ID A0A0D1Z0B2_9EURO Unreviewed; 836 AA.
AC A0A0D1Z0B2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein B {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV11_07903 {ECO:0000313|EMBL:KIV80403.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV80403.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV80403.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV80403.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN846953; KIV80403.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1Z0B2; -.
DR STRING; 1016849.A0A0D1Z0B2; -.
DR HOGENOM; CLU_012383_1_0_1; -.
DR OrthoDB; 2961161at2759; -.
DR Proteomes; UP000053599; 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; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
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; 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:UP000053599};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..836
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002252337"
FT TRANSMEM 712..733
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 274..493
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 518..608
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 743..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 431
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 836 AA; 89238 MW; BE616CFC7CDCE6FD CRC64;
MRLLQQFATI AVSCLFLIFG ADAHSKSRNP LNYLSLLENP RIHTPSQRVH VSSHFDLTFD
LHRSSEHIRL SLEPNHDIVH EDSYIEYLDQ NGNVKHAEKM QREDYKVYQG KSFLVDEDGL
STNVGWARIV VRRDGIRPLF EGAFTVMGNH HHIQMKSTYT ATKHLLDPEL DDDEDEYMAV
WRDSDVSRQS RRDLKRDAGL TCASDRLAFN TDPAHPIFQD LVLKRDDGYW GSMTLTNLLG
KRQSIDGGGA GNGNSAGVSL KSTIGSTAGC PTTRKVALIG AATDCTYTAS FNSTDTVRQH
VITQVNTASD LYQSTFNITL GLRNMTVSDA ACPGTASSTT PWNLDCTGNN QTMDSRLNLF
SAWRGERGDS NAYWSLFTTC STDAEVGVAW LGQLCNTGST SQQDTSGTSQ SVTGANVVAK
TSTEWQVFAH ESGHTFGAVH DCDSSTCADA NTVNSGQCCP LSGSTCDANA QYMMNPYASS
SISTFSPCSV GNICSALGRN SVQSGCLTDN KGVVTITGNQ CGNGIVEEGE DCDCGGTEGC
AGNTCCDATT CKFNSGAVCD PANEGCCTTS CQFSSSGTVC RASTGSCDPQ EVCSGTNGTC
PADSTAKDGT SCTSGNSTGL ACASGQCTSR NLQCKTLMGS YTSDNDTYAC DSGSCTISCA
SPSFGANVCY SMQQNFLDGT PCNGDGKCEN GVCSGSTVGG EVKSWIDNNK TLVIALASAL
GGIILLAILG CCVRACRRRK QPKYNGNGRR RGAAAATSAP RGWNGPAIPP QMRARQYGNS
WQTSPIQTQQ PQQEWAPPQP SMMQSDQNWY PSTPAPAYAS WVTGARPKPP NSVRYA
//
