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Database: UniProt
Entry: E3H821_ILYPC
LinkDB: E3H821_ILYPC
Original site: E3H821_ILYPC 
ID   E3H821_ILYPC            Unreviewed;      1138 AA.
AC   E3H821;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   OrderedLocusNames=Ilyop_1472 {ECO:0000313|EMBL:ADO83252.1};
OS   Ilyobacter polytropus (strain ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1).
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   Ilyobacter.
OX   NCBI_TaxID=572544 {ECO:0000313|EMBL:ADO83252.1, ECO:0000313|Proteomes:UP000006875};
RN   [1] {ECO:0000313|EMBL:ADO83252.1, ECO:0000313|Proteomes:UP000006875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51220 / DSM 2926 / LMG 16218 / CuHBu1
RC   {ECO:0000313|Proteomes:UP000006875};
RX   PubMed=21304735; DOI=10.4056/sigs.1273360;
RA   Sikorski J., Chertkov O., Lapidus A., Nolan M., Lucas S., Del Rio T.G.,
RA   Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Brambilla E., Yasawong M.,
RA   Rohde M., Pukall R., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Ilyobacter polytropus type strain (CuHbu1).";
RL   Stand. Genomic Sci. 3:304-314(2010).
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; CP002281; ADO83252.1; -; Genomic_DNA.
DR   RefSeq; WP_013387919.1; NC_014632.1.
DR   AlphaFoldDB; E3H821; -.
DR   STRING; 572544.Ilyop_1472; -.
DR   KEGG; ipo:Ilyop_1472; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_0; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000006875; 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; 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; 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   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; PF01336; tRNA_anti-codon; 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   Reference proteome {ECO:0000313|Proteomes:UP000006875};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..73
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1138 AA;  130907 MW;  DBCA1FE4D610AB2E CRC64;
     MKNNFVHLHL HTEYSLLDGV GKIDEYLDRA KKLGMRSMAI TDHGNMFGAV EFYKKALSKG
     IKPIVGMEAY LSEFSMEEKS GRNFHLVLLA KNETGYKNLM KLSSEAYLKG FYYRPRIDKE
     ILAQHSKGII ALSACMQGEL SKRILDEESE EDLDKAVNEY VEIFGKEDFY VELQSNGIKK
     QEKLNDALYT LAKKHDLKVV ATNDTHYVYY GDHTLQDILI CVQTGSKISD EKRMKIETDQ
     LFLKSREQML EELGKYDRAV DNTVEIADKC NLELEFGVFK FPEYKIPTCV DSIREFLRKL
     VYQGLKRRYK NDLEKDVIER VEYELDVINK MDYAGYFVVV WDFIDYAKKN RIPVGPGRGS
     AAGSMVAYSL GITELDPMKY NLIFERFLNP ERISMPDIDI DICQERRQEV IDYVGEKYGK
     DRVAQIITFG TMKARAAIRD VGRVMNVPLF KVDKIAKLIP PFFSLDRALK EVEELREVYE
     TDSESQELIE YSKRLENTVR HASIHAAGVV ITKDPLTDDV PLYSDTKTKV VSTQYQMKEL
     EELGLLKMDF LGLRNLTILQ RTVDYIREDT NEEIDLNKIP LDSLEVYRLL QKGDTLGVFQ
     LESHGIRKLL MKLKPDRFED IIAVLALYRP GPLGSGMVDD FIEVKNGRAA IKYPHQSLED
     VLKETYGVIL YQEQVMKIAN IMADYTLGEA DLLRRAMGKK NMAIMEENRN KFVKRAVKKG
     YSEEKATEIF NLIDKFAGYG FNKSHSAAYA LVAYWTAYFK GCYPKHYYAA LMTSERNNIE
     KLAVYVEDAK EHGIGVALPN INKISTRFIV DGDLVRFGMS AIKNVGETLI ERIKAEHARN
     GDYTTFENFV TRGKKEGVNK KALEALILSG ALDSIPGNRR QKYESMEKAL NYATKVMKED
     DIQQMNLFGE ARATIEKFQM PSVEEYKMEN LLTGEKEFLG FYFTGHPLDK YRQMLKVYRL
     TEIKDIVSDM PVHIKTYGMV RNLKKVITKK SGQVMGVFDL EDYYGRIGAV VFPRDYQKMG
     HYLLDGAPLY VEGVVQTDHF GGHEEKKIII RELRPLDEIG EILKFKVYIL IEEEDKPKLP
     ALKKIISRHQ GDHRIYLALR EKGEKKTVEL ANKYRVTPSK YFISEVVGLL GIENIVIK
//
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