ID A0A7L0QW88_SETKR Unreviewed; 780 AA.
AC A0A7L0QW88;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 18.
DE RecName: Full=tRNA (cytosine(34)-C(5))-methyltransferase {ECO:0000256|ARBA:ARBA00012629};
DE EC=2.1.1.203 {ECO:0000256|ARBA:ARBA00012629};
DE AltName: Full=NOL1/NOP2/Sun domain family member 2 {ECO:0000256|ARBA:ARBA00032770};
DE AltName: Full=mRNA cytosine C(5)-methyltransferase {ECO:0000256|ARBA:ARBA00032819};
DE AltName: Full=tRNA cytosine C(5)-methyltransferase {ECO:0000256|ARBA:ARBA00032179};
DE Flags: Fragment;
GN Name=Nsun2 {ECO:0000313|EMBL:NXL22784.1};
GN ORFNames=SETKIR_R07731 {ECO:0000313|EMBL:NXL22784.1};
OS Setophaga kirtlandii (Kirtland's warbler) (Dendroica kirtlandii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Passeroidea; Parulidae; Setophaga.
OX NCBI_TaxID=298831 {ECO:0000313|EMBL:NXL22784.1, ECO:0000313|Proteomes:UP000550059};
RN [1] {ECO:0000313|EMBL:NXL22784.1, ECO:0000313|Proteomes:UP000550059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-001-45 {ECO:0000313|EMBL:NXL22784.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXL22784.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in mRNA + S-adenosyl-L-methionine = a 5-
CC methylcytidine in mRNA + S-adenosyl-L-homocysteine + H(+);
CC Xref=Rhea:RHEA:61464, Rhea:RHEA-COMP:15145, Rhea:RHEA-COMP:15826,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000256|ARBA:ARBA00049365};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61465;
CC Evidence={ECO:0000256|ARBA:ARBA00049365};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(34) in tRNA precursor + S-adenosyl-L-methionine = 5-
CC methylcytidine(34) in tRNA precursor + S-adenosyl-L-homocysteine +
CC H(+); Xref=Rhea:RHEA:42940, Rhea:RHEA-COMP:10291, Rhea:RHEA-
CC COMP:10295, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.203;
CC Evidence={ECO:0000256|ARBA:ARBA00049286};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42941;
CC Evidence={ECO:0000256|ARBA:ARBA00049286};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(48) in tRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(48) in tRNA + S-adenosyl-L-homocysteine + H(+);
CC Xref=Rhea:RHEA:42948, Rhea:RHEA-COMP:10293, Rhea:RHEA-COMP:10297,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000256|ARBA:ARBA00049323};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42949;
CC Evidence={ECO:0000256|ARBA:ARBA00049323};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(49) in tRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(49) in tRNA + S-adenosyl-L-homocysteine + H(+);
CC Xref=Rhea:RHEA:42952, Rhea:RHEA-COMP:10294, Rhea:RHEA-COMP:10385,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000256|ARBA:ARBA00048755};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42953;
CC Evidence={ECO:0000256|ARBA:ARBA00048755};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(50) in tRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(50) in tRNA + S-adenosyl-L-homocysteine + H(+);
CC Xref=Rhea:RHEA:61488, Rhea:RHEA-COMP:15838, Rhea:RHEA-COMP:15839,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000256|ARBA:ARBA00048936};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61489;
CC Evidence={ECO:0000256|ARBA:ARBA00048936};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC Secreted, extracellular exosome {ECO:0000256|ARBA:ARBA00004550}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NXL22784.1}.
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DR EMBL; VXAS01017136; NXL22784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L0QW88; -.
DR Proteomes; UP000550059; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030488; P:tRNA methylation; IEA:TreeGrafter.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023270; RCMT_NCL1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22808:SF1; RNA CYTOSINE-C(5)-METHYLTRANSFERASE NSUN2-RELATED; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF25376; Pre-PUA_NSUN2; 1.
DR Pfam; PF25378; PUA_NSUN2; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02011; RCMTNCL1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000550059};
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}; tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 49..413
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 418..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 304
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 167..173
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 198
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 225
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 251
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXL22784.1"
FT NON_TER 780
FT /evidence="ECO:0000313|EMBL:NXL22784.1"
SQ SEQUENCE 780 AA; 89044 MW; 1621FFD79E4CD974 CRC64;
ERRGRWTDGG GAFVQGWAGG YPEIVKENEL FERYYRELGI VPAGEWDAFM AALREPLPAT
LRITGYRSHA REILHCLKEK YFRELQDLEV DGQKVEMPQS LSWYPEELAW HTNLSRKILR
KSPQLEKFHQ FLVSETECGN ISRQEAVSMI PPLLLNVSPH HKILDMCAAP GSKTAQLIEM
LHADMNVPFP SGFVIANDVD NKRCYLLVHQ AKRLNSPCIM VVNHDASSIP NLQIDVDGRK
EILFYDRILC DVPCSGDGTM RKNIDVWKKW TTQNSLQLHG LQLRIATRGV EQLAEGGRMV
YSTCSLNPIE NEAVIASLLE KSQGALELAD VSSELPGLKR MPGITKWKVM LKDGQWFEEW
KDVPSNRQTQ IRPTMFPVKD EEKLKAMNLE RCLRILPHHQ NTGGFFVAVL IKKSPMPWNK
RQPKVHQKLP QRTGDTEVTA ANSGNGSDSI IEEPTLAENE ESKKMQELQN LDTEQSKKEG
VCGPPPSKKM KLFGFKEDPF VFLPEDDPLF IPIQKFYALD PSFPKMNLLT RTQEGKKRQL
YMVSKELRNV LLNNSEKMKV INTGIKVWSR NSDGEQFGCA FRLAQEGIYT LYPFIHARII
NVCIEDVKIL LTQENPFLSK FSSETQKKVK DMAMGSIVLK YDPDPEKPHD LQCPIVLCGW
QGKTSLRAFV PKNERLHYLR MMGVEVFKAK RKEEDLEDKT EEEVQHRLVQ TEEKMDVEDK
EHDLVPKMEA EIGEESSQSP VKSSAMEIEN KIEDLDQSSR NANSHVSQEG KDTDASNVKD
//
