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Database: UniProt
Entry: A0A2S6CR28_9CYAN
LinkDB: A0A2S6CR28_9CYAN
Original site: A0A2S6CR28_9CYAN 
ID   A0A2S6CR28_9CYAN        Unreviewed;       425 AA.
AC   A0A2S6CR28;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=[cytidine(C)-cytidine(C)-adenosine (A)]-adding enzyme {ECO:0000313|EMBL:PPJ62169.1};
GN   ORFNames=CUN59_17110 {ECO:0000313|EMBL:PPJ62169.1};
OS   Cuspidothrix issatschenkoi CHARLIE-1.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC   Cuspidothrix.
OX   NCBI_TaxID=2052836 {ECO:0000313|EMBL:PPJ62169.1, ECO:0000313|Proteomes:UP000239589};
RN   [1] {ECO:0000313|EMBL:PPJ62169.1, ECO:0000313|Proteomes:UP000239589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHARLIE-1 {ECO:0000313|EMBL:PPJ62169.1,
RC   ECO:0000313|Proteomes:UP000239589};
RA   Kust A., Mares J., Jokela J., Urajova P., Hajek J., Saurav K., Voracova K.,
RA   Fewer D.P., Haapaniemi E., Permi P., Rehakova K., Sivonen K., Hrouzek P.;
RT   "Discovery of a pederin family compound in a non-symbiotic bloom-forming
RT   cyanobacterium.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC       polymerase family. {ECO:0000256|ARBA:ARBA00007265,
CC       ECO:0000256|RuleBase:RU003953}.
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:PPJ62169.1}.
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DR   EMBL; PGEM01000139; PPJ62169.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S6CR28; -.
DR   OrthoDB; 9805698at2; -.
DR   Proteomes; UP000239589; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd05398; NT_ClassII-CCAase; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR   InterPro; IPR032810; CCA-adding_enz_C.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002646; PolA_pol_head_dom.
DR   InterPro; IPR032828; PolyA_RNA-bd.
DR   PANTHER; PTHR47545:SF2; CC-ADDING TRNA NUCLEOTIDYLTRANSFERASE; 1.
DR   PANTHER; PTHR47545; MULTIFUNCTIONAL CCA PROTEIN; 1.
DR   Pfam; PF01743; PolyA_pol; 1.
DR   Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR   Pfam; PF13735; tRNA_NucTran2_2; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239589};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU003953};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   DOMAIN          27..139
FT                   /note="Poly A polymerase head"
FT                   /evidence="ECO:0000259|Pfam:PF01743"
FT   DOMAIN          164..222
FT                   /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT                   and SrmB- binding"
FT                   /evidence="ECO:0000259|Pfam:PF12627"
FT   DOMAIN          267..417
FT                   /note="CCA-adding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13735"
SQ   SEQUENCE   425 AA;  47557 MW;  55B4FEF80710FE52 CRC64;
     MTIDEFFGSR LAAKNWPFSL ECLPEPVYMV GGAVRDAILG RVREYVDLDF IIPWDTVKVA
     KKIAQRYDAG FVLLDAERQI ARVVFPTGTA DFAQLEGENL LTDLYRRDFT INAIAYNPHN
     QEIIDPLHGC QDIDSGILRM ISPVNLQNDP LRLMRAYRQA AQLDFTIEPN TQEAIRSLAS
     SITEVAAERV RVEVGYLLAS SQGTFWLDQA WQDGVLGSLF KNSTASSFIK LNAVDEAFAV
     IRDKWQKLAE QLTNYVRDTI KTSWLSVAKL ACLVHSQAEI AEIELQELTY SRAEIRGVTT
     ALRLFAEIKA VDMPLRKQYF LFREMGILFP VVLVLALAND IVAKGIFEES MLFTYQPLIE
     RYLNPDDVVA HPRPLISGKE IMTVLKVPAS PLVGELLMEI GVAQAEGKIS TIAAALEYAA
     NLVKP
//
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