ID A0A0D1XR74_EXOME Unreviewed; 693 AA.
AC A0A0D1XR74;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU366014};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU366014};
GN ORFNames=PV10_07867 {ECO:0000313|EMBL:KIV90581.1};
OS Exophiala mesophila (Black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV90581.1, ECO:0000313|Proteomes:UP000054302};
RN [1] {ECO:0000313|EMBL:KIV90581.1, ECO:0000313|Proteomes:UP000054302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV90581.1,
RC ECO:0000313|Proteomes:UP000054302};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala mesophila CBS40295.";
RL Submitted (JAN-2015) 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU366014}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family.
CC {ECO:0000256|RuleBase:RU366014}.
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DR EMBL; KN847524; KIV90581.1; -; Genomic_DNA.
DR RefSeq; XP_016222155.1; XM_016372823.1.
DR AlphaFoldDB; A0A0D1XR74; -.
DR STRING; 212818.A0A0D1XR74; -.
DR GeneID; 27325712; -.
DR VEuPathDB; FungiDB:PV10_07867; -.
DR HOGENOM; CLU_008698_4_1_1; -.
DR OMA; RTVGCAI; -.
DR OrthoDB; 1367231at2759; -.
DR Proteomes; UP000054302; 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; 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; IPR002054; DNA-dir_DNA_pol_X.
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; DNA POLYMERASE TYPE-X FAMILY MEMBER; 1.
DR PANTHER; PTHR11276:SF29; DNA POLYMERASE TYPE-X FAMILY PROTEIN POL4; 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; SSF47802; DNA polymerase beta, N-terminal domain-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81585; PsbU/PolX domain-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000054302};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366014}.
FT DOMAIN 307..691
FT /note="DNA-directed DNA polymerase X"
FT /evidence="ECO:0000259|SMART:SM00483"
FT REGION 88..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 78279 MW; 5D99A56C6C3D0953 CRC64;
MSTIPVTDLS LKSTPPIFIL PTHLQTDELH QTEDLIYRFQ GTLTYDPHEA RLFIGKITQK
KRAAFELRSR GIWTYEVPLP HIPSGTVVDS IQPSRKRRKL STVSDARRSS QRLKLPSSSS
SLSSEVEDVV SQAAKASSQV WPDLTEHIIV LKLSWLSACL KQECIVPITP HHVYYAKIIA
KPQGEAATKP HSNLDVTYIK ATPEHTQSDG ASLHSLRNRT VTVSADILER AKADAPAAAS
QTTPSRRRFG DHKSHVSTSA HPRRPKLTHQ TTSESEDQAK NPLPPLPEWA ASPNASYACC
RSTPLHTVNS AFISQLTKIR DARLLTLDEI GVRAYSTSIA SISAYPYRIT RVDELKRLPG
CERKIASLWA EWHHSAEVDE ERHLQAVREI EANEDLRHLS VFWNIWGVGP DTARKFYYDH
GWKDLDDIVE YGWGTLNRVQ QIGVKYYDDF MKKIPRREVE AIRDIILRHA RMALNIKPKD
FDTFRDVECV IVGGYRRGKT ECGDVDVILA HRDESLTHDL VVEVVRSLET EGWVTHTLSL
HTTTSDRGGA TLPYRSEGRG HGFDSLDKAL CVWQDPNYEG RESGNKNPNI HRRVDIIISG
WRTVGCAVLG WSGGTTFQRD IRRFVSKTRG WKFDSSGVRD RGSGHVLDLE KARQVTRDGK
TVMDDADTWQ DRERRLMEGL GIGYRPATER CTG
//
