(data stored in ACNUC7421 zone)

SWISSPROT: C7PYW0_CATAD

ID   C7PYW0_CATAD            Unreviewed;       314 AA.
AC   C7PYW0;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 53.
DE   SubName: Full=Peptidase M48 Ste24p {ECO:0000313|EMBL:ACU69516.1};
GN   OrderedLocusNames=Caci_0579 {ECO:0000313|EMBL:ACU69516.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69516.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69516.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003983};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU003983};
CC   -!- SIMILARITY: Belongs to the peptidase M48B family.
CC       {ECO:0000256|RuleBase:RU003983}.
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DR   EMBL; CP001700; ACU69516.1; -; Genomic_DNA.
DR   STRING; 479433.Caci_0579; -.
DR   MEROPS; M48.004; -.
DR   EnsemblBacteria; ACU69516; ACU69516; Caci_0579.
DR   KEGG; cai:Caci_0579; -.
DR   eggNOG; ENOG4105D0M; Bacteria.
DR   eggNOG; COG0501; LUCA.
DR   HOGENOM; HOG000227303; -.
DR   OMA; THIWNNN; -.
DR   OrthoDB; POG091H01BW; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   InterPro; IPR001915; Peptidase_M48.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   3: Inferred from homology;
DR   PRODOM; C7PYW0.
DR   SWISS-2DPAGE; C7PYW0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Hydrolase {ECO:0000256|RuleBase:RU003983};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003983};
KW   Protease {ECO:0000256|RuleBase:RU003983};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|RuleBase:RU003983}.
FT   TRANSMEM     20     43       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     49     66       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    160    181       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    193    217       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       85    306       Peptidase_M48. {ECO:0000259|Pfam:
FT                                PF01435}.
SQ   SEQUENCE   314 AA;  33326 MW;  1BC05B80A258706B CRC64;
     MSSSLSDRRT DARFRADRNL SARMLSVMVL LAAVYGAAIL LMIRFMGRAW PLGLAVVVAF
     AVFQILTSGK VAMRTMGARE VSAEEEPELH ALVDRLCALS GMKKPTIAVA ESRIPNACAV
     GRSKGGATLC VTRSLLDTLD PPELEGVIAH EMAHIEHGDA AVMTVAAFVG VLAGLVARVG
     LRFIYIGGRA RGLWHIIVAA IGLIALATAT WFVSLVLTRS LSRYREFAAD RSAAQLTGNP
     SALASALAKV EAKVHGGGGI PQTDLRKAGA LNAFYFAPVT SAKTTAHHLL STHPTTQARL
     DRLVKMSTEM SKNG
//

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