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TRMYL_VIBCH
ID   TRMYL_VIBCH             Reviewed;         201 AA.
AC   Q9KKP3;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Putative pseudouridine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00587};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00587};
GN   OrderedLocusNames=VC_A1059;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RG   Midwest center for structural genomics (MCSG);
RT   "Crystal structure of unknown function protein VCA1059.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00587}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. TrmY family.
CC       {ECO:0000255|HAMAP-Rule:MF_00587}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF96953.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE003853; AAF96953.1; ALT_INIT; Genomic_DNA.
DR   PIR; A82384; A82384.
DR   RefSeq; NP_233441.1; NC_002506.1.
DR   RefSeq; WP_001256106.1; NZ_LT906615.1.
DR   PDB; 2QWV; X-ray; 2.60 A; A/B=1-201.
DR   PDBsum; 2QWV; -.
DR   AlphaFoldDB; Q9KKP3; -.
DR   SMR; Q9KKP3; -.
DR   STRING; 243277.VC_A1059; -.
DR   PRIDE; Q9KKP3; -.
DR   DNASU; 2612057; -.
DR   EnsemblBacteria; AAF96953; AAF96953; VC_A1059.
DR   GeneID; 57742410; -.
DR   KEGG; vch:VC_A1059; -.
DR   PATRIC; fig|243277.26.peg.3665; -.
DR   eggNOG; COG1901; Bacteria.
DR   HOGENOM; CLU_107018_0_0_6; -.
DR   OMA; HADHCII; -.
DR   EvolutionaryTrace; Q9KKP3; -.
DR   Proteomes; UP000000584; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR   CDD; cd18087; TrmY-like; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   HAMAP; MF_00587; tRNA_methyltr_TrmY; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR007158; TrmY.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   PANTHER; PTHR40703; PTHR40703; 1.
DR   Pfam; PF04013; Methyltrn_RNA_2; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..201
FT                   /note="Putative pseudouridine methyltransferase"
FT                   /id="PRO_0000157956"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
FT   BINDING         186
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
FT   STRAND          2..14
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   HELIX           15..20
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   TURN            21..23
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   HELIX           29..39
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   STRAND          42..45
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   STRAND          47..57
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   STRAND          63..68
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   TURN            69..71
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   HELIX           80..93
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   TURN            94..96
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   STRAND          102..106
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   STRAND          109..112
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   HELIX           116..124
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   STRAND          127..132
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   TURN            139..141
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   STRAND          146..152
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   TURN            166..170
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   STRAND          172..175
FT                   /evidence="ECO:0007829|PDB:2QWV"
FT   HELIX           183..199
FT                   /evidence="ECO:0007829|PDB:2QWV"
SQ   SEQUENCE   201 AA;  22275 MW;  83AAB4EF25C7A632 CRC64;
     MRSFILRARS APTDSQRLLD EIGGKCHTEI LAHCMMNSLF TAQSHREDVV IHLVLESTRD
     YSRTITVEAN EISDVGGFHE AALIALLVKA LDASVGMGKE QTRVVQPGLT VRTISFEALL
     GELAEHHSLY MMDKKGDSIR DIKIGPNPCF ILTDHIPMPK KSGNSMKRLG VEKISLGPKM
     LFASQCVTLI HNEIDHQEAG W
 
 
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