(data stored in ACNUC7421 zone)

SWISSPROT: D6ZCG9_SEGRD

ID   D6ZCG9_SEGRD            Unreviewed;       317 AA.
AC   D6ZCG9;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Proline iminopeptidase {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
DE            Short=PIP {ECO:0000256|PIRNR:PIRNR006431};
DE            EC=3.4.11.5 {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
DE   AltName: Full=Prolyl aminopeptidase {ECO:0000256|PIRNR:PIRNR006431};
GN   OrderedLocusNames=Srot_0527 {ECO:0000313|EMBL:ADG97011.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG97011.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG97011.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.;
CC         EC=3.4.11.5; Evidence={ECO:0000256|PIRNR:PIRNR006431,
CC         ECO:0000256|RuleBase:RU003421};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR006431}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421}.
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DR   EMBL; CP001958; ADG97011.1; -; Genomic_DNA.
DR   RefSeq; WP_013137467.1; NC_014168.1.
DR   STRING; 640132.Srot_0527; -.
DR   ESTHER; segrd-d6zcg9; Proline_iminopeptidase.
DR   MEROPS; S33.001; -.
DR   EnsemblBacteria; ADG97011; ADG97011; Srot_0527.
DR   KEGG; srt:Srot_0527; -.
DR   eggNOG; ENOG4108HGY; Bacteria.
DR   eggNOG; COG0596; LUCA.
DR   HOGENOM; HOG000171480; -.
DR   KO; K01259; -.
DR   OMA; PDKWERF; -.
DR   OrthoDB; 665798at2; -.
DR   BioCyc; SROT640132:G1GLH-530-MONOMER; -.
DR   Proteomes; UP000002247; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR002410; Peptidase_S33.
DR   InterPro; IPR005944; Pro_iminopeptidase.
DR   PANTHER; PTHR43722; PTHR43722; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF006431; Pept_S33; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00793; PROAMNOPTASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01249; pro_imino_pep_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6ZCG9.
DR   SWISS-2DPAGE; D6ZCG9.
KW   Aminopeptidase {ECO:0000256|PIRNR:PIRNR006431,
KW   ECO:0000256|RuleBase:RU003421, ECO:0000313|EMBL:ADG97011.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR006431};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006431,
KW   ECO:0000256|RuleBase:RU003421, ECO:0000313|EMBL:ADG97011.1};
KW   Protease {ECO:0000256|PIRNR:PIRNR006431,
KW   ECO:0000256|RuleBase:RU003421};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247}.
FT   DOMAIN       38    301       AB hydrolase-1. {ECO:0000259|Pfam:
FT                                PF00561}.
FT   ACT_SITE    114    114       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006431-1}.
FT   ACT_SITE    269    269       {ECO:0000256|PIRSR:PIRSR006431-1}.
FT   ACT_SITE    297    297       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006431-1}.
SQ   SEQUENCE   317 AA;  35874 MW;  A4F5D72730E45D24 CRC64;
     MRSLYPEIEP RATGHLDVGD GQRIFWEQVG NPEGKPAVFL HGGPGGGINP KQRRFFDPKR
     YNVLLFDQRG CGRSTPHAGE NPDLSLNTTW NLVSDIEKLR EQMGVERWLV FGGSWGSTLA
     LAYAQTHPER VSELVLRGVF LCRESELDWF YNPGGASQIF PDLWEEYLAP IPPAARGGNL
     IEEHAKLLWG RDQSAAEASA FAWTGWEDRT IGLTVDPHDR EKDPRTALAF ARIENWYFQN
     KAFLRENQLL EDVDKIRHIP AAIVHGRYDV ICPVASAWEL HRRWPESKLT ITAQSGHTAF
     EAENTHHLVE ATDAFAQ
//

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