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Database: UniProt
Entry: A0A093SUH0_9PASS
LinkDB: A0A093SUH0_9PASS
Original site: A0A093SUH0_9PASS 
ID   A0A093SUH0_9PASS        Unreviewed;       469 AA.
AC   A0A093SUH0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Putative methyltransferase NSUN6 {ECO:0000313|EMBL:KFW86139.1};
GN   ORFNames=N305_13889 {ECO:0000313|EMBL:KFW86139.1};
OS   Manacus vitellinus (golden-collared manakin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX   NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW86139.1, ECO:0000313|Proteomes:UP000053258};
RN   [1] {ECO:0000313|EMBL:KFW86139.1, ECO:0000313|Proteomes:UP000053258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW86139.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC       ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; KL672544; KFW86139.1; -; Genomic_DNA.
DR   RefSeq; XP_008928342.1; XM_008930094.2.
DR   AlphaFoldDB; A0A093SUH0; -.
DR   SMR; A0A093SUH0; -.
DR   STRING; 328815.ENSMVIP00005008804; -.
DR   GeneID; 103763334; -.
DR   CTD; 221078; -.
DR   OrthoDB; 1077100at2759; -.
DR   Proteomes; UP000053258; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd21150; PUA_NSun6-like; 1.
DR   Gene3D; 2.30.130.10; PUA domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22807:SF34; TRNA (CYTOSINE(72)-C(5))-METHYLTRANSFERASE NSUN6; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR   PROSITE; PS50890; PUA; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000053258};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}.
FT   DOMAIN          141..466
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        373
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         242..248
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         266
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         293
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         323
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   469 AA;  51823 MW;  7A87A82B5B1BF65B CRC64;
     MSFFPKISFQ HEVEEYLTKV FRNNELIAAL GGQEAENKYQ SLLSRLSHPP SFTTVRVNTH
     LASVKHAKKL LFEEIQKQFK GLCVPVLEHP KLQDILLIPV IGPRRDLKKH PSEVIVGAQC
     GYAVLRGAHV YVPGIVSASR FVKAGDLVSV YSDIEGKCKR GAKEFKGVKV FLGNGISELS
     RSEIFSSSSP LKGLGVRMIE PVYLSPSFDN VLPSYLFLQN LPSVVVSHIL NPQPGEKILD
     MCAAPGGKAT HLATLMHDQG EVIAMDKIAN KVKKVKLNAE LLQLNCIKAF CYDGTKALSV
     EKREDEQEGP PFSPESFDRI LLDAPCSGMG QRPNMAYSST LKEVTSYQPL QRKLFTVAVK
     LLKPGGVLVY STCTITLSEN EEQVAWALKR FPYLQLHPQE PHIGGEGMKG AGLTLDQLKL
     LQRFDPAAVT LEGMDINSLQ DSREDDLISL ANKDCIGFFI AKFIKSKSK
//
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