ID A0A0W0ZUV2_9GAMM Unreviewed; 1148 AA.
AC A0A0W0ZUV2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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:KTD72940.1};
GN ORFNames=Ltuc_0787 {ECO:0000313|EMBL:KTD72940.1};
OS Legionella tucsonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=40335 {ECO:0000313|EMBL:KTD72940.1, ECO:0000313|Proteomes:UP000054693};
RN [1] {ECO:0000313|EMBL:KTD72940.1, ECO:0000313|Proteomes:UP000054693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49180 {ECO:0000313|EMBL:KTD72940.1,
RC ECO:0000313|Proteomes:UP000054693};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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:KTD72940.1}.
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DR EMBL; LNZA01000001; KTD72940.1; -; Genomic_DNA.
DR RefSeq; WP_058520027.1; NZ_LNZA01000001.1.
DR AlphaFoldDB; A0A0W0ZUV2; -.
DR STRING; 40335.Ltuc_0787; -.
DR PATRIC; fig|40335.7.peg.827; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000054693; 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 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; IPR048472; DNA_pol_IIIA_C.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; PF20914; DNA_pol_IIIA_C; 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; SSF50249; Nucleic acid-binding proteins; 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:KTD72940.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054693};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KTD72940.1}.
FT DOMAIN 6..73
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1148 AA; 128578 MW; 9F41BA65F34F6725 CRC64;
MQQRFVHLRV HTEFSVVDGL TRVMPLMKVL PSRGMCAVAV TDYCNLFAAV KHYKNAVDMG
IKPIIGSDLP CHDPEQPERV FSLVLLCLNS QGYKNLTCLI SKAYQEGQYQ GQPRVQNQWI
QEYSAGLIAL SGGKFGDIGQ ALLANDDPLA KSRAIYWQTL FPNRFYLEIQ RTGRPDETRY
NEKLIALADE LKLPLVATND VRFLDQEDFE AHEARVCIHE GYTLADPRRV QKYSAQQYLR
SADEMIALFS DLPSAIENTV EIGKRCTVKL DLGNNYLPNF PIPDGSTVEE YLSHLSQVGL
EERLLQIFKS KSPEELQASR EEYDKRLQVE LNVINNMGFA GYFLIVADFI QWAKKNGVPV
GPGRGSGAGS LVAYALKITD LDPLEYELLF ERFLNPERVS MPDFDIDFCM EGRDRVIDYV
AEKYGRQSVS QIITFGTMAA KAVVRDVGRV LGHPYGFVDK LAKLIPFEIG ITLSKALEQE
EELKRRYEEE EEVKELIDLA LKLEGITRNA GKHAGGVVIA PSQLTDFTAI YCEEGSTQIV
SQFDKDDVEA AGLVKFDFLG LRTLTIIDWA LTTVNKKRAV EGLPAVDISQ IPTDDTATFD
LLKACKTTAV FQLESRGMKE LISRLQPDCF EDIIALVALF RPGPLQSGMV DDFIDRKHGR
AAVDYPHPDL EPILKPTYGV ILYQEQVMQI AQVLANYTLG AADLLRRAMG KKKPEEMAKQ
REIFTQGATA RGVDEKIATH IFDLMEKFAG YGFNKSHSAA YALVAYQTAW LKAHYPAAFM
AAVMSSDMDN TDKVVTFIDE CAHMKLKVLP SSINHSMYPF TVVDDATIIY GLGAIKGVGE
SAIDCIMEER EAGGKYTDLF SFCQRLDLRK VNRRVLEALI KSGAFDDWNV ERAILTASLE
KALKVAEKEH QNQSSGQFDL FSLLEDDTNK QDYVQCKPWS EAQRLEGERE VLGFYLTGHP
ADQYRREFGD FIVSISQLNP SMHKKAIICA QIVGIRKILT KRGKKLVILG MDDSTGRLDV
VVFGELFESS APGLATGDMV VIEGEVAHDD YNGGVKMTAN YLYDVPTART KFARCLELRL
HSRNQGILGS IKALLKAHVG RCAVQFSYCN DYASAQLSLA QQWQVMPSDE LLGLLMNLLG
DEQVLMRY
//