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Database: UniProt
Entry: A0A256CU27_9GAMM
LinkDB: A0A256CU27_9GAMM
Original site: A0A256CU27_9GAMM 
ID   A0A256CU27_9GAMM        Unreviewed;      1163 AA.
AC   A0A256CU27;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=B9T19_02650 {ECO:0000313|EMBL:OYQ81588.1};
OS   Ignatzschineria sp. F8392.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC   Ignatzschineriaceae; Ignatzschineria.
OX   NCBI_TaxID=1980117 {ECO:0000313|EMBL:OYQ81588.1, ECO:0000313|Proteomes:UP000215803};
RN   [1] {ECO:0000313|EMBL:OYQ81588.1, ECO:0000313|Proteomes:UP000215803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F8392 {ECO:0000313|EMBL:OYQ81588.1,
RC   ECO:0000313|Proteomes:UP000215803};
RA   Gulvik C.A.;
RT   "Wohlfahrtiimonas and Ignatzschineria genomes.";
RL   Submitted (APR-2017) 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   -!- 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:OYQ81588.1}.
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DR   EMBL; NEFF01000001; OYQ81588.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A256CU27; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000215803; Unassembled WGS sequence.
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   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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..71
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1163 AA;  132270 MW;  C4275AB5C5A8605D CRC64;
     MTFTHFNLHT EFSMVDGLIR IKPFFAKLKE MGMRAAALTD LGNEFAAIKF YETALKSGIK
     PIFGADCLVI DEESSVGRIT LIAQDYQGYL NLAELLSYGY RYHQIRGVPY ITHEKLMEYQ
     AGLIVIMAKE SHFGQKLLNQ GAPAAERFLQ SVYPAFLEDR LYIGIKRLEQ QDDERFIQMA
     APFAEAHHLP LIALNDVRFM QEDEFEAHEV RVAIQSGYSM LDPNRPRNYS PKQYLRSIEE
     MEALFADFPD AIENSIELVK RCNVTLTLHK PQLPAFPIPE GMTIEEYFKA ESYRGLEERI
     GKQSEANQHY WERLDIELNV INNMGFPGYF LIVADFIQWA KDHQIPVGPG RGSGAGSLVA
     WALKITDLDP LPYDLLFERF LNPERVSMPD FDIDFCMEGR DRVIEYVANR YGREAVSQIA
     THGTMAAKAV IRDVGRALGH PYGFVDRIAK LIPMDIGITL EKAMMQEPEL HDLYHQDEEV
     KILIDLAKQL EGLAKSVGRH AGGVVIAPTK LTDFSPLYCE EGSTALVTQY DKDDIEAAGL
     VKFDFLGLRT LTIIDWAIKN IAYNRGETID LHDLPLDDKP TFELLKACQT TSVFQLESRG
     MKDLLRRLQP DNFEDIVALV ALFRPGPLES GMVEDFINRK HGREEVIYPF PELEPVLKPT
     YGVIVYQEQV MQISQIIGNY SLGGADLLRR AMGKKLPEEM EKQRALFMQG AETLGFDSEK
     AGRLFDLMEK FAGYGFNKSH SAAYALLSYQ TAYLKQHYPP EFMAAVLSAD LDHTDKIIII
     IEEVLAMKIP IIRPSINHSY HQFTVNREGA IIYGLGALKG YGKAAALQLI EEREENGPYL
     DLFDFCRRID LSKTTKRAID ILIRAGALDC LNPEIESIQE RAAYRAQLLA TMEEAIRLAD
     QNRKNENSGQ GDIFGLFSDE PSDEPQYQLQ SAMPLTETAL LHAEKSVLGF FFSGHPIDQY
     RAEIKEVANT TLTALQAMPE PQYHSRNEDN VIVAGLVTAF YTRISKAGKK MFFVVLDDGH
     ARAEFRLFEE PIETLNEAGE EIEPDTILFI RGSHSWDSFN NCMTLRVSEL QTLKQVRERH
     GHFILIENRR PLSLTTVQEI FQKLMPHRDD EKGLQLIFKY HNPRSAGVLQ MQQEKVIADD
     ELLVSLKQQY HDEIDLSVGY RKR
//
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