ID A0A1D7QHK7_9SPHI Unreviewed; 1476 AA.
AC A0A1D7QHK7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=BFS30_13850 {ECO:0000313|EMBL:AOM78155.1};
OS Pedobacter steynii.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=430522 {ECO:0000313|EMBL:AOM78155.1, ECO:0000313|Proteomes:UP000094313};
RN [1] {ECO:0000313|EMBL:AOM78155.1, ECO:0000313|Proteomes:UP000094313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DX4 {ECO:0000313|EMBL:AOM78155.1,
RC ECO:0000313|Proteomes:UP000094313};
RA Seilhamer J.J.;
RL Submitted (AUG-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}.
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DR EMBL; CP017141; AOM78155.1; -; Genomic_DNA.
DR RefSeq; WP_069379820.1; NZ_CP017141.1.
DR KEGG; psty:BFS30_13850; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000094313; Chromosome.
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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd06127; DEDDh; 1.
DR CDD; cd04485; DnaE_OBF; 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; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
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 Pfam; PF00929; RNase_T; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF53098; Ribonuclease H-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 Reference proteome {ECO:0000313|Proteomes:UP000094313};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..192
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT DOMAIN 262..350
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1476 AA; 166941 MW; BB8B2349EDC7706F CRC64;
MYLIFDTETT GLPRNWNAPI TDTDNWPRCI QIAWQLHDEF GNLVEHQDYL VRPDGFNIPY
DAERIHGIST ELAQEQGIPL SEVLEKFNIA LAKSKFVVGQ NIGFDVNIMG CEFHRLGVES
PMGQMPVLDT CTEVTAELLR LPGGRGGKFK LPTLTELHQY LFGEPFAEAH NATADVEATT
RCFLQLIKLD VFSPDQLQAD PDYLRSYKER NPGVIQRVGL NHLNLKAASD EIRKRLQKAE
GPKVSKKTLE ENKQELASAT YVHLHNHTQF SVLQSTINIP SLIKATAAYK MPAVAMTDHA
NMMGAFHFVA QVLNHNKGVE ARNQAAIEKG ETPDEITIKP IVGCEFFVCE NHEDKKRKDD
GYQVVLLAKN KNGYHNLAKM SSIAYTKGFY YIPRIDKAVI EQYKDDILVL SGNLYGEISS
KLLNLGEKQA EEALLWWKSQ FGDDFYIELM RHNQEDEDIV NISLIALARK HEVKVIATNN
TYYINKKDAN AHDILLCVKE GEKQATPIGR GRGYRFGLPN QEYYFKTPEE MKELFADTPE
AIFNIQEIVD KIEIYKLARE VLLPKFDISE EFLVKEDEED GGKRGENKYL RHLTYVGAKK
RYGEITEAIA ERLDFELQTI EKTGYPGYFL IVQDFIAEAR NLDVSVGPGR GSAAGSAVAY
CLGITNIDPI KYDLLFERFL NPDRVSMPDI DIDFDDEGRG RVMDYVINKY GANQVAQIIT
YGTMAAKSSV KDTARVLDLP LYEAEKIAKL IPNMKLAKIF SLDEKSLKAA LRADEYEKVL
ELKGLANAND LGAKTLEQAQ ILEGSLRNTG IHACGVIITP SDITNFVPVA TAKDSDLYVT
QFDNSVVESA GLLKMDFLGL KTLTLIKDTV KLVKHRHNID LDPDNFPIDD AKTYELFQRG
ETIGIFQYES NGMQKYMKEL KPTVFGDLIA MNALYRPGPL EYIPSFVRRK NGEEEIKYDL
DACEEYLKET YGITVYQEQV MLLSQKLAGF TKGEADVLRK AMGKKQKDVL DKMKPKFVAQ
AAEKGHDATV LEKIWKDWEA FASYAFNKSH STCYAWIAYQ TAYLKAHYPA EYMAAVLSNN
MSDIKQVAFF MEECKQMGVS VLGPDVNESG TKFSVNISGQ VRFGLSGIKG VGDKAVESII
VERNENGQYK SVYDFAKRSN TRTVNKKAYE SFVYSGAFDG FGYHRAQYFF VGINDKMNGI
EKMIKFANDF QNNESSAQSS LFGGSVADMI YEPSLPVAPE WSLIDRLKYE KDAIGIFLSG
HPLDNYKLEL KEFCQHKVKH LSLVNKIRTG DSNEEVLAEF ETIKNRELVV GGLVVIAAQR
MTKTGKPFGT IVFEDYDDTC ELALFGDDFI KFKQFLTDGY FLQIRGRVGE RFRKEGDWEF
KITSINLLSE LRDKLAKSVT IQVPIEKITD DFMGKIHAIL EENKANTEHQ NCQLLFDVYD
REQNVNVKLP SKSLKINPNN IFLDQLTALN VNPKLN
//