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Database: UniProt
Entry: R7SQX5_DICSQ
LinkDB: R7SQX5_DICSQ
Original site: R7SQX5_DICSQ 
ID   R7SQX5_DICSQ            Unreviewed;       601 AA.
AC   R7SQX5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-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=DICSQDRAFT_110674 {ECO:0000313|EMBL:EJF58150.1};
OS   Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Dichomitus.
OX   NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF58150.1, ECO:0000313|Proteomes:UP000053319};
RN   [1] {ECO:0000313|EMBL:EJF58150.1, ECO:0000313|Proteomes:UP000053319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF58150.1,
RC   ECO:0000313|Proteomes:UP000053319};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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; JH719439; EJF58150.1; -; Genomic_DNA.
DR   RefSeq; XP_007369112.1; XM_007369050.1.
DR   AlphaFoldDB; R7SQX5; -.
DR   GeneID; 18833931; -.
DR   KEGG; dsq:DICSQDRAFT_110674; -.
DR   HOGENOM; CLU_012703_4_2_1; -.
DR   OMA; AKLVYIQ; -.
DR   OrthoDB; 2786251at2759; -.
DR   Proteomes; UP000053319; 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|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU364017}; Protease {ECO:0000256|RuleBase:RU364017};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053319};
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..23
FT                   /evidence="ECO:0000256|RuleBase:RU364017"
FT   CHAIN           24..601
FT                   /note="Extracellular metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU364017"
FT                   /id="PRO_5009369314"
FT   DOMAIN          105..140
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   REGION          250..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        407
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601842-1"
FT   BINDING         406
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
FT   BINDING         410
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
FT   BINDING         435
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
SQ   SEQUENCE   601 AA;  64970 MW;  6D9BB4AF1E5DB10C CRC64;
     MFSFSKVFAS VFLAVLCAST ATAVPYPASS KYATHRTREI SPALKIETYH PLSSYETFGE
     GIDHPLSKRA DASLEDSAVA FVQSRHQLDS DAVHVRSSFE SDSARHVYVK QQHNGIPFAN
     AVANVALNKD NKVVAFGSSF VKFSKIADST PAVAVEDAIA TAEAQLNGKF DTENFPEPTL
     QYFVKEDDSA VLVHAFQVRN EGAGTWYQAY VDAHTGELVS ITDFVNKASY YVLPIWKEYP
     TDGFATITDP QDTTSSPQGW HNDGSKSYTT TSGNNAIAYK SSTSSTTSES SSGLVFNYPA
     ALSKAPTTTA NVNAARVNAF YVVNSVHDIH YKYGFTESAY NFQTSNFGKG GKGGDRVTIS
     VQDSAGTDNA DFSTPPDGQS GHMRMFLWDE TSPERDGALE NDIIAHENTH GLTNRMTGGG
     TGECLQTDEA GGMGEGWSDA FAEWLTHTDD SVPDFIMGAY VINDSAGIRN YPYSTSAKTN
     PLRYSSIATL DEVHNIGEVW ANLLHNVYAA LVGEHGFSST ARTDPSGTEG NVVFLHLFID
     ALALQPCNPT FPTARDAWIQ ADANRYGGAN KCLLWKAFAS KGLGVNAKNY KDDTTVPSDC
     S
//
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