ID A0A397SKX8_9GLOM Unreviewed; 412 AA.
AC A0A397SKX8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=C1645_741676 {ECO:0000313|EMBL:RIA85296.1};
OS Glomus cerebriforme.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Glomus.
OX NCBI_TaxID=658196 {ECO:0000313|EMBL:RIA85296.1, ECO:0000313|Proteomes:UP000265703};
RN [1] {ECO:0000313|EMBL:RIA85296.1, ECO:0000313|Proteomes:UP000265703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 227022 {ECO:0000313|EMBL:RIA85296.1,
RC ECO:0000313|Proteomes:UP000265703};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) 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 -!- 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:RIA85296.1}.
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DR EMBL; QKYT01000434; RIA85296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397SKX8; -.
DR Proteomes; UP000265703; 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-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
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; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Reference proteome {ECO:0000313|Proteomes:UP000265703}.
FT DOMAIN 107..257
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
SQ SEQUENCE 412 AA; 48329 MW; 818DB6722B2704FB CRC64;
MVKTYENKSD QKSLFPKISE NLLIMQNRVK AQLKLLRKKK DYMREVKSRM DSNSISESFL
VMSAIEDVLF LTIDKKKHAE MADILNPFIS SLYNSFSKEY DSVCFDHNSL NSKQKVIKLF
MNSFYGEMSN SDFPFKFIEL TKGITSAGRE NIKLVAEFVK KKGFGIKYGD TNSLYLTCPD
SCYKKCDLAY NDGKGTISKL EYWTEMIKIT MVIMKKLYNE LNTFLRLKIR SDYLKMAYEE
VLFPVVFTGK KKYFSTPHED MIIGERIINE VRNVNNERSL HKIVEDVFRD AITNPKQWDF
EQFIETNIWK PDIDNKAVQQ FISQIREKYN SKISVSGECF SYIVTHPENT FNLHSKKLTS
TKGEKIEFAD VTKEFGKELD LYHYFKKTIV GLYARFIMYE KKYEPASSSR IM
//
