ID A0A167DDS1_9ASCO Unreviewed; 879 AA.
AC A0A167DDS1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein B {ECO:0008006|Google:ProtNLM};
GN ORFNames=AWJ20_1073 {ECO:0000313|EMBL:ANB12801.1};
OS Sugiyamaella lignohabitans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trichomonascaceae; Sugiyamaella.
OX NCBI_TaxID=796027 {ECO:0000313|EMBL:ANB12801.1, ECO:0000313|Proteomes:UP000189580};
RN [1] {ECO:0000313|EMBL:ANB12801.1, ECO:0000313|Proteomes:UP000189580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10342 {ECO:0000313|EMBL:ANB12801.1,
RC ECO:0000313|Proteomes:UP000189580};
RA Bellasio M., Peymann A., Valli M., Sipitzky M., Graf A., Sauer M., Marx H.,
RA Mattanovich D.;
RT "Complete genome sequence and transcriptome regulation of the pentose
RT utilising yeast Sugiyamaella lignohabitans.";
RL Submitted (FEB-2016) 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; CP014501; ANB12801.1; -; Genomic_DNA.
DR RefSeq; XP_018735278.1; XM_018877924.1.
DR AlphaFoldDB; A0A167DDS1; -.
DR GeneID; 30032835; -.
DR KEGG; slb:AWJ20_1073; -.
DR OrthoDB; 2961161at2759; -.
DR Proteomes; UP000189580; Chromosome a.
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 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; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
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:UP000189580};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..879
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007885145"
FT TRANSMEM 783..805
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 334..553
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 578..667
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 297..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..856
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 492
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 491
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 495
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 501
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 879 AA; 94641 MW; 68E5E8C48ADBF62E CRC64;
MPSWASLICL FISVHLALST SVDRLRPLSH LSSVSRISIE TDNHRVAADD PFTLTVEIPS
LNHLHNLRRR WWAITDPNEQ AFGFESEGLY SYLTRNESLV SGAPEVPEDV LQFKLVLEPN
TAVTSHQVVT TDEQGKIVPH PDFVEDSSST KARAFKGTAY RRVAFISPTT GNLIHQYRPV
GWARIVVHED GIDPIVEGAW KVDDEEGLGV PSSIYHLNRL EAMEQTLGNR YDEEYDLLDT
VDSRLVVWRD FDMRLSRTFT LSDKDFTRLT NHQKRDVDSF QTKGFLGDRV LSNIFPRASN
DSDTNNDTGG NSGFSSGANL QNSIGDTAGC PSPREVALMG IAADCNFLAG FNSSSEANSH
IINIVNTASH AFESAFNITL GLSQVYMVNI SQGCPDNPGG TKDAWNFNCS SSQNNNIGNR
LSLFSEWRGQ RSDDQLATWS LLTSCSQGSI VGISWLGMAC VSTASESGNN TFTAGTNVIS
RTSLDWRVLA HELGHSYGAV HDCDSDTCAQ NLEATSQCCP LSASSCDAGA QFLMNPVSSE
SQDSFSKCTQ GNVCGALGRN SVNSTCLTSN TGVKLVTSNE CGNGIVEEGE ECDCGGPEGC
GNNTCCDPLT CKFTAGSQCD PANESCCQDC KFASSTTLCR ASQGSCDPAE FCTGNSSTCP
PNVRAPNGQS CDAPGLTGQT CISGHCTSRD QQCVTLLGNS SVTSDGSVLN VTKACADDSS
CQLSCVDPRF GNTCFTTSQN FLDGTPCQGT GQCQRGNCVG GSGHSGPTFI TPFGEGWLQR
HQAVIIGIAA GLGGLFLASI LFAGIRRHFM HRRRIQNLIN SQKQPPPYPP MQPPPAYQMT
PIYRPPPPPP PPLPNSRGFI SADGTYMPRP PPTIPTNHY
//
