ID Q98ZP7_SV40 Unreviewed; 537 AA. AC Q98ZP7; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 123. DE RecName: Full=Large T antigen {ECO:0000256|ARBA:ARBA00018805}; OS Simian virus 40 (SV40). OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes; OC Sepolyvirales; Polyomaviridae; Betapolyomavirus. OX NCBI_TaxID=1891767 {ECO:0000313|EMBL:AAK29054.1, ECO:0000313|Proteomes:UP000146988}; OH NCBI_TaxID=9539; Macaca (macaques). RN [1] {ECO:0007829|PDB:2TBD} RP STRUCTURE BY NMR OF 131-260. RX PubMed=8946857; DOI=10.1038/nsb1296-1034; RA Luo X., Sanford D.G., Bullock P.A., Bachovchin W.W.; RT "Solution structure of the origin DNA-binding domain of SV40 T-antigen."; RL Nat. Struct. Biol. 3:1034-1039(1996). RN [2] {ECO:0000313|EMBL:AAK29054.1, ECO:0000313|Proteomes:UP000146988} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GM00637H {ECO:0000313|EMBL:AAK29054.1}; RA Lednicky J.A., Butel J.S., Lewis A.M.; RT "Complete DNA sequence of SV40-GM00637H, defective variant 12."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0007829|PDB:2IPR, ECO:0007829|PDB:2ITJ} RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 131-259, AND DISULFIDE BONDS. RX PubMed=17139255; DOI=10.1038/sj.emboj.7601452; RA Bochkareva E., Martynowski D., Seitova A., Bochkarev A.; RT "Structure of the origin-binding domain of simian virus 40 large T antigen RT bound to DNA."; RL EMBO J. 25:5961-5969(2006). RN [4] {ECO:0007829|PDB:2IF9, ECO:0007829|PDB:2NTC} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 131-260, AND DISULFIDE BONDS. RX PubMed=17253903; DOI=10.1371/journal.pbio.0050023; RA Meinke G., Phelan P., Moine S., Bochkareva E., Bochkarev A., Bullock P.A., RA Bohm A.; RT "The crystal structure of the SV40 T-antigen origin binding domain in RT complex with DNA."; RL PLoS Biol. 5:e23-e23(2007). CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147}. CC Nucleus {ECO:0000256|ARBA:ARBA00004123}. 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; AF345345; AAK29054.1; -; Genomic_DNA. DR PDB; 2IF9; X-ray; 2.59 A; A/B=131-260. DR PDB; 2IPR; X-ray; 1.50 A; A/B=131-259. DR PDB; 2ITJ; X-ray; 2.50 A; A/B=131-259. DR PDB; 2ITL; X-ray; 1.65 A; A/B=131-259. DR PDB; 2NL8; X-ray; 2.30 A; A=131-259. DR PDB; 2NTC; X-ray; 2.40 A; A/B=131-260. DR PDB; 2TBD; NMR; -; A=131-260. DR PDBsum; 2IF9; -. DR PDBsum; 2IPR; -. DR PDBsum; 2ITJ; -. DR PDBsum; 2ITL; -. DR PDBsum; 2NL8; -. DR PDBsum; 2NTC; -. DR PDBsum; 2TBD; -. DR SMR; Q98ZP7; -. DR Proteomes; UP000146988; Genome. 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; 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 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 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:2IF9, ECO:0007829|PDB:2IPR}; 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 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..537 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 COMPBIAS 120..134 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 216 FT /note="Interchain" FT /evidence="ECO:0007829|PDB:2IF9, ECO:0007829|PDB:2IPR" SQ SEQUENCE 537 AA; 61675 MW; 3337EFB55B957FA1 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 INNLSHITSV EVLLALKNLP HLPLNLKHKM NAIVVVNLFI AAYNGYK //