RMT2_ASPOR
ID RMT2_ASPOR Reviewed; 413 AA.
AC Q2TZM9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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}; ORFNames=AO090011000791;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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}.
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DR EMBL; AP007171; BAE65236.1; -; Genomic_DNA.
DR RefSeq; XP_001826369.1; XM_001826317.2.
DR AlphaFoldDB; Q2TZM9; -.
DR SMR; Q2TZM9; -.
DR STRING; 510516.Q2TZM9; -.
DR EnsemblFungi; BAE65236; BAE65236; AO090011000791.
DR GeneID; 5998472; -.
DR KEGG; aor:AO090011000791; -.
DR VEuPathDB; FungiDB:AO090011000791; -.
DR HOGENOM; CLU_033831_0_0_1; -.
DR OMA; YWVVDNY; -.
DR Proteomes; UP000006564; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019702; F:protein-arginine N5-methyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IEA:EnsemblFungi.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
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; PS51559; SAM_RMT2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..413
FT /note="Protein arginine N-methyltransferase 2"
FT /id="PRO_0000228971"
FT DOMAIN 192..413
FT /note="RMT2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT REGION 65..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..169
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 201
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 250..255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 271..273
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 298..299
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 318
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
SQ SEQUENCE 413 AA; 46476 MW; D51E31AD1BFEF42F CRC64;
MTDPTTEIDV DLDVQEILLA ASQHDIPKLR QLIRSNQTIA NPVNVKDPET GYAPLHAAIA
ACEPDDEEPN GVQTNGEQGD EQKSVEEKGS ATVRFLLQEG AIWNDLDNNN ETPGCVARRL
GLTELYEQLV DAGVRAELLL NRLDGYEELE DDDEEEEEGQ EEQTGTEEVE VEGESAPQLV
EATTTTETAM ETGPDVTNSR YLDSNLTFQN DRLLDQDQNG VMMAWETDIM AKSAKKLLPT
SGLRVLNVGH GMGIVDGFIQ EQSPAEHHII EAHPEVVAEM KRKGWGEKPG VTIHEGRWQD
ILPDLVGQGV MFDAIYYDTF AESYGDFREF FSEQVIGLLE QEGKWSFFNG MGADRQISYD
VYQKVAEMDL MDAGFDVEWE EIALPKLDNE WDGVRRAYWQ IESYRLPLCK YMD
