ID A0A923PK57_9BACT Unreviewed; 1709 AA.
AC A0A923PK57;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 02-APR-2025, entry version 9.
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:MBC6995550.1};
GN ORFNames=H9S92_15380 {ECO:0000313|EMBL:MBC6995550.1};
OS Neolewinella lacunae.
OC Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
OC Lewinellaceae; Neolewinella.
OX NCBI_TaxID=1517758 {ECO:0000313|EMBL:MBC6995550.1, ECO:0000313|Proteomes:UP000650081};
RN [1] {ECO:0000313|EMBL:MBC6995550.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KCTC 42187 {ECO:0000313|EMBL:MBC6995550.1};
RA Zhong Y.;
RT "Lewinella bacteria from marine environments.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC EC=2.7.7.7; Evidence={ECO:0000256|ARBA:ARBA00049244};
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:MBC6995550.1}.
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DR EMBL; JACSIT010000139; MBC6995550.1; -; Genomic_DNA.
DR Proteomes; UP000650081; 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 GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd01038; Endonuclease_DUF559; 1.
DR CDD; cd00081; Hint; 2.
DR CDD; cd12113; PHP_PolIIIA_DnaE3; 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; 2.170.16.10; Hedgehog/Intein (Hint) domain; 2.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 3.40.960.10; VSR Endonuclease; 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; IPR007569; DUF559.
DR InterPro; IPR047216; Endonuclease_DUF559_bact.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR006141; Intein_N.
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; IPR011335; Restrct_endonuc-II-like.
DR NCBIfam; TIGR01443; intein_Cterm; 1.
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; 2.
DR Pfam; PF04480; DUF559; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF14890; Intein_splicing; 1.
DR Pfam; PF02811; PHP; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF160975; AF1531-like; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 4: Predicted;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
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:MBC6995550.1};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Reference proteome {ECO:0000313|Proteomes:UP000650081};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:MBC6995550.1}.
FT DOMAIN 5..72
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 697..795
FT /note="Hint"
FT /evidence="ECO:0000259|SMART:SM00306"
FT DOMAIN 1185..1230
FT /note="Hint"
FT /evidence="ECO:0000259|SMART:SM00305"
FT REGION 956..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1709 AA; 190875 MW; A0283B8A19F5A8C0 CRC64;
MPEFCHLHCH TQYSLLDGAA EIGTMMDKAV ADGQKGVALT DHGNMFGAFK FVNEATKRGI
KPMLGCEFYL VEDRHKKVFS RAAGEKDNRY HQLMLAKNKQ GYINLSKLCS IGYIEGLYGK
YPRIDKELIL KYHEGLVVTS CCIGAEIPQL LLQRKDEAAE EALRWWLDVF GEDYYIEIQR
HRGMEDIDGL GISQEDVNQK LLLLAKKYNV KVICTNDSHY VEEDDFLPHD ILLCVNTGSL
MDDPTRFKFP SSDFYFKQQI EMANLFRDVP ESVANTLEVY DKIETLQLAS DVLLPNFPMP
PNFSSQDEYL RHLTYEGARK RYGEITEKTR ERLDFELDVI KASGYPGYFL IVQDFTTAAR
QMGVSVGPGR GSAAGSAVAY CVGITNVDPI KYDLLFERFL NPERVSMPDI DIDFDDVGRQ
KVIDYVIDKY GQEQVAQIVT YGTMAAKSSL RDVGRVMDVP LSEVDRVAKS FPQQLGASLG
QVLAKNDIDP KLKGKMNSED IDRAYAFREL AQGQNQIGEM IRMAQKLEGS VRNTGIHACG
VVITPSNITE HVPVTADKDT GMYVSQYDNS VAESAGLLKM DFLGLKTLTI IKDALAMIKE
NHGVDIDVDA IPLDDEKTYE LFQRGETNGI FQYESGGMQK HMKNLKPTTF DDLIAMNALY
RPGPLEYIPE FIERKHGRNE IVYDLPAMEE YLHETYGICV TGDTLVHDAV SGKRVRIDEL
EHRVGDFLCQ GVDAENQQAT GWLTHWVCNG VKPVFEVVLR SGKRVKMTEN HRVLTEDGWR
ELRDLGVGSF IGTPRGVLGR NVYSSVESSA SIYPSPGPCA TRLASPVPQG RGDGEPGLEC
LQREDVGKME RVNPTLGRDL SDLFYPSPGP CATRLASPVP QERGDGEPGL ECLQREDVGK
MERVNPTLGR DLSVSFYPSP GPCATRLASP VPQGRGDGEP GLECLQRGGA GFGRDFSASI
YPTPGPSPQG RGDSQDLTYT LQRKDVTGLE RLHAALGLRN NAPYADGVVT HDYWEVPTAV
TRAVYAYAKG MRKAPTLAER IMWLVVRNGK IAGYTFQRQK PMGDCIPDFI CLQKRIVVEV
DGAYHQRPEM MLSDAERDAK FAAVGYRTIR FTNEEIRNDL PSVIQRLTEA VCSAEDRPLP
YPVEVFSFSK NLSSKHSSSA PGSPLPCGEG PGEGSNYNDG PRESSSQVIW DEIISITPAG
NEKVYDITVE GIHNYVGNNI LLHNCVYQEQ VMLLSQKLAN FTKGEADTLR KAMGKKQKAV
LDKMYPSFIA GGTANGHPED KLGKIWKDWE AFASYAFNKS HSTCYALVAY QTAYLKAHYP
AEYMASVLTH NKSDQTKLTF FLRECKRMDV PVLGPDINES QADFSVNKKG AIRIGMTALK
GVGEGPVEAI LDARKSGPFT SLFNLLQRIE PGAINKRVLE ALVDAGAFDC FQNVHRAQYF
APSEKFDSYL EHVTKYANAY HAQLASAASS LFGAFQAEIL PDEPTPPEAK EWLLPEKLAR
EKEITGVYVS GHPLDGYKLE IDNYVTCSLG EVNPIKYGRS TVRLAGMIVG ARHMVSKNGN
GWGIFELGDY DATLEFKLFG EDYQKYRHIL HQGTALFLTA TYRKKWNSEE LELNISDVKL
LEGVGREMTE AIVLKLPLED LNERMVVALD DLCQRFPGQQ KLRMVFYDRE EDVQLKMFSL
KRTVEADTDF VREVERLGIT YRLESAVRG
//
