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Database: UniProt
Entry: A0A220VD92_9GAMM
LinkDB: A0A220VD92_9GAMM
Original site: A0A220VD92_9GAMM 
ID   A0A220VD92_9GAMM        Unreviewed;       387 AA.
AC   A0A220VD92;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Multifunctional CCA tRNA nucleotidyl transferase/2'3'-cyclic phosphodiesterase/2'nucleotidase/phosphatase {ECO:0000313|EMBL:ASK78307.1};
DE            EC=2.7.7.72 {ECO:0000313|EMBL:ASK78307.1};
DE            EC=3.1.4.16 {ECO:0000313|EMBL:ASK78307.1};
GN   Name=cca {ECO:0000313|EMBL:ASK78307.1};
GN   ORFNames=CF386_04395 {ECO:0000313|EMBL:ASK78307.1};
OS   Paraphotobacterium marinum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Paraphotobacterium.
OX   NCBI_TaxID=1755811 {ECO:0000313|EMBL:ASK78307.1, ECO:0000313|Proteomes:UP000242175};
RN   [1] {ECO:0000313|EMBL:ASK78307.1, ECO:0000313|Proteomes:UP000242175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NSCS20N07D {ECO:0000313|EMBL:ASK78307.1,
RC   ECO:0000313|Proteomes:UP000242175};
RX   PubMed=27154455; DOI=10.1099/ijsem.0.001142;
RA   Huang Z., Dong C., Shao Z.;
RT   "Paraphotobacterium marinum gen. nov., sp. nov., a member of the family
RT   Vibrionaceae, isolated from surface seawater.";
RL   Int. J. Syst. Evol. Microbiol. 66:3050-3056(2016).
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|RuleBase:RU003953}.
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DR   EMBL; CP022355; ASK78307.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A220VD92; -.
DR   KEGG; pmai:CF386_04395; -.
DR   Proteomes; UP000242175; Chromosome large.
DR   GO; GO:0008663; F:2',3'-cyclic-nucleotide 2'-phosphodiesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004810; F:CCA tRNA nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:InterPro.
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; IPR012006; CCA_bact.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002646; PolA_pol_head_dom.
DR   InterPro; IPR032828; PolyA_RNA-bd.
DR   PANTHER; PTHR47545; MULTIFUNCTIONAL CCA PROTEIN; 1.
DR   PANTHER; PTHR47545:SF1; MULTIFUNCTIONAL CCA PROTEIN; 1.
DR   Pfam; PF01743; PolyA_pol; 1.
DR   Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR   PIRSF; PIRSF000813; CCA_bact; 2.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:ASK78307.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:ASK78307.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242175};
KW   RNA repair {ECO:0000256|ARBA:ARBA00022800};
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}.
FT   DOMAIN          13..132
FT                   /note="Poly A polymerase head"
FT                   /evidence="ECO:0000259|Pfam:PF01743"
FT   DOMAIN          160..221
FT                   /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT                   and SrmB- binding"
FT                   /evidence="ECO:0000259|Pfam:PF12627"
SQ   SEQUENCE   387 AA;  45210 MW;  C11B3A84ACF2D63B CRC64;
     MGIYYFFEII MKIYLVGGAV RDQLLGLIPK DNDYVVVGSS PNEMLKKGFK KVGKFFPVFI
     NPQTGNEYAL ARKEIKKGKG HQGFRVIFSK DISLEEDLLR RDLTINAIAE DELGTKIDPF
     GGLSDLKNRQ LRHISNAFIE DPLRVLRVAR FKAQLHKFKF EIAPETMSLM QRISISGELE
     TISQERIWNE WHKSLLSGVP EVFINTLRHS SALSVICPEI NQLYSIKINN TNLGSQTERL
     IKKVRNISGT YQTIFIATIF YLLHSNYEEQ LNSFINRIKI PKELKKLILT FQKCHFYFKC
     SLKETPEFSL SFLEKLNVFR QPNNLDIFFK IYNIENKDQC EETQIYYQNV FKILSEFKLD
     IPSHIHPNQI KNYVREKKII EIQSKLH
//
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