CCA2_SCHPO
ID CCA2_SCHPO Reviewed; 484 AA.
AC Q9Y7U9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=tRNA nucleotidyltransferase cca2 {ECO:0000303|PubMed:30528393};
DE EC=2.7.7.- {ECO:0000269|PubMed:30528393};
DE AltName: Full=A-adding enzyme cca2 {ECO:0000303|PubMed:16823372};
DE AltName: Full=tRNA adenylyltransferase cca2 {ECO:0000303|PubMed:30528393};
GN Name=cca2 {ECO:0000303|PubMed:30528393}; ORFNames=SPCC645.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION, DOMAIN, AND CATALYTIC ACTIVITY.
RX PubMed=30528393; DOI=10.1016/j.bbrc.2018.11.131;
RA Reid N.E., Ngou J.S., Joyce P.B.M.;
RT "Schizosaccharomyces pombe contains separate CC- and A-adding tRNA
RT nucleotidyltransferases.";
RL Biochem. Biophys. Res. Commun. 508:785-790(2019).
RN [4]
RP FUNCTION.
RX PubMed=30988468; DOI=10.1038/s41592-019-0370-6;
RA Preston M.A., Porter D.F., Chen F., Buter N., Lapointe C.P., Keles S.,
RA Kimble J., Wickens M.;
RT "Unbiased screen of RNA tailing activities reveals a poly(UG) polymerase.";
RL Nat. Methods 16:437-445(2019).
CC -!- FUNCTION: tRNA nucleotidyltransferase involved in the synthesis of the
CC tRNA CCA terminus. In contrast to what is usually observed in
CC eukaryotes for which one enzyme synthesizes the whole tRNA CCA
CC terminus, in S.pombe, cca1 specifically adds two cytidine residues to a
CC tRNA substrate lacking this sequence while cca2 specifically adds the
CC terminal adenosine residue thereby completing the CCA sequence.
CC {ECO:0000269|PubMed:30528393, ECO:0000269|PubMed:30988468}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tRNA with a 3' CC end + ATP = a tRNA with a 3' CCA end +
CC diphosphate; Xref=Rhea:RHEA:60012, Rhea:RHEA-COMP:10468, Rhea:RHEA-
CC COMP:15488, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83069,
CC ChEBI:CHEBI:83071; Evidence={ECO:0000269|PubMed:30528393};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The B/A element (residues 122-124) is present in cca2 but not
CC cca1 and is thought to position tRNA-NCC for terminal A addition.
CC {ECO:0000305|PubMed:30528393}.
CC -!- DOMAIN: The absence of a C-terminal alpha-helix in cca2 as compared to
CC cca1 might allow for binding of the tRNA-NCC substrate, or prevents
CC binding of the tRNA-N or tRNA-NC substrates.
CC {ECO:0000305|PubMed:30528393}.
CC -!- DOMAIN: The ERhxxExxxhh motif (residues 234-244) has been suggested to
CC serve to distinguish between A-adding and CC-adding proteins as A-
CC adding enzymes have a small amino acid in the first position while CC-
CC adding enzymes have an E in the first position.
CC {ECO:0000305|PubMed:30528393}.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329672; CAB39906.1; -; Genomic_DNA.
DR PIR; T41527; T41527.
DR RefSeq; NP_588119.1; NM_001023109.2.
DR AlphaFoldDB; Q9Y7U9; -.
DR SMR; Q9Y7U9; -.
DR STRING; 4896.SPCC645.10.1; -.
DR MaxQB; Q9Y7U9; -.
DR PaxDb; Q9Y7U9; -.
DR PRIDE; Q9Y7U9; -.
DR EnsemblFungi; SPCC645.10.1; SPCC645.10.1:pep; SPCC645.10.
DR GeneID; 2539578; -.
DR KEGG; spo:SPCC645.10; -.
DR PomBase; SPCC645.10; cca2.
DR VEuPathDB; FungiDB:SPCC645.10; -.
DR eggNOG; KOG2159; Eukaryota.
DR HOGENOM; CLU_019592_2_1_1; -.
DR InParanoid; Q9Y7U9; -.
DR OMA; WVSTAIN; -.
DR PhylomeDB; Q9Y7U9; -.
DR PRO; PR:Q9Y7U9; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; EXP:PomBase.
DR GO; GO:0005739; C:mitochondrion; EXP:PomBase.
DR GO; GO:0005524; F:ATP binding; IDA:PomBase.
DR GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IDA:PomBase.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IDA:PomBase.
DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IDA:PomBase.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; Transferase; tRNA-binding.
FT CHAIN 1..484
FT /note="tRNA nucleotidyltransferase cca2"
FT /id="PRO_0000316214"
FT REGION 125..142
FT /note="Flexible loop"
FT /evidence="ECO:0000305|PubMed:30528393"
FT MOTIF 122..124
FT /note="B/A element"
FT /evidence="ECO:0000305|PubMed:30528393"
FT MOTIF 234..244
FT /note="ERhxxExxxhh motif"
FT /evidence="ECO:0000305|PubMed:30528393"
SQ SEQUENCE 484 AA; 54723 MW; 6BB5758A8548BB91 CRC64;
MYSRIVLNDV EKKVVNLLKK TADFIESKSS SSSSLEVRLA GGWVRDKLLG LSSDDLDVTL
NKVTGVDFAN SIFEYVHSLD SDSVIPYKDA LGKLTVNPDQ SKHLETATLS LFDLDIDFVG
LRAESYDDKS RIPSVTPGTV ETDALRRDFT VNTLFFNIRT EKIEDITKRG YKDLQTKVLV
TPISPLQSFL EDPLRILRGI RFASRFEFTI DPSVVSAIQD PKVCKAFEKK VSKERVGEEI
EKMLKGANAK LALQLLYSTN TYQFTFDTLP AEKEFQIPKA LEATESLFQS LALTFPKLMK
LSEDEKIGLW LYVALIPWSS QTVMVKKKQF YIPAIIAKDK LKLRSTYVNQ LNQCCTFNPI
FDELVNDTST KNCSSIGSLI RQLNKSWEVV FLTSVIYSCC KTPAASVSNT FSSYKSLYDF
IYDKNLQNAY NMKPLLDGKQ IMKNVGVKPG PQLKETMDNM ISWQFKHPEG SVEDCVAYLQ
SLKI
