ID F7XXZ4_MOREP Unreviewed; 1160 AA.
AC F7XXZ4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
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:AEI74970.1};
GN OrderedLocusNames=MEPCIT_337 {ECO:0000313|EMBL:AEI74970.1};
OS Moranella endobia (strain PCIT).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Moranella.
OX NCBI_TaxID=903503 {ECO:0000313|EMBL:AEI74970.1, ECO:0000313|Proteomes:UP000000504};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCIT;
RA McCutcheon J.P., von Dohlen C.D.;
RT "An interdependent metabolic patchwork in the nested three-way symbiosis of
RT mealybugs.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEI74970.1, ECO:0000313|Proteomes:UP000000504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCIT {ECO:0000313|EMBL:AEI74970.1,
RC ECO:0000313|Proteomes:UP000000504};
RX PubMed=21835622; DOI=10.1016/j.cub.2011.06.051;
RA McCutcheon J.P., von Dohlen C.D.;
RT "An interdependent metabolic patchwork in the nested symbiosis of
RT mealybugs.";
RL Curr. Biol. 21:1366-1372(2011).
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 ---------------------------------------------------------------------------
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; CP002243; AEI74970.1; -; Genomic_DNA.
DR RefSeq; WP_013975720.1; NC_015735.1.
DR AlphaFoldDB; F7XXZ4; -.
DR STRING; 903503.MEPCIT_337; -.
DR KEGG; men:MEPCIT_337; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_6; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000000504; 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; 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; IPR048472; DNA_pol_IIIA_C.
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; 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; SSF89550; PHP domain-like; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000000504};
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 1160 AA; 130310 MW; 59E1CFD8F4D51C7B CRC64;
MVEPSFIHLH VHSDYSMIDG LVKVGQLVEQ AALLHMPALA ITDFTNLCGL VKFYCHAHDA
GIKPIIGADL LVHSDMLGGE LAELTILATN NVGYQHLTLL ISNSYKRGYG ALGPVIDRDW
LIEHNEGLIL LSGARKGDVG KYLVRGNIGG ISQVERCLAF YERYFPDRYY LELIRTGRTD
EEHYLQAAVE LAARRGLPVV ATNDVRFISP DDFEAHEIRV AIHDGYTLDD LKRPRNYSPQ
QYLRSDKEMC ALFADLPEAL VNSVEIARRC NVVIRLGEYF LPQFPTGKMS TDDYLVKCAR
EGLEKRLELQ FTDTDMRSEK RQIYYERLNM ELHVINNMGF PGYFLIVMEF IQWSKDHGVP
VGPGRGSGAG SLVAYALNIT DLDPLAFDLL FERFLNQERV SMPDFDIDFC MDKRDMVIDH
VTETYGRDAV AQIITFGTMA AKAVIRDVGR VLGYSYGFVA RIAKLVPPDP GMTLEKSLVL
EPKLQALYDY DEDVKELIDM ARKLEGVTRN AGKHAGGVVI APTKITDFAP LYCDSGGNHP
VTQFDKKDVE YAGLVKFDFL GLRTLTIIHW ALEMINARLV WQGLAPIDIT VISLDDQKSF
DMLQRSETTA VFQLESRGMK DLIKRLKPDC FEDIIALVAL FRPGPLQSGM VDNFINRKHG
LEAISYPDKK WQHSSLQPVL ESTYGIILYQ EQVMQIAQVL AGYTLGGADI LRCAMGQKKP
AEMEKQRSVF KAGAERIGVD GALAMKIFDL LEKFAGYGFN KSHSAAYALV SYQTLWLKAH
YPSEFMAAVM TADMDNTEKI VGLVDECLRM GLKVLTPDIN SGQYNFHVNE EGAIVYGIGA
IKGIGAGPIE AIIAARNHGG HFRELFDLCE RTDIKKINRR VLEKLIMSGA CDRLGQHRAA
LMHSLDKALN SSNQHAKAEA IGQSDMFGVL VNDQDVMTAT VKPWSEQVVL NGERETLGLY
LTGHPINQYL REIERYSGGV QLKDLQATKR GKIVTAVGLV LSTRVMVTKR GNKIGVCTLD
DRSSRVDIIL FTDVLEKYQH LLEKDRLLIA KGYIDGEDLN GGVKMTVREL MDISEARKKY
VRGIAIYLTD SQINDQLLNR LRVSLEQYRS DMIPVHLYYQ RQEARARLRF GANWQVTPTD
NLLNDLRTIV GPKQVELEFD
//
