ID Q2GJ87_ANAPZ Unreviewed; 1127 AA.
AC Q2GJ87;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=dnaE {ECO:0000313|EMBL:ABD43721.1};
GN OrderedLocusNames=APH_1003 {ECO:0000313|EMBL:ABD43721.1};
OS Anaplasma phagocytophilum (strain HZ).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma; phagocytophilum group.
OX NCBI_TaxID=212042 {ECO:0000313|EMBL:ABD43721.1, ECO:0000313|Proteomes:UP000001943};
RN [1] {ECO:0000313|EMBL:ABD43721.1, ECO:0000313|Proteomes:UP000001943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ {ECO:0000313|EMBL:ABD43721.1,
RC ECO:0000313|Proteomes:UP000001943};
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC responsible for most of the replicative synthesis in bacteria. This DNA
CC polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain
CC is the DNA polymerase. {ECO:0000256|ARBA:ARBA00025611}.
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 -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, epsilon
CC and theta chains) that associates with a tau subunit. This core
CC dimerizes to form the POLIII' complex. PolIII' associates with the
CC gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC and with the beta chain to form the complete DNA polymerase III
CC complex. {ECO:0000256|ARBA:ARBA00026073}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC subfamily. {ECO:0000256|ARBA:ARBA00009496}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000235; ABD43721.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2GJ87; -.
DR STRING; 212042.APH_1003; -.
DR PaxDb; 212042-APH_1003; -.
DR EnsemblBacteria; ABD43721; ABD43721; APH_1003.
DR KEGG; aph:APH_1003; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_5; -.
DR Proteomes; UP000001943; 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; 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; 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 SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 3: Inferred from homology;
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:ABD43721.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABD43721.1}.
FT DOMAIN 6..73
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1127 AA; 126624 MW; 4DCE1176B2B47A7C CRC64;
MDGIFVHLRT HSDYSLLEGM IKVESLVAMC VEQKMPAVAL TDSGNLFGSL EFSDCAARAG
LQPIIGCNIM VEESGNNLGN ILLLAKSAEG FANLTNLISN GFNNSQLEKI NRVNIDDLLK
LNGGLIALTG GHDDILARAL LNNGDDLRAL DSILQVFKDN VYVELQRHGL NGQREVEELL
IRFAYERNIP LVATNDVFFA CRGDFQAHDI LSCISTGAYV VQEDRHRLTP EHYFKTASEM
YELFSDVPEA VLNTSLIAQR CSFIQEVRKP QLPHFPCFEG RTEAEELTEC ALAGLEIRLK
SKGIGDDEEQ RDLYLKRLKY ELGVVISMEY SGYFLIVADF IRWSKQNDIM VGPGRGSGAG
SLIAWSLGIT DLDPIEFGLI FERFLNPDRV SMPDFDIDFC QEKRDKVIEY VKEKYGYVAH
IITFGKLQAR AVLRDVGRVM QIPYAQIDRI CKMIPHDPIS PVTLLEAIEM DQNLKAEQEN
DETVAKLIEI SLKLEGLYRH ASVHAAGIVI CDQPLENFVP LYYDKSSSLP ITQYNMKYVE
KAGLVKFDFL GLRTLTMIDQ ICSLIRARGE EIELSKIPLN DKKTYEMLSA GDSIGVFQLE
SAGMREAISK LRPDSIQDII ALISLYRPGP MNNIAIYISR KHGLEEPDYI HPMLECVLKE
TFGVIIYQEQ VMEIARILAG YSLGEADLLR RAMGKKIKEE MDRQRQDFVD GAVSNGIEES
KASYIFDLVA KFAGYGFNKS HAAAYALISF QTAYLRANYT KEFFTASMNL DIDDKDKLGL
LCQQAKMCGI DVMPPDINLS SAEFTVSGNS IRYGLGALKN VGQLTAHEIL PVEGGRYSDI
WDFAGNVRIR SPLKRTLESL IKSGSLDGIH PNRRQLFASL GIILNIIENK KVSMDAHQFS
LFSEKEEGQL EEVDDWTEDE KIEHEFATIG FYLRYHPLSK YEQVLGKFGV RFVSSTQEEK
ESGVTKRAGV VSSVKMRSAN KERFAIVRVS DPHGVNDVAF YNSKTIEENR DLFNSGVPVM
IDMDYNASKG RLVGRNICNF HESISLMMRR VRSIAIHTGQ NTLIAHMLQE VLKRDAMGAE
VYIELLSKGH LVLIKLPGAF LVTPEILAQI FNISWVDDIT INHRGYL
//
