ID A0A165ZRH5_EXIGL Unreviewed; 593 AA.
AC A0A165ZRH5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=EXIGLDRAFT_263332 {ECO:0000313|EMBL:KZV85209.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV85209.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV85209.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV85209.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU364017}.
CC -!- SIMILARITY: Belongs to the peptidase M36 family.
CC {ECO:0000256|ARBA:ARBA00006006, ECO:0000256|RuleBase:RU364017}.
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DR EMBL; KV426196; KZV85209.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165ZRH5; -.
DR InParanoid; A0A165ZRH5; -.
DR OrthoDB; 2786251at2759; -.
DR Proteomes; UP000077266; 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 CDD; cd09596; M36; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 3.10.450.40; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR025711; PepSY.
DR InterPro; IPR001842; Peptidase_M36.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR33478; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR PANTHER; PTHR33478:SF1; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF03413; PepSY; 1.
DR Pfam; PF02128; Peptidase_M36; 1.
DR PRINTS; PR00999; FUNGALYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU364017};
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 Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU364017};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364017};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601842-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|RuleBase:RU364017}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU364017"
FT CHAIN 21..593
FT /note="Extracellular metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU364017"
FT /id="PRO_5009361784"
FT DOMAIN 100..135
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 147..213
FT /note="PepSY"
FT /evidence="ECO:0000259|Pfam:PF03413"
FT ACT_SITE 400
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-1"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
SQ SEQUENCE 593 AA; 63424 MW; D16A69529BBFF21A CRC64;
MKFTSGFLAV AFMIASGALA APWPSSSKHA THRLRSLPNG KRVLAFHREP TFETFAEGIE
HVAEKRAPGD WKALGLSFLE SRLGAGSLHQ TSSFTNDVAS HVFVQQSVKG IPVVNAVANV
ALNKGEKVVS FGHTFVTPKT ISSTTPKLTA AEAIARAEEQ LSGTHDGTPT KIEFVFTEND
HLALVHTVQV ESNDNGHLLE SFIDAATGEV VQVHDFTNSI TYRVLPIRKQ APTEGFEVLT
DPADLTASPN GWQQVPGSTA TTTTSGNNAI AFKTSQTTGL SSENVSNGFQ FVWNSTAQPT
VSPNIDVARV NAFYIVNTIH DITYRYGFTE SAFNFQQNNN GKGGAANDRV TISVQDSAGT
DNADFTTPAD GQSGRMRMFL WDFTNPRRDG AIENDIVAHE NTHGLSNRLT GGGTGRCLQT
TEAGGMGEGW SDAFADWTEQ AGPTIRDFTM GAFVISDSAG IRSHPYSTST TTNPLNYGSI
KTLNEVHDIG EAWANILHNV HAALITAHGF STDAFTNPNG TGGNVVFLHL LIDALALQPC
NPTFLTARDA WIQADVNRFA GANKCTLWKA FASRGLGVNA ANHTNNAAVP AGC
//
