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Database: UniProt
Entry: L8MA83_9CYAN
LinkDB: L8MA83_9CYAN
Original site: L8MA83_9CYAN 
ID   L8MA83_9CYAN            Unreviewed;       116 AA.
AC   L8MA83;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Putative nucleotidyltransferase {ECO:0000313|EMBL:ELS05132.1};
GN   ORFNames=Xen7305DRAFT_00048720 {ECO:0000313|EMBL:ELS05132.1};
OS   Xenococcus sp. PCC 7305.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Xenococcaceae;
OC   Xenococcus.
OX   NCBI_TaxID=102125 {ECO:0000313|EMBL:ELS05132.1, ECO:0000313|Proteomes:UP000011203};
RN   [1] {ECO:0000313|EMBL:ELS05132.1, ECO:0000313|Proteomes:UP000011203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7305 {ECO:0000313|EMBL:ELS05132.1,
RC   ECO:0000313|Proteomes:UP000011203};
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELS05132.1}.
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DR   EMBL; ALVZ01000077; ELS05132.1; -; Genomic_DNA.
DR   AlphaFoldDB; L8MA83; -.
DR   STRING; 102125.Xen7305DRAFT_00048720; -.
DR   PATRIC; fig|102125.3.peg.519; -.
DR   eggNOG; COG1669; Bacteria.
DR   OrthoDB; 428157at2; -.
DR   Proteomes; UP000011203; Unassembled WGS sequence.
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:UP000011203};
KW   Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649};
KW   Transferase {ECO:0000313|EMBL:ELS05132.1}.
FT   DOMAIN          25..107
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
SQ   SEQUENCE   116 AA;  13483 MW;  9372E4CC3F4B653A CRC64;
     MSSLKPVINQ NQIEQRLGVS LLTVTQFCQR WQITELALFG SVLRDDFNPN SDLDFLVTFS
     PDAKIGLAEV NEMEQELKNM VKRKIDLIWK KSIEASQNWI RRQNILETAK VIYGER
//
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