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Database: UniProt
Entry: M5CE93_THACB
LinkDB: M5CE93_THACB
Original site: M5CE93_THACB 
ID   M5CE93_THACB            Unreviewed;       490 AA.
AC   M5CE93;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Extracellular metalloproteinase {ECO:0000256|RuleBase:RU364017};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU364017};
DE   AltName: Full=Fungalysin {ECO:0000256|RuleBase:RU364017};
GN   ORFNames=BN14_11656 {ECO:0000313|EMBL:CCO37500.1};
OS   Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS   rot fungus) (Rhizoctonia solani).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX   NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO37500.1, ECO:0000313|Proteomes:UP000012065};
RN   [1] {ECO:0000313|EMBL:CCO37500.1, ECO:0000313|Proteomes:UP000012065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065};
RX   PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA   Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA   Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA   Schlueter A.S.;
RT   "Establishment and interpretation of the genome sequence of the
RT   phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL   J. Biotechnol. 0:0-0(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601842-2};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR601842-2};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU364017}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family.
CC       {ECO:0000256|RuleBase:RU364017}.
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:CCO37500.1}.
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DR   EMBL; CAOJ01017210; CCO37500.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5CE93; -.
DR   HOGENOM; CLU_012703_4_2_1; -.
DR   Proteomes; UP000012065; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.170.10; -; 1.
DR   InterPro; IPR025711; PepSY.
DR   InterPro; IPR001842; Peptidase_M36.
DR   PANTHER; PTHR33478; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR   PANTHER; PTHR33478:SF1; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR   Pfam; PF03413; PepSY; 1.
DR   Pfam; PF02128; Peptidase_M36; 2.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU364017, ECO:0000313|EMBL:CCO37500.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601842-2,
KW   ECO:0000256|RuleBase:RU364017};
KW   Metalloprotease {ECO:0000256|RuleBase:RU364017};
KW   Protease {ECO:0000256|RuleBase:RU364017};
KW   Secreted {ECO:0000256|RuleBase:RU364017};
KW   Signal {ECO:0000256|RuleBase:RU364017};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601842-2};
KW   Zymogen {ECO:0000256|RuleBase:RU364017}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU364017"
FT   CHAIN           21..490
FT                   /note="Extracellular metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU364017"
FT                   /id="PRO_5009368178"
FT   DOMAIN          152..217
FT                   /note="PepSY"
FT                   /evidence="ECO:0000259|Pfam:PF03413"
FT   BINDING         223
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
SQ   SEQUENCE   490 AA;  52977 MW;  F9D9760EA978E11A CRC64;
     MVLITRFAIL AFLTAQCVLA APWKEPRCWT THSVRSIGPT GSQFKSYHPK PIFESYGVDG
     IVHPLAKRDI SGTNEEAAKA FLEEKFGIEV QELSHKSGHS STNVANEYFK QVINNITVAN
     AVANVALKGQ KVVSFGASFV KPKRVAAATP ELTEEDAISK AEDAIGGKYN TLPTSVEYFA
     KDSGDVVLTR VVQVQNDDTD EWYEVFVDAN SGEIVNVISF VAHAKYRVIP FALQNPNDGF
     QVLSDPQDPI TSPDGWHRYR LNFSNTTVIT NATSGNNAHV YKSSVAEGLT GQNSAPDVNV
     YEHTFDPSKE PSGNKDAASV NVFYLANMIH DLLYHYGFIE SSYNFQYYNY GKGGSGNDPV
     YISVQDGGKT NFNNANFATP PDGANAGEVW ANIGHEIYAA LVAKSGLSTD KKSVSSTAGN
     VVALHLLIDA LATQPCNPTF ISARDAIIQA DANRYGSANK CTLWNAFAKR GLGLGATMTK
     VDSKTLPSGC
//
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