ID A0AA39X1R9_9PEZI Unreviewed; 633 AA. AC A0AA39X1R9; DT 24-JAN-2024, integrated into UniProtKB/TrEMBL. DT 24-JAN-2024, sequence version 1. DT 29-MAY-2024, entry version 3. DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU366014}; DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU366014}; GN Name=POLL {ECO:0000313|EMBL:KAK0625712.1}; GN ORFNames=DIS24_g10967 {ECO:0000313|EMBL:KAK0625712.1}; OS Lasiodiplodia hormozganensis. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae; OC Lasiodiplodia. OX NCBI_TaxID=869390 {ECO:0000313|EMBL:KAK0625712.1, ECO:0000313|Proteomes:UP001175001}; RN [1] {ECO:0000313|EMBL:KAK0625712.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBS 339.90 {ECO:0000313|EMBL:KAK0625712.1}; RA Felix C., Meneses R., Goncalves M.F.M., Tilleman L., Duarte A.S., RA Jorrin-Novo J.V., Van De Peer Y., Deforce D., Van Nieuwerburgh F., RA Esteves A.C., Alves A.; RT "Multi-omics analyses reveal the molecular pathogenesis toolkit of RT Lasiodiplodia hormozganensis, a cross-kingdom pathogen."; RL Submitted (JUN-2023) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DNA polymerase that functions in several pathways of DNA CC repair. Involved in base excision repair (BER) responsible for repair CC of lesions that give rise to abasic (AP) sites in DNA. Also contributes CC to DNA double-strand break repair by non-homologous end joining and CC homologous recombination. Has both template-dependent and template- CC independent (terminal transferase) DNA polymerase activities. Has also CC a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity. CC {ECO:0000256|RuleBase:RU366014}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, CC ChEBI:CHEBI:173112; EC=2.7.7.7; CC Evidence={ECO:0000256|ARBA:ARBA00024632, CC ECO:0000256|RuleBase:RU366014}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU366014}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. CC {ECO:0000256|ARBA:ARBA00008323, ECO:0000256|RuleBase:RU366014}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAK0625712.1}. 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; JAUJDW010000135; KAK0625712.1; -; Genomic_DNA. DR Proteomes; UP001175001; Unassembled WGS sequence. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR CDD; cd00141; NT_POLXc; 1. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1. DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1. DR Gene3D; 3.40.50.10190; BRCT domain; 1. DR Gene3D; 1.10.150.110; DNA polymerase beta, N-terminal domain-like; 1. DR Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 1. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR036420; BRCT_dom_sf. DR InterPro; IPR002054; DNA-dir_DNA_pol_X. DR InterPro; IPR019843; DNA_pol-X_BS. DR InterPro; IPR010996; DNA_pol_b-like_N. DR InterPro; IPR028207; DNA_pol_B_palm_palm. DR InterPro; IPR018944; DNA_pol_lambd_fingers_domain. DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf. DR InterPro; IPR037160; DNA_Pol_thumb_sf. DR InterPro; IPR022312; DNA_pol_X. DR InterPro; IPR002008; DNA_pol_X_beta-like. DR InterPro; IPR043519; NT_sf. DR InterPro; IPR029398; PolB_thumb. DR PANTHER; PTHR11276:SF43; DNA POLYMERASE IV; 1. DR PANTHER; PTHR11276; DNA POLYMERASE TYPE-X FAMILY MEMBER; 1. DR Pfam; PF14792; DNA_pol_B_palm; 1. DR Pfam; PF14791; DNA_pol_B_thumb; 1. DR Pfam; PF10391; DNA_pol_lambd_f; 1. DR Pfam; PF14716; HHH_8; 1. DR PRINTS; PR00869; DNAPOLX. DR PRINTS; PR00870; DNAPOLXBETA. DR SMART; SM00483; POLXc; 1. DR SUPFAM; SSF52113; BRCT domain; 1. DR SUPFAM; SSF47802; DNA polymerase beta, N-terminal domain-like; 1. DR SUPFAM; SSF81301; Nucleotidyltransferase; 1. DR SUPFAM; SSF81585; PsbU/PolX domain-like; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS00522; DNA_POLYMERASE_X; 1. PE 3: Inferred from homology; KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU366014}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU366014}; KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932, KW ECO:0000256|RuleBase:RU366014}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, KW ECO:0000256|RuleBase:RU366014}; Nucleus {ECO:0000256|RuleBase:RU366014}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366014}. FT DOMAIN 39..135 FT /note="BRCT" FT /evidence="ECO:0000259|PROSITE:PS50172" FT REGION 149..204 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 230..269 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 170..198 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 347 FT /note="Nucleophile; Schiff-base intermediate with DNA; for FT 5'-dRP lyase activity" FT /evidence="ECO:0000256|PIRSR:PIRSR622312-50" SQ SEQUENCE 633 AA; 70757 MW; AA6CA3503EEF4711 CRC64; MFSAKRKPMQ LKRSLDQLKQ MPRALSKGKK YSKIKLVPES RRVFKDLVFF FFPNNDINLA RRRRIAKAIE YGASWVVEWC DDITHVIVDR DLQFEHLTAH LKIDALPQHI VVVNENYPAD CIMYLDIIDH KQPQYRIQGY ELSDARSVGA QSSNPLSASK GVAVAHSTIP PKSKESSTEH TQHAPSAQDN QGPEQKDSAE GGATSGAYAD ALENIIAGAK NADYLPLKPL DLEDEDSSPQ TSDIEDFDTE DERPKKVAKT SVDQHAGSSE QFQCMKKNDG KMKDTNANAR TIEVLTQMGD YYEQIKDEWR SRAYRKAISV LRKQDRKITT KEEAIQLPCI GSRLAAKIEE IVWTNRLRRL DNARLEPGDE ALQTFLKIYG VGLSKASKWV MAGLRTLDDL KSHKIPLTPA QQVGLTHYSD FNTRIPRDEV TQHAAIVRAA LQAIDPACTA TVGGSYRRGA LDSGDIDVLI SHPTADLARL QQIVFDVLVP ALTASGFLKV ALATHRSGSG SRANNTADYG TKWHGVSALP ATNHEQGKKG DGIWRRIDLL LVPEPQLGAA LIYFTGNDIF NRSIRLLASR KGMRLNQRGL YKDVLRGWGR EKITEGELVE GRSEKRIFDV LGVPWRPPEH RIG //