ID   A0A0N4W3Y1_HAEPC        Unreviewed;       799 AA.
AC   A0A0N4W3Y1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 {ECO:0000256|RuleBase:RU368012};
DE            EC=2.1.1.57 {ECO:0000256|RuleBase:RU368012};
DE   AltName: Full=Cap1 2'O-ribose methyltransferase 1 {ECO:0000256|RuleBase:RU368012};
OS   Haemonchus placei (Barber's pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX   NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0000455501-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HPLM_0000455501-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC       mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of
CC       RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-
CC       capped mRNA to produce m(7)GpppNmp (cap1).
CC       {ECO:0000256|RuleBase:RU368012}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC         in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC         triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC         Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC         EC=2.1.1.57; Evidence={ECO:0000256|RuleBase:RU368012};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU368012}.
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DR   AlphaFoldDB; A0A0N4W3Y1; -.
DR   WBParaSite; HPLM_0000455501-mRNA-1; HPLM_0000455501-mRNA-1; HPLM_0000455501.
DR   OMA; RYITCKG; -.
DR   Proteomes; UP000038042; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-UniRule.
DR   GO; GO:0097309; P:cap1 mRNA methylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.12760; -; 1.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR025816; RrmJ-type_MeTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR16121:SF0; CAP-SPECIFIC MRNA (NUCLEOSIDE-2'-O-)-METHYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR16121; UNCHARACTERIZED; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS51613; SAM_MT_RRMJ; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|RuleBase:RU368012};
KW   mRNA capping {ECO:0000256|RuleBase:RU368012};
KW   mRNA processing {ECO:0000256|RuleBase:RU368012};
KW   Nucleus {ECO:0000256|RuleBase:RU368012};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU368012};
KW   Transferase {ECO:0000256|RuleBase:RU368012}.
FT   DOMAIN          9..55
FT                   /note="G-patch"
FT                   /evidence="ECO:0000259|PROSITE:PS50174"
FT   DOMAIN          158..385
FT                   /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000259|PROSITE:PS51613"
SQ   SEQUENCE   799 AA;  91429 MW;  D47F3D27BED3FA80 CRC64;
     LEPPPPKVPM TAAERMMAKM GHVEGKGLGK TKQGLIEPVA LSTQRGRVGL GHSITKTVGR
     DFLETWDESK EDKSIEERVY WMAECPESTR DWVVDYLEGS EWIEIGEKLK IDDETNFCDG
     EILRDMLNSK DVFNVVPDRD LREARARANP YETIGAAFFQ NRAAMKVANL DRTFNFLFSG
     ETEERLLSKN PLKSERPTSN CDREAPLFYF ADVCAGPGGF SEYMLWRKAF YNVKGFGFTL
     KGKDDFKLGK FTASSAHYFE PFYGKEGDGD VTKPDNINSL EEFIMKGTND VGVDLMMADG
     GFSVEGQENI QEILSKHIYL CQLLVSLCIV REGGVFFCKL FDVFTPFSAG LIYLMYIAYD
     QISLHKPHTS RPANSERYII CKGLRKNYSD AVRDYLKRYV VNVKLYEFTK AGSSKDVVSV
     VPLETLKSDE EFFKYLKEHN ERLADRQSTY LRKYLSFAKN SSLIDRDQGT LREECLKLWL
     VPNKTLDRRE RGAERQQIDP DQYFGRFTRK VMIFVAILFQ WLYSRKGTSP IYAEFSLNIL
     SNRASTQPEL LISTGDAVFV WRKHWEKIDN NVMRIPDRTV LLVERVDNKR LESVSTDGLV
     RILDAAVLNG DDVSGLLYSK RMAAAQKFCQ ALKLVNRTQD QTGSGELYIV YNDISMKIRR
     KFSRLRHSGE EVLIYDENGH LLMCKAIRVA RLLKGKIPFR CLPHSPEHDS WFYRGVEDGM
     VIHECCSSFW ESAMPSKQTS GHVPMQCIWS WENSCKFVLD NYGPRVILEN DSHKSGPTVN
     SILQEVAETD EKCRKSVAA
//