GenomeNet

Database: UniProt
Entry: A0A0J8QHT1_COCIT
LinkDB: A0A0J8QHT1_COCIT
Original site: A0A0J8QHT1_COCIT 
ID   A0A0J8QHT1_COCIT        Unreviewed;       640 AA.
AC   A0A0J8QHT1;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=tRNA (Cytosine-5-)-methyltransferase ncl1 {ECO:0000313|EMBL:KMU72005.1};
GN   ORFNames=CISG_00314 {ECO:0000313|EMBL:KMU72005.1};
OS   Coccidioides immitis RMSCC 3703.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU72005.1, ECO:0000313|Proteomes:UP000054559};
RN   [1] {ECO:0000313|Proteomes:UP000054559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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}.
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; DS268118; KMU72005.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J8QHT1; -.
DR   STRING; 454286.A0A0J8QHT1; -.
DR   Proteomes; UP000054559; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:UniProt.
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; 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; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   PRINTS; PR02011; RCMTNCL1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054559};
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..405
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        352
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         239
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         299
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   640 AA;  72805 MW;  05720A01BA8CA822 CRC64;
     MGRRSKKFGG GGKRGTRPTN YAAIEKSNEK FESYYNGLKV VPEDEKEQFW EALRRDLPNS
     FRFTGSRKHA LAVQERLKDF YIPNITSIRY EGELVEPPKP VPWYPDQLAW SMTTPKQVVR
     RFPPFASFHK FLVSETEVGN ISRQEVVSMI PPLLLDVRPG MVVLDMCAAP GSKSAQLMEM
     IHAGEEEQMK SMTDRLENKD AQVARQQGRV EIADLLNGEA ELDGFEDDGR STGLLIANDS
     DYKRAHMLIH QMKRLNSPNL LVTNHDATMY PSIRLPSLPV ADGKRSPNRY LKFDRILADV
     PCSGDGTARK NVNVWKDWNP ANGIGLHPTQ ARILVRALQM LKPGGRVVYS TCSMNPIENE
     AVIASAIDRF SQTRAVAPAS KPETALSRPI KQKSGQQFEE PFKYLDSQLK EFDTIFKFYD
     LSPQFPKDRF MVRNADGRPH KTIYYTTALA RDILTENEGT GMKFVHCGVK MFVKQDVQRP
     DVCPWRIQKD GLTLLEPWIG TGRTVKIYKK TTLRKLLVEM FPKVNDGGWK ELGELGEWAR
     DVDMGCCVLK LIPTNEEDGF HEHMVLPLWR SLYSLNLMLP KEERRAMLLR LFNDETPLVN
     TTHKRDAATA KKEEESLETS QALGEDGRES EDVIKQEAIL
//
DBGET integrated database retrieval system