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Database: UniProt
Entry: A0A420E901_9ALTE
LinkDB: A0A420E901_9ALTE
Original site: A0A420E901_9ALTE 
ID   A0A420E901_9ALTE        Unreviewed;      1159 AA.
AC   A0A420E901;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=DBZ36_13995 {ECO:0000313|EMBL:RKF15936.1};
OS   Alginatibacterium sediminis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alginatibacterium.
OX   NCBI_TaxID=2164068 {ECO:0000313|EMBL:RKF15936.1, ECO:0000313|Proteomes:UP000286482};
RN   [1] {ECO:0000313|EMBL:RKF15936.1, ECO:0000313|Proteomes:UP000286482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALS 81 {ECO:0000313|EMBL:RKF15936.1,
RC   ECO:0000313|Proteomes:UP000286482};
RA   Wang Z.;
RL   Submitted (SEP-2018) 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:RKF15936.1}.
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DR   EMBL; RAQO01000008; RKF15936.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420E901; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000286482; 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   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; SSF160975; AF1531-like; 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:RKF15936.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286482};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RKF15936.1}.
FT   DOMAIN          9..76
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1159 AA;  130722 MW;  404E0AA700E83EB7 CRC64;
     MTLNPPQFVH LRIHSDYSMV DGMNKVKPIV AHCQQLGMPA MAITDQCNFC GLVKYYGAAH
     NAGIKPLVGA DFWVRSDSFG DELFRLVLLA KNNDGYQNIT RLISDAYLRG AIEDKPVIDL
     DWLIKYNSGI IVLSGGREGD VGKALLRGKT EVAQECIEFY QRHFNHHFYL ELIRTGREDE
     ERYIHLAVEV ALQFQLPVVA TNEVMFLKPQ DFEAHSVRVA IHDGFAMDDK RRPRRYSAQQ
     YLRTEAEMLE LFSDIPVALQ NSVEIAKRCN VTIRLGEYFL PDFPTNGKSI EEFFCDVSRV
     GLEERLEFLF PDPLVRAEKR PAYDERLEIE LGVINKMGFP GYFLIVMEFI QWSKDNNIPV
     GPGRGSGAGS LVAYAQKITD LDPLEFDLLF ERFLNPERVS MPDFDVDFCM DRRDEVIEHV
     AELYGRDAVS QIITFGTMAA KAVVRDVGRV QGQPFGFVDR ISKLIPGDPG MTLAKAFEVE
     PRLQEIYDAD EEVQELINMA RTLEGVTRNA GKHAGGVVIS PTTITDFAPL YCDAEGNNPV
     TQFDKNDVEY AGLVKFDFLG LRTLTIIQWA LDMLNPVLLS QGKDPIDIAS IPVDDPASFR
     LLQKYQTTAV FQLESRGMKD LIKRLQPDCF EDMIALVALF RPGPLQSGMV DNFIERKHGR
     EAVSYPDEKW QHDSLQEILE PTYGIILYQE QVMQIAQVLA GYTLGGADML RRAMGKKNAD
     EMAKQRAIFK EGAINNNVDG ELAMKIFDLV EKFAGYGFNK SHSAAYALVS YQTLWLKTHF
     PSYFMAAVMS ADMDNTDKIV TLVDECNSTN IPIIPPDVNS GEYKFSVNEQ QQIVYGIGAI
     KGVGEGPVEA ILEAREAGPF IDLFDFCNRV DLKRINRRVL EKLIMAGALD QLGPHRAALM
     ATLETAMKSA SQHAAASARG QEDLFGLIAS SDQESRPDFV TIDPWIDRVW LEGEKETLGL
     YLTGHPINQY VKEFKSYTSS RLIDLRPSNK DTITVAGLVL SSRVMMTKRG SKMGILQIDD
     RSARLDVMLF SEAFEKYQDL IEKDRILIIQ GQVSFDDFSG GLKMTAREIM DLGQARERWA
     KRLVLNINED DTHEQYWQRF CEIIEPHRHG TCPVAIRYQG SKASAEYILA NDWRITPSEE
     LLDGLSEMLG QANLALEFS
//
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