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Database: UniProt
Entry: A0A2Z6QMQ2_9GLOM
LinkDB: A0A2Z6QMQ2_9GLOM
Original site: A0A2Z6QMQ2_9GLOM 
ID   A0A2Z6QMQ2_9GLOM        Unreviewed;       476 AA.
AC   A0A2Z6QMQ2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=RclHR1_16870008 {ECO:0000313|EMBL:GBB90002.1};
OS   Rhizophagus clarus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=94130 {ECO:0000313|EMBL:GBB90002.1, ECO:0000313|Proteomes:UP000247702};
RN   [1] {ECO:0000313|EMBL:GBB90002.1, ECO:0000313|Proteomes:UP000247702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HR1 {ECO:0000313|EMBL:GBB90002.1,
RC   ECO:0000313|Proteomes:UP000247702};
RA   Kobayashi Y.;
RT   "The genome of Rhizophagus clarus HR1 reveals common genetic basis of
RT   auxotrophy among arbuscular mycorrhizal fungi.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755}.
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:GBB90002.1}.
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DR   EMBL; BEXD01000765; GBB90002.1; -; Genomic_DNA.
DR   STRING; 94130.A0A2Z6QMQ2; -.
DR   Proteomes; UP000247702; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00136; DNA_pol_B; 2.
DR   PRINTS; PR00106; DNAPOLB.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022932};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247702};
KW   Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT   DOMAIN          12..234
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          266..463
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
SQ   SEQUENCE   476 AA;  55335 MW;  BCD1FF265088E4DB CRC64;
     MAISTRVHEN IEKGKYPGAY VYPPKKGIES KRPVTELDFA SLYPSIIMAY NLSPEKFIFD
     LKDADIAQNN ENNLHKIEFL FNNHIVQAWC THHDNQTEKI GLYLAVLKDL FNKRLDLKAR
     LALLGKKKQH LGKMISSTKE RGKKIPESLN LEYSSVCFDY DYWDLKQKAL KVYMNTFYGK
     AGNSLSPIFL HELACGITTA GKYNLNLVAE FVTKKGFGIK YGDTDSLYLT CPDKYYEICD
     RAFNXGKLSK EAYWTEMVKI TMDVMRKLRD QVNAYLRIKS GTSYLKMAYE VVLFPICFTG
     KKKYFGIEHE DVVNFKPKNL FKKGIETVKQ GKSQLLKFIR EKIMREVMDI NNTCPIHKIV
     KDTLREARNK EWDFNEFIIM GTWKPKKNNL CNNRFMGHMR EKNERISDSG ECFSYITMRK
     TGTTVGMCVR FINDDDSYQP LPSHKIMQIK DSDVKEKMYF DDSSKADIDE IIKLYG
//
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