ID E2IPS1_9POLY Unreviewed; 739 AA.
AC E2IPS1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Large T antigen {ECO:0000313|EMBL:ADN93276.1};
DE Flags: Fragment;
OS Merkel cell polyomavirus.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Alphapolyomavirus;
OC Alphapolyomavirus quintihominis.
OX NCBI_TaxID=493803 {ECO:0000313|EMBL:ADN93276.1};
RN [1] {ECO:0000313|EMBL:ADN93276.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CH4US {ECO:0000313|EMBL:ADN93276.1};
RX PubMed=20865165; DOI=10.1371/journal.ppat.1001076;
RA Laude H.C., Jonchere B., Maubec E., Carlotti A., Marinho E., Couturaud B.,
RA Peter M., Sastre-Garau X., Avril M.F., Dupin N., Rozenberg F.;
RT "Distinct merkel cell polyomavirus molecular features in tumour and non
RT tumour specimens from patients with merkel cell carcinoma.";
RL PLoS Pathog. 6:e1001076-e1001076(2010).
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; HM587435; ADN93276.1; -; Genomic_DNA.
DR SMR; E2IPS1; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1310.20; -; 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; IPR014015; Helicase_SF3_DNA-vir.
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 SUPFAM; SSF55464; Origin of replication-binding domain, RBD-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 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 Host nucleus {ECO:0000256|ARBA:ARBA00022562};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00671}.
FT DOMAIN 238..352
FT /note="T-ag OBD"
FT /evidence="ECO:0000259|PROSITE:PS51287"
FT DOMAIN 359..450
FT /note="T-ag D1-type"
FT /evidence="ECO:0000259|PROSITE:PS51341"
FT DOMAIN 489..649
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51206"
FT DNA_BIND 238..352
FT /note="T-ag OBD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00620"
FT REGION 23..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..162
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADN93276.1"
SQ SEQUENCE 739 AA; 83251 MW; 284949203A2E78B4 CRC64;
VDEAPIYGTT KFKEWWRSGG FSFGKAYEYG PNPHGTNSRS RKPSSNASRG APSGSSPPHS
QSSSSGYGSF SASQASDSQS RGPDIPPEHH EEPTSSSGSS SREETTNSGR ESSTPNGTSV
PRNSSRTDGT WEDLFCDESL SSPEPPSSSE EPEEPPSSRS SPRQPPSSSA EEASSSQFTD
EEYRSSSFTT PKTPPPFSRK RKFGGSRSSA SSASSASFTS TPPKPKKNRE TPVPTDFPID
LSDYLSHAVY SNKTVSCFAI YTTSDKAIEL YDKIEKFKVD FKSRHACELG CILLFITLSK
HRVSAIKNFC STFCTISFLI CKGVNKMPEM YNNLCKPPYK LLQENKPLLN YEFQEKEKEA
SCNWNLVAEF ACEYELDDHF IILAHYLDFA KPFPCQKCEN RSRLKPHKAH EAHHSNAKLF
YESKSQKTIC QQAADTVLAK RRLEMLEMTR TEMLCKKFKK HLERLRDLDT IDLLYYMGGV
AWYCCLFEEF EKKLQKIIQL LTENIPKYRN IWFKGPINSG KTSFAAALID LLEGKALNIN
CPSDKLPFEL GCALDKFMVV FEDVKGQNSL NKDLQPGQGI NNLDNLRDHL DGAVAVSLEK
KHVNKKHQIF PPCIVTANDY FIPKTLIARF SYTLHFSPKA NLRDSLDQNM EIRKRRILQS
GTTLLLCLIW CLPDTTFKPC LQEEIKNWKQ ILQSEISYGK FCQMIENVEA GQDPLLNILI
EEEGPEETEE TQDSGTFSQ
//
