(data stored in SCRATCH zone)

SWISSPROT: Q3IIA7_PSEHT

ID   Q3IIA7_PSEHT            Unreviewed;       683 AA.
AC   Q3IIA7;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 87.
DE   SubName: Full=Oligopeptidase A {ECO:0000313|EMBL:CAI85459.1};
DE            EC=3.4.24.70 {ECO:0000313|EMBL:CAI85459.1};
GN   Name=prlC {ECO:0000313|EMBL:CAI85459.1};
GN   OrderedLocusNames=PSHAa0361 {ECO:0000313|EMBL:CAI85459.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85459.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85459.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; CR954246; CAI85459.1; -; Genomic_DNA.
DR   RefSeq; WP_011327072.1; NC_007481.1.
DR   STRING; 326442.PSHAa0361; -.
DR   MEROPS; M03.004; -.
DR   EnsemblBacteria; CAI85459; CAI85459; PSHAa0361.
DR   KEGG; pha:PSHAa0361; -.
DR   PATRIC; fig|326442.8.peg.344; -.
DR   eggNOG; ENOG4105DGW; Bacteria.
DR   eggNOG; COG0339; LUCA.
DR   HOGENOM; HOG000245986; -.
DR   KO; K01414; -.
DR   OMA; KNFQSAM; -.
DR   OrthoDB; 1935578at2; -.
DR   BioCyc; PHAL326442:PSHA_RS01790-MONOMER; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 1.10.1370.10; -; 1.
DR   InterPro; IPR034005; M3A_DCP.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR001567; Pept_M3A_M3B.
DR   Pfam; PF01432; Peptidase_M3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IIA7.
DR   SWISS-2DPAGE; Q3IIA7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Hydrolase {ECO:0000256|RuleBase:RU003435,
KW   ECO:0000313|EMBL:CAI85459.1};
KW   Metal-binding {ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN      225    680       Peptidase_M3. {ECO:0000259|Pfam:PF01432}.
SQ   SEQUENCE   683 AA;  76876 MW;  E3F48F4B1265ADAB CRC64;
     MTNANTNPLI GLEGLPPFSK IKPEHVVPAL KHGIEQCRQA IEDVLAKKSY TWNDLVLPLE
     EADDKLSRMF SPVSHLNSVM NNDELREQYE QCLPLISEYS TFVGQHQGLF AAYNALYNSD
     EFKTLTTAQQ KSITNALRDF KLSGIALEPA QQKRYGEISA RLSELASKFG NNVMDATLAW
     HKHITDESEL AGLPESALAL AADTAKSKEL DGWVFTLDFP SYLPIMTYAD NRELREETYT
     AFSTRASDQG PNAGEFDNSA IMSEELALRH ELAQLLGFNS YAEKSLATKM AETPAQVFSF
     LEDLAAKSKP QAEQELAELQ AYAEQKHGIT ELAAWDFGYY GEKLKQDKYA ISDEVLRPYF
     PANKVLSGLF ETVNRLFGIS VKEVSDFDSY HKDVRFFEIY DSSNTLRGRF YLDLYARDHK
     RGGAWMDDCM GRKVRASGEL QTPVAYLVCN FNKAIGDKPA LFTHNEVTTL FHEFGHGIHH
     MLTQVDAAPV AGINGVAWDA VELPSQFLEN WCYEEQALSF ISGHYETGEP LPKELLDKLL
     AAKNYNSGMQ MLRQLEFSLF DFKIHNDYVA GEPCNIQAVL NDVRSRTSVI KAPEFNRFQH
     GFSHIFAGGY SAGYYSYKWA EVLSADAYSK FEEEGIFNPE TGRAFMQHIL EKGGSEEPME
     LFKNFRGREP NVDALLRHSG IAA
//

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