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Database: UniProt
Entry: A0A0R3WDT9_TAEAS
LinkDB: A0A0R3WDT9_TAEAS
Original site: A0A0R3WDT9_TAEAS 
ID   A0A0R3WDT9_TAEAS        Unreviewed;       657 AA.
AC   A0A0R3WDT9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR015894};
GN   ORFNames=TASK_LOCUS8945 {ECO:0000313|EMBL:VDK41349.1};
OS   Taenia asiatica (Asian tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX   NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000894401-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TASK_0000894401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK41349.1, ECO:0000313|Proteomes:UP000282613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. {ECO:0000256|PIRNR:PIRNR015894}.
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DR   EMBL; UYRS01018936; VDK41349.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R3WDT9; -.
DR   STRING; 60517.A0A0R3WDT9; -.
DR   WBParaSite; TASK_0000894401-mRNA-1; TASK_0000894401-mRNA-1; TASK_0000894401.
DR   Proteomes; UP000046400; Unplaced.
DR   Proteomes; UP000282613; 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; 1.
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:UP000282613};
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          67..249
FT                   /note="PRMT5 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF17285"
FT   DOMAIN          261..461
FT                   /note="PRMT5 arginine-N-methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF05185"
FT   DOMAIN          473..655
FT                   /note="PRMT5 oligomerisation"
FT                   /evidence="ECO:0000259|Pfam:PF17286"
FT   ACT_SITE        436
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT   ACT_SITE        445
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT   BINDING         287
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         296..297
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         390
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   BINDING         418..419
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT   SITE            290
FT                   /note="Critical for specifying symmetric addition of methyl
FT                   groups"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ   SEQUENCE   657 AA;  74015 MW;  6157D452FFCD2379 CRC64;
     MMNSNLVGLR IETFDDVRKH FQIARNEGFA FIGIDLFPVL HLCPQSPHDV DEMLPLVRSG
     DVYPKKDCDS KDIRVSCISE HCLRKELSWA VHLALPAIEV PLRHDNNVKL AQLLTAFIKS
     EVASIKIWIS VPMYTEGDVG QDASSPWHWW SQLVGLAGPA ACESLGLLLE VPTDLPEEDV
     VSRWLSEPVS CLALSTHLFI TNSKGFPILS RAHQHVLRQF LKINSQVLIM GPSHHERGPS
     IYRQYISWIW KCTVEAKSLY EKHSMGFEDQ LQEPLQPLQD NLSSATYGVF EMDPYKYKAY
     EEAICLALVH RCTSRKVVES YQSPLPEVDS KGDSSVKQAM LYPVYSKVVS LDISTNIVIY
     ILGAGQGPFV DASLQASRRS GCPVRVYVIE KNSNALLTLK HRMQTDWSGE DVHLVPGDMR
     CLSIPPPEKA DIFVSELLGS FGDNELSPEC LDGAQYLLKG ESLRYDGISI PASYTSYVAP
     LQSLRIYIDT SRCMENLKFQ ERIQRHSETP YVIRLSNCQI LAAPEEAFTF KHPRKGGPLS
     PVGYQDIDTT PNARYCRLTF VPRGDGVVHG FAGYFEAVLY DKITLSTHPQ RHSPNMFSWF
     PMVFPLVSAM PVKAGQRITF HLWRCISPRH VWYEWATTEP TVSKIHNSAG SAYKIGL
//
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