ID A1DE29_NEOFI Unreviewed; 864 AA.
AC A1DE29;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR015894};
GN ORFNames=NFIA_075660 {ECO:0000313|EMBL:EAW17636.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW17636.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000256|PIRNR:PIRNR015894}.
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DR EMBL; DS027696; EAW17636.1; -; Genomic_DNA.
DR RefSeq; XP_001259533.1; XM_001259532.1.
DR AlphaFoldDB; A1DE29; -.
DR STRING; 331117.A1DE29; -.
DR EnsemblFungi; EAW17636; EAW17636; NFIA_075660.
DR GeneID; 4586253; -.
DR KEGG; nfi:NFIA_075660; -.
DR VEuPathDB; FungiDB:NFIA_075660; -.
DR eggNOG; KOG0822; Eukaryota.
DR HOGENOM; CLU_010247_2_1_1; -.
DR OMA; WEFSHPI; -.
DR OrthoDB; 5489665at2759; -.
DR Proteomes; UP000006702; Unassembled 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:UP000006702};
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 35..363
FT /note="PRMT5 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF17285"
FT DOMAIN 372..593
FT /note="PRMT5 arginine-N-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05185"
FT DOMAIN 596..857
FT /note="PRMT5 oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF17286"
FT REGION 819..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 563
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT ACT_SITE 572
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT BINDING 398
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 407..408
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 469
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 496..497
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT SITE 401
FT /note="Critical for specifying symmetric addition of methyl
FT groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ SEQUENCE 864 AA; 94920 MW; 721C5DB2901A19D5 CRC64;
MDSEDLAPAF CVGQHESNRT IPITTQIVQS AHESNYDMLT TPITTPHFHS RVLSLLSGHL
SKLQAVSPDP NGTLATTENT RPVVIPPLGP SDTHLTPNQT MSQLMGVTSP WIDLCSPDPL
IADISRQVLM LEVAYAAFCG IGYLLVPGPK LHHGNMHSEG LVFYARAVQD AINLGPYIQF
HIWLRIVDNP DLEVDSMGDL APLARDEFLW GSDDGQSLKV DLFGTWDAWD VIRRTCKYHT
RLFVALSLPK QLPPMSVQSR WHSEPVHLLT MDANTFIKNQ KGYPVLSKAH QALISKFMRL
RTPPWILLCD VGPIPGVEAP EASEATQLNL SSSEYPSLSQ AAVSSKKFID PTPHLSYIRN
LQQRQPPRSA IERFGVGYQD YLQAPLQPLT VNLESITYEV FEKDPIKYEW YERAIAKALS
DWAEQKKPTS NPDGRVVLAV VGAGRGPLVT RAIRASAETG VDIDLWVVEK NPNAFVLLQR
HNEELWGGKA TLVQSDMRSW KGPQRAKDSG LPLATVGQSL GIEDSLLYKP EPDQKGNMPA
PESVKSMASS DLSSGQIDIV VSELLGSFGD NELSPECLDG ITHLLNPVHG ISIPASYTAH
LTPISAPKLH ADVVNQSISN PAAPETPYVV MLHAIDFLST NQPPAGTTSG DSGNSYISHT
RSSISTIPVP ESTTPYVQTA WSFSHPNRDI PPQSPFTSII SNSHNVRRTR LAFPTQNRGV
CHGLAGYFET VLYRDVELST NPVTMDSKSA NMISWFPIYF PLKTPLNVPD NGEIVVTMTR
QTDDRKVWYE WMVEVFSLER IADAPAIELP VMSGARAVSP AADGASGKDN GTDKPQKAGK
HSGFRRVRVG MSDLHSSIKE GCLM
//
