ID D1YUN3_METPS Unreviewed; 443 AA.
AC D1YUN3;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 01-MAY-2013, entry version 19.
DE RecName: Full=CCA-adding enzyme;
DE EC=2.7.7.72;
DE AltName: Full=CCA tRNA nucleotidyltransferase;
DE AltName: Full=tRNA CCA-pyrophosphorylase;
DE AltName: Full=tRNA adenylyl-/cytidylyl- transferase;
DE AltName: Full=tRNA nucleotidyltransferase;
DE AltName: Full=tRNA-NT;
GN Name=cca; OrderedLocusNames=MCP_0083;
OS Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS SANAE).
OC Archaea; Euryarchaeota; Methanomicrobia; Methanocellales;
OC Methanocellaceae; Methanocella.
OX NCBI_TaxID=304371;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE;
RX PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA Mori K., Fujita N., Imachi H., Takai K.;
RT "Genome sequence of a mesophilic hydrogenotrophic methanogen
RT Methanocella paludicola, the first cultivated representative of the
RT order Methanocellales.";
RL PLoS ONE 6:E22898-E22898(2011).
CC -!- FUNCTION: Catalyzes the addition and repair of the essential 3'-
CC terminal CCA sequence in tRNAs without using a nucleic acid
CC template. Adds these three nucleotides in the order of C, C, and A
CC to the tRNA nucleotide-73, using CTP and ATP as substrates and
CC producing inorganic pyrophosphate (By similarity).
CC -!- CATALYTIC ACTIVITY: A tRNA precursor + 2 CTP + ATP = a tRNA with a
CC 3' CCA end + 3 diphosphate.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- MISCELLANEOUS: A single active site specifically recognizes both
CC ATP and CTP and is responsible for their addition (By similarity).
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. Archaeal CCA-adding enzyme subfamily.
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DR EMBL; AP011532; BAI60155.1; -; Genomic_DNA.
DR RefSeq; YP_003355138.1; NC_013665.1.
DR EnsemblBacteria; BAI60155; BAI60155; MCP_0083.
DR GeneID; 8682940; -.
DR KEGG; mpd:MCP_0083; -.
DR HOGENOM; HOG000226400; -.
DR KO; K07558; -.
DR OMA; YASHPYV; -.
DR BioCyc; MPAL304371:GI7G-2587-MONOMER; -.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IEA:EC.
DR GO; GO:0052928; F:CTP:3'-cytidine-tRNA cytidylyltransferase activity; IEA:EC.
DR GO; GO:0052927; F:CTP:tRNA cytidylyltransferase activity; IEA:EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0004810; F:tRNA adenylyltransferase activity; IEA:HAMAP.
DR GO; GO:0000049; F:tRNA binding; IEA:HAMAP.
DR GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:HAMAP.
DR GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:HAMAP.
DR HAMAP; MF_01264; CCA_arch; 1; -.
DR InterPro; IPR008229; CCA-adding_arc.
DR InterPro; IPR002934; Nucleotidyltransferase.
DR InterPro; IPR011068; NuclTrfase_I_C.
DR InterPro; IPR015329; tRNA_NucTransf2.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF09249; tRNA_NucTransf2; 1.
DR PIRSF; PIRSF005335; CCA_arch; 1.
DR SUPFAM; SSF55003; PAP_C; 1.
DR TIGRFAMs; TIGR03671; cca_archaeal; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleotidyltransferase; RNA repair; RNA-binding;
KW Transferase; tRNA processing.
FT METAL 64 64 Magnesium (By similarity).
FT METAL 66 66 Magnesium (By similarity).
FT METAL 115 115 Magnesium (By similarity).
FT BINDING 52 52 ATP or CTP (By similarity).
FT BINDING 55 55 ATP or CTP (By similarity).
FT BINDING 138 138 ATP or CTP (By similarity).
FT BINDING 157 157 ATP or CTP (By similarity).
FT BINDING 166 166 ATP or CTP (By similarity).
SQ SEQUENCE 443 AA; 50221 MW; 5E8FDD6FCEEC63B0 CRC64;
MPDELYREVL ERIKPSAVED AHMRSVAHEV IDKLDSEARE HGLDVYTIHV GSTARDTWLK
GKKDIDIFLM FPPDTPLEKL KEDGLRLARE VSPRFEERYA EHPYITALYK GLDVDLVPCY
HVEDAAHIQS AVDRSPFHNT YVLKHIDGLH DEVRLLKQFT RGVGVYGSEL RTQGFSGYLC
ELLVLKYGSF DGAVEHGAGF KRGRVIDIEG HMDKSVEHPD PLIVIDPVDP KRNVAAALSG
QKFCEFVDAC RRFLKAPSID FFFPPAAEPM KKGALEGLLA SRGTKLLAIT FKTPDIVEDT
LYPQLRKAED SLAKLLERHE FKAYRTDVWS NDRSAIVLEM LVWELPAIER HLGPPLDERE
HCEKFIEKYP GAYIMGCRYV VDIPRKYDTA VELINAQLKS CGLGKHVCAS IGQGFEILTN
EKTLELGPEF ARFLTKFLRA PET
//
