ID A0A2U8UTF9_9CAUD Unreviewed; 1161 AA.
AC A0A2U8UTF9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=54 {ECO:0000313|EMBL:AWN07422.1};
GN ORFNames=SEA_MANEEKUL_54 {ECO:0000313|EMBL:AWN07422.1};
OS Streptomyces phage Maneekul.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Arquatrovirinae; Likavirus.
OX NCBI_TaxID=2182320 {ECO:0000313|EMBL:AWN07422.1, ECO:0000313|Proteomes:UP000246721};
RN [1] {ECO:0000313|EMBL:AWN07422.1, ECO:0000313|Proteomes:UP000246721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Maneekul J., Bhuiyan S., Nayek S., Layton S.R., Kim T., Hughes L.E.,
RA Garlena R.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W.,
RA Hatfull G.F.;
RL Submitted (APR-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}.
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DR EMBL; MH171095; AWN07422.1; -; Genomic_DNA.
DR Proteomes; UP000246721; Genome.
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:UP000246721};
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 1161 AA; 128158 MW; 32E337DB5042531A CRC64;
MTEFVHLHNH SEYSLLDGAA RMKQMVAEVA RQGAPAVAVT DHGNLHGAYD FFTSAQAAGV
KPIIGIEAYM APDSRFDQER VQWGEPEQKR YDVSGRGAYT HLTILSTNKT GLHNLMKLSS
RSYQEGLLGK YPRMDFELVA EHNEGLVVTT GCPGGAIMTR LNLGQYDEAV KEAGRYLEVF
GRDRYFLELM DHGIEIERRV REDLYRLGKH LALTPVVTND SHYVTAEESV AHDALLCVQT
GTTLDNPNRF RFEGSGYFLK SAAEMAAIDS SPIWEWGMRT TLDIAEMVDT TGMFEHENLM
PKFPVPQGHT EITWFENEVQ EGARRRYPNG TDYEHGKQLQ YEIDMIIQMG FPSYFLVVAD
FIRWAKENGV WVGPGRGSAA GSLVAYVLGI TDLDPLEHGL IFERFLNPER VSMPDVDIDF
DDRRRGEVIQ YVTQKYGADK VAQIATYGRI KARNAMKDAA RVLDKPFQVG EKLTKAYPAD
VMGNSMPLEG IFNPEHKRYD EAGEIRGLYV SDPDAKEVID TALGLEGLVR QMGVHAAGVI
MSDEPLVDHI PVWVRPQDGA TITQFDYPSC EALGLLKMDF LGLRNLTIMG DAVENIRRNR
GEHVDLENIP LDDAPTYELL ARGDTLSVFQ LDGGAMRSLL RLLKPDHFED ISAVVALYRP
GPMGVGSHTN YALRKNGQQA ITPIHPEVAE SLSEILDPTF QLIIYQEQVQ KVAQVMAGYT
LGQADLLRRA MGKKKPEVLA KEFENFQKGA KERGYSDDAI RTVWDVLVPF AGYAFNKAHS
AAYGLIAYRT AYLKTHYPAE YMAAVLTSVG DDKNKMATYL GEARRMGLHV LPPDVSVSNS
SFTPNGESEI RFGLTAVKNV GEGMVAEIAE LREAWGKFTS LPDFLKAATQ ATVSKRAIES
LIKAGAFDST GATRKGLAEQ HEALADNADR LGAPGLFIPA DTEPIKLAVG EDWAKGPLLS
IEREMLGLYV SDHPLAGLGA SLRAQATHSV ADVLDDRAQE GMTVLIGCLV SSVEIKTNKR
GQKWAVAELE DQTGSVECAF FAGSYGDVKD VLVQDAIVFV RGRLEYRDGS PQLIGMGVQL
AQNLARVQDG PVVIELPVTG LNDKTAPVLA KILDRHPGET EVILRLVGPG VTQHMRVGKY
QVTRSPAFDA ELSQFTQSVH N
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