ID H3KG45_9BURK Unreviewed; 1145 AA.
AC H3KG45;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=HMPREF9440_01720 {ECO:0000313|EMBL:EHY30921.1};
OS Sutterella parvirubra YIT 11816.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=762967 {ECO:0000313|EMBL:EHY30921.1, ECO:0000313|Proteomes:UP000004956};
RN [1] {ECO:0000313|EMBL:EHY30921.1, ECO:0000313|Proteomes:UP000004956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11816 {ECO:0000313|EMBL:EHY30921.1,
RC ECO:0000313|Proteomes:UP000004956};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2011) 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}.
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:EHY30921.1}.
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DR EMBL; AFBQ01000259; EHY30921.1; -; Genomic_DNA.
DR RefSeq; WP_008542801.1; NZ_JH604988.1.
DR AlphaFoldDB; H3KG45; -.
DR STRING; 762967.HMPREF9440_01720; -.
DR PATRIC; fig|762967.3.peg.1353; -.
DR HOGENOM; CLU_001600_0_2_4; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000004956; 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 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 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; 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:UP000004956};
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 1145 AA; 127555 MW; 97554A890A18DB1E CRC64;
MAEPKFVHLR LHSEYSVTDG IVRIDPAIHK MMERGGGALA LTDLMNIFGG LRFYTHALAA
GLKPILGCDL KIRNGNDAAK PYRMGVLCMN REGYHSLSVL LTKAFLTDDD AFRGQIDPKW
FEKGGDAGLI ALSGGAEGEL GALLLNKRWK LADEAAQRWK RIFGDRFYVE VQRAGRHGDD
LATARLANLA VEHGIAVVAT HPVQFLDPED FEAHEVRTSI AEGYTLQDPR RTKRYSPEQY
LKTEEEMIEL FADMPAAVAN SVEIAKRCNL DGVLSKPQLP LFPTPDGMSL DDYIDLLSHQ
GLERRLEFLY PDEKVRNEKR PAYEERLTYE LGIIKGMKFP GYFLIVQDFI NWSKKNGIPV
GPGRGSGAGS LVAYSLGITD LDPLHFDLLF ERFLNPERVS MPDFDVDFCQ YNRDRTIDYV
KRTYGAEAVS QIVTFGTLGA KAVVRDVGRA LDVPYMKTDA LAKLIPQQPG KNITLDDALR
DVPEFKEAVE SDDEYREILR LAKPLEGLTR NLGMHAGGVL IAPGRLTDFC PLYNPDGKPE
NTVCQFDKKD VENVGLVKFD FLGLTTLSII TRAVSYIDKL HPEAKFDIDR IPVDDAETYA
LFQNANTEAV FQFESEGMRA LLKQAKPDRL EDLVALNALY RPGPMDLIPS FIARKFGREK
VEYLDPRMES VLAETYGIMV YQEQVMRVAQ VVGGYSLGGA DLLRRAMGKK NVEEMKRQRA
VFTQGAGERG VSEETATEIF NLMEKFAGYG FNKSHAAAYS YVAYQTAYLK THHIAAFMAA
NLCMVMDQSE KIKKLIDDAA ENGVKLLPPD VNESEWFFVP PDEKSIRFGL GGIKGMARTV
ADDIVAARKK GGPFVDIFDF AARVPGMNGR FLDGLIRAGA FDSIDPDRGK LHANKEQAIR
ASQTIRASEG QGSLFDEPGE TVRIVNWLPA AAWSMRRKLA EEKSALGYWL SGHLYDAYRE
ELKSFAPKSL KDIVPGGRAA SKMAGIISSV RQVQSKRGPM GIVTIDDGTA VVDLMCFGEV
WSKYRRQLTP DAVVCVTGRA RYDEFSKRLS VSLDDVMTVD KFRVGHCRFM EVEVRDDAAR
QELTDVKSIC AGYAKAGTEG VQIALRLHTK ASEGLVFVPM EAAQTEELAG KLREQRAVAH
VRFIY
//
