ID A0A151JN23_9HYME Unreviewed; 621 AA.
AC A0A151JN23;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR015894};
GN ORFNames=ALC57_02739 {ECO:0000313|EMBL:KYN27875.1};
OS Trachymyrmex cornetzi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN27875.1, ECO:0000313|Proteomes:UP000078492};
RN [1] {ECO:0000313|EMBL:KYN27875.1, ECO:0000313|Proteomes:UP000078492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN27875.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN27875.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex cornetzi WGS genome.";
RL Submitted (SEP-2015) 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; KQ978878; KYN27875.1; -; Genomic_DNA.
DR RefSeq; XP_018378118.1; XM_018522616.1.
DR AlphaFoldDB; A0A151JN23; -.
DR STRING; 471704.A0A151JN23; -.
DR GeneID; 108770877; -.
DR OrthoDB; 5489665at2759; -.
DR Proteomes; UP000078492; 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 CDD; cd02440; AdoMet_MTases; 1.
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:UP000078492};
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 30..273
FT /note="PRMT5 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF17285"
FT DOMAIN 282..448
FT /note="PRMT5 arginine-N-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05185"
FT DOMAIN 451..619
FT /note="PRMT5 oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF17286"
FT ACT_SITE 419
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT ACT_SITE 428
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT BINDING 309
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 318..319
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 376
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT BINDING 403..404
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-2"
FT SITE 312
FT /note="Critical for specifying symmetric addition of methyl
FT groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-3"
SQ SEQUENCE 621 AA; 71572 MW; A5D1A7EDA348B00C CRC64;
MTNQRLSCGL DLCCAVNLND CLIYASESRY EFICISLVHP LFKREFISGP AKNRPGPLTR
PDLVLNSSDW NNRIIAKFSS LINVDSTNPI IRKNSEETLN QELGLASHFG LSGVTLKLKY
GINKNVNLAR IISDKISNNN CTFQVWIQVP MENPIRQTYS YRTEDYSEDE NPWEWWNSFR
VICDYNKKLG VSLIVSHDLP EEEEIDRWLG EPVRCLILPT TLFLTNKKGY PVLSKAHQAL
VKRFAMQDVQ FILTGASRYQ SVSYYHNYLD YLWKGCQNDG TVEKFARGYE DYLQCPLQPL
MDNLESQTYE IFEKDPVKYR EYQSAIYEAI NAMVYKMQEE RTIVIMVVGA GRGPLVTASL
NAAKMAYREV KVYAVEKNPN AIITLQALQR DMWKEKVTVI SCDMREWNPP EKADIIVSEL
LGSFGDNELS PECLDNVLKF LRDDGINIPQ SYTSFIAPMQ SSKLYNEVRQ LRDKDKHPLA
HFETLYVVHL QNKYDIANPK PLFTFKHPNT DALADNSRYE IKTFQVEQNC VLHGFSGYFT
AVLYENITLS IEPSTYSSDM FSWFPIFFPL KEPVQLKAGD EIVVHFWRRC GSKKVWYEWC
LSKPIPVSIH NTTGRSSVIG L
//
