ANM3_SCHPO
ID ANM3_SCHPO Reviewed; 543 AA.
AC O13648; Q7LWE1;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ribosomal protein arginine N-methyltransferase rmt3;
DE EC=2.1.1.-;
GN Name=rmt3; Synonyms=prmt3; ORFNames=SPBC8D2.10c;
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 [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=10620777;
RX DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT yeast chromosome II: sequence analysis and characterization of the genomic
RT DNA and cDNAs encoded on the segment.";
RL Yeast 16:71-80(2000).
RN [2]
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EF1A-C; RPS2 AND RPS24,
RP AND ASSOCIATION WITH THE 40S RIBOSOMAL PARTICLE.
RX PubMed=15175657; DOI=10.1038/sj.emboj.7600265;
RA Bachand F., Silver P.A.;
RT "PRMT3 is a ribosomal protein methyltransferase that affects the cellular
RT levels of ribosomal subunits.";
RL EMBO J. 23:2641-2650(2004).
RN [4]
RP FUNCTION.
RX PubMed=16478994; DOI=10.1128/mcb.26.5.1731-1742.2006;
RA Bachand F., Lackner D.H., Baehler J., Silver P.A.;
RT "Autoregulation of ribosome biosynthesis by a translational response in
RT fission yeast.";
RL Mol. Cell. Biol. 26:1731-1742(2006).
CC -!- FUNCTION: Methylates (mono and asymmetric dimethylation) the guanidino
CC nitrogens of arginyl residues in ribosomal protein rps2.
CC {ECO:0000269|PubMed:15175657, ECO:0000269|PubMed:16478994}.
CC -!- SUBUNIT: Interacts with ef1a-c, rps2 and rps24. Note=Associates with
CC the 40S ribosomal particle. {ECO:0000269|PubMed:15175657}.
CC -!- INTERACTION:
CC O13648; O74892: rps2; NbExp=2; IntAct=EBI-367706, EBI-367715;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15175657}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA21436.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB004538; BAA21436.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CU329671; CAA17825.2; -; Genomic_DNA.
DR PIR; T40755; T40755.
DR RefSeq; NP_595572.1; NM_001021467.2.
DR AlphaFoldDB; O13648; -.
DR SMR; O13648; -.
DR BioGRID; 277762; 236.
DR IntAct; O13648; 3.
DR STRING; 4896.SPBC8D2.10c.1; -.
DR iPTMnet; O13648; -.
DR MaxQB; O13648; -.
DR PaxDb; O13648; -.
DR PRIDE; O13648; -.
DR EnsemblFungi; SPBC8D2.10c.1; SPBC8D2.10c.1:pep; SPBC8D2.10c.
DR GeneID; 2541248; -.
DR KEGG; spo:SPBC8D2.10c; -.
DR PomBase; SPBC8D2.10c; rmt3.
DR VEuPathDB; FungiDB:SPBC8D2.10c; -.
DR eggNOG; KOG1499; Eukaryota.
DR HOGENOM; CLU_017375_6_0_1; -.
DR InParanoid; O13648; -.
DR OMA; EWIADST; -.
DR PhylomeDB; O13648; -.
DR Reactome; R-SPO-3214858; RMTs methylate histone arginines.
DR Reactome; R-SPO-8876725; Protein methylation.
DR PRO; PR:O13648; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IMP:PomBase.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; EXP:PomBase.
DR GO; GO:0043022; F:ribosome binding; IDA:PomBase.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:PomBase.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Methyltransferase; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; S-adenosyl-L-methionine; Transferase;
KW Zinc; Zinc-finger.
FT CHAIN 1..543
FT /note="Ribosomal protein arginine N-methyltransferase rmt3"
FT /id="PRO_0000351450"
FT DOMAIN 217..543
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ZN_FING 58..81
FT /note="C2H2-type"
FT BINDING 230
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ 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
