ID A0A2S6C2D9_9PEZI Unreviewed; 844 AA.
AC A0A2S6C2D9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Disintegrin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CBER1_04595 {ECO:0000313|EMBL:PPJ53902.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ53902.1, ECO:0000313|Proteomes:UP000237631};
RN [1] {ECO:0000313|Proteomes:UP000237631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT mechanisms and extends production to the genus Colletotrichum.";
RL bioRxiv 0:0-0(2017).
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:PPJ53902.1}.
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DR EMBL; PNEN01000574; PPJ53902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6C2D9; -.
DR STRING; 357750.A0A2S6C2D9; -.
DR OrthoDB; 2961161at2759; -.
DR Proteomes; UP000237631; 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; 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:UP000237631};
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..844
FT /note="Disintegrin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015676907"
FT TRANSMEM 721..743
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 279..507
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 532..621
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 752..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..828
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 445
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"
FT BINDING 448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 454
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 844 AA; 90580 MW; EB3249841871C40B CRC64;
MRCQLPFSLL AYAASTLLSA SASSTTRNPI GAISTIQNAT IHTPNHRVTA LHEFDLTFAV
RDELHVRFHL EPNHDILPEG ATISYVDEDG TIFRHEIVDR LAHKVYRGTA WIQKLGNEVD
EWRHVGWARA SIMKDGREPI FQGAFSIERD AHHVQTSRNY MRTRHLDDPV IEAGDEHSMV
MWRDSDILRD FQALGHQELK RDAVPEPICQ ADTLGFNTRD DHPVFMAMKS KRSESRYGRM
DFAHLFGKRQ DLDGMTGGNS AGGNLIASLG STAGCPTTRK VALMGVATDC TYTSDFEDEQ
AARENVIDQV NRASAIYENT FNISLGLQNL TVFPANCPGT PVAASEFNQQ CSDSVDVSNR
LNMFSRWRGT QTDSNAFWTL LSSCGTGSAV GLAWLGQACV GTTITTNGSV TGDGQSNGGG
QESVTGANVV IRTNGASEWQ IIAHEVGHTF GAVHDCTSSS CQNAEFVRSQ QCCPLDANNC
PAGGRYIMNP QTSDGVTEFS PCSVGNICSA LLRNSVNGEC LTDNRGVTTI SGQQCGNGIV
EPGEDCDCGG EEGCRDDPCC NPTTCEFTSG SVCDDSNEDC CRNCQFASAG TVCRSSTGQC
DPEETCSGSS ATCPEDQTQE DGTSCGDGLE CASGQCTSRN QQCRTVMGSY TQNNDTYACD
SQGCLIRCAS PEFGRNVCYS LQQNFIPGTP CGGGGRCAQA GQCRGATTGG QIKSWIEDNK
AIVIGVASAV GGLILFAVLG CLYRCCKRGG RRRKAPVAPR PPPGGWQGWN GPNNNNNNRG
GPPPMQHSNS FYAPSSHPSQ GWATSNQNAG GWDAPPVPPP PSYHQAGSPP PPMQNQRSNS
VRYA
//
