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Database: UniProt
Entry: K9YI15_CYASC
LinkDB: K9YI15_CYASC
Original site: K9YI15_CYASC 
ID   K9YI15_CYASC            Unreviewed;       103 AA.
AC   K9YI15;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=DNA polymerase beta domain protein region {ECO:0000313|EMBL:AFZ46611.1};
GN   OrderedLocusNames=Cyast_0635 {ECO:0000313|EMBL:AFZ46611.1};
OS   Cyanobacterium stanieri (strain ATCC 29140 / PCC 7202).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Geminocystaceae; Cyanobacterium.
OX   NCBI_TaxID=292563 {ECO:0000313|EMBL:AFZ46611.1, ECO:0000313|Proteomes:UP000010483};
RN   [1] {ECO:0000313|Proteomes:UP000010483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29140 / PCC 7202 {ECO:0000313|Proteomes:UP000010483};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the MntA antitoxin family.
CC       {ECO:0000256|ARBA:ARBA00038276}.
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DR   EMBL; CP003940; AFZ46611.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9YI15; -.
DR   STRING; 292563.Cyast_0635; -.
DR   KEGG; csn:Cyast_0635; -.
DR   PATRIC; fig|292563.3.peg.665; -.
DR   eggNOG; COG1669; Bacteria.
DR   HOGENOM; CLU_130257_10_0_3; -.
DR   BioCyc; CSTA292563:G1353-640-MONOMER; -.
DR   Proteomes; UP000010483; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR   CDD; cd05403; NT_KNTase_like; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR   PANTHER; PTHR33571:SF14; PROTEIN ADENYLYLTRANSFERASE MJ0128-RELATED; 1.
DR   PANTHER; PTHR33571; SSL8005 PROTEIN; 1.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010483};
KW   Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649}.
FT   DOMAIN          15..102
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
SQ   SEQUENCE   103 AA;  11979 MW;  C2ADF3AF670D13A4 CRC64;
     MVHSTEKLTH LQAKIREIKK EIGDKYQIEE LGLFGSYVRG EETENSDIDI LVKFHSDHTI
     GLFKYCELQN LLSEKLGKKV DLVMKDSLKT YIGKYILDEV IYL
//
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