ID A0A8J5CFR0_CHIOP Unreviewed; 622 AA. AC A0A8J5CFR0; DT 25-MAY-2022, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 1. DT 29-MAY-2024, entry version 8. 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:KAG0711901.1}; GN ORFNames=GWK47_019608 {ECO:0000313|EMBL:KAG0711901.1}; OS Chionoecetes opilio (Atlantic snow crab) (Cancer opilio). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura; OC Eubrachyura; Majoidea; Majidae; Chionoecetes. OX NCBI_TaxID=41210 {ECO:0000313|EMBL:KAG0711901.1, ECO:0000313|Proteomes:UP000770661}; RN [1] {ECO:0000313|EMBL:KAG0711901.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MADBK_172401_WGS {ECO:0000313|EMBL:KAG0711901.1}; RC TISSUE=Digestive gland {ECO:0000313|EMBL:KAG0711901.1}; RA Jeong J.-H., Ryu S.; RT "The High-quality genome of the commercially important snow crab, RT Chionoecetes opilio."; RL Submitted (JUL-2020) 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:KAG0711901.1}. 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; JACEEZ010022913; KAG0711901.1; -; Genomic_DNA. DR Proteomes; UP000770661; 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:0006303; P:double-strand break repair via nonhomologous end joining; IEA:TreeGrafter. 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:SF44; DNA POLYMERASE LAMBDA; 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 synthesis {ECO:0000256|ARBA:ARBA00022634}; 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 Reference proteome {ECO:0000313|Proteomes:UP000770661}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366014}. FT DOMAIN 24..122 FT /note="BRCT" FT /evidence="ECO:0000259|PROSITE:PS50172" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 128..160 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 194..268 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 129..159 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 217..231 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 232..246 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 358 FT /note="Nucleophile; Schiff-base intermediate with DNA; for FT 5'-dRP lyase activity" FT /evidence="ECO:0000256|PIRSR:PIRSR622312-50" SQ SEQUENCE 622 AA; 69310 MW; 35CDCD2237D93452 CRC64; MKRRNKGSLP CAKRSKGECE AGEPPPPFLD GVKCHVHPAS FGLMRRRIFE NHVTRYGGEL VASLPLASDV AYHVVFEETV DQERLKRLLD PSALPKSLFL RCTWLVACVK AMAKAGTEDH LIVPMNSVEE QSPEETGATQ PKGTNGTCLG VNTQAEETNR VPMEEPDRMH QKEIDTTSPE SQRTINYSTI NEKPKVKDTF PSGDPLTRVA SHPSPHEQME SLESQASTVV RRENTKLEDK KEPSNLMAGE EQGNTSVARR EGGGSEEDSL ASLIRPFPKN LQEKFACARP SSSKRVDLNA HITSELQKLA TTYKSKNDTW RAVGYERAIS AIKNYGKKIT SREEALALPG IGGRLADKVA EILESGRLRK VAEVCEGEEA ECLRLFLGVW GAGPNTAQAW YLQGFRTLED LRTKATLTRH QQVGLKHYQD INDRIPRCEV VEIEDHVREA AVSLVRGVEV TVCGSYRRGK ATCGDVDVLI THPDGNSHQA IFKPLLARLR DTGFLTDDLV TQEDNGNQQK YLGVCRLPGR DRKHRRLDVI VVPYSERATA IMYFTGSAHF NRSMRLLATK KGMSLSEHSL RVGIVRQGGE KLNDGCMLET PTEESVFTHL GLEYRPPQER DH //