ID A0A3B4D9Y3_PYGNA Unreviewed; 878 AA.
AC A0A3B4D9Y3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000021152.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000021152.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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}.
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 STRING; 42514.ENSPNAP00000021152; -.
DR Ensembl; ENSPNAT00000032232.1; ENSPNAP00000021152.1; ENSPNAG00000028223.1.
DR GeneTree; ENSGT00940000157172; -.
DR OMA; IDSMCDF; -.
DR Proteomes; UP000261440; 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 Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 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 80..126
FT /note="G-patch"
FT /evidence="ECO:0000259|PROSITE:PS50174"
FT DOMAIN 224..443
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51613"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 99884 MW; C2C455135C3B1B63 CRC64;
MMKRRLDAVD EASGRKKARR EEASSDEDEE SSQRTTSQDS SQSESLSDAE DHRPSFSKPT
ASQNSQSNDA TQGSSKFSMY NSVSQKLMAK MGFKEGEGLG KFGQGRREIV EASTQRGRRG
LGLTLQGFQG ELNVEWQDEP EPNALEEVSW FPECSTEIPD ADELSDWMTT GESKMKIDDE
TEFCSEDLLQ VLLRCKSVFD DLEGEEMRRA RTRSNPYETI RGAFFLNRAA MKMANMDHVF
DYMFTNPKDG QGKPLVRDKE GELLYFGDVC AGPGGFSEYV LWRKRWHAKG FGMTLKGAND
FKLEDFYAAP SELFEPYYGE GGVDGDGDIT RPENITAFRN FVLENTERRG LHFLMADGGF
SVEGQENIQE ILSKQLLLCQ FLMALSVVRT GGHFVCKTFD LFTPFSVGLT YLLYLCFERV
SLFKPVTSRP ANSERYVVCR SLKPGSDAVR DYLFNVNLKL NHLRHSERDV TDVVPLDIIK
GDTDFYQYMI KSNESHCAVQ IKALSKIHAY VRDTTLSEPR QADIRKDCLK LWGIPDQARV
TPSPSDPKSK FYELVKGLDI DSFNSRPTPL SSSTLDRLQH VLDHRCIVGG GEQIFLLGLG
KSQIYTWDGK APLRWRKLEN FKMELPRDTL LSVEIVQELK GEGKAQRRIN AVHVLDALVL
NGTDVREQHF NQRIQMAEKF VKAVSKPSRP DMNPIRVKEV YRLEEMDKIF VRLEMKVTKS
SGGMPRLSYT GRDDRHFLPS GLYIIKTVSD PWTMAFSKSS KKKFFFNRQT KXXXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXVSLSL SLSLSLSLSL SLSLSLSLSL SVCHHDRLFW
AWEEGVRVHD SQTRVDPEKL SKDDVLSFIR KHCQQWET
//
