ID A0A397TYU2_9GLOM Unreviewed; 639 AA.
AC A0A397TYU2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=C2G38_2229118 {ECO:0000313|EMBL:RIB01987.1};
OS Gigaspora rosea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Gigasporaceae; Gigaspora.
OX NCBI_TaxID=44941 {ECO:0000313|EMBL:RIB01987.1, ECO:0000313|Proteomes:UP000266673};
RN [1] {ECO:0000313|EMBL:RIB01987.1, ECO:0000313|Proteomes:UP000266673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 194757 {ECO:0000313|EMBL:RIB01987.1,
RC ECO:0000313|Proteomes:UP000266673};
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 -!- 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:RIB01987.1}.
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DR EMBL; QKWP01002860; RIB01987.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397TYU2; -.
DR STRING; 44941.A0A397TYU2; -.
DR Proteomes; UP000266673; 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; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 2.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
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.
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:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000266673};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 231..407
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 418..575
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
SQ SEQUENCE 639 AA; 74716 MW; 48A2355972A71D63 CRC64;
MRDRTLILTW GIKTQSRELG EFAKIHDEET FALYWKAFIP DIQFGFSDSK YDWPFIIERA
CRLNLLEWMW KQMTGSFKSS KEIQKWNYYG KIGVKSKNSF QIKKGATDNN EEENDRTQSI
IIKISSEDNY ISIFFKIPGC VPIDVRACFM KLYPRAEVDK KKVKESISLN KSHPSTIQNM
CEVAHYCIID ALCCQELMVK RNVINDYREV ASIAYVSLFD SHYRANGMKV RNLLGAYANK
HNILFSTRQC KNIEKGEYPG IYVFPPKKGI ETKRPVTGLD FASLYPSLIM AYNLSPEKMI
LTYREADIGL YPIVLEDLFN KRVNLKAQLA SLGKKKKHLG KMISLVKEKG KKIPESLNSE
YSSICFDYNC LNSKQFALKV YMNTFYGEAG NSKSPFFFHE LAGGITPVVK ITMDVMKKLR
DQVNAYLRIK NSTSYLKMVY EEVLFPVCFT GKKKYFGVPH EEVVNFKPDN LFKKGIDTVK
QDQSQLFKFI GEKIMWEAID INNTRSVHKI VEDTLIEVQN KEWDFNEFII MGTWRPKKKN
LCNNRFIERM RERNERIPNS VGDFMKYANI AKEFNMEIDI NYYLEKTVAR FIIDDNRYQP
PSSHKIMQLK DLDEKEKQID AYSQKEAKKW LTKYIKALN
//
