ID A0A4P2VFJ5_9POLY Unreviewed; 799 AA. AC A0A4P2VFJ5; A0A4P2VJ04; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 22-APR-2020, sequence version 2. DT 02-OCT-2024, entry version 25. DE RecName: Full=Large T antigen {ECO:0000256|ARBA:ARBA00018805}; DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808}; DE AltName: Full=DNA 3'-5' helicase large T antigen {ECO:0000256|ARBA:ARBA00045019}; GN Name=LTAg {ECO:0000313|EMBL:BBG62133.2}; OS Rhinolophus affinis polyomavirus 1. OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes; OC Sepolyvirales; Polyomaviridae. OX NCBI_TaxID=2447809 {ECO:0000313|EMBL:BBG62133.2}; RN [1] {ECO:0000313|EMBL:BBG62133.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PyV22-DXC12 {ECO:0000313|EMBL:BBG62133.2}, PyVB-FN02C RC {ECO:0000313|EMBL:BBG62006.2}, and PyVB-FN04C RC {ECO:0000313|EMBL:BBG62011.2}; RA Tan Z., Gonzalez G., Xu L., Zhang P., Zhu A., He B., Carr M., Tu C.; RT "Extensive diversity of polyomaviruses in Chinese bats and evidence of RT intra- and inter-genera host-switching in their hosts."; RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4; CC Evidence={ECO:0000256|ARBA:ARBA00034618}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by CC translocating in the 3'-5' direction.; EC=5.6.2.4; CC Evidence={ECO:0000256|ARBA:ARBA00034617}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147}. 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; LC426678; BBG62006.2; -; Genomic_DNA. DR EMBL; LC426679; BBG62011.2; -; Genomic_DNA. DR EMBL; LC426701; BBG62133.2; -; Genomic_DNA. DR Proteomes; UP001235463; Segment. 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:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0039645; P:symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint; IEA:UniProtKB-KW. DR GO; GO:0052170; P:symbiont-mediated suppression of host innate immune response; IEA:UniProtKB-KW. DR GO; GO:0039576; P:symbiont-mediated suppression of host JAK-STAT cascade via inhibition of JAK1 activity; IEA:UniProtKB-KW. DR GO; GO:0039502; P:symbiont-mediated suppression of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0019049; P:virus-mediated perturbation of host defense response; 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; 1.20.120.1860; Small t-antigen, unique domain; 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; IPR003354; Papo_T_antigen. DR InterPro; IPR036092; Papo_T_antigensf. 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; PF02380; Papo_T_antigen; 1. DR Pfam; PF06431; Polyoma_lg_T_C; 1. DR Pfam; PF02217; T_Ag_DNA_bind; 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 SUPFAM; SSF161240; T-antigen specific domain-like; 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}; Helicase {ECO:0000256|ARBA:ARBA00022806}; 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:ARBA00023258}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235}; 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..77 FT /note="J" FT /evidence="ECO:0000259|PROSITE:PS50076" FT DOMAIN 284..398 FT /note="T-ag OBD" FT /evidence="ECO:0000259|PROSITE:PS51287" FT DOMAIN 405..497 FT /note="T-ag D1-type" FT /evidence="ECO:0000259|PROSITE:PS51341" FT DOMAIN 537..697 FT /note="SF3 helicase" FT /evidence="ECO:0000259|PROSITE:PS51206" FT DNA_BIND 284..398 FT /note="T-ag OBD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00620" FT REGION 232..277 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 769..799 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 232..250 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 251..269 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 769..784 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 785..799 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 799 AA; 92638 MW; 51160A2873A2175B CRC64; MDKFLSRQEM TELMELLQVP MHCYGNLPMM KINYKKMCKS YHPDKGGDEN KMKRLNELWQ KLQDNVCSAR QEYPRDQVNF WFWEDDFPTC GEYLGPKFAS KLCKAYPECV KYPKQDCGCL VCLLDKQHHI YKEVRQKRCL VWGECFCYSC YLNWFGFPNT TECFNWWGNI IHATDLQLLN VIGSQHWGNL YLQPSSQGTS SPRPPPYGSS SWEQWWHDFN KEWDDLFCDE SISSSDEDDH PRRRSSRNSP EPDGRNCPGS SQGSFATPPK PKKQKTFHVP KDFPRELDSF LSNAVYSNKT VCSFLIYTTK EKADFLYNQL EKFKPEFKSK HSYEDAALVF IMTPSKHRVS AIKNFCATHC TVSFLLCKAV IKPVDCYRAL CSEPFSLVEE NKPGIYEFQF EEEKQPSVDW NKIAEFAELN RLDDPLVIMG FYLDFASDPG LCIKCNKQTL KMHFKYHDKH HKNAMLFKDS KAQKNICQQA ADVVIAKRRV KVIECTRKEL LSERFQLHFE KLADIFSDTQ LHYYMAGVAW YTCLFEHIDE IVFKILKLLV ENVPKKRNIL FRGPINSGKT TLAAAILDLV GGKTLNVNCP AEKLPFELGC AIDQFAVVFE DVKGQIALNK NLQPGQGVCN LDNLRDYLDG SVKVNLEKKH VNKKSQIFPP CITTMNDYML PQTLYARYAY IVNFSPKDHL KKSLEANDDL MTKRVLQSGI TILLMMVYYL PTSSFTEDIQ ETVTNWKQTI DKYVGYGKLL DMQGNILQGR DPLEGILYDY EDEEQEEEEQ QEQNTENTND SGINTQQTV //