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Database: UniProt
Entry: A0A222SJ85_9CHLB
LinkDB: A0A222SJ85_9CHLB
Original site: A0A222SJ85_9CHLB 
ID   A0A222SJ85_9CHLB        Unreviewed;      1189 AA.
AC   A0A222SJ85;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=CHL67_06630 {ECO:0000313|EMBL:ASQ90644.1};
OS   Prosthecochloris sp. GSB1.
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Prosthecochloris.
OX   NCBI_TaxID=281093 {ECO:0000313|EMBL:ASQ90644.1, ECO:0000313|Proteomes:UP000201322};
RN   [1] {ECO:0000313|Proteomes:UP000201322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TY Vent \ GSB1 \ Ty-1 {ECO:0000313|Proteomes:UP000201322};
RA   Bryant D.A., Liu Z., Li T., Zhao F., Garcia Costas A.M.;
RL   Submitted (JUL-2017) 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; CP022571; ASQ90644.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A222SJ85; -.
DR   KEGG; pros:CHL67_06630; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000201322; 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   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; 2.
DR   PANTHER; PTHR32294; 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   Reference proteome {ECO:0000313|Proteomes:UP000201322};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..71
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1189 AA;  133151 MW;  1722C2ABB370DEEE CRC64;
     MDFVHLHTHT HYSMQSSPVF PQELFAACLR QGMDSVAVTD YAAMFNMPEL FSLARDAGVR
     LIIGSEIYLL EQDAWHDSRT SVSPSLILLV KDEAGYRNLC ILLSRAAREG FVNGTPHVDS
     SWLAQYRDGL VCLSAYYAGR IGRALLAGNH DEASSFASFY REIYGDDFYL ELQRHFTPFD
     DRLNEDTLAL AGELGIGVVA TNNVHYLERK DADRYRALVA VKTKQKLSSS QLQSLPNNEN
     YLKAPGEMSK LFDDAYGELS NTLRIAEKCS YSFQTQDPRL PRFPLPEGFE DEAVYLRHLT
     YEGAREKYAD PEAGGLTWKM VEERIEKELG VIISMGFSSY FLIVSDLIAA SRRMGYSVGP
     GRGSAAGSIV AYLTGITRID PLRYKLLFER FLNPERVSMP DIDIDFTPVG KQKVLEYTVE
     KYGEESVAKV IAIGTLGAKA AIRDAGRVLE VPLPVVDRLA KLVPGKPGIT LRQALEEVKE
     LDAQVNGSSQ NQRLMEYARA LEGRARNVSM HAGAVVITNG SLQEQVPLYV SNKIETEERK
     FADEMDADEL ERGGARTGGD EKQVVTQFDK NWIENAGLLK IDYLGLETLA VIDETLHLIR
     KRHDIHIDLE KVPMNDRKTF GIFQEGKMAG IFQFESQGMQ NYMTKLQPTQ IGDIIAMSAL
     YRPGALNARV DEKRNAVDLF VDRKHNREPI DYMHPMLEEI LKETYGVIVY QEQVMQISQV
     MGGFSLAKAD NLRKAMGKKK PEIMQKFKAD FVEGAVEQGV HDKLANRIFD LMAEFAGYGF
     NKSHSAAYGV LAYWTGYLKA HYPAEFMTAI LNSEIGDAAR MKHLSDEAKS FGIAVLPPCV
     NTSDALFTIE ECEDGRTAIR IGLSAIKQVG NAARAVVSAR LLRKKPFVNL FDLAASVDLR
     LMNRKALECL ISAGTLDEID PDRAKLLANI DKAIRFGQMQ NKSVTLGQCG FFSDESGGAI
     HDALYPEMDA AAEPMTESEK LQAEKKLVGF YMSRHPLERY RRDWEAFANL PLDTKEVQPM
     RQYKVIGVVV SIKHHQDRKG KQMLFGLLED FTGKADFTVF ASVYEQYRHL IKPEAVLMMI
     VEAEASGGSL KLLVREVVPV RQVRESCIDR VILRIDADDP SELERLMRVK KVFEEHRGGT
     AVDFDVKVQS AENIEVLRLF ARNATIEPGE EALGKLEKIL GPDNVRIAG
//
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