RMT2_DEBHA
ID RMT2_DEBHA Reviewed; 434 AA.
AC Q6BNS9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=DEHA2E19228g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
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DR EMBL; CR382137; CAG88414.1; -; Genomic_DNA.
DR RefSeq; XP_460141.1; XM_460141.1.
DR AlphaFoldDB; Q6BNS9; -.
DR SMR; Q6BNS9; -.
DR STRING; 4959.XP_460141.1; -.
DR EnsemblFungi; CAG88414; CAG88414; DEHA2E19228g.
DR GeneID; 2902891; -.
DR KEGG; dha:DEHA2E19228g; -.
DR VEuPathDB; FungiDB:DEHA2E19228g; -.
DR eggNOG; KOG1709; Eukaryota.
DR HOGENOM; CLU_033831_0_0_1; -.
DR InParanoid; Q6BNS9; -.
DR OMA; YWVVDNY; -.
DR OrthoDB; 1297303at2759; -.
DR Proteomes; UP000000599; Chromosome E.
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; 3.40.50.150; -; 1.
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; SSF53335; SSF53335; 1.
DR PROSITE; PS51559; SAM_RMT2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..434
FT /note="Protein arginine N-methyltransferase 2"
FT /id="PRO_0000228974"
FT DOMAIN 193..434
FT /note="RMT2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT REGION 155..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 200
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 230
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 258..263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 279..281
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 306..307
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 327
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
SQ SEQUENCE 434 AA; 50020 MW; FAB25B428C9824A5 CRC64;
MSDLHELCGF QTRPIGPKYI EDLKFYLKNG IPATYTIEEA YNYTNNIEEE PTTTTTPLHI
ICSHIPNDAS NDEIDIINQM VEILLEYGAG WCLTDINDDT PGCILIRRKL NNTPIYNQVV
AAGVRAELLL RKVSEYDMEI IEDTDDLNHE QFEGIQGEET TEEERKEEEP SNTSDIIDEQ
KVEQPKEDLK EDPSSNQETY LKTKLEYKDG ALVTKDRKDG VMMSWETDLM RMGCDSLFKG
ASIDGEIDDE VNILNIGFGM GIIDTMINNK NPTKQYICEA HPDVLAKLRL DGWYEKQNVV
ILEGRWQEQL NKLLSEGNVF FNGIYYDTYS EHYEDMLELF DIVVGILKPH GVFSFFNGLG
ADRQVVYEVY KQLVEMDLAN YGLICKFEQI EVPESTLQLE VQNSTDNKSV WDDIKRAYWT
CPTYYHPEAR FMDV
