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Database: UniProt
Entry: A0A1D7Y339_9ACTN
LinkDB: A0A1D7Y339_9ACTN
Original site: A0A1D7Y339_9ACTN 
ID   A0A1D7Y339_9ACTN        Unreviewed;       688 AA.
AC   A0A1D7Y339;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Peptidase S53 domain-containing protein {ECO:0000259|PROSITE:PS51695};
GN   ORFNames=BFF78_01820 {ECO:0000313|EMBL:AOR29988.1};
OS   Streptomyces fodineus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1904616 {ECO:0000313|EMBL:AOR29988.1, ECO:0000313|Proteomes:UP000094960};
RN   [1] {ECO:0000313|Proteomes:UP000094960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW1S1 {ECO:0000313|Proteomes:UP000094960};
RA   Kim M.-K., Kim S.B.;
RT   "Streptomyces puniciscabiei strain:TW1S1 Genome sequencing and assembly.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP017248; AOR29988.1; -; Genomic_DNA.
DR   RefSeq; WP_069776642.1; NZ_CP017248.1.
DR   AlphaFoldDB; A0A1D7Y339; -.
DR   KEGG; spun:BFF78_01820; -.
DR   Proteomes; UP000094960; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR006644; Cadg.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   PANTHER; PTHR14218:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR   Pfam; PF05345; He_PIG; 1.
DR   Pfam; PF20773; InhA-like_MAM; 1.
DR   SMART; SM00736; CADG; 1.
DR   SUPFAM; SSF49313; Cadherin-like; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           40..688
FT                   /note="Peptidase S53 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009102575"
FT   DOMAIN          114..446
FT                   /note="Peptidase S53"
FT                   /evidence="ECO:0000259|PROSITE:PS51695"
SQ   SEQUENCE   688 AA;  69579 MW;  73CF8E084CDB79B1 CRC64;
     MRESRPSGRR RSLRRLVAVA FPALTLTVAG FTAAPTAGAQ PAATHPQISK VTQNAKALTA
     PGRQTYHSTG KAGQKVPTQH LCATAEPGHA SCFAQRRTDI KQRLAAAVAA APSGLSPANL
     HSAYNLPTAA GSGMTVGIVD AYNDPNAESD LGTYRSTYGL SSCTKANGCF KQVSQTGSTT
     SLPTNDTGWA GEEMLDIDMV SAVCPNCSII LVEANSASMA DLGAAENEAV ALGAKFVSNS
     WGGSESSSQT SDDTSYFKHP GVAITVSSGD SAYGAEYPAT SQYVTAVGGT ALTTASNSRG
     WSESVWHTNS TEGTGSGCSA YDPKPSWQTD TGCSKRMEAD VSAVADPATG VAVYDTYGGT
     GWAVYGGTSA SSPIIASVYA LAGTPGSSDY PAKYPYQHTG NLYDVTSGNN GSCSPSYFCA
     AGTGYDGPTG WGTPNGTTAF TAGSTGGNTV SVTNPGSQST TTGSSVSLQI KATDSGGASL
     TYSASGLPTG LSINSSTGLI SGTASTAGTY QVTVTAKDST GASGSTSFTW TVGSGGGGCT
     SSQLLANPGF ESGSTGWSAT SGVITNDTGE AAHGGSYYAW LDGYGSSHTD TLSQSVTIPA
     GCKATLTFYL HIDTAETTTS TAYDKLTVTA GSTTLATYSN LNHNSGYAQK SFDLSSFAGS
     TVTLKFNGVE DSSLQTSFVV DDTALTTS
//
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