ID W9CP77_SCLBF Unreviewed; 1133 AA.
AC W9CP77;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Peptidase M16 inactive domain-containing protein {ECO:0000313|EMBL:ESZ97818.1};
GN ORFNames=SBOR_1827 {ECO:0000313|EMBL:ESZ97818.1};
OS Sclerotinia borealis (strain F-4128).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=1432307 {ECO:0000313|EMBL:ESZ97818.1, ECO:0000313|Proteomes:UP000019487};
RN [1] {ECO:0000313|EMBL:ESZ97818.1, ECO:0000313|Proteomes:UP000019487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-4157 {ECO:0000313|Proteomes:UP000019487};
RX PubMed=24459262; DOI=10.1128/genomeA.01175-13;
RA Mardanov A.V., Beletsky A.V., Kadnikov V.V., Ignatov A.N., Ravin N.V.;
RT "Draft genome sequence of Sclerotinia borealis, a psychrophilic plant
RT pathogenic fungus.";
RL Genome Announc. 2:E0117513-E0117513(2014).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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:ESZ97818.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYSA01000068; ESZ97818.1; -; Genomic_DNA.
DR AlphaFoldDB; W9CP77; -.
DR STRING; 1432307.W9CP77; -.
DR MEROPS; M16.008; -.
DR HOGENOM; CLU_004639_1_2_1; -.
DR OrthoDB; 129328at2759; -.
DR Proteomes; UP000019487; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR032632; Peptidase_M16_M.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000019487};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 55..205
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 231..410
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 417..706
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 710..891
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1133 AA; 128984 MW; F383CEA9F713C8C9 CRC64;
MANLPQPQST IAPDSPLREQ REHHRLVERL TDRLETPSLD DRSYRVIKLP NQLEVLLVHD
AETDKASAAM DVNVGNFSDP EDFPGMAHAV EHLLFMGTKK YPVENAYSQY LSSHSGSSNA
YTGATSTNYY FEVAAKSGED GDSEDANLSP LYGALDRFAQ FFIDPLFLDS TLDRELKAVD
SENKKNLQSD QWRLHQLDKS LSNPKHPYCH FSTGNLEVLK IQPESRGINV REKFMEFHEK
HYSANRMKLV ILGGEPLDKL ESWAADLFAG VRNKDLPQNR WEDEQPYGPE QLSTQCFAKP
VMDSRTLDIS IPFIDEELLF ESQPSRYLTH LIGHEGPGSI MAYIKSKGWA NALSAGVYEI
CPGTPGLFSC QIRLTEDGLK NYKEVVKVFF QYIALLKDTP PQEWIFDEQK GLADVDFKFK
QKTPASRFTS KISAVMQTPL PREWLLSGHS RLRKFDGERI SAGLDCLRAD NFRMAISSQT
FPGGWDSKEK WYGTEYKYEK IPADFLEEIK KAASSKKGER FPELHLPHVN QFIPTKLEVE
KKEVQTPAIS PKLIRNDDSV RTWFKKDDTF WVPKANLFMQ CRNPLPMATA ENSLKARMYT
DLVYDALEDY AYDAELAGLE YSVSSHSMGL EISVSGYNDK LPVLLEKVLT TMRDLEVKED
RFEIIKERLT RGLKNWDFQQ PYNQVGDYMR WLSSEKGYIN EQYLAELSHV TVADIQQFYP
HLLRQMHIET FVHGNLYKED ALKLADLTES ILKPRVLPQT QWPIGRALVF PPGANFVYHK
TLKDPANVNH CIEYVLSIGD KAVRPQRAKA LLLDQMTHEP AFDQLRTKEQ LGYVVFSGCS
TTTTTIAYRF IIQSEKTPQY LEERIDSFLV GYAEILKNMS DSEFEGHKRS LVTKRLEKLK
NLDQESNRLW SHIDYEYFDF ELVHHDAANV KALTKEDMVQ FYDQFILPSS PLRSKLAIHL
IAQGISLPEE KPEEQTVLAV NKDRKDAEDG EAVAVKVEGN GTVPYVITDV RQFKSMLQVT
AGPQPVKHIK YKYFENLPRK FQGWDCGRVG GAEEGGVLVV DVVDNGFDLG VWEDERWEVK
GMGEVRGERW MGDGREKGDG MGTLERGGEG RGRMAEGEGD AVWGSVEMGG GGI
//
