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TRM61_CRYNB
ID   TRM61_CRYNB             Reviewed;         433 AA.
AC   P0CS09; Q55J46; Q5KCL4;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRM61;
DE            EC=2.1.1.220;
DE   AltName: Full=tRNA(m1A58)-methyltransferase subunit TRM61;
DE            Short=tRNA(m1A58)MTase subunit TRM61;
GN   Name=TRM61; OrderedLocusNames=CNBL1390;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase,
CC       which catalyzes the formation of N(1)-methyladenine at position 58
CC       (m1A58) in initiator methionyl-tRNA. {ECO:0000250|UniProtKB:P46959}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC         methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43152, Rhea:RHEA-COMP:10365, Rhea:RHEA-COMP:10366,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.220;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00952};
CC   -!- SUBUNIT: Heterotetramer; composed of two copies of TRM6 and two copies
CC       of TRM61. {ECO:0000250|UniProtKB:P46959}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46959}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TRM61 family. {ECO:0000255|PROSITE-ProRule:PRU00952}.
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DR   EMBL; AAEY01000056; EAL17877.1; -; Genomic_DNA.
DR   RefSeq; XP_772524.1; XM_767431.1.
DR   AlphaFoldDB; P0CS09; -.
DR   SMR; P0CS09; -.
DR   EnsemblFungi; AAW45025; AAW45025; CNH01430.
DR   EnsemblFungi; EAL17877; EAL17877; CNBL1390.
DR   GeneID; 4939188; -.
DR   KEGG; cnb:CNBL1390; -.
DR   VEuPathDB; FungiDB:CNBL1390; -.
DR   HOGENOM; CLU_025402_4_0_1; -.
DR   Proteomes; UP000001435; Chromosome 12.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IEA:EnsemblFungi.
DR   GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR014816; tRNA_MeTrfase_Gcd14.
DR   PANTHER; PTHR12133; PTHR12133; 1.
DR   Pfam; PF08704; GCD14; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51620; SAM_TRM61; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Nucleus; S-adenosyl-L-methionine; Transferase;
KW   tRNA processing.
FT   CHAIN           1..433
FT                   /note="tRNA (adenine(58)-N(1))-methyltransferase catalytic
FT                   subunit TRM61"
FT                   /id="PRO_0000410316"
FT   REGION          295..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..309
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         92
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT   BINDING         119..121
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT   BINDING         140
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FX7,
FT                   ECO:0000255|PROSITE-ProRule:PRU00952"
FT   BINDING         145
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT   BINDING         167..168
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT   BINDING         185
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FX7,
FT                   ECO:0000255|PROSITE-ProRule:PRU00952"
SQ   SEQUENCE   433 AA;  48397 MW;  06DD8BF443935F2D CRC64;
     MDIRKPMFHS RVHIEAGDIV ILYMARDNMT AITITPGETF HNKYGRYPHD MLIGQKYGSK
     IHSPPPHPGY VHVLRPTPEL WTLSLPHRTQ ILYLPDISYI TMRLGVRVGG KVIEAGTGSG
     SMTHSLSRSV GPSGQVMSFE YHRQRFETAL KEFESHGLTN VRLQHRNVCK EGFGDAQGVE
     GVFLDLPAPW EAIPHAVKAL RRDIITRICC FSPCLEQVLK TVTCLRSEGF SDISTQEVLI
     RTHELVTPPP NTTYLSSISS VVSYLREHEQ RKEERRLLQI KTAKENNRKV KGIEADDAIP
     VEGETGSKRK LEQPSVTGSD NAAPANSRPK TNLLWTEPPN TLPSTVLTKP SPEMKGHTSY
     LTFAILYPES VRLSMVAQET SSRVETPTNI TKAPETHSQE THYSEGSEIE KIGAMTSKEM
     DDWMKSGSTS LSI
 
 
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