ID B3ES44_AMOA5 Unreviewed; 1148 AA.
AC B3ES44;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN OrderedLocusNames=Aasi_0650 {ECO:0000313|EMBL:ACE06046.1};
OS Amoebophilus asiaticus (strain 5a2).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Amoebophilaceae;
OC Candidatus Amoebophilus.
OX NCBI_TaxID=452471 {ECO:0000313|EMBL:ACE06046.1, ECO:0000313|Proteomes:UP000001227};
RN [1] {ECO:0000313|EMBL:ACE06046.1, ECO:0000313|Proteomes:UP000001227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5a2 {ECO:0000313|EMBL:ACE06046.1,
RC ECO:0000313|Proteomes:UP000001227};
RX PubMed=20023027; DOI=10.1128/JB.01379-09;
RA Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA Rattei T., Horn M.;
RT "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT reveals common mechanisms for host cell interaction among amoeba-associated
RT bacteria.";
RL J. Bacteriol. 192:1045-1057(2010).
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; CP001102; ACE06046.1; -; Genomic_DNA.
DR RefSeq; WP_012472814.1; NC_010830.1.
DR AlphaFoldDB; B3ES44; -.
DR STRING; 452471.Aasi_0650; -.
DR KEGG; aas:Aasi_0650; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_10; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000001227; 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 Reference proteome {ECO:0000313|Proteomes:UP000001227};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..72
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1148 AA; 130112 MW; 4E287935E6A214E8 CRC64;
MIQFTHLHCH TQYSLLDGTA KIDKLFGKAK QLGMQALAIT DHGNMFGVPH FVAQAKKQGI
KPIIGCEFYL AADMHNLKEK TRYHQLLLAK NEVGYKNIVK LCSISFLEGY YYKPRIDKEL
LKKYSEGLIA TTCCLAGEVP QAIMRKGEEE AEKVFLSWLN IFGEDYYIEL QRHGLKEQDK
CNEVLLKWAQ KYQVKVIATN DVHYVEQQDS LAQDILLCLQ TGKDYNDPNR MRFDGDQFFL
KSPQEMLTLF HDIPQAVSNT QEIIDKINTP SLERDILLPV FQIPQGFTSQ DSYLRHLAIE
GAKKRFGAIS ADLEARINYE LGVIQQMGFP GYFLIVQDFI QAAKNLQVVV GPGRGSVAGS
VVAYCIGITD IDPIRYNLFF ERFLNPERVS MPDIDIDFDD EGRQKVIEYV VDKYGKNQVA
HIITFGSMAA KSAIRDVARV LGLPLERTNY IAKLVPEKLG ITLPESFEEV LELAELKKNS
NTLEGKVLSL AETLEGSARH TGVHAAGIII APDDLLNHIP VKTDKNSDLL VTQYDGSIVE
KVGMLKMDFL GLKTLSIIKD AIALIEKLHG TKIDLEQLPL DDLKTFKLYQ QGDTIATFQF
ESEGMRQWLK KLQPTEFEEL IAMNALYRPG PMQFIPNFIA RKHGQEKIDY PHPLLVDILK
NTYGIMVYQE QVMQTAQIIA GYSLGGADLL RKAMGKKQPE EMAKQREIFV QGAQEKNNLP
STKAIEIFEV MEKFAQYGFN RAHSAAYSVI AYQTAYLKAH YPAEYMASVL THNQNDIGKI
SFFMEECIRQ GIQVLGPDVN ESQVNFDVTP KQGIRFGLTA IKGAGEGAVS HIIAEREKNG
HFTDIFSFVE RVDLRMVNKK TLESLAMSGA FDGFTGCHRR QYLFAADGEH NLLVKAIQYG
NQIKQEKASA QQSLFAMDDN FQYIQKPPIP TCEPYDKIEK LRMEKELVGF YISGHPLDQF
RVELANFCDG HTQNILTFKQ KEVRLAGIIT ECSIKYNKQG RPFGLFILED YHGTLDLALF
GEDFLKNQHM LQKGMFVHIT GVVTERYNQQ DTWEYKPQKI SLLGELRDKL GKNLSIAVPI
EKITPQFITE LRSLVTKNTG NCCLKLHIAD PSEAMQVSLQ AFKYRVYPSD ELLHTLSQLT
ESSYQLTH
//
