ID   ATE1_SCHPO              Reviewed;         391 AA.
AC   O14133;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 3.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Arginyl-tRNA--protein transferase 1;
DE            Short=Arginyltransferase 1;
DE            Short=R-transferase 1;
DE            EC=2.3.2.8;
DE   AltName: Full=Arginine-tRNA--protein transferase 1;
GN   ORFNames=SPAC3C7.07c;
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
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).
CC   -!- FUNCTION: Involved in the post-translational conjugation of arginine to
CC       the N-terminal aspartate or glutamate of a protein. This arginylation
CC       is required for degradation of the protein via the ubiquitin pathway.
CC       Does not arginylate cysteine residues (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-terminal L-alpha-aminoacyl-[protein] + L-arginyl-
CC         tRNA(Arg) = H(+) + N-terminal L-arginyl-L-amino acid-[protein] +
CC         tRNA(Arg); Xref=Rhea:RHEA:10208, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC         COMP:9673, Rhea:RHEA-COMP:10636, Rhea:RHEA-COMP:10638,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:78442, ChEBI:CHEBI:78513,
CC         ChEBI:CHEBI:78597, ChEBI:CHEBI:83562; EC=2.3.2.8;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the R-transferase family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB16746.2; -; Genomic_DNA.
DR   PIR; T38693; T38693.
DR   RefSeq; NP_593608.2; NM_001019039.2.
DR   AlphaFoldDB; O14133; -.
DR   BioGRID; 279382; 3.
DR   STRING; 4896.SPAC3C7.07c.1; -.
DR   MaxQB; O14133; -.
DR   PaxDb; O14133; -.
DR   EnsemblFungi; SPAC3C7.07c.1; SPAC3C7.07c.1:pep; SPAC3C7.07c.
DR   GeneID; 2542941; -.
DR   KEGG; spo:SPAC3C7.07c; -.
DR   PomBase; SPAC3C7.07c; -.
DR   VEuPathDB; FungiDB:SPAC3C7.07c; -.
DR   eggNOG; KOG1193; Eukaryota.
DR   HOGENOM; CLU_020349_0_0_1; -.
DR   InParanoid; O14133; -.
DR   OMA; NLRTSCC; -.
DR   PRO; PR:O14133; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0004057; F:arginyltransferase activity; ISO:PomBase.
DR   GO; GO:0016598; P:protein arginylation; IBA:GO_Central.
DR   GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; ISO:PomBase.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR030700; N-end_Aminoacyl_Trfase.
DR   InterPro; IPR007472; N-end_Aminoacyl_Trfase_C.
DR   InterPro; IPR007471; N-end_Aminoacyl_Trfase_N.
DR   PANTHER; PTHR21367; PTHR21367; 2.
DR   Pfam; PF04377; ATE_C; 1.
DR   Pfam; PF04376; ATE_N; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Nucleus; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..391
FT                   /note="Arginyl-tRNA--protein transferase 1"
FT                   /id="PRO_0000351080"
SQ   SEQUENCE   391 AA;  45092 MW;  68CA0F88F243E9DA CRC64;
     MVLDKLLYTG YNVSTECGYC KSGRKTEHFG LLAEKLSCED YQRLIDLGWR RSGHYLYKPN
     GKTSCCSLYT IRLDSYNFKI AKEQKKAIKK WVKYVNGKPL KPMKSEISTD YLNNAFQTIE
     SLGAEKYSVT MEPCTYTDEK FEVFKKYQMQ VHLEKEEEIT KKGFSRFLCN SPLFNEDKGI
     KYGSYHQMYR FQGRLVAVGV LDLLPHGVSS VYLFYDPDMS KFSLGRISAC REIWLALECG
     YRYYYMGYYI HTCPKMKYKA TYSPSYLLNP GTNKWIPIEN FTSLWNTGAP KYISFGDENN
     SDIQTAVDYD SSEDSSQNED DYTLFNRQLP GILSVNVAES LVSENFANIG NSTFPTRHVL
     SYFPQVKHWF VEINAAVGEE VAKSYTLVLS S