RMT2_CRYNB
ID RMT2_CRYNB Reviewed; 363 AA.
AC P0CQ69; Q55ZU0; Q5KP51;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Protein arginine N-methyltransferase 2 {ECO:0000250|UniProtKB:Q03305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q03305};
DE AltName: Full=Protein-arginine N5-methyltransferase {ECO:0000250|UniProtKB:Q03305};
DE AltName: Full=Type IV protein arginine N-methyltransferase {ECO:0000250|UniProtKB:Q03305};
DE Short=Type IV PRMT {ECO:0000250|UniProtKB:Q03305};
GN Name=RMT2 {ECO:0000250|UniProtKB:Q03305}; OrderedLocusNames=CNBA4000;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-arginine N-
CC methyltransferase that methylates the delta-nitrogen atom of arginine
CC residues to form N5-methylarginine (type IV) in target proteins.
CC Monomethylates ribosomal protein L12. {ECO:0000250|UniProtKB:Q03305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q03305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q03305}. Nucleus
CC {ECO:0000250|UniProtKB:Q03305}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RMT2 methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00892}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL23284.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAEY01000002; EAL23284.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_777931.1; XM_772838.1.
DR AlphaFoldDB; P0CQ69; -.
DR SMR; P0CQ69; -.
DR EnsemblFungi; EAL23284; EAL23284; CNBA4000.
DR GeneID; 4933659; -.
DR KEGG; cnb:CNBA4000; -.
DR HOGENOM; CLU_033831_1_0_1; -.
DR Proteomes; UP000001435; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017408; Arginine_N-MeTrfase_2.
DR InterPro; IPR026480; RMT2_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PIRSF; PIRSF038148; Arginine_N-mtfrase-2; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51559; SAM_RMT2; 1.
PE 3: Inferred from homology;
KW ANK repeat; Cytoplasm; Methyltransferase; Nucleus; Repeat;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..363
FT /note="Protein arginine N-methyltransferase 2"
FT /id="PRO_0000410245"
FT REPEAT 22..46
FT /note="ANK 1"
FT REPEAT 48..80
FT /note="ANK 2"
FT DOMAIN 111..363
FT /note="RMT2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 186..191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 209..211
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 236..237
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 265
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
SQ SEQUENCE 363 AA; 40439 MW; 23A0519EA8A9E22D CRC64;
MDMDSAHLDS SLLTLAFRLI KAAQTAAPSV LADLLAEGAP AWFQDDDLGW SCLHYAAERK
EPECLEVLLQ GGAVWNAVDK WGRTAGEICL SLGDEEGWSI IRNEGIRSED KTSAGDNLVF
LKSKLTWDVG KDGKERVLDA DGNGVMMGWE EPLSYCIVVE HVKRLTEEHP KAELGAEGMS
ILNVGFGLGI VDRLFQECDP KPSHHTIIEA HPQVLEYIHK KGVHLLPNVR ILQGRWQDWL
LDGEKVGDVL SGTPDGMGFD AIFVDTFAEG YEDLKAFFEV IPDILNADNG RFSFWNGLGA
TNPTIYAVSS SLAELHLEDV GLQVEWHDVL IPESMREEVW KGVRRRYWDL PGYRLPIAKM
SLI
