ID K9UIC3_CHAP6 Unreviewed; 1219 AA.
AC K9UIC3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=Cha6605_3879 {ECO:0000313|EMBL:AFY94847.1};
OS Chamaesiphon minutus (strain ATCC 27169 / PCC 6605).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Chamaesiphonaceae;
OC Chamaesiphon.
OX NCBI_TaxID=1173020 {ECO:0000313|EMBL:AFY94847.1, ECO:0000313|Proteomes:UP000010366};
RN [1] {ECO:0000313|EMBL:AFY94847.1, ECO:0000313|Proteomes:UP000010366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27169 / PCC 6605 {ECO:0000313|Proteomes:UP000010366};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Chamaesiphon sp. PCC 6605.";
RL Submitted (MAY-2012) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003600; AFY94847.1; -; Genomic_DNA.
DR RefSeq; WP_015160962.1; NC_019697.1.
DR AlphaFoldDB; K9UIC3; -.
DR STRING; 1173020.Cha6605_3879; -.
DR KEGG; cmp:Cha6605_3879; -.
DR PATRIC; fig|1173020.3.peg.4441; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_3; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000010366; 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 ECO:0000313|EMBL:AFY94847.1};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000010366};
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 1219 AA; 137989 MW; DA52BED354E6B4A7 CRC64;
MTFVGLHMHS DYSLLDGASQ LPNLVDRAVE LGMPAIALTD HGVMYGAIEL IKVCRTRNVK
PIIGNEMYVI NGDFTQQKRY QKFHQVVLAK NTQGYRNLVK LTTVSHLEGF QGRGIFARPC
INKEYIEKYK EGLIVTSGCL GGEVPQAIMM GRPDAARKVA KWYKERFGED YYLEIQDHGL
KEDRVVNVEI VKIARELDIK IIATNDSHFV SCYDVEAHDA LLCIQTGQLI REDKRMRYSG
NEYLKSAEEM ALLFRDHLSD EVIAEAIANT VEVADKIQPY NILGEPKIPD FPIPVGHTPA
TYVEEISREG LKERLKVQRY SDIDREYQER LDFELKMIER MGFSTYFLVV WDYIKFARDR
AIPVGPGRGS AAGSLVAYAM KITNIDPVHH CLLFERFLNP DRKSMPDIDT DFCIERRAEV
IDYVTEKYGK ERVAQIITFN RMTSKAVLKD VARVLNIPYG AANELGKMIP VVRGKPTKLA
VMISDKTPAP EFKQIYETGE YADPETGEKI TARQWVDMAM RIEGTNKTFG VHAAGVVISA
QPLDEIVPLQ RNNDGSVITQ YYMEDLDSMG LLKMDFLGLR NLTIIQNAID TIEQTKGDKI
DPDDITFEER RTYKILNKGS LNKRPPNVEK TYKQVESGDL EGVFQLESSG MLDVVARLKP
SSIEDLSSIL ALYRPGPLDA GLIPIFIDRK HGREKITYEH PILETILEET YGVIVYQEQI
MKIAQDLAGY TLGEADILRR CMGKKKADEM NKQREKFLDG AAKKGVSHAI ADALFDKMVL
FAEYCFNKSH STAYAYVTYQ TAFLKANYPA EYMSALLTAN SGDQDKVTRY LNNCEQTLDI
KVEPPDINRS YVKFRPVVDP ERPNRLNILF GLSAIKNVGE AAIENILKAR EEGGEFTSLA
DLCQRVSLQA VNKRTLESLI QCGTFDNLDR NRRQLINDLD VIIPWSQSKA KEKAIGQGNL
FDLLGDLKPE IGGFDAVPKS PLVSDFSSSE RLQFEQELLG VYVSDHPLKN AEKIAKMQKH
DFKRIIEIEK PCKDVKLVVM LTEVKIVQTK KDNKSMAILK LTDIASSKLE AVAFPEAYEK
IKELLIPNSS VILVGKVSRK KDNDELQMIV DEAIEIDRTA VHKPVDIELE PQHLVLIELP
VNVAIDEIRS QALKTMLEEY SGDTSAVKTP VYAIVRSENS YRLVQFGKQF WVQDPSELVD
RMHDRGFDIK VKQISSIET
//
