ID W7QEI9_9ALTE Unreviewed; 1159 AA.
AC W7QEI9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=DS2_03995 {ECO:0000313|EMBL:EWH11304.1};
OS Catenovulum agarivorans DS-2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Catenovulum.
OX NCBI_TaxID=1328313 {ECO:0000313|EMBL:EWH11304.1, ECO:0000313|Proteomes:UP000019276};
RN [1] {ECO:0000313|EMBL:EWH11304.1, ECO:0000313|Proteomes:UP000019276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-2 {ECO:0000313|EMBL:EWH11304.1,
RC ECO:0000313|Proteomes:UP000019276};
RX PubMed=24604650;
RA Shan D., Li X., Gu Z., Wei G., Gao Z., Shao Z.;
RT "Draft Genome Sequence of the Agar-Degrading Bacterium Catenovulum sp.
RT Strain DS-2, Isolated from Intestines of Haliotis diversicolor.";
RL Genome Announc. 2:e00144-14(2014).
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 -!- 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:EWH11304.1}.
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DR EMBL; ARZY01000005; EWH11304.1; -; Genomic_DNA.
DR RefSeq; WP_035013358.1; NZ_ARZY01000005.1.
DR AlphaFoldDB; W7QEI9; -.
DR STRING; 1328313.DS2_03995; -.
DR PATRIC; fig|1328313.3.peg.827; -.
DR eggNOG; COG0587; Bacteria.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000019276; 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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd07433; PHP_PolIIIA_DnaE1; 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; IPR048472; DNA_pol_IIIA_C.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR012340; NA-bd_OB-fold.
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 InterPro; IPR049821; PolIIIA_DnaE1_PHP.
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; PF20914; DNA_pol_IIIA_C; 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; SSF160975; AF1531-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000019276};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1159 AA; 131004 MW; 1ED104A8BDB7F990 CRC64;
MADPKFVHLR VHSDFSMVDG LAKTKPIIAK IAEYQMPAVA ITDQMNLCGL VRFYSGANGA
GIKPIIGADF WVRSNEMEEE LCRLVILASD NDGYKNLTLL ISKGYLRGDY QGKTVIDQEW
LVEHAKGLIL LSGGREGDLG KALLKGNYKQ AQRITDFYKT HFADNYYIEL IRTGRDNEET
YLHHAVKWAD ETELPVVATN EVVFLNEEDF DAHEIRVAIH DGYTLDDKNR PRRYSNQQYL
RTEEEMCEVF SDIPEALENS VEIAKRCNVT VLLGKYFLPS CPTGGMGEDE YLVKVSEEGL
QERLEFLFPD EKERAEKRGE YDERLRIELE CINQMGFPGY FLIVMEFIQW SKDNNIPVGP
GRGSGAGSLV AYALKITDLD PLEFDLLFER FLNPERVSMP DFDVDFCMDR RDEVIDHVAQ
LYGRDAVSQI ITFGTMAAKA VVRDVGRVLG HPFGFVDRIS KLIPGDPGMT LAKAFDVEPR
LNELYEADEE VRALIDMARI LEGTTRNAGK HAGGVVISPT KITDFAPLYC DSEGKQPVTQ
FDKNDVETAG LVKFDFLGLR TLTIMQWAID MANEKLARVN KPLIDINAIP LDDKKSFETL
KKYETTAVFQ LESRGMKDLI KRLQPDCFED MIALVALFRP GPLQSGMVDN FIDRKRGREE
ISYPDAQYQH ECLKEILDPT YGIILYQEQV MQIAQVMAGY SLGGADLLRR AMGKKKPEEM
AKQRSTFEDG AKNNGIDPDL AMKIFDLVEK FAGYGFNKSH SAAYALVSYQ TLWMKTHYPA
EFMAAVMSAD MDNTDKVVTL VDECERMRMP LIPPDVNQGC YKFTVNDDGA IVYGIGAIKG
VGEGPIEAII EARNEGGPFK DLFDFCARVD LKRINRRVLE KLVQAGAMDA LGPHRASIMA
TLSDAIGAAE QHAKDALAGQ SDLFGLLTTE PEEVEQAFVK VAKWPEEIWL EGERETLGLY
LTGHPINRYR EELKHYARSR INELSPTRRD DEVSTSGLII AVKSMVNKRS GRRWAIVTLD
DKSGRIDVRF FADMFEQYEE LLVKDQVIVV SGPVEDDDFT GGYCMTAKNC MDLVSLREKY
AKSLTVSLDQ QSLKPDIIEQ IHEKIEPHKE GVTPLVFEYQ NHRAKAEIKT GVQWYVTPHD
SLLYDLRHIV GEEHISLRF
//
