GenomeNet

Database: UniProt
Entry: A0A091Q199_LEPDC
LinkDB: A0A091Q199_LEPDC
Original site: A0A091Q199_LEPDC 
ID   A0A091Q199_LEPDC        Unreviewed;       764 AA.
AC   A0A091Q199;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 {ECO:0000256|ARBA:ARBA00021134};
DE            EC=2.1.1.296 {ECO:0000256|ARBA:ARBA00012770};
GN   ORFNames=N330_08144 {ECO:0000313|EMBL:KFQ13301.1};
OS   Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX   NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ13301.1, ECO:0000313|Proteomes:UP000053001};
RN   [1] {ECO:0000313|EMBL:KFQ13301.1, ECO:0000313|Proteomes:UP000053001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ13301.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-
CC         ribonucleoside)-(ribonucleotide) in mRNA + S-adenosyl-L-methionine =
CC         a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-
CC         ribonucleoside)-(2'-O-methyl-ribonucleotide) in mRNA + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:67024, Rhea:RHEA-COMP:17169,
CC         Rhea:RHEA-COMP:17170, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:167612, ChEBI:CHEBI:167614;
CC         EC=2.1.1.296; Evidence={ECO:0000256|ARBA:ARBA00024560};
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   EMBL; KK682788; KFQ13301.1; -; Genomic_DNA.
DR   RefSeq; XP_009952254.1; XM_009953952.1.
DR   AlphaFoldDB; A0A091Q199; -.
DR   GeneID; 104348619; -.
DR   KEGG; ldi:104348619; -.
DR   CTD; 55783; -.
DR   OrthoDB; 5488054at2759; -.
DR   PhylomeDB; A0A091Q199; -.
DR   Proteomes; UP000053001; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProt.
DR   Gene3D; 3.40.50.12760; -; 2.
DR   InterPro; IPR025807; Adrift-typ_MeTrfase.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR16121:SF2; CAP-SPECIFIC MRNA (NUCLEOSIDE-2'-O-)-METHYLTRANSFERASE 2; 1.
DR   PANTHER; PTHR16121; UNCHARACTERIZED; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51614; SAM_MT_ADRIFT; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00946,
KW   ECO:0000313|EMBL:KFQ13301.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053001};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU00946};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU00946,
KW   ECO:0000313|EMBL:KFQ13301.1}.
FT   DOMAIN          109..322
FT                   /note="Adrift-type SAM-dependent 2'-O-MTase"
FT                   /evidence="ECO:0000259|PROSITE:PS51614"
FT   ACT_SITE        275
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT   BINDING         148
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT   BINDING         167
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT   BINDING         235
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
SQ   SEQUENCE   764 AA;  87262 MW;  E01992C3FE4018FA CRC64;
     MNKCKKPFVD QTTTLEKFSP EIVSEIEKLF VKKFTYTKPV NNEWQLPDPS DAFTCDHKEF
     DSLLALKDSM NEVKNQLSDK NLNEWHQHTS FTNKAGKIIP HVKKSVNAEL CTQAWCKFHE
     ILCSFPLLPE EALQDGELNS VHLCEAPGAF IASLNHYLKS HHVPCDWNWV ANTLNPYHEA
     NDTLMMIMDD RLIANTLPWW YFGPDNTGDV MTLKHLTGLQ NFVSNMATVH LVTADGSFDC
     QGNPGEQEAL VSPLHYCETV TALMILGTGG SFVLKMFTLF EHCSTNLLFL LNCSFEEVHV
     FKPATSKAGN SEAYVICLRY MGRESIHLLL SKMIQNFGTE MVNKALFPQH MLPESFLKVH
     EKCCIFFHKC QVETISENIH LFERMEEAEQ AKLNKLRDCA VELFMQRLHM KPIARNNWLV
     KKSQTGCSMN AKWFGQRNKY FSTYNERKMM ETLTWNDKVA KGYLNHWAEE HSFNNVGKMC
     ILEGSSSNLE CSLWYILEGK RLPMVKCSPF CDGQVLENLN EAMNEVVGRK LKSRQMLQTC
     HLCEVLPGEL MLAEVSDLSR CHQELLNERC SDQFRCLVVD LPSLCGTESQ LSMEIKLLDS
     ATLLTFSFSL LYDGEPKYQQ QLLECVLHSL NQLTMGDALI LPILSCFTRF TAGLIFVLHC
     CFRYITFACP TSHEPLKTSA ALLCVGYRGL PNPVVEYLQH LNKLMSSLLD TESPQQVLQF
     VPMEVLLQGK LLEFLWDLNT AIAKRQLHLI VQAKQQQMTS NVSL
//
DBGET integrated database retrieval system