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Database: UniProt/TrEMBL
Entry: G0BL75_9ENTR
LinkDB: G0BL75_9ENTR
Original site: G0BL75_9ENTR 
ID   G0BL75_9ENTR            Unreviewed;       314 AA.
AC   G0BL75;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   26-NOV-2014, entry version 16.
DE   RecName: Full=tRNA pseudouridine synthase B {ECO:0000256|HAMAP-Rule:MF_01080, ECO:0000256|SAAS:SAAS00043051};
DE            EC=5.4.99.25 {ECO:0000256|HAMAP-Rule:MF_01080, ECO:0000256|SAAS:SAAS00043054};
DE   AltName: Full=tRNA pseudouridine(55) synthase {ECO:0000256|HAMAP-Rule:MF_01080};
DE   AltName: Full=tRNA pseudouridylate synthase {ECO:0000256|HAMAP-Rule:MF_01080};
DE   AltName: Full=tRNA-uridine isomerase {ECO:0000256|HAMAP-Rule:MF_01080};
GN   Name=truB {ECO:0000256|HAMAP-Rule:MF_01080};
GN   ORFNames=SerAS12_0431 {ECO:0000313|EMBL:AEF48539.1};
OS   Serratia sp. AS12.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Serratia.
OX   NCBI_TaxID=768490 {ECO:0000313|EMBL:AEF48539.1, ECO:0000313|Proteomes:UP000008884};
RN   [1] {ECO:0000313|EMBL:AEF48539.1, ECO:0000313|Proteomes:UP000008884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS12 {ECO:0000313|EMBL:AEF48539.1};
RX   PubMed=22768360; DOI=10.4056/sigs.2705996;
RA   Neupane S., Finlay R.D., Alstrom S., Goodwin L., Kyrpides N.C.,
RA   Lucas S., Lapidus A., Bruce D., Pitluck S., Peters L.,
RA   Ovchinnikova G., Chertkov O., Han J., Han C., Tapia R., Detter J.C.,
RA   Land M., Hauser L., Cheng J.F., Ivanova N., Pagani I., Klenk H.P.,
RA   Woyke T., Hogberg N.;
RT   "Complete genome sequence of Serratia plymuthica strain AS12.";
RL   Stand. Genomic Sci. 6:165-173(2012).
CC   -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-
CC       55 in the psi GC loop of transfer RNAs. {ECO:0000256|HAMAP-
CC       Rule:MF_01080, ECO:0000256|SAAS:SAAS00043052}.
CC   -!- CATALYTIC ACTIVITY: tRNA uridine(55) = tRNA pseudouridine(55).
CC       {ECO:0000256|HAMAP-Rule:MF_01080, ECO:0000256|SAAS:SAAS00043049}.
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC       Type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01080}.
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DR   EMBL; CP002774; AEF48539.1; -; Genomic_DNA.
DR   RefSeq; YP_004498896.1; NC_015566.1.
DR   EnsemblBacteria; AEF48539; AEF48539; SerAS12_0431.
DR   GeneID; 10624624; -.
DR   KEGG; srs:SerAS12_0431; -.
DR   KO; K03177; -.
DR   BioCyc; SSP768490:GH4I-457-MONOMER; -.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.30.130.10; -; 1.
DR   HAMAP; MF_01080; TruB_bact; 1.
DR   InterPro; IPR002501; PsdUridine_synth.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom.
DR   InterPro; IPR015947; PUA-like_domain.
DR   InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR   InterPro; IPR015240; tRNA_sdUridine_synth_fam1_C.
DR   PANTHER; PTHR13767; PTHR13767; 1.
DR   Pfam; PF09157; TruB-C_2; 1.
DR   Pfam; PF01509; TruB_N; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR00431; TruB; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008884};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01080,
KW   ECO:0000256|SAAS:SAAS00043050};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01080,
KW   ECO:0000256|SAAS:SAAS00043048}.
FT   ACT_SITE     48     48       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01080}.
FT   BINDING      43     43       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01080}.
FT   BINDING      76     76       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01080}.
FT   BINDING     179    179       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01080}.
FT   BINDING     200    200       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01080}.
SQ   SEQUENCE   314 AA;  35108 MW;  35269DF87BEF8B6F CRC64;
     MSRPRRRGRD IHGVLLLDKP QGLSSNDALQ KVKRLYNANR AGHTGALDPL ATGMLPICLG
     EATKFSQFLL DSDKRYRVIA KLGQRTDTSD ADGQIVQERP VNFTQTQLDT ALDSFRGDIK
     QVPSMYSALK YQGKKLYEYA RQGIEVPREA RSITVYELQF IRWEGDELEL EIHCSKGTYI
     RTITDDLGEL LGCGAHVIYL RRLQVATYPI ERMVTLEQLN ALLEQAQARE IAPGELLDPL
     LMPMDSPVEN YPEVNLLPVV AGYVKQGQPV QVAGAPASGM VRMTEGEERK FIGVGDIADD
     GRVAPRRLVV EHFD
//
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