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Database: UniProt
Entry: A0A2Z6R7V7_9GLOM
LinkDB: A0A2Z6R7V7_9GLOM
Original site: A0A2Z6R7V7_9GLOM 
ID   A0A2Z6R7V7_9GLOM        Unreviewed;       528 AA.
AC   A0A2Z6R7V7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=RclHR1_31970001 {ECO:0000313|EMBL:GBB98303.1};
OS   Rhizophagus clarus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=94130 {ECO:0000313|EMBL:GBB98303.1, ECO:0000313|Proteomes:UP000247702};
RN   [1] {ECO:0000313|EMBL:GBB98303.1, ECO:0000313|Proteomes:UP000247702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HR1 {ECO:0000313|EMBL:GBB98303.1,
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         ECO:0000256|RuleBase:RU000442};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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:GBB98303.1}.
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DR   EMBL; BEXD01002443; GBB98303.1; -; Genomic_DNA.
DR   STRING; 94130.A0A2Z6R7V7; -.
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   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_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   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247702};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          233..353
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          417..485
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
SQ   SEQUENCE   528 AA;  60380 MW;  C0ACDE7E64F26E52 CRC64;
     MWKSDESLKG IRSILEIFSS DIHLSFNDSG YNWPFIIEKA TKLDVLKWIV QRMSANPHKK
     ADAESILTWN YFGGKGEPLT NGFFRSDPYV KKEDRGPKKA LGRESINIKI NPSLTFESSF
     LKLLGCVPID VCMSFLQLHP RSEKWSLRYF LEKYGLDGKA DMPMSKLWKY YSEAKDRVSD
     SSKKHMHEIA NYCVIDALRC QKFMVKSNVI NDYREVALIA HISLFDSHYY AIGTKKASGK
     FSGAYVFLPK KGLENKRPIT GLDFVSLYPS IIMTYNLSSE KMVSTLSEAN KLKRENKVLY
     SIKSKYGSKP VQAWIIRHRN KSDQKGLFPK ILKNLLNIQN ELKAWLKPFR KKKEYMGLVK
     SRIDAGGSIS IANAIEDVCS QSEPKKCAEI AGILNPFIGS SYDNFRKEYD STCFDYNSLS
     SKQKAIKLYM NLFYGVPGQN DSPFYILELA GGVTSAGQEI IKRVTEYVRK KGFRIKYGDT
     DSLYLTGPDX CYEKYDLAYN DGKGEISKLE YWTEIVKTGP RNIYIGVR
//
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