ID A0A1G8U5W5_9SPHI Unreviewed; 1061 AA.
AC A0A1G8U5W5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
DE AltName: Full=Error-prone DNA polymerase {ECO:0000256|ARBA:ARBA00017273};
GN ORFNames=SAMN04487898_10375 {ECO:0000313|EMBL:SDJ49216.1};
OS Pedobacter sp. ok626.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1761882 {ECO:0000313|EMBL:SDJ49216.1, ECO:0000313|Proteomes:UP000198594};
RN [1] {ECO:0000313|EMBL:SDJ49216.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK626 {ECO:0000313|EMBL:SDJ49216.1};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC subfamily. {ECO:0000256|ARBA:ARBA00007391}.
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DR EMBL; FNEX01000003; SDJ49216.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8U5W5; -.
DR STRING; 1761882.SAMN04487898_10375; -.
DR Proteomes; UP000198594; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd07434; PHP_PolIIIA_DnaE2; 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 HAMAP; MF_01902; DNApol_error_prone; 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; IPR023073; DnaE2.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
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:SF4; ERROR-PRONE DNA POLYMERASE; 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 Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..71
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1061 AA; 120012 MW; 612B08BF46AC9968 CRC64;
MEYSELQMTS NFSFLRGASH AHELVAQAAI LGYKKIAVTD RNTLAGIVRA HAAAKEKGLG
FIPACRLDLL DGPSLLAYPT DKEAYGRLSA LLTKGNLRAE KGECHISRAD VYEHGKGMLF
TVVTPNQLDR RFKFEDDFVN ALAQYHEALT GQLYLSASMS YSGYDEKLMF RIQQLSDRFG
ILMVATGDVH YHDPSRRELQ DVLTCVREKC TIQEAGFRLH MNAERYMKPV GEMHRLFRKY
PQALHSTLEI SEACGFSLDE LRYVYPAEIN QSGRMPQEEL EYLCWKGAHD FYGEIVPEKV
VKMIAHEMEF VKKMDYANYF LFVEDIVREA RSRGILCQGR GSAANSAVCF CLGITSVNPM
KFELLFERFI SSDRNEPPDI DVDFEHERRE EIIQYIYDKY GRDRAAIVAT VTQLHQKGAI
RDVGKAMGLS VDTINRLSNS IWEFTDEWFE GKRITELGLN PRDPHLKKTL ELTAQMMGFP
RQLGQHTGGF VVTNGQLTDL CPILNARMED RTNIEWNKDD IDALGFLKVD VLALGMLTCI
RKGFDLCKQH YGLNLTLANV PQDDPAVYDM ICLADTLGVF QIESRAQMSM LPRLKPRVFY
DLVIEVAIVR PGPIQGDMVH PYLRRRNGEE PIVYPSPELK EILGRTLGVP LFQEQAMKIA
IVAAGFTPAE ADGLRRSMAT FKSKGLVNQY ERKLIDGMME KGYTEEFAKR IFKQLEGFGS
YGFPESHAAS FALLVYVSCW LKHYYPDAFA VGLLNSMPMG FYQPAQIVID AQKHGVEVRP
ADINFSTWDN LLEEKSGRYY AVRLGFREIK GLREDEMNVL VDNRAEGYKT ITSLRDAGIS
IGTLERLADA DAFRSIGLDR RKALWEVTAL QDMPVEIFKG QPSESVLEAQ VELPLMTQAE
HVVQDYATVG LSLKAHPVSF VRPQLEMLRI LSTHTINNDS SNGQLVKVAG LVLVRQRPGT
AGGVCFITIE DETGYSNLVV FEKLFETYRK EILHSRLLMV EGRLQREGLV VHVIVSKCVD
LTKMLGKLVQ REQDDLPVLT LSRSDEKSAP NEAFHGGRNF R
//
