ID A0A397SLE2_9GLOM Unreviewed; 583 AA.
AC A0A397SLE2;
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_829240 {ECO:0000313|EMBL:RIA86472.1};
OS Glomus cerebriforme.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Glomus.
OX NCBI_TaxID=658196 {ECO:0000313|EMBL:RIA86472.1, ECO:0000313|Proteomes:UP000265703};
RN [1] {ECO:0000313|EMBL:RIA86472.1, ECO:0000313|Proteomes:UP000265703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 227022 {ECO:0000313|EMBL:RIA86472.1,
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:RIA86472.1}.
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DR EMBL; QKYT01000362; RIA86472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397SLE2; -.
DR STRING; 658196.A0A397SLE2; -.
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 Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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 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; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000265703};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 441..571
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
SQ SEQUENCE 583 AA; 67735 MW; D7E5844D82126878 CRC64;
MIQSDFFEDA PALLFHPEAE KDKMEAQVIR YSGENYLNGI LTRDDIVAEN DGGLTAILDN
ALSNYQEIPF MAVDFGGSSE KIGEKNCYVL HLYGSLINGQ KAVVTLIGIW VFFDIRVLEK
ESVDDFKIKI DKILCSTINA YKIEPIEAFP FHGYHTEKKL YLRVFTHGTE DRKKALQAIQ
DNDFETASDD ISSFHRKIAR ENGIAISDWS MMSKYCCKKY PQYTYDFHVS VNHFRAVEDL
KMISDRFPFP ALIRDPQFND SDYDWPFIVE RASRLNLFEW MWKQITGDFK SSEEIQKWNY
YGKIGVNSKN TFQKKKGVTD NEEEEEFRVQ LIKVKICPEE DFISTFLKIP GCVPIDVRVC
FKKLYPHAEV DRKSSLAFYL KKCELDGKAD MPYNKIWRIY SEAKAGTSLR ESHSSAMQNM
HEVAYYSYVS LFDSHYRANG MKVRNLLGAY ATKLDMLFST RQSKNIEKGK YPGAYVFPPK
KGIEIKRPVT GLDFASLYLS LIMSYNLSPE KIILTYEEVD NAQKNGNILH KIEFPFNDRF
IHAWCVRHDN QFEKKGLYLV VLEDLFNKRV QAIPKNFSKY SEH
//
