ID G4TUS3_SERID Unreviewed; 603 AA.
AC G4TUS3;
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_09051 {ECO:0000313|EMBL:CCA75066.1};
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:CCA75066.1, ECO:0000313|Proteomes:UP000007148};
RN [1] {ECO:0000313|EMBL:CCA75066.1, ECO:0000313|Proteomes:UP000007148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA75066.1,
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:CCA75066.1}.
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DR EMBL; CAFZ01000393; CCA75066.1; -; Genomic_DNA.
DR AlphaFoldDB; G4TUS3; -.
DR eggNOG; ENOG502SIXN; Eukaryota.
DR HOGENOM; CLU_012703_4_2_1; -.
DR InParanoid; G4TUS3; -.
DR OMA; SKFATHR; -.
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; 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; 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, 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..19
FT /evidence="ECO:0000256|RuleBase:RU364017"
FT CHAIN 20..603
FT /note="Extracellular metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU364017"
FT /id="PRO_5009366861"
FT DOMAIN 90..138
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT ACT_SITE 408
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-1"
FT BINDING 407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
SQ SEQUENCE 603 AA; 64592 MW; 3C9A10566EC0FD14 CRC64;
MVLFSKLALA AASIAAVSAA PWEPSVKLST HRPRAVSDDL TVESFHPTNI YETYGTGVTT
PLKKRGEPSG SIEQSAASFV EEKLQLSSGE YNIRSSANTE TGGSVWIQQL VNGIPVANAV
ANVALNKNED VVAFGANFHG TSVSRRAANV APPTPTISKE QAITSAERKL HGKHNDKAPT
LEYYVKQDGS LALTYVVEVQ TADGNHWYEA FVDASNAQIV ATNDFVAGAS YVAVDPQVQD
ITKGYNTYTN PADTVASPNG WHQVGSTVST DTSGNNVISY KGSTTGTTKQ SASGQVFNYK
YDTSVGPTSG SNVDAARVNA FFIANKIHDI NYRYGFTEKT FNFQNDNFGK GGSGNDRIKI
SVQDSSGTNN ANFATPADGS SGQMRMYIWT RTTPNRDGDL SNDVIAHEQT HGTTNRMTGG
GTGRCLQTTE AGGMGEGWSD AFAEWLEHKD SSVPDFVLGV WVYNNSKGIR NYPYSTSTSV
NPLKYSSVAS LNEVHNIGEV WANILHNVYA QLVGSYGFAA DAFTNPDSSA GNVVFLRLFY
DALLLQPCNP TMVQARAAWI QADTNRYSGK HACTLWKAFA SRGLGSGAVS GTYRDSTTVP
SGC
//
