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Database: UniProt
Entry: A0A2H5BCJ5_9ACTN
LinkDB: A0A2H5BCJ5_9ACTN
Original site: A0A2H5BCJ5_9ACTN 
ID   A0A2H5BCJ5_9ACTN        Unreviewed;       823 AA.
AC   A0A2H5BCJ5;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Peptidase M60 domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Precursor;
GN   ORFNames=CFP65_7539 {ECO:0000313|EMBL:AUG82113.1};
OS   Kitasatospora sp. MMS16-BH015.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=2018025 {ECO:0000313|EMBL:AUG82113.1, ECO:0000313|Proteomes:UP000239175};
RN   [1] {ECO:0000313|EMBL:AUG82113.1, ECO:0000313|Proteomes:UP000239175}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS16-BH015 {ECO:0000313|EMBL:AUG82113.1,
RC   ECO:0000313|Proteomes:UP000239175};
RA   Kim S.B., Yun B.-R.;
RT   "Genome sequence of Kitasatospora sp. MMS16-BH015.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP025394; AUG82113.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H5BCJ5; -.
DR   KEGG; kit:CFP65_7539; -.
DR   OrthoDB; 3177623at2; -.
DR   Proteomes; UP000239175; Chromosome.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd00161; RICIN; 2.
DR   Gene3D; 2.80.10.50; -; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.60.120.1250; Peptidase M60, enhancin-like domain 1; 1.
DR   Gene3D; 3.40.390.80; Peptidase M60, enhancin-like domain 2; 1.
DR   Gene3D; 1.10.390.30; Peptidase M60, enhancin-like domain 3; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR042279; Pep_M60_3.
DR   InterPro; IPR031161; Peptidase_M60_dom.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   Pfam; PF13402; Peptidase_M60; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 2.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM01276; M60-like; 1.
DR   SMART; SM00458; RICIN; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 2.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS51723; PEPTIDASE_M60; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 2.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239175};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..823
FT                   /note="Peptidase M60 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014124620"
FT   DOMAIN          320..404
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          449..749
FT                   /note="Peptidase M60"
FT                   /evidence="ECO:0000259|PROSITE:PS51723"
FT   REGION          304..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          431..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   823 AA;  86231 MW;  D1BAF31C90F5E5FC CRC64;
     MPSPATLRTA ASLALSALLL PLTGAPPALA HPPGRAGGTW SELRVLGQCL TARDSQEVRL
     RSCSSELGEP TPAGQRWQLD GQGTLRSALP GSLALGLPPG ATAANGARLA AVPEATASGA
     WSYDSATGHL VWRGGGYTLD FNTGTDLATL WTAGTGDNQK WSFDPGYTAT TAPSGADAAE
     LRTEGQCLTL SQVTTPNRSV TVEPCASTAG RPTPATQRWT VTAQGQVQSS AAPYPVLDVQ
     GDPGSRYVVA RPVGNGTDRS RWQYDPTAHT LLWAADPTLA LDHSRTTAFA GLYRSHGGPN
     QLWTQSPVAD QAGPARTQAA PGPVSATATS PADATLRWTA PTGPAPATYA VYQDGGRIAL
     TYSTSYQDPG LGPGGLHRYR VTAISADGVE SAPSAETVLT APACPRPTGP DGTAPFLPPV
     AGQPYTLTLT GRPSAQREQQ RQGLRQLPSD IRPTGLYLPP DALLTATTTG AAGTGALSVL
     IGPPVGAGGL AAARRYPIVT TGTGTRITDH RGGMVHLVFD GAPTDRVTLT LSGDTQLAPV
     FVLGSSTPDQ WRADLAARPT RYAELLAGRT VVTLSRDSAA RYAYSSPEAV LRHLECARAV
     EDAVNGLAAP TAEDATTAPG PDSPGVFPFH YVEVERRVGG AFATDRYMGF KDESVAWLAD
     SAAAEWGVWH EQGHHRQQSA ITPTELIEVS NNIDSQSLRT AYARPSRLVT QGSYDTALPK
     LGKPGVAYAT SFDGFEQLVM LQQLALQYGA GFWPEVRHRV RTTPPTDPDR WAAIAVLTSQ
     VAGQDLTAFY LAWGVPLTTH AQQAVAALRL PSAPGDLTTR REP
//
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