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Database: UniProt
Entry: A0A0C1YF87_9ACTN
LinkDB: A0A0C1YF87_9ACTN
Original site: A0A0C1YF87_9ACTN 
ID   A0A0C1YF87_9ACTN        Unreviewed;       460 AA.
AC   A0A0C1YF87;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Protease {ECO:0000313|EMBL:KIF79322.1};
GN   ORFNames=QR77_31275 {ECO:0000313|EMBL:KIF79322.1};
OS   Streptomyces sp. 150FB.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF79322.1, ECO:0000313|Proteomes:UP000031584};
RN   [1] {ECO:0000313|EMBL:KIF79322.1, ECO:0000313|Proteomes:UP000031584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=150FB {ECO:0000313|EMBL:KIF79322.1,
RC   ECO:0000313|Proteomes:UP000031584};
RA   Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.;
RT   "Genome sequence of the mycoparasite antagonist Streptomyces sp. strain FB
RT   150.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIF79322.1}.
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DR   EMBL; JTHL01000001; KIF79322.1; -; Genomic_DNA.
DR   RefSeq; WP_040028953.1; NZ_JTHL01000001.1.
DR   AlphaFoldDB; A0A0C1YF87; -.
DR   STRING; 1576605.QR77_31275; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000031584; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF224; PROCESSING PROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KIF79322.1};
KW   Protease {ECO:0000313|EMBL:KIF79322.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031584}.
FT   DOMAIN          34..165
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          185..373
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   460 AA;  48519 MW;  A9F17F80FCF4708F CRC64;
     MDLHPQPTAG EARPWAFPAP ERGALDNGMT VLRCHRPGQQ VVAVEISLAA PLDAEPEGLD
     GIATIMVRAF SEGTDKHSAE EFAAELERCG ATLDAAADHP GVRVSLEVPV SRLPKGLGLL
     AEALRAPAFL ESEIERLVNN RLDEIPHESA NPARRAAKQL SKELFPASLR MSRPRQGTAE
     TVARIDAAGV RAFYDAHVRP ATATAVVVGD LTDVDLDTLL AETLGTWTGN MAAARPVPPI
     TADDTGRVVI VDRPGAVQTQ LLIGRIGADR HDRVWPAQVL GTYCLGGTLT SRLDRVLREE
     KGYTYGVRAY GQVIRSSDPA TPGGPTGAAM LAISGSVDTE STGPALDDLW KVLRTLAAEG
     LTDAERDVAV QNLVGVAPLK YETAASVADT LADQVEQHLP DDFQAQLYAR LAETGTVEAT
     AAAVNAFPVD RLVTVLVGDA AQIKDAVTAL GIGEVTVVTG
//
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