(data stored in SCRATCH zone)

SWISSPROT: C7QJB7_CATAD

ID   C7QJB7_CATAD            Unreviewed;       314 AA.
AC   C7QJB7;
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:ACU69259.1};
GN   OrderedLocusNames=Caci_0306 {ECO:0000313|EMBL:ACU69259.1};
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:ACU69259.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69259.1, 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; ACU69259.1; -; Genomic_DNA.
DR   RefSeq; WP_012784554.1; NC_013131.1.
DR   STRING; 479433.Caci_0306; -.
DR   EnsemblBacteria; ACU69259; ACU69259; Caci_0306.
DR   KEGG; cai:Caci_0306; -.
DR   eggNOG; ENOG4108PXH; Bacteria.
DR   eggNOG; COG0501; LUCA.
DR   HOGENOM; HOG000243187; -.
DR   OMA; VAYCLPG; -.
DR   OrthoDB; POG091H08UR; -.
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; C7QJB7.
DR   SWISS-2DPAGE; C7QJB7.
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      6     24       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     36     58       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     93    114       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    292    313       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      122    192       Peptidase_M48. {ECO:0000259|Pfam:
FT                                PF01435}.
SQ   SEQUENCE   314 AA;  33475 MW;  E0E4814F310C9BDA CRC64;
     MFADAWPLAV LAILLAWPVP VFLARAAWPR RHARAAIALW QAVGVAGGLA LIGAPLAVGV
     APLDGHLRTG LVELWRDAFH LRVPAALGLA QEIALALAAV LTVRLVGVTL LSAWRIERDL
     RRQRDAVDLA AEHADRDLRV LEHAAPAAYC LPGTRPRIVI TEGTIAALAP DELEAVLAHE
     RAHARWRHEL VVQPFVAWES ALPLPPARRA TASVTALVEM LADDHAARSV GRPALARALV
     AIGGTAGPVP NQRTDGAPGS GSDPNPVRAT PTLDRVQRLV RRPKATSLAE RLIGPAAWLA
     AVLLVAGPTW YVLR
//

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