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Database: UniProt
Entry: D9W1D7_9ACTN
LinkDB: D9W1D7_9ACTN
Original site: D9W1D7_9ACTN 
ID   D9W1D7_9ACTN            Unreviewed;       363 AA.
AC   D9W1D7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Protease {ECO:0000313|EMBL:EFL15989.1};
GN   ORFNames=SSNG_03241 {ECO:0000313|EMBL:EFL15989.1};
OS   Streptomyces sp. C.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL15989.1, ECO:0000313|Proteomes:UP000005763};
RN   [1] {ECO:0000313|EMBL:EFL15989.1, ECO:0000313|Proteomes:UP000005763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C {ECO:0000313|EMBL:EFL15989.1,
RC   ECO:0000313|Proteomes:UP000005763};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces sp. strain C.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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DR   EMBL; GG657750; EFL15989.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9W1D7; -.
DR   STRING; 253839.SSNG_03241; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_013364_3_0_11; -.
DR   Proteomes; UP000005763; Unassembled WGS sequence.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013595; Pept_S33_TAP-like_C.
DR   PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF08386; Abhydrolase_4; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000313|EMBL:EFL15989.1}.
FT   DOMAIN          261..363
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   363 AA;  38230 MW;  BF63FDC081D17A9E CRC64;
     MECLTGPAMD RFTQVDQTPD DPAERAKLVA AFKEFAAGCE TRSKRVLPHV STVDAARDMD
     VLRAVLGDEK LNYVGASYGT FLGATYADLF PARVGRVVLD GAMDPSRSSL DLNRDQTAGF
     ETAFRSFAKD CAKQADCPLG RGGPDAVAQR LKEFFRKVDA QPVPSGDPAR PLGEALATTG
     VIAALYDESA WPQLREALTG AMDGDGAGLL ALADSYYERE ADGSYANLMY ANAAVNCLDQ
     PPAFGGPEAV DAALPSFEKA SPVFGAGLAW ASLNCAYWPV KATGAAKPLK AAGAAPIVVV
     GTTRDPATPY KWAQALAGQL ESGTLLTYDG DGHTAYGRGS DCVDTAINRY LLQGQPPTDG
     KRC
//
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