ID L0N113_9POLY Unreviewed; 697 AA.
AC L0N113;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Large T antigen {ECO:0000256|ARBA:ARBA00018805};
OS Yellow baboon polyomavirus 1.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Sepolyvirales; Polyomaviridae; Alphapolyomavirus;
OC Alphapolyomavirus pacynocephalus.
OX NCBI_TaxID=1286213 {ECO:0000313|EMBL:BAM71847.1, ECO:0000313|Proteomes:UP000105764};
RN [1] {ECO:0000313|EMBL:BAM71847.1, ECO:0000313|Proteomes:UP000105764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS20 {ECO:0000313|EMBL:BAM71847.1};
RX PubMed=23426354; DOI=10.1099/vir.0.050740-0;
RA Yamaguchi H., Kobayashi S., Ishii A., Ogawa H., Nakamura I., Moonga L.,
RA Hang'ombe B.M., Mweene A.S., Thomas Y., Kimura T., Sawa H., Orba Y.;
RT "Identification of a novel polyomavirus from vervet monkeys in Zambia.";
RL J. Gen. Virol. 94:1357-1364(2013).
CC -!- SUBUNIT: Forms homohexamers in the presence of ATP. Interacts with host
CC HDAC1. Interacts (via LXCXE domain) with host RB1; the interaction
CC induces the aberrant dissociation of RB1-E2F1 complex thereby
CC disrupting RB1's activity. Interacts (via LXCXE domain) with host pRB-
CC related proteins RBL1 and RBL2. Interacts (via C-terminus) with host
CC TOP1 and POLA1 allowing DNA replication. Interacts with host
CC preinitiation complex components TBP, TFIIA and TFIID to regulate
CC transcription initiation. {ECO:0000256|ARBA:ARBA00026077}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AB767294; BAM71847.1; -; Genomic_DNA.
DR RefSeq; YP_009111352.1; NC_025894.1.
DR GeneID; 22520974; -.
DR KEGG; vg:22520974; -.
DR OrthoDB; 14669at10239; -.
DR Proteomes; UP000105764; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
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; SM00382; AAA; 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 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};
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 203..323
FT /note="T-ag OBD"
FT /evidence="ECO:0000259|PROSITE:PS51287"
FT DOMAIN 330..422
FT /note="T-ag D1-type"
FT /evidence="ECO:0000259|PROSITE:PS51341"
FT DOMAIN 463..663
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51206"
FT DNA_BIND 203..323
FT /note="T-ag OBD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00620"
FT REGION 131..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 697 AA; 79735 MW; 76025C6F7DAFF2D2 CRC64;
MDQTLSKTER NELMDLLQIT RAAWGNLSLM KKAYKTVSKL YHPDKGGDPA KMQRLNELFQ
RVQVTLMEIR SQSGSSSSQG YFSEDFFFGP TTFQFCPMDR DACREDLPNP GEGSWGKWWR
QFANSQSSDD LFCSETMSSS SDEETPAAQP APPPPTPEEE EDDIEFVEET PSSCDDQSSS
QSSYTCTPPK KRKTEEKKPD DFPVCLYSFL SHAIYSNKTM NSFLIYTTLE KARQLYRSVE
KSKIKVDFKA SFSYKDEEGE GCLLFLMTLG KHRVSAVKHF CVSQCTFSFI HCKGVVKPLE
LYKVLGKPPF KLLEENKPGV SMFDFQEEKE QAVNWQEICN FANEANISDV LLLLGIYIDF
AVDPGKCGKC EKKQHKFHYN YHKAHHANAC LFLESRAQKN ICQQAVDQVL AAKRLKLVEC
SRMELLEERF LQLFEEMDDF LHGEIEILRW MAGVAWYTIL LDNSWDIFQN ILQLITVSQP
KKRNVLIKGP INSGKTTLAS AFMHFFDGKA LNINCPADKL SFELGCAIDQ FCVLLDDVKG
QITLNKHLQP GQGVNNLDNL RDHLDGTIKV NLEKKHVNKR SQIFPPVLMT MNEYLLPPTI
GVRFALHIHL KPKAYLKQSL EKSDLVARRI LNSGYTILLL LLWYNPVDSF TPKVQEKVVQ
WKETLERHVS ITQFGKIQQN IIDGNDPLHG IVIEEQM
//
