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Database: UniProt
Entry: A0A3G6J729_9CORY
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Original site: A0A3G6J729_9CORY 
ID   A0A3G6J729_9CORY        Unreviewed;      1183 AA.
AC   A0A3G6J729;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   Name=dnaE1 {ECO:0000313|EMBL:AZA13921.1};
GN   ORFNames=CCHOA_07645 {ECO:0000313|EMBL:AZA13921.1};
OS   Corynebacterium choanae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1862358 {ECO:0000313|EMBL:AZA13921.1, ECO:0000313|Proteomes:UP000269019};
RN   [1] {ECO:0000313|EMBL:AZA13921.1, ECO:0000313|Proteomes:UP000269019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=200CH {ECO:0000313|EMBL:AZA13921.1,
RC   ECO:0000313|Proteomes:UP000269019};
RA   Kleinhagauer T., Glaeser S.P., Spergser J., Ruckert C., Kaempfer P.,
RA   Busse H.-J.;
RL   Submitted (NOV-2018) 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};
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DR   EMBL; CP033896; AZA13921.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G6J729; -.
DR   KEGG; ccho:CCHOA_07645; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000269019; Chromosome.
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   CDD; cd12113; PHP_PolIIIA_DnaE3; 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   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; 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   ECO:0000313|EMBL:AZA13921.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000269019};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AZA13921.1}.
FT   DOMAIN          7..74
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1183 AA;  130534 MW;  C826F5BF1798F9E1 CRC64;
     MSAGSFVHLH NHTEYSMLDG MAKVDLLAEE VVRQKMPAVG MTDHGNMFGA DAFYHAMTKA
     GVKPIIGIEA YMAPESRFNK DRIRWGDMSQ KSDDVSGSGA YLHQTMVAEN ATGLKNLFYL
     SSMASYEGQL GKWPRMDAEL IAEHSTGIIA TTGCPSGDVQ TRLRLGQFDE ALAAAAKWQD
     IYGKENFFLE LMDHGIDIER RVRDELLEIG KKLNLPPLVT NDCHYVLESQ AGPHEALLCV
     QTGATLQDTN RFKFDGSGYY VKSAEQMRAQ WDDLVPGACD NTLAIAERVE SYAEIWEPHT
     HDRMPIANVP DGHTPTSWLK HQVEEGLRER FPGAEVPQEY TDRAAYEIEV IDIKGYPSYF
     LIVAELIKHA RSVGIRVGPG RGSAAGSLVA YALTITNIDP IEHGLLFERF LNPERPSAPD
     IDIDFDDRRR GEMVRYAAEN WGVDKVAQVI TFGTVKTKQA IKDAARVHYG QEGYRKADDI
     TKALPPAIMA KDIPLKGIQD PQHERYAEAA EVRAMIENDQ QVATIYETAL GMEGVIRQAG
     VHACAVIMAS VPLLDHIPMW KRPADGALIT GWPYPACEQI GLLKMDFLGL RNLTVIGDCL
     ENIKTNRGID LDLENLSVVD EPTYELLSRG DTLGVFQLDS GGMRELLKRM EPTRFDDIVA
     ALALYRPGPM GMGAHWAYAD RKNGRQDITP IHPELEEPLR EILEETHGLI VYQEQIMRIS
     QKVANYTAGQ ADGFRKAMGK KKPEVLAAEF KNFSAGMQSN GFSDAAIKAL WGTIEPFASY
     AFNKSHAAGY GLVSFWTAYL KANYTSEYMA ALLTSVSDNK DKSAIYLSDC RHLGVRVLSP
     DVNDSALTFQ SVGEDIRFGL GAIRNVGADV VASIVKTRTE KGAFTSFSDY LDKIELTACN
     KRVTESLIKA GAFDSLDCSR QGLHLVFEDA IDSILSTKKA AEQGQGDLFA GFGEVSSDAA
     FSVKVPEGEW DRKAKLSFEK EMLGLYVSSH PLDGFEQSLM AQVNTSLTEI LSGEVRDRQD
     VVIGGIITKV DRRISKKDGA TWAIVTIEDH NGASVELLLF ARAFAAYQSL VAEDNIVIAQ
     ARINIRDDRM SVFCSELKLA DLGTGSGTGA PLRLVLQSHQ CSPQRLEKLK DVLHQNPGES
     DVYVRIECND RQTTLLLPQE YRVDRSSSLM GDLKASLGPG ILG
//
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