ADMB_ARTOC
ID ADMB_ARTOC Reviewed; 796 AA.
AC C5FUK3;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein B;
DE Short=ADAM B;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=ADM-B; ORFNames=MCYG_06406;
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480;
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- FUNCTION: Probable zinc protease. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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DR EMBL; DS995706; EEQ33587.1; -; Genomic_DNA.
DR RefSeq; XP_002844442.1; XM_002844396.1.
DR AlphaFoldDB; C5FUK3; -.
DR SMR; C5FUK3; -.
DR STRING; 63405.XP_002844442.1; -.
DR EnsemblFungi; EEQ33587; EEQ33587; MCYG_06406.
DR GeneID; 9230883; -.
DR eggNOG; KOG3607; Eukaryota.
DR HOGENOM; CLU_012383_1_0_1; -.
DR OMA; DSNEDCC; -.
DR OrthoDB; 162519at2759; -.
DR Proteomes; UP000002035; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of 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:UniProtKB-KW.
DR CDD; cd04271; ZnMc_ADAM_fungal; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR041645; ADAMTS_CR_2.
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 Pfam; PF17771; ADAM_CR_2; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..796
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein B"
FT /id="PRO_0000390773"
FT TOPO_DOM 24..706
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 707..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 728..796
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 271..510
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 519..608
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT REGION 737..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..789
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 395..495
FT /evidence="ECO:0000250"
FT DISULFID 448..459
FT /evidence="ECO:0000250"
FT DISULFID 580..600
FT /evidence="ECO:0000250"
SQ SEQUENCE 796 AA; 86526 MW; 5B7FCD2038E5B8F9 CRC64;
MKALSCLLAV IATAGSLFQH VDARSHARDR LNNISRVERP VIHTPSHRVH AHSHFDLTFD
LYPRSSRIKL QLEPNHDVLS HDARVAFLDG EGNVDRMERI ERRDHRVFKG WAWVQRKSGS
WERVGWARVM MQRDGEDPLF EGVFTVMHDH HQIIPKTKYV HKRHPHDPPL DATPGEYMLL
FRGSDIRTQT HDTVERSITS SPSCDADTLA YGTQSDFMFP PLPQENNTNL WGSLMTSIGR
RQNSDTVGTV PGSQNLRDTI GNTDGCPNTR RVALIGVVAD CTYTSTFASE MDAKTDIISV
VNAASVVYEH TFNISLTLGE VNILPKNCPA TASSATPFNQ MCGERVGDES FTLADRLNTF
SAWRGKKSDD FAFWTLMTDC TTENQVGLAW AAQLCVKGVQ GDSNTRNASS QAVSGANVVS
KTDNTWQVFA HEAGHIFGAV HDCDSALCQD PSNPDNSRCC PSTATTCDAG GKFMMNPTSG
SQITAFSPCS VGQICSRMAK HSILTNCLTT NRGVDTISGQ QCGNGIVEDG EDCDCGGDES
CKGNKCCDPK TCKYTSGSQC DDANEECCRD CKFASSSTIC RLSSGPCDPE EKCTGNSGDC
PRDTHSKNGE TCGTNLQCAS GQCTSRDLQC QMHLGSQVAG SRTVAFDSYG CQVACKDPYR
PDVRYEGSLT FLDGTPCGGG GTCENGQCTG STFGNEVSDW VSRHKPIVIG VAVGVGCLLL
LAILSCICGR SKKRRPRNRK MAPINMRPMP PVYNGWTGPP PNAESPGGHP QYNHVPPPIN
APPPAYPGRM PSTRYA
