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RMT2_EMENI
ID   RMT2_EMENI              Reviewed;         426 AA.
AC   Q5B058; C8V2T0;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, 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=AN6072;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000104; EAA58047.1; -; Genomic_DNA.
DR   EMBL; BN001301; CBF70243.1; -; Genomic_DNA.
DR   RefSeq; XP_663676.1; XM_658584.1.
DR   AlphaFoldDB; Q5B058; -.
DR   SMR; Q5B058; -.
DR   STRING; 162425.CADANIAP00006945; -.
DR   EnsemblFungi; CBF70243; CBF70243; ANIA_06072.
DR   EnsemblFungi; EAA58047; EAA58047; AN6072.2.
DR   GeneID; 2871023; -.
DR   KEGG; ani:AN6072.2; -.
DR   VEuPathDB; FungiDB:AN6072; -.
DR   eggNOG; KOG1709; Eukaryota.
DR   HOGENOM; CLU_033831_0_0_1; -.
DR   InParanoid; Q5B058; -.
DR   OMA; YWVVDNY; -.
DR   OrthoDB; 1297303at2759; -.
DR   Proteomes; UP000000560; Chromosome I.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0019702; F:protein-arginine N5-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0018216; P:peptidyl-arginine methylation; IBA:GO_Central.
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..426
FT                   /note="Protein arginine N-methyltransferase 2"
FT                   /id="PRO_0000228975"
FT   DOMAIN          207..426
FT                   /note="RMT2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT   REGION          65..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          155..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         214
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT   BINDING         243
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT   BINDING         263..268
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT   BINDING         284..286
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT   BINDING         311..312
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT   BINDING         331
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
SQ   SEQUENCE   426 AA;  47392 MW;  ECDE41561E5BB01A CRC64;
     MANPVTEIDV DLNTQEVLLA ASQHDTAKLR RLLRANDAAG NPANVKDPET GYSPLHAAIA
     ACEPDEEEDV KSNGVQTNGD RQTHGQESTV EAAVQTVKLL LQEGAIWNDL DLNNETPGCI
     ARRLGLTELY DMVVDAGVRA ELLLNRLDGY EQLSDEEMEE DGEQEQEQQD AAVAADASIT
     NTAEDESVPQ LVDTTAAAPP QTADAEPSVT SSRYLNSDLT FQQDRLLDQD QNGVMMAWES
     DIMAKSAKQL LPTPGLRVLN VGHGMGIVDG FIQEQSPSAH HIIEAHPAVV AEMKRKGWHE
     KPGVVIHEGK WQDILPGLVA EGVMFDAIYY DTFAESYADF REFFTEQVIG VLEQEGKWSF
     FNGMGADRQI SYDVYQKVVE MDLFEAGFDV EWEEIDVPKL EGEWNGVRRP YWSIDKYRLP
     LCKYMD
 
 
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