ID D6RLK0_COPC7 Unreviewed; 393 AA.
AC D6RLK0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Arginine N-methyltransferase 2 {ECO:0000256|PIRNR:PIRNR038148};
DE EC=2.1.1.- {ECO:0000256|PIRNR:PIRNR038148};
GN ORFNames=CC1G_14139 {ECO:0000313|EMBL:EFI28112.1};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EFI28112.1, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EFI28112.1, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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:0000256|ARBA:ARBA00002207,
CC ECO:0000256|PIRNR:PIRNR038148}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC ECO:0000256|PIRNR:PIRNR038148}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR038148}.
CC Nucleus {ECO:0000256|PIRNR:PIRNR038148}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RMT2 methyltransferase family.
CC {ECO:0000256|PIRNR:PIRNR038148}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFI28112.1}.
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DR EMBL; AACS02000003; EFI28112.1; -; Genomic_DNA.
DR RefSeq; XP_002911606.1; XM_002911560.1.
DR AlphaFoldDB; D6RLK0; -.
DR STRING; 240176.D6RLK0; -.
DR GeneID; 9379631; -.
DR KEGG; cci:CC1G_14139; -.
DR VEuPathDB; FungiDB:CC1G_14139; -.
DR eggNOG; KOG1709; Eukaryota.
DR HOGENOM; CLU_033831_1_0_1; -.
DR InParanoid; D6RLK0; -.
DR OMA; YWVVDNY; -.
DR OrthoDB; 36729at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
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 GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 PANTHER; PTHR32379; GUANIDINOACETATE N-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR32379:SF1; GUANIDINOACETATE N-METHYLTRANSFERASE; 1.
DR Pfam; PF13637; Ank_4; 1.
DR PIRSF; PIRSF038148; Arginine_N-mtfrase-2; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR038148};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR038148}; Nucleus {ECO:0000256|PIRNR:PIRNR038148};
KW Reference proteome {ECO:0000313|Proteomes:UP000001861};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR038148}.
FT REPEAT 59..91
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 154..393
FT /note="RMT2"
FT /evidence="ECO:0000259|PROSITE:PS51559"
SQ SEQUENCE 393 AA; 43766 MW; EE93C297BB552B07 CRC64;
MTTETQASPE IIEVDIDAED SATIFGEHLV NSILEHEPLD TIKQILESGA PVWYSSQAEG
TSALHAAAYT RNPELARILI EKGAIWNAVD HLGITAGEIA LSQNDTETYT IIRDAGIRAE
LLLNLLSSKA LKAGKTTDAN QLEADNLLLR EEDLTAAGST ETFLSSKLTY SVDKYGQKVC
TVQAGDDEVG VMMGWEKGIM EETVKKLCDG HPNSKELRVL NVGFGLGIID ELFQSLPTRP
EHHVIIEPHP DVLKHMKETG WYEKPGVKIL EGKWQDYIES EELLAFGGFD VVYTDTFSED
YATLRLFFEH LPNILAGPES RFSFFHGLGA TNALFYDVYT HISEMHLLEV GLKVEWSDVD
VVGDEEEDRW GESREYFKVP LYRLPVASMA PVS
//
