ID A0A267GD22_9PLAT Unreviewed; 703 AA.
AC A0A267GD22;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR015894};
GN ORFNames=BOX15_Mlig014197g2 {ECO:0000313|EMBL:PAA83913.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA83913.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA83913.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA83913.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA83913.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000256|PIRNR:PIRNR015894}.
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:PAA83913.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NIVC01000396; PAA83913.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267GD22; -.
DR STRING; 282301.A0A267GD22; -.
DR Proteomes; UP000215902; 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:UP000215902};
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 90..349
FT /note="PRMT5 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF17285"
FT DOMAIN 360..524
FT /note="PRMT5 arginine-N-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05185"
FT DOMAIN 527..700
FT /note="PRMT5 oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF17286"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 495
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT ACT_SITE 504
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT BINDING 383
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 392..393
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 451
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 478..479
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT SITE 386
FT /note="Critical for specifying symmetric addition of methyl
FT groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ SEQUENCE 703 AA; 77659 MW; 882539AE17123177 CRC64;
MSSSEKRDCN GADKEEPMES ASGSATAAAE AVAVEPAKED SAADAGKSSG YSGGNRSKRG
GGNSGRALCG IDLAFCSDQK AGMLEAHSLG YAFVCLPLFH PRNVVRTGAD VGGHADQEEE
EGQRHRQLDQ LRLLPATRPD HLVIDSEDWT RFVVGKISAW IRCDSSWEAE RLQSLAALRQ
ELSWAAHIGL VACLIDLPDG GRVSNLARAL LAFHRAERSA PLMWVRVPMA AEQVGDDGDI
ASNDPWLWWH RLCRLCDLIL GQLGVALEVT ADLPGPAAVQ RWLAEPVKAL VLPTSLFLTN
QSGYPVLSKA HQALLMKFFR LQLQVIITGS CRHDKGIEYY QQYINWLYSR RSTDLYSSQG
KGYEDTLQDP LQPLADNLHS ATYQVFEMDP YKYRAYREAV RQALVEMVPD SEAESRLITI
AVLGAGRGPL VQECLIAGRQ SGRRIRVFAV EKNGNAVNTL LNRSLSEWPD SVVVLPTDMR
QLKPTDLQAD IFVSELLGSF GDNELSPECL DGAMHCLAEG GVSIPMSYTS YLAPMHSSTV
YKEVTRQRDP EKPYYTFLET PYVVNLVNSE LLAPPQPVFT FRHPAESAGP DGRPASNERY
IELTYRAERT GVLHGFAGYF DSRLYGSVSM SILPEDHSPD LFSWFPLVFP LHYPVPVKCG
DAITVAMWRV VSATAVWYEW ALLAPVVLPI HNAGGRSFTI NLY
//
