ID C1GUS9_PARBA Unreviewed; 836 AA.
AC C1GUS9;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 2.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR015894};
GN ORFNames=PAAG_02402 {ECO:0000313|EMBL:EEH40347.2};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH40347.2, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH40347.2, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000256|PIRNR:PIRNR015894}.
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DR EMBL; KN293996; EEH40347.2; -; Genomic_DNA.
DR RefSeq; XP_015701678.1; XM_015844630.1.
DR AlphaFoldDB; C1GUS9; -.
DR STRING; 502779.C1GUS9; -.
DR GeneID; 9099059; -.
DR KEGG; pbl:PAAG_02402; -.
DR VEuPathDB; FungiDB:PAAG_02402; -.
DR eggNOG; KOG0822; Eukaryota.
DR HOGENOM; CLU_010247_2_1_1; -.
DR OMA; WEFSHPI; -.
DR OrthoDB; 5489665at2759; -.
DR Proteomes; UP000002059; Partially assembled WGS sequence.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR007857; Arg_MeTrfase_PRMT5.
DR InterPro; IPR035075; PRMT5.
DR InterPro; IPR035248; PRMT5_C.
DR InterPro; IPR035247; PRMT5_TIM.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10738; PROTEIN ARGININE N-METHYLTRANSFERASE 5; 1.
DR PANTHER; PTHR10738:SF0; PROTEIN ARGININE N-METHYLTRANSFERASE 5; 1.
DR Pfam; PF05185; PRMT5; 1.
DR Pfam; PF17286; PRMT5_C; 1.
DR Pfam; PF17285; PRMT5_TIM; 1.
DR PIRSF; PIRSF015894; Skb1_MeTrfase; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR015894};
KW Reference proteome {ECO:0000313|Proteomes:UP000002059};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR015894};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR015894}.
FT DOMAIN 36..376
FT /note="PRMT5 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF17285"
FT DOMAIN 383..571
FT /note="PRMT5 arginine-N-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05185"
FT DOMAIN 574..829
FT /note="PRMT5 oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF17286"
FT REGION 319..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 541
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT ACT_SITE 550
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT BINDING 410
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 419..420
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 481
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 508..509
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT SITE 413
FT /note="Critical for specifying symmetric addition of methyl
FT groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ SEQUENCE 836 AA; 92071 MW; B680821C43128937 CRC64;
MEGDEDWAPT FCIGQHETRR TVPVSPQLVQ LAQEGDYDML TTPITTPLFH SRVLTLLSTH
LSDSKPPVYD ATITLGTSHN THPVTVPPLS PDDTFLTPNE CTSQLVGITS PWIDLCSPDP
LIADISRQVL DLEVAYAAFC GVSFIIVPGP RLCHGNLHGE GLIYFGRAIQ DILNVGLYIQ
VHIWFNMIDT SELETNDVGD LAPFARAEYL TPAIGPSLKV DLFGTWEAWD VIRKLCKYQS
RLFVALSLPK QLPPMSVQLR WQSEPVHILT IAGSSFIKNQ KGYPVLSKAH QALIARMMRL
RNPPWIILCD VGPIAGYEVS QSGSETDPTP KISPESDSNS AAPTPAETHR QFKSGSNKKN
FDPTPHLSYI RNLQQKQPGR TPMERFGVGY QDYLQAPLQP LTVNLESITY EVFEKDPIKY
EWYERAIAKA LKDWAAQGKP TCHPEGHVVL AVVGAGRGPL VTRAIRASVE AGVVIEVWAV
EKNPNAYVLL QRHNASLWGG CVNLVKSDMR SWKGPHRLAP ESGSGEEQKI IHTPIDILVS
ELLGSFGDNE LSPECLDGVT HLLNPVHGIS IPASYSAHLS PISSPRLHAD IAAQSITNPA
APETPYVVML HAFDFLSTIQ PSTPAPIATA GRQSDKSPSP PANDPSTPII QSAWSFSHPN
HNIPPHSSTS STILNSHNVR RTRLAFPCQK RGTCHGLAGY FETVLYDDVE LSTNPVTMDE
KSPGMISWFP IYFPLKTPLI VPPNSEIIVT MYRQTDNRKV WYEWIVEVFA WDTSLATTAA
DITNVALSPP SKSSSLLEAK DNENRRDSVA APVSPMKRVR VAMSELHSSI KDGCLM
//
