic_DNA.
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; 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; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
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..75
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 140..255
FT /note="T-ag OBD"
FT /evidence="ECO:0000259|PROSITE:PS51287"
FT DOMAIN 266..358
FT /note="T-ag D1-type"
FT /evidence="ECO:0000259|PROSITE:PS51341"
FT DOMAIN 401..561
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51206"
FT DNA_BIND 140..255
FT /note="T-ag OBD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00620"
FT REGION 115..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 688 AA; 79307 MW; 3E9A4770AE417513 CRC64;
MDKVLNREES MELMDLLGLD RSAWGNIPVM RKAYLKKCKE LHPDKGGDED KMKRMNFLYK
KMEQGVKVAH QPDFGTWNSS EVPTYGTDEW ESWWNTFNEK WDEDLFCHEE MFASDDENTG
SQHSTPPRRK KKVEDPKDFP VDLHAFLSQA VFSNRTVASF AVYTTKEKAQ ILYKKLMEKY
SVTFISRHGF GGHNILFFLT PHRHRVSAIN NYCQKLCTFS FLICKGVNKE YLFYSALCRQ
PYAVVEESIQ GGLKEHDFNP EEPEETKQVS WKLVTQYALE TKCEDVFLLM GMYLDFQENP
QQCKKCEKKD QPNHFNHHEK HYYNAQIFAD SKNQKSICQQ AVDTVAAKQR VDSIHMTREE
MLVERFNFLL DKMDLIFGAH GNAVLEQYMA GVAWIHCLLP QMDTVIYDFL KCIVLNIPKK
RYWLFKGPID SGKTTLAAAL LDLCGGKSLN VNMPLERLNF ELGVGIDQFM VVFEDVKGTG
AESRDLPSGH GISNLDCLRD YLDGSVKVNL ERKHQNKRTQ VFPPGIVTMN EYSVPRTLQA
RFVRQIDFRP KAYLRKSLSC SEYLLEKRIL QSGMTLLLLL IWFRPVADFA AAIHERIVQW
KERLDLEISM YTFSTMKANV GMGRPILDFP REEDSEAEDS GHGSSTESQS QCSSQVSEAS
GADTQENCTF HICKGFQCFK KPKTPPPK
//
