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Database: UniProt
Entry: J7HD82_9POLY
LinkDB: J7HD82_9POLY
Original site: J7HD82_9POLY 
ID   J7HD82_9POLY            Unreviewed;       801 AA.
AC   J7HD82;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Large T-antigen {ECO:0000313|EMBL:AFP94187.1};
OS   bat polyomavirus 2c.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Sepolyvirales; Polyomaviridae; Betapolyomavirus;
OC   Betapolyomavirus arplanirostris.
OX   NCBI_TaxID=2758133 {ECO:0000313|EMBL:AFP94187.1, ECO:0000313|Proteomes:UP000153654};
RN   [1] {ECO:0000313|EMBL:AFP94187.1, ECO:0000313|Proteomes:UP000153654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R104 {ECO:0000313|EMBL:AFP94187.1};
RX   PubMed=22971823; DOI=10.1099/vir.0.044149-0;
RA   Fagrouch Z., Sarwari R., Lavergne A., Delaval M., de Thoisy B., Lacoste V.,
RA   Verschoor E.J.;
RT   "Novel polyomaviruses in South American bats and their relationship to
RT   other members of the family Polyomaviridae.";
RL   J. Gen. Virol. 93:2652-2657(2012).
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; JQ958887; AFP94187.1; -; Genomic_DNA.
DR   Proteomes; UP000153654; Segment.
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; 1.10.287.110; 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; 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   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; 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   Reference proteome {ECO:0000313|Proteomes:UP000153654};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00671}.
FT   DOMAIN          308..423
FT                   /note="T-ag OBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51287"
FT   DOMAIN          429..520
FT                   /note="T-ag D1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51341"
FT   DOMAIN          559..719
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51206"
FT   DNA_BIND        308..423
FT                   /note="T-ag OBD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00620"
FT   REGION          98..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..291
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   801 AA;  90773 MW;  1162EABA185CA2E5 CRC64;
     MDHALSSEER KELCNLLGIA RHCYGNYPLM KSNFKHACLK YHPDKGGDQE KMARLNFLWQ
     KFLSYFMEMR RNIPEEDEEP IYGTTAFRHW WYRQHSRSHG RTQASTSGTS SRSSGYGSQP
     SQSSSTGSQD GFQQRQQHGE SGDPDHSFDS EQQHNQHQST DSEQQHQQQN SKKQKQQSKK
     SHHSSSSSSS RSDIPSSHGS HGFSGGNIYG NSSRVPPWDD DSLLCEESLS SSPSPEPAPT
     STEEEPSFSE SSSFRGPPGT PSQSTDDDFS MPRSPPKRRR APSPPSSYSS TPPRPKKNKP
     TSVPTDFPDD LLDCLSHAVY SNKTMSAFAI FTTQEKGKFF YEKLSEKFKV EYKGRFGCKE
     GCILVIVTLT KHRVSAVKNF ALPFCTVSFL LIKGINKLME MYDLLQSEPY RLIEENKSLS
     AHEFTEKKEI TCNWNLVADF AHEHGIDDPL LILAHYLDFA KPYPCNKCSS KSALKPHKSH
     EQHHKNAKLF IESKSQKSIC LQAAETVQAK RRLLMLELTR EEMLCEKFKS ILEKLKDLDP
     PDLKIYMAGV AWYYCLFDNF PQKVLKILKL LTENIPKKRN VLFKGPINSG KTSLAAAFLD
     LLDGKALNVN CPADKLPFEL GCALDKFCVC FEDVKGQLGA NKDLQPGQGF HNLDNLRDHL
     DGAVPVSLEK KHINKRHQIF PPCIITANEY AIPVTVAARI AYTLNFSLQP NLKASLDKNH
     DLRKMRVLQS GTTLLLCLIW HLDIEDFKST LHDDVQTWKD ILRAEVGRGM YYNMVENVEK
     GENPLFGIVD EEEEEEEPTN E
//
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