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Ribosomal protein arginine N-methyltransferase rmt3 (EC 2.1.1.-)

 ANM3_SCHPO              Reviewed;         543 AA.
O13648; Q7LWE1;
14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 3.
25-OCT-2017, entry version 120.
RecName: Full=Ribosomal protein arginine N-methyltransferase rmt3;
EC=2.1.1.-;
Name=rmt3; Synonyms=prmt3; ORFNames=SPBC8D2.10c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=10620777;
DOI=10.1002/(SICI)1097-0061(20000115)16:1<71::AID-YEA505>3.0.CO;2-5;
Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q.,
Yanagida M.;
"A 38 kb segment containing the cdc2 gene from the left arm of fission
yeast chromosome II: sequence analysis and characterization of the
genomic DNA and cDNAs encoded on the segment.";
Yeast 16:71-80(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EF1A-C; RPS2 AND
RPS24, AND ASSOCIATION WITH THE 40S RIBOSOMAL PARTICLE.
PubMed=15175657; DOI=10.1038/sj.emboj.7600265;
Bachand F., Silver P.A.;
"PRMT3 is a ribosomal protein methyltransferase that affects the
cellular levels of ribosomal subunits.";
EMBO J. 23:2641-2650(2004).
[4]
FUNCTION.
PubMed=16478994; DOI=10.1128/MCB.26.5.1731-1742.2006;
Bachand F., Lackner D.H., Baehler J., Silver P.A.;
"Autoregulation of ribosome biosynthesis by a translational response
in fission yeast.";
Mol. Cell. Biol. 26:1731-1742(2006).
-!- FUNCTION: Methylates (mono and asymmetric dimethylation) the
guanidino nitrogens of arginyl residues in ribosomal protein rps2.
{ECO:0000269|PubMed:15175657, ECO:0000269|PubMed:16478994}.
-!- SUBUNIT: Interacts with ef1a-c, rps2 and rps24. Note=Associates
with the 40S ribosomal particle. {ECO:0000269|PubMed:15175657}.
-!- INTERACTION:
O74892:rps2; NbExp=2; IntAct=EBI-367706, EBI-367715;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15175657}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. Protein arginine N-
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU01015}.
-!- SEQUENCE CAUTION:
Sequence=BAA21436.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AB004538; BAA21436.1; ALT_SEQ; Genomic_DNA.
EMBL; CU329671; CAA17825.2; -; Genomic_DNA.
PIR; T40755; T40755.
RefSeq; NP_595572.1; NM_001021467.2.
ProteinModelPortal; O13648; -.
SMR; O13648; -.
BioGrid; 277762; 21.
IntAct; O13648; 3.
MINT; MINT-4666941; -.
STRING; 4896.SPBC8D2.10c.1; -.
iPTMnet; O13648; -.
MaxQB; O13648; -.
PRIDE; O13648; -.
EnsemblFungi; SPBC8D2.10c.1; SPBC8D2.10c.1:pep; SPBC8D2.10c.
GeneID; 2541248; -.
KEGG; spo:SPBC8D2.10c; -.
EuPathDB; FungiDB:SPBC8D2.10c; -.
PomBase; SPBC8D2.10c; rmt3.
HOGENOM; HOG000198521; -.
InParanoid; O13648; -.
KO; K11436; -.
OMA; ITKTSMC; -.
OrthoDB; EOG092C393Q; -.
PhylomeDB; O13648; -.
Reactome; R-SPO-3214858; RMTs methylate histone arginines.
Reactome; R-SPO-8876725; Protein methylation.
PRO; PR:O13648; -.
Proteomes; UP000002485; Chromosome II.
GO; GO:0005737; C:cytoplasm; IDA:PomBase.
GO; GO:0005829; C:cytosol; IDA:PomBase.
GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008168; F:methyltransferase activity; IDA:PomBase.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IMP:PomBase.
GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IBA:GO_Central.
GO; GO:0043022; F:ribosome binding; IDA:PomBase.
GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; IPI:PomBase.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
GO; GO:0042254; P:ribosome biogenesis; IMP:PomBase.
InterPro; IPR025799; Arg_MeTrfase.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF57667; SSF57667; 1.
PROSITE; PS51678; SAM_MT_PRMT; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Metal-binding; Methyltransferase;
Reference proteome; Ribonucleoprotein; Ribosomal protein;
S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
CHAIN 1 543 Ribosomal protein arginine N-
methyltransferase rmt3.
/FTId=PRO_0000351450.
DOMAIN 217 543 SAM-dependent MTase PRMT-type.
{ECO:0000255|PROSITE-ProRule:PRU01015}.
ZN_FING 58 81 C2H2-type.
BINDING 230 230 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 239 239 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 263 263 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250}.
BINDING 285 285 S-adenosyl-L-methionine. {ECO:0000250}.
BINDING 314 314 S-adenosyl-L-methionine. {ECO:0000250}.
SEQUENCE 543 AA; 61761 MW; 6E60B9F6813D6873 CRC64;
MLVKPMACYF EIWTRKVTTI EDFSLAIANR FKQMGSHSDS EVDWDNEEEV WEDEVHEFCC
LFCDSTFTCL KDLWSHCKEA HNFDFYQVKQ QNNLDFYACI KLVNYIRSQV KEGKTPDLDK
LSDILRSDEY MISVLPDDSV LFSLGDELDS DFEDDNTLEI EVENPADVSK DAEIKKLKLQ
NQLLISQLEE IRKDKMNELT SQTTDQLSVT PKKADNDSYY FESYAGNDIH FLMLNDSVRT
EGYRDFVYHN KHIFAGKTVL DVGCGTGILS MFCAKAGAKK VYAVDNSDII QMAISNAFEN
GLADQITFIR GKIEDISLPV GKVDIIISEW MGYALTFESM IDSVLVARDR FLAPSGIMAP
SETRLVLTAT TNTELLEEPI DFWSDVYGFK MNGMKDASYK GVSVQVVPQT YVNAKPVVFA
RFNMHTCKVQ DVSFTSPFSL IIDNEGPLCA FTLWFDTYFT TKRTQPIPEA IDEACGFTTG
PQGTPTHWKQ CVLLLRNRPF LQKGTRVEGT ISFSKNKKNN RDLDISVHWN VNGKADSQSY
VLN


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