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Database: UniProt
Entry: A0A0W0ZUV2_9GAMM
LinkDB: A0A0W0ZUV2_9GAMM
Original site: A0A0W0ZUV2_9GAMM 
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
//
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