ID A4Y558_SHEPC Unreviewed; 1157 AA.
AC A4Y558;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN OrderedLocusNames=Sputcn32_1363 {ECO:0000313|EMBL:ABP75091.1};
OS Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=319224 {ECO:0000313|EMBL:ABP75091.1};
RN [1] {ECO:0000313|EMBL:ABP75091.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN-32 {ECO:0000313|EMBL:ABP75091.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella putrefaciens CN-32.";
RL Submitted (APR-2007) 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; CP000681; ABP75091.1; -; Genomic_DNA.
DR AlphaFoldDB; A4Y558; -.
DR STRING; 319224.Sputcn32_1363; -.
DR KEGG; spc:Sputcn32_1363; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_6; -.
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 GO; GO:0006412; P:translation; 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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:ABP75091.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABP75091.1}.
FT DOMAIN 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1157 AA; 129675 MW; 6FC6ECBAF2C52D6B CRC64;
MSDPRFVHLR VHSDFSMSDG VAKVKPILAQ VEALGMAAVA LTDQNNFCGL VKFYSGCHGA
GIKPIIGADF WMQVPGFEGE FCALTIIAMN NVGYQNLTQI ISQAYLRGQV AGRVVIDQEW
LLTYNEGILL LSGAKEGDIG KALLKGNNTQ VESLCEFYQT HFAERYFLEL IRTGRPDEER
YLHMAVVLAQ EKGFPVVATN QVVFLKPEDF DAHEIRVAIH DGFTLADPRR PKKYSEQQYL
RSEEEMCELF ADIPAALSNT VEIAKRCNVT IRLYEYFLPN FPTGDMSIED FLVDCSKKGL
EERLAFLFPD PQVRAERRGE YDERLDIELQ VINQMGFPGY FLIVMEFIQW GKDNGIPVGP
GRGSGAGSLV AYALKITDLD PLEFDLLFER FLNPERVSMP DFDVDFCMDR RDEVIDHVAE
LYGREAVSQI ITFGTMAAKA VIRDVGRVLG HPYGFVDRIS KLIPPEPGMT LAKAFEVEPA
LQESYDADED VKDLIDMCRK LEGVTRNAGK HAGGVVIAPT KITDFAPLYC DAEGKNPVTQ
FDKNDVETAG LVKFDFLGLR TLTIVDWALE MINKVEVKNG RPPVRIEAIP LDDPASFRLL
QRYETTAVFQ LESRGMKDLI KRLQPDCFED MIALVALFRP GPLQSGMVDN FIERKHGREE
VSYPDSQYQH ESLKELLSPT YGIILYQEQV MQIAQVLSGY TLGGADMLRR AMGKKKPEEM
AKQRSIFKEG AIKNGVDGEL SMKIFDLVEK FAGYGFNKSH SAAYALVSYQ TLWLKTHYPS
QFMAAVMSAD MDNTDKIVTL VDECERMGLT LIPPDVNKGL FKFTVDDDLR IVYGIGAIKG
VGEGPVESIL EARKDGPFVD LFDFCARIDL KKLNKRVIEK LICAGALDSL GPHRASMMAT
LPEAMRAADQ HAKAQAIGQH DMFGLLNSEP EDSKQQFVEC TPWPDKIWLE GERETLGLYL
TGHPINQYLK ELKYYTSGRL KDVHPTERGK TVKAAGLVVA TRVMLTKRGS KMGLLTLDDK
SARLEVMLFT EAFEKFNHLL EKDRILICEG EVSFDDFAGG NRMTARNIID IGEARSHFAK
ALEVDLDAEK LTPAVLDSIE QAMSPWRSGA VPVLINYSQT QAKGQFRLAE SWRVNPSDEL
VFALESLLGP NKVRIVF
//
