ID A0A0N5AN47_9BILA Unreviewed; 508 AA.
AC A0A0N5AN47;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=protein-histidine N-methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00898};
DE EC=2.1.1.85 {ECO:0000256|PROSITE-ProRule:PRU00898};
OS Syphacia muris.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000602201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMUV_0000602201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:19369, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:11600,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16367, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.85;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00898};
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. SETD3 actin-histidine methyltransferase family.
CC {ECO:0000256|PROSITE-ProRule:PRU00898}.
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DR AlphaFoldDB; A0A0N5AN47; -.
DR STRING; 451379.A0A0N5AN47; -.
DR WBParaSite; SMUV_0000602201-mRNA-1; SMUV_0000602201-mRNA-1; SMUV_0000602201.
DR Proteomes; UP000046393; Unplaced.
DR GO; GO:0018064; F:protein-L-histidine N-tele-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd19176; SET_SETD3; 1.
DR Gene3D; 3.90.1420.10; Rubisco LSMT, substrate-binding domain; 1.
DR Gene3D; 3.90.1410.10; set domain protein methyltransferase, domain 1; 1.
DR InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR025785; SETD3.
DR InterPro; IPR044428; SETD3_SET.
DR PANTHER; PTHR13271:SF47; ACTIN-HISTIDINE N-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR13271; UNCHARACTERIZED PUTATIVE METHYLTRANSFERASE; 1.
DR SUPFAM; SSF81822; RuBisCo LSMT C-terminal, substrate-binding domain; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51565; SAM_MT85_SETD3; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00898};
KW S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU00898};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU00898}.
SQ SEQUENCE 508 AA; 59062 MW; BF289DBA0F2D7BC0 CRC64;
MSSSSLVQRN EILQKLRNKC DYLWQSKLTQ SAPESPMNAL WEEHLEIRQQ LKEIFKLQEE
LGAVVPKAND RQQSLIAFMN WCDRMKIKRN NVTVKYFDNI GFELQTTGEV KEGEDMVTVP
RNALLSWDLA RKSVLLKKCF ERDIIVRSMD NVALALMLCC QKLSSDSFWH PYFNILPETF
DTPLYYSENE LQALKPSPAF EDALLLFRDI TRQFLYFMIE VIHVVEYRSA KLQKKQQAQM
HEPTFLNTPL TPENFTFDLY RWSVACVSTR INMIPSQDLR NHNDAPVLIP CLIPLLDMAN
HEVCMNASLP HVYFSAENDC ASITAVRNYN AGETVRIYYG KRCSSDFLLH NGFVPESDSF
EDTCKLKIGI TKKSEFYNAR LKMMQDYGYT TNSNIFHFDL SLKEPYVDES LLYFARVFVL
NNPDENGKSQ LETYDVTLKA WDFLRKRLEL TLSTYGKLDN IKPATSREAT ILRLKRNEVK
VLRKAFHYSS EQYLKLLSQS QQEGQVAA
//