ID D4IJP7_9BACT Unreviewed; 1269 AA.
AC D4IJP7;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 08-NOV-2023, entry version 64.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=AL1_05260 {ECO:0000313|EMBL:CBK63159.1};
OS Alistipes shahii WAL 8301.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=717959 {ECO:0000313|EMBL:CBK63159.1, ECO:0000313|Proteomes:UP000008794};
RN [1] {ECO:0000313|EMBL:CBK63159.1, ECO:0000313|Proteomes:UP000008794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK63159.1,
RC ECO:0000313|Proteomes:UP000008794};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J.;
RT "The genome sequence of Alistipes shahii WAL 8301.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK63159.1, ECO:0000313|Proteomes:UP000008794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAL 8301 {ECO:0000313|EMBL:CBK63159.1,
RC ECO:0000313|Proteomes:UP000008794};
RA Pajon A.;
RL Submitted (MAR-2010) 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};
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DR EMBL; FP929032; CBK63159.1; -; Genomic_DNA.
DR RefSeq; WP_015546099.1; NZ_CP102253.1.
DR AlphaFoldDB; D4IJP7; -.
DR STRING; 717959.AL1_05260; -.
DR KEGG; ash:AL1_05260; -.
DR PATRIC; fig|717959.3.peg.2060; -.
DR HOGENOM; CLU_001600_0_0_10; -.
DR OrthoDB; 9803237at2; -.
DR BioCyc; ASHA717959:AL1_RS02525-MONOMER; -.
DR Proteomes; UP000008794; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd12113; PHP_PolIIIA_DnaE3; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 1.10.10.1600; Bacterial DNA polymerase III alpha subunit, thumb domain; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR041931; DNA_pol3_alpha_thumb_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR NCBIfam; TIGR00594; polc; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR PANTHER; PTHR32294:SF0; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 1.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:CBK63159.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008794};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBK63159.1}.
FT DOMAIN 5..118
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1269 AA; 144516 MW; DCD7BD496BE7E6BE CRC64;
MPQFVHLHVH TQYSILDGQA SVQRLVDKAM ADGQPGIAVT DHGDMFGIKE FYNYVQKVKG
KCKDKAAEAE ARIAALRDGT ETCADPAAEI AKCERQLEEC RRKLAFKPII GCEVYVARRR
LHDKEGKPDQ SGYHLILLAK NLKGYHNLIK IVSKAWTEGF YMRPRTDRTE IEKYHEGLIC
CSACLAGEVP RAITANDLEK AEESIRWHKK VFGDDYYLEL QLHKATVERA NHEAYPMQLH
VNKHLRELAA KHNVRMVCTN DVHFVDEDNA EAHDRLICLS TGKDLDDPKR MLYSKQEWLK
TTAEMAAIFG QTDPEAMSTT VDICNQIECY SIDHAPIMPN FEIPEEFGTE AEYRARLTEK
DLFDEFTRDE NGNVVMSEEE GLKKIQKLGG YDKLYRIKFE ADYLAKLTMD GAHRRYGEQL
TEEQEERLKF ELHIMKTMGF PGYFLIVQDF IRAAREELDV SVGPGRGSAA GSAVAYCLGI
TQIDPIAYDL LFERFLNPDR ISLPDIDVDF DDDGRGRVLN WVTQKYGKEK VAHIITYGTM
ATKLAIKDVA RVQKLMLSES DRLCKLVPDK IPDKKLNLQN AIDYVPELKA AEQSDNPILR
DTIRYAKMLE GNVRNTGVHA CGTIICRDDI TDWVPVSTAD DKETGEKMLV TQYEGSVIED
TGLIKMDFLG LKTLSIIKDA VENIRLTKGV KIDIDDFTII NDPATYRLYG EGRTVGTFQF
ESAGMQKYLR ELQPSTFEDL IAMNALYRPG PMDYIPDFIA RKHGRSPIEY DIPVMEKYLK
DTYGITVYQE QVMLLSRLLA NFTRGESDTL RKAMGKKLKD KLDHLKPKFI EGGRKNGHDP
KVLEKIWGDW EKFASYAFNK SHATCYSWVA YQTAYLKANY PSEYMAAVLS RNLTNIEQLT
LYMNECKRMG ISVMGPDINE SMRTFSSNAA GDVRFGLAAV KGVGAAAVES IIAERKANGP
FKDIYDFVER VNYSLVNRKC LENLAYAGAF DSISDFARCK YFGVDLRDSS GITFIEQLMR
YGQRFQTEQN NAQQSLFGGG EHVDIQRPVL PACADWSQLE KLTKEREMVG LYLSAHPLDD
YKIIIDHMCK TQLSELENLD ALKGQEIAVA GMVVGVQNLM TKTGKPWGKF KLEDYNGGHE
FALFGKDYEN FRKYLFPDYF LFVRGRVQAK PYNDKELEFK IISMVQLQEM RDTIKEMIVQ
LPIEEVTEAF IHDLTERVRE SKGDTLLRLN VYDRGAQVSL RLFSKSHKVS LSQSLVGYLD
DNSIHYSIA
//
