(data stored in ACNUC7421 zone)

SWISSPROT: Q47TM3_THEFY

ID   Q47TM3_THEFY            Unreviewed;       449 AA.
AC   Q47TM3;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   SubName: Full=Pectate lyase/Amb allergen {ECO:0000313|EMBL:AAZ54191.1};
GN   OrderedLocusNames=Tfu_0153 {ECO:0000313|EMBL:AAZ54191.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54191.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU361173}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000256|RuleBase:RU361173}.
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DR   EMBL; CP000088; AAZ54191.1; -; Genomic_DNA.
DR   RefSeq; WP_011290600.1; NC_007333.1.
DR   STRING; 269800.Tfu_0153; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   EnsemblBacteria; AAZ54191; AAZ54191; Tfu_0153.
DR   KEGG; tfu:Tfu_0153; -.
DR   eggNOG; ENOG4105DBA; Bacteria.
DR   eggNOG; COG3866; LUCA.
DR   HOGENOM; HOG000216909; -.
DR   KO; K01728; -.
DR   OMA; YLKAYDP; -.
DR   OrthoDB; 163648at2; -.
DR   BioCyc; TFUS269800:G1G4Q-156-MONOMER; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR002022; Pec_lyase.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF00544; Pec_lyase_C; 1.
DR   SMART; SM00656; Amb_all; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47TM3.
DR   SWISS-2DPAGE; Q47TM3.
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Lyase {ECO:0000256|RuleBase:RU361173, ECO:0000313|EMBL:AAZ54191.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361173};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Secreted {ECO:0000256|RuleBase:RU361173};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    449       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004233596.
FT   DOMAIN      129    372       Amb_all. {ECO:0000259|SMART:SM00656}.
SQ   SEQUENCE   449 AA;  49894 MW;  BFA71C448240A9A4 CRC64;
     MRRAATLGVA LALPLTLAAP SSALAQPHHH AGVSPKAEQV AREVLAPNDG WAAYDGGTTG
     GAAADPEHVY VVTTYAELRE ALAGGRTNDT PKIVFLKGRI DANTDEHGNQ LTCDDYADPE
     YDFDAYLATY DPEVWGWDQE PSGPLEEARE RSYRNQRDQV VIEVGSNTTL IGLGDDATLV
     GAQVMVDSVD NVIIRNIIFE TAQDCFPQWD PTDGPEGNWN SEFDGVSVRR STHVWIDHNE
     FSDGAVLDRD LPEYFGREFQ VHDGLLDITH GADLVTVSYN VLRDHDKTML IGSTDSPTYD
     VGKLRVTLHH NRWENVLQRA PRVRYGQVHV YNNHYVIPAT PEGEKTYEYS WGVGVESALY
     AENNYFDIDP SVDFSQVVAH WKGTQMYEKG SYANGRSRHH QVSFLDEYNA VHSPTIENKQ
     TWSPPLHGRI DPTQSVPAKV QKAGVGHIL
//

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