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Database: UniProt
Entry: A0A2I1G9A3_9GLOM
LinkDB: A0A2I1G9A3_9GLOM
Original site: A0A2I1G9A3_9GLOM 
ID   A0A2I1G9A3_9GLOM        Unreviewed;       199 AA.
AC   A0A2I1G9A3;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU366014};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU366014};
GN   ORFNames=RhiirA4_111052 {ECO:0000313|EMBL:PKY43217.1};
OS   Rhizophagus irregularis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY43217.1, ECO:0000313|Proteomes:UP000234323};
RN   [1] {ECO:0000313|EMBL:PKY43217.1, ECO:0000313|Proteomes:UP000234323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4 {ECO:0000313|EMBL:PKY43217.1,
RC   ECO:0000313|Proteomes:UP000234323};
RA   Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA   Kruger M., Pelin A., Brachmann A., Corradi N.;
RT   "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT   ancient asexual fungus.";
RL   Submitted (OCT-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|RuleBase:RU366014};
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:PKY43217.1}.
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DR   EMBL; LLXI01000241; PKY43217.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I1G9A3; -.
DR   VEuPathDB; FungiDB:FUN_023326; -.
DR   VEuPathDB; FungiDB:GLOIN_2v1634623; -.
DR   VEuPathDB; FungiDB:RhiirA1_358450; -.
DR   OrthoDB; 1367231at2759; -.
DR   Proteomes; UP000234323; 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   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 1.
DR   InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR   InterPro; IPR019843; DNA_pol-X_BS.
DR   InterPro; IPR028207; DNA_pol_B_palm_palm.
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   PRINTS; PR00869; DNAPOLX.
DR   PRINTS; PR00870; DNAPOLXBETA.
DR   SMART; SM00483; POLXc; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|RuleBase:RU366014};
KW   DNA repair {ECO:0000256|RuleBase:RU366014};
KW   DNA-directed DNA polymerase {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:UP000234323};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366014}.
FT   DOMAIN          1..198
FT                   /note="DNA-directed DNA polymerase X"
FT                   /evidence="ECO:0000259|SMART:SM00483"
SQ   SEQUENCE   199 AA;  22770 MW;  E6BE52FDD29BE508 CRC64;
     MSRQDIQEIL DILNKVIKTM YPDCMITPVG GYRRGKEFSG DLDVVVSHPQ ETVANNLLKD
     IVEILINKGH LKHKLFYGQP SAKNKKDVPS ELISSHKNIM DNLDKCFCAF IQPSTQICRQ
     VDLIIAPYSQ YPTAVLGWTG SKQFERSIRN FAKKERKMTF ASHGLFLNVV PRRRVCVTSE
     KDVFDILGIP WVEPEMRNC
//
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