ID M7UA00_BOTF1 Unreviewed; 862 AA.
AC M7UA00;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Putative adam 8 protein {ECO:0000313|EMBL:EMR90579.1};
GN ORFNames=BcDW1_818 {ECO:0000313|EMBL:EMR90579.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR90579.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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; KB707697; EMR90579.1; -; Genomic_DNA.
DR AlphaFoldDB; M7UA00; -.
DR STRING; 1290391.M7UA00; -.
DR HOGENOM; CLU_012383_1_0_1; -.
DR Proteomes; UP000012045; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT TRANSMEM 742..763
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 308..525
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 550..640
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 18..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..43
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..862
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 463
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 462
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 466
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 472
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 862 AA; 91433 MW; 102761EBE0D84841 CRC64;
MEKIKFIHRS KISGLKDWKD KLQGLEEEEE EEEEEEEDAA AAAAAAEEDS HSNERNPLTY
ISKVETPIIK TPSHRVHALS SFDVEFGLHG GQQRVKLSLK PNHDVIAEGA TITHLAADGT
VRTSETIDRS AHRVFKGSTW LQPYDGADWT NVGWARIIVK KDGDEPLFEG AFKLDGDHHH
IQTKTSFKST RHALDPSPPD EEKEYMVVWR DSDIGTGYTE DNEGLMHPDL RRSAREGPSC
SADGLNFNTM NNPINNYEPM AKREEGFWGS ISTRAIFGRQ LDTQSGGNSA GVNLATTIGS
TAGCPSTRKV ALVGIATDCT YTAAFNSTET ARENVIQILN SASVQYEDSF NITLGLQNLT
VSDAACPATA SSSAPWNVGC SDSVTIQDRL NLFSAWRGER QDTNAYWTLL STCGTGSAVG
LAWLGQACVT GAQVASTSSG NETVSGANVV VRTSTEWQVL AHETGHTFGA VHDCTSSTCN
DGQTVAAQQC CPLSSTTCDA GGAYIMNPST SSGITQFSPC SIGNICSAIG RNGVKTNCLT
ANRDITIITA SQCGNGIVES GEDCDCGGTS GCGSNSCCDP TTCKFRTNAV CDPSNEDCCT
STCQFASSGT VCRASTGVCD PQEVCSGTAA TCPVDATAPD GTSCGNSSSL SCASGQCTSR
DLQCKTIMGS YTTGNDTYAC SSSGCQISCA SPEFGSHVCY SMQQNFLDGT SCQGGGKCSN
GDCKGASVSK EITSWIQEHR NLVIGIASAV GALLIFAILS CCIGRMRRRR AIRLAKERAV
SNPHGWSQGP NMWQAPLSGA RGGRGAAAPS GGTWVDGRWI QPPPPGWQPS ARGTLRLSEE
SEESEESEES EESEESEESV SD
//
