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Database: UniProt
Entry: A0A094C950_9PEZI
LinkDB: A0A094C950_9PEZI
Original site: A0A094C950_9PEZI 
ID   A0A094C950_9PEZI        Unreviewed;       799 AA.
AC   A0A094C950;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Disintegrin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=V496_09220 {ECO:0000313|EMBL:KFY50696.1};
OS   Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY50696.1, ECO:0000313|Proteomes:UP000029302};
RN   [1] {ECO:0000313|EMBL:KFY50696.1, ECO:0000313|Proteomes:UP000029302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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:KFY50696.1}.
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DR   EMBL; JPJY01001808; KFY50696.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094C950; -.
DR   STRING; 1420909.A0A094C950; -.
DR   HOGENOM; CLU_012383_1_0_1; -.
DR   OrthoDB; 2961161at2759; -.
DR   Proteomes; UP000029302; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd04271; ZnMc_ADAM_fungal; 1.
DR   Gene3D; 3.40.1620.60; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR034028; ZnMc_ADAM_fungal.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF159; MIND-MELD, ISOFORM J; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF13688; Reprolysin_5; 1.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029302};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..799
FT                   /note="Disintegrin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001898363"
FT   TRANSMEM        711..733
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          280..497
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          522..614
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   ACT_SITE        435
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         434
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         438
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         444
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   799 AA;  83948 MW;  682BC722BF0D3FB3 CRC64;
     MRLLRCVAAA IVSAGFSHIA QAHSVKRAPL SYLSIVDEPV IHTPSHRVHA HSSFDLSFHL
     HGRQQYIKLT LDPNDDVIAE GATVNYIGAD GQVREVELIE RTDHRVFKGH AWVRTHEDTQ
     WTHAGWARVV IHRDGVDPLF EGAFRIDGNH HHIHPRNSYI ATKHELDPYV EDDREDIMVV
     WRDSDITPDD SSRGELKRDV NTGSCLSDDL AFNLMPEHPV YSQGYSQSTI LRKGESFWGS
     ISTGSIFGRD IDPASTMPGN GAGVNLLNSI GNPDGCPTSR KVALVGIATD CTYTGFFNST
     SSVRSNIITQ MNSASVLYED SFNISLGIQN LTITDAACPG ASQANTPWNR DCNSGLQIQD
     RLNLFSAWRG ASPDTNAYWT LLTTCGTGSA VGLAWLGQAC VNTAQASSQE GSNDTVSGAN
     VVVKTDTEWL VIAHEVGHTF GAVHDCDSTT CADGKTVAAQ QCCPLSADSC PAGGKFVMNP
     STSSGITNFS PCSIGNICSA IGGQSVKTHC LTSNRNVPTI TGSQCGNGIV EMGEDCDCGG
     ESGCGDNPCC NPTTCKFKTE NNAVCDPSNE DCCLSTCQFA TAGTVCRAST GECDPQETCS
     GTAASCPADA HKDEGSGCGA DGEGLSCASG QCTSRDKQCK TLMGPQYYQC SDDGCQLFCA
     SDASQFTCDG LTQNFLDGTK CGGGGKCSNG VCKGSSVAGR IKEWVDQHKP LVIGLSAGVG
     GLLLLAILSC IFSSCKRRRR ARKYVPGGAM PPGNGRGEWE GGAGVGAAGA GEGVCACADA
     AGDAAARDGR AADGRAAAV
//
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