ADMB_ARTBC
ID ADMB_ARTBC Reviewed; 799 AA.
AC D4B1G0;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 48.
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=ARB_02289;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFE30799.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; ABSU01000026; EFE30799.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003011439.1; XM_003011393.1.
DR AlphaFoldDB; D4B1G0; -.
DR SMR; D4B1G0; -.
DR STRING; 663331.D4B1G0; -.
DR EnsemblFungi; EFE30799; EFE30799; ARB_02289.
DR GeneID; 9526391; -.
DR KEGG; abe:ARB_02289; -.
DR eggNOG; KOG3607; Eukaryota.
DR HOGENOM; CLU_012383_1_0_1; -.
DR Proteomes; UP000008866; 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 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..799
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein B"
FT /id="PRO_0000397720"
FT TOPO_DOM 24..707
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 708..728
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 729..799
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 272..511
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 520..609
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT REGION 753..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..792
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 433
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 442
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 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 396..496
FT /evidence="ECO:0000250"
FT DISULFID 449..460
FT /evidence="ECO:0000250"
FT DISULFID 581..601
FT /evidence="ECO:0000250"
SQ SEQUENCE 799 AA; 86637 MW; 3001BCECBA6F46E2 CRC64;
MKAFSCLLSV IATAASLFQH VDARSHARDK LNNISRVERP VIHTPSRRVH AHSHFDLTFD
LYPRSSRIKL QLEPNHDVLS HDARVTFLDT EGNVDRTERI ERRDHSVFKG WAWTQAKSGA
WERVGWARII LHRDGEDPLF EGVFTVMHDH HQVIAKSKYV RKRHQQDPPL DNTPGEYMLL
FRGSDIAQTQ STGNVERSIM SSPSCDADTL AYDSNSNFMF PPLPEENNTS IWNYFMTSIG
KRQMTDTGGV VPGSRDLKET IGSTSGCPNT RKVALIGVVA DCTYTNTFAS EMDARADIIS
VVNAASVVYE HSFNISLTLG EINILPKNCP ATASSATPFN QQCDDRAGGG SFTLADRLNT
FSAWRGKKTD DFAFWTLMTD CTTENQVGLA WAAQLCVKGV QGNPDSRNSS SQAVAGANVV
SKTDNTWQVF AHEAGHIFGA VHDCDSMLCQ NPANPDNSRC CPATASTCDA RGRFMMNPTS
GSQITDFSPC SIGQICSRMA RRTILTSCLT TNRGVDTISG QQCGNGIVED GEDCDCGDEE
SCKGNTCCDP KTCKYTSGSQ CDDANEECCK GCKFASSSTI CRTSSGPCDP EEKCSGNSGD
CPHDIHSKDG ETCGTDLQCA SGQCTSRDLQ CQMHLGNQVA GSRTVAFDSY GCEVACKDPD
RPNVRYEGSL TFLDGTPCGG GGTCKNGQCS GSTFGNEVSD WVSRHKPIVI GVAVGAGCLL
LLAIASCICG RSRRQRPRNR KMPPINMRPM APVYNGWNGA PPNAQQSSPG GHPPYNNIPP
PINAPPPAYP GHLPSTRYA
