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Database: UniProt
Entry: A0A344LKL6_9PSEU
LinkDB: A0A344LKL6_9PSEU
Original site: A0A344LKL6_9PSEU 
ID   A0A344LKL6_9PSEU        Unreviewed;      1196 AA.
AC   A0A344LKL6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=A4R43_17930 {ECO:0000313|EMBL:AXB48590.1};
OS   Amycolatopsis albispora.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=1804986 {ECO:0000313|EMBL:AXB48590.1, ECO:0000313|Proteomes:UP000250434};
RN   [1] {ECO:0000313|EMBL:AXB48590.1, ECO:0000313|Proteomes:UP000250434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP1 {ECO:0000313|EMBL:AXB48590.1,
RC   ECO:0000313|Proteomes:UP000250434};
RA   Wang H., Chen S., Wu Q.;
RT   "Complete genome sequence and analysis of deep-sea sediment isolate,
RT   Amycolatopsis sp. WP1.";
RL   Submitted (APR-2016) 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}.
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DR   EMBL; CP015163; AXB48590.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A344LKL6; -.
DR   KEGG; aab:A4R43_17930; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000250434; 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; 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; 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; 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   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; 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   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
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   1196 AA;  131820 MW;  CBC2ADED6DE79360 CRC64;
     MSKDSFVHLH VHTEYSMLDG AAKIAPLFAE ASRLGMPAVG MTDHGNMYGA DEFYQQARKA
     GITPIIGIEA YVAPESRFHK KPVFWGQSNQ RGADEFGEGG DVSGGGAYTH MTMLAENAAG
     LRNLFRLSSL ASLEGYYRKP RMDRELISEH HEGIIATTGC PSGEVQTRLR LGQKAEAIQA
     ASDYKDIFGP DNFFLELMDH GLPIERSVRE GLLEIGRQLG IRPLATNDSH YVTRDQADTH
     SALLCVQAGK TLNDPNRFKF DGDGYYLKSA AEMREYWDTE VPGAADSTLM IAERVQSYEE
     VYAHKDRLPF FEVPEGYDQG AWLREEVQRG LKWRFPNGAP EGYQERLEVE LDVIIGKGFP
     AYFLIVADLI NYARRVGIRV GPGRGSAAGS LVAYVLGITN LDPIPQKLLF ERFLNPERVS
     MPDIDIDFDD RRRGEMIRYA TDKYGVDKVA QVITFGTIKT KAAIKDAARV HYGQPGYAIA
     DKISKALPPP IMAKDIPLSG IVDPKHERYG EAAEVRSLIE TDSEVATIFE TARGLEGLIR
     NAGVHACAVI MSSEPLTNAI PLWQRDDGSI ITGWDYPSCE AIGLLKMDFL GLRNLTVIGD
     AIDNIKANRG VDIDLDTLGV DDPETYKLLA RGDTLGVFQL DGGPMRDLLR RMQPTRFDDI
     VAVGALYRPG PMGMNAHNDY ADRKNGRQNV KPIHPELDEP LKEILADTYG LIVYQEQIMH
     IGQKVAGYSM GRADVLRRAM GKKKQEVLEK EFEGFEAGMK ASDLVPGGFS DEAIKALWDT
     ILPFAGYAFN KSHAAAYGLI SYWTAYLKAN YTAEYMAALL TSVGDNKDKS AIYLSECRRL
     GIKVLPPDVN ESAQRFAAVG DDIRFGMGAV RNVGANVVES IIKTREEKGK YTSFTDFLDK
     SELVACNKRV IESLIKAGAF DSMGNTRLSM VQAHEEAVEA VVPLKRQQAM GQFDLFGPMG
     DEPDDAAAAA ASSPLAHLKF SDEEYPRKQL LSYEREMLGL YVSAHPLDGA ERILRKHAKK
     PIAAILADPP KEGEIVVSGL ITSLERRVNK KGEPWAICTV EDMDASLEVL FFPKSYAIFA
     ADLVEDNAVL VKGRVNWREE KMSVFGGGLV PLDLSDAAIG DEEPPLVLLV AAEKLDQSVV
     SELKSTLLAH KGDTPAHLKL MGKQGQRMYA LDDYPVRVSS MLMGELKSIQ GITANT
//
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