ID A0A195BMI1_9HYME Unreviewed; 700 AA.
AC A0A195BMI1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR015894};
GN ORFNames=ALC53_03702 {ECO:0000313|EMBL:KYM87085.1};
OS Atta colombica.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=520822 {ECO:0000313|EMBL:KYM87085.1, ECO:0000313|Proteomes:UP000078540};
RN [1] {ECO:0000313|EMBL:KYM87085.1, ECO:0000313|Proteomes:UP000078540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Treedump-2 {ECO:0000313|EMBL:KYM87085.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYM87085.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Atta colombica 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; KQ976435; KYM87085.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195BMI1; -.
DR STRING; 520822.A0A195BMI1; -.
DR Proteomes; UP000078540; 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; 2.
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:UP000078540};
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..384
FT /note="PRMT5 arginine-N-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05185"
FT DOMAIN 411..476
FT /note="PRMT5 arginine-N-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF05185"
FT DOMAIN 479..647
FT /note="PRMT5 oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF17286"
FT ACT_SITE 447
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015894-1"
FT ACT_SITE 456
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 431..432
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 700 AA; 81165 MW; 816C0A0D3F3BC5ED CRC64;
MTNQRLSCGL DLCCAVNLND CLIYASESRY DFICVSLVHP LFKREFISGS AKNRPGPLTR
PDLILNSSDW NNRIIAKFSS LINVDSTNPI IRKNSEETLN QELGLASHFG LSGVTLKLKY
GINKNVNLAR IISDKISNHN CTFQVWIQVP MENPIRQTYS YRTEDYPEDE NPWEWWNSFR
VICDYNKKLG VSLIVSHDLP EEEEIDRWLG EPVRCLILPT TLFLTNKKGY PVLSKAHQAL
VRRFAVQEVQ FILTGASRYQ SVSYYHNYLD YLWKGCQNDG TVEKFARGYE DYLQCPLQPL
MDNLESQTYE IFEKDPIKYR EYQSAIYEAI NAIVYKMQEE RTIIIMVVGA GRGPLVTASL
NAAKMAYREV KIYAVEKNPN AIITEDFLSN NFNQILNNRE LHVFIISFYV YSLQALQRDM
WKEKVTVISC DMREWNPPDK ADIIVSELLG SFGDNELSPE CLDNVLKFLR DDGINIPQSY
TSYIAPMQSS KLYNEVRQLR DKDKHPLAHF ETLYVVHLQN KYDIANPKPL FTFKHPNTDA
LADNSRYEIK TFQVEQNCVL HGFSGYFTAV LYENITLSIE PSTYSSDMFS WFPIFFPLKE
PVQLKAGDEI VVHFWRRCGS KKVWYEWCLS KPIPVSIHNI TGRSSVIFYV HLPNVQNLAA
DYNAINAFIL SKFQHIRTCY PWYILCLIML TRSNLVQLNF
//
