ID A0A0D1YKZ9_9EURO Unreviewed; 817 AA.
AC A0A0D1YKZ9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein B {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV08_05761 {ECO:0000313|EMBL:KIW15711.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW15711.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW15711.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW15711.1,
RC ECO:0000313|Proteomes:UP000053328};
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 spinifera CBS89968.";
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; KN847495; KIW15711.1; -; Genomic_DNA.
DR RefSeq; XP_016235927.1; XM_016380100.1.
DR AlphaFoldDB; A0A0D1YKZ9; -.
DR STRING; 91928.A0A0D1YKZ9; -.
DR GeneID; 27332844; -.
DR VEuPathDB; FungiDB:PV08_05761; -.
DR HOGENOM; CLU_012383_1_0_1; -.
DR OrthoDB; 2961161at2759; -.
DR Proteomes; UP000053328; 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:UP000053328};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..817
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002237153"
FT TRANSMEM 712..733
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 275..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..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..786
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 817 AA; 87734 MW; 018DCDF584DCEAE1 CRC64;
MRFLHRLALL ASSILLFSFG EGHSQSRNPL NYLSLIENPR IHTPSQRVHA TSHFDLTFDL
HKHSEHIRLS LEPNHDIIHD DSYVEFVDKD GIVRHAEKMQ RGDFKVYQGK SFVVDEDGLS
TNVGWARVVV RRDGVRPLFE GAFTIMGNHH HIQMKSTYMA TKHLQDPHLE DEEDEYMAVW
RDTDVSRQPH RDLRRSAAAD LTCASDKLPF NTDPEHPLFR DLKLKKEEGY WGSMPLSHLF
GKRQNIDGGG AGNGNSAGVN LKDSIGSTAG CPTTRRVALI GVATDCTYTA SFNSTDSVRQ
NIITQVNTAS DLYQSTFNIT LGLRNLTVSE AECPATAAAQ TPWNVGCSGS TDMTARLNLF
SQWRGQRGDS NAYWSLFTTC NTGAEVGLAW LGQLCNSGAT SQQDTSGTSQ SVTGANVIAK
TSTEWQVFAH ESGHTFGAVH DCDSSTCGDA NTVNSGQCCP LSSSTCDANA QYMMNPYSSP
GITRFSPCSI GNICSALGRN SVQSGCLTDN KGVVTITGNQ CGNGIVEEGE DCDCGGAEGC
SGNSCCNPDT CKYNTGAVCD PSNEGCCTSQ CQFASANTIC RASTGVCDPQ ETCSGTNGTC
PTDTTAPDGT SCNSGNATGL HCASGQCTSR DLQCKTLMGD YTSTNDTYAC NSQTCIISCG
SPDFGANVCY SMQQNFLDGT PCGGDGKCRN GVCRGSTVGG EVRSWIDHNK TLVIALASAL
GGLLLLAVLG CCVRACRKPR AKQMVAGAPR QRNRPPRGWD GPPVPMQMQS RGYGQGNWDS
TPQAPPPTYW ANQPPQNHWP QGGGYDNGNR GASVRYA
//
