ID G4T620_SERID Unreviewed; 617 AA.
AC G4T620;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=PIIN_00425 {ECO:0000313|EMBL:CCA66744.1};
OS Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS (Piriformospora indica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Sebacinales; Serendipitaceae; Serendipita.
OX NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA66744.1, ECO:0000313|Proteomes:UP000007148};
RN [1] {ECO:0000313|EMBL:CCA66744.1, ECO:0000313|Proteomes:UP000007148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA66744.1,
RC ECO:0000313|Proteomes:UP000007148};
RX PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA Kogel K.H.;
RT "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT the Mutualistic Root Symbiont Piriformospora indica.";
RL PLoS Pathog. 7:e1002290-e1002290(2011).
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}.
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:CCA66744.1}.
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; CAFZ01000005; CCA66744.1; -; Genomic_DNA.
DR AlphaFoldDB; G4T620; -.
DR eggNOG; ENOG502QTDC; Eukaryota.
DR HOGENOM; CLU_012703_4_2_1; -.
DR InParanoid; G4T620; -.
DR OMA; VIWHEIT; -.
DR OrthoDB; 2786251at2759; -.
DR Proteomes; UP000007148; 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; 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:UP000007148};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU364017};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601842-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|RuleBase:RU364017}.
FT DOMAIN 44..93
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 110..173
FT /note="PepSY"
FT /evidence="ECO:0000259|Pfam:PF03413"
FT REGION 559..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 361
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-1"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
SQ SEQUENCE 617 AA; 66188 MW; EC8DA5792B7691B4 CRC64;
MRPIATFVTY GAGVESPLKK RGQVASIEDS AISFVEEQLN ISKDGFRVRS SASTESGGHV
WVQQVVNGIP VANAVGSVGF NKAENVVAFS SNFGGNSLVP QQVASPTPRL SKEQAITAAE
KKLNGKSNKK VPTLEYVVKS DGSLVLTWVV EVQTADGNHW FEAFVDASNG DIASTNDFVA
DASYWAVDPQ VQDVTKGYNN YVDPADTGAS PNGWHTVGST TSTDTSGNNV VSYKGSTSAT
TQQSSSGQVF NYKYDTSVGP TSGQNVDAAR VNAFFISNKI HDINYRYGFT EKTFNFQNDN
FGKGGSGNDR IKISVQDSSG TNNANFATPA DGSSGQMRMY IWTRTTPNRD GDLSNDVIAH
EQTHGTTNRM TGGGTGRCLQ TTEAGGMGEG WSDAFAEWLE HKDSSVPDWV LGVWVYNNPK
GIRSYPYSTS TSTNPYKYST TKTKSEVHDI GEIWANMLHN VYAELVGSFG WAADAFTNAE
SGSGNVVFLR VFYAALLLQP CNPTMVQARD AWVQADQNLY NGAHVCSIWK AFASRGLGVG
AANYVDSFTV PSQCSGGSTT VSTASQTRTV TSSSTRSSPS STRQTTTMSS SVPSCPWWWW
PFCDFAANAD VAGPTAL
//
