ID A7XWN5_SV40 Unreviewed; 712 AA. AC A7XWN5; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 02-SEP-2026, entry version 88. 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}; OS Simian virus 40 (SV40). OC Viruses; Floreoviria; Shotokuvirae; Cossaviricota; Papovaviricetes; OC Sepolyvirales; Polyomaviridae; Betapolyomavirus. OX NCBI_TaxID=1891767 {ECO:0000313|EMBL:ABU86079.1}; OH NCBI_TaxID=9539; Macaca (macaques). RN [1] {ECO:0000313|EMBL:ABU86079.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SV40 {ECO:0000313|EMBL:ABU86079.1}; RX PubMed=17900651; DOI=10.1016/j.virol.2007.06.045; RA Peden K., Sheng L., Omeir R., Yacobucci M., Klutch M., Laassri M., RA Chumakov K., Pal A., Murata H., Lewis A.M.Jr.; RT "Recovery of strains of the polyomavirus SV40 from rhesus monkey kidney RT cells dating from the 1950s to the early 1960s."; RL Virology 370:63-76(2008). RN [2] {ECO:0007829|PDB:4B8O} RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 123-132. RX PubMed=23250448; DOI=10.1105/tpc.112.104422; RA Chang C.W., Counago R.L., Williams S.J., Boden M., Kobe B.; RT "Crystal structure of rice importin-alpha and structural basis of its RT interaction with plant-specific nuclear localization signals."; RL Plant Cell 24:5074-5088(2012). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + phosphate + H(+); 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:ARBA00048988}; 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; EF579664; ABU86079.1; -; Genomic_DNA. DR PDB; 4B8O; X-ray; 2.08 A; B/C=123-132. DR MDRepo; A7XWN5; -. DR SMR; A7XWN5; -. DR EvolutionaryTrace; A7XWN5; -. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:UniProtKB-EC. 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:0008270; F:zinc 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 CDD; cd06257; DnaJ; 1. DR FunFam; 1.10.287.110:FF:000161; Small t antigen; 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. DR PDBsum; 4B8O; -. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4B8O}; 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 Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE- KW ProRule:PRU00551}; 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..75 FT /note="J" FT /evidence="ECO:0000259|PROSITE:PS50076" FT DOMAIN 139..254 FT /note="T-ag OBD" FT /evidence="ECO:0000259|PROSITE:PS51287" FT DOMAIN 265..357 FT /note="T-ag D1-type" FT /evidence="ECO:0000259|PROSITE:PS51341" FT DOMAIN 400..560 FT /note="SF3 helicase" FT /evidence="ECO:0000259|PROSITE:PS51206" FT DNA_BIND 139..254 FT /note="T-ag OBD" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00620" FT REGION 109..134 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 632..689 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 633..642 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 643..663 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 666..683 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 712 AA; 82037 MW; 765224F4005D5B55 CRC64; MDKVLNREES LQLMDLLGLE RSAWGNIPLM RKAYLKKCKE FHPDKGGDEE KMKKMNTLYK KMEDGVKYAH QPDFGGFWDA TEIPTYGTDE WEQWWNAFNE ENLFCSEEMP SSDDEATADS QHSTPPKKKR KVEDPKDFPS ELLSFLSHAV FSNRTLACFA IYTTKEKAAL LYKKIMEKYS VTFISRHNSY NHNILFFLTP HRHRVSAINN YAQKLCTFSF LICKGVNKEY LMYSALTRDP FSVIEESLPG GLKEHDFNPE EAEETKQVSW KLVTEYAMET KCDDVLLLLG MYLEFQYSFE MCLKCIKKEQ PSHYKYHEKH YANAAIFADS KNQKTICQQA VDTVLAKKRV DSLQLTREQM LTNRFNDLLD RMDIMFGSTG SADIEEWMAG VAWLHCLLPK MDSVVYDFLK CMVYNIPKKR YWLFKGPIDS GKTTLAAALL ELCGGKALNV NLPLDRLNFE LGVAIDQFLV VFEDVKGTGG ESRDLPSGQG INNLDNLRDY LDGSVKVNLE KKHLNKRTQI FPPGIVTMNE YSVPKTLQAR FVKQIDFRPK DYLKHCLERS EFLLEKRIIQ SGIALLLMLI WYRPVAEFAQ SIQSRIVEWK ERLDKEFSLS VYQKMKFNVA MGIGVLDWLR NSDDDDDDDS QENADKNEDG GEKNMEDSGH ETGIDSQSQG SFQAPQPSQS SQSVHDHNQP YHICRGFTCF KKPPTPPPEP ET //