(data stored in ACNUC7421 zone)

SWISSPROT: B4SSN9_STRM5

ID   B4SSN9_STRM5            Unreviewed;       624 AA.
AC   B4SSN9;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   10-APR-2019, entry version 46.
DE   SubName: Full=Patatin {ECO:0000313|EMBL:ACF49921.1};
GN   OrderedLocusNames=Smal_0216 {ECO:0000313|EMBL:ACF49921.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49921.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49921.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49921.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01161}.
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DR   EMBL; CP001111; ACF49921.1; -; Genomic_DNA.
DR   STRING; 391008.Smal_0216; -.
DR   EnsemblBacteria; ACF49921; ACF49921; Smal_0216.
DR   KEGG; smt:Smal_0216; -.
DR   eggNOG; ENOG4108SKZ; Bacteria.
DR   eggNOG; ENOG4111HC6; LUCA.
DR   HOGENOM; HOG000270179; -.
DR   OMA; ECDLVMK; -.
DR   BioCyc; SMAL391008:SMAL_RS01090-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   4: Predicted;
DR   PRODOM; B4SSN9.
DR   SWISS-2DPAGE; B4SSN9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01161};
KW   Lipid degradation {ECO:0000256|PROSITE-ProRule:PRU01161};
KW   Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU01161}.
FT   DOMAIN        8    392       PNPLA. {ECO:0000259|PROSITE:PS51635}.
FT   MOTIF        38     42       GXSXG. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01161}.
FT   MOTIF       379    381       DGA/G. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01161}.
FT   ACT_SITE     40     40       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01161}.
FT   ACT_SITE    379    379       Proton acceptor. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01161}.
SQ   SEQUENCE   624 AA;  67821 MW;  5E7918FE23468E5E CRC64;
     MAAKYCDLVM KGGITSGIVY PNAVLALARE YRFKSIGGTS AGAIAAAVAA AAACGDRRQQ
     AGEHLPGDAG YSGLSAVSAQ LSRRGFIYSL FQPARGARAA YRLLVVLTGN ARLPHKLLCL
     AVAVFEIAPL EVLVSLSLLL GLGWWGGGWS GVAATLLPSL LCAYGAGVAG AALRVARVAR
     RNLLGLCSGL GRDARRPALT EWLHESLQQL SGKPLDAPLT FADLHDAPRY AGEPDSPHAI
     SLQMITTCVS HNEPRTLPLG GAQFWFLREE FEQLFPASVV QWLVTQAGPP LEVEGRRYYH
     LPQGPKLPVL VATRMSLSFP LLISAVPLHE PSRRERRCEP TAPAADQEHN VADSMEGLTS
     AGQTCGPVIT AFRICWFSDG GISSNFPIHL FDAALPRWPT FAINLVYPQH AEDVSHGSSG
     RQALEHAVFL PTENRHGWQR TYQSIATPLA AAELGRFLFA VVATMQNWRD LLQARAPGYR
     DRIVHVSLQG DEGGMNLDMP QDVLTRIADK GSLAGARFCS FSFENHYWIR WRNLASAYQR
     YTLEVARTDD PAQQVLAYRA AYAMVASGQP APPSYKLGSE DKRLASQQLW GLMVEQGRSW
     DDLGPDLTDG APRPLPQMKV TPIY
//

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