ADMB_TRIVH
ID ADMB_TRIVH Reviewed; 798 AA.
AC D4DCV9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 46.
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=TRV_04965;
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517;
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=EFE40271.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACYE01000253; EFE40271.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003020889.1; XM_003020843.1.
DR AlphaFoldDB; D4DCV9; -.
DR SMR; D4DCV9; -.
DR EnsemblFungi; EFE40271; EFE40271; TRV_04965.
DR GeneID; 9577741; -.
DR KEGG; tve:TRV_04965; -.
DR HOGENOM; CLU_012383_1_0_1; -.
DR Proteomes; UP000008383; 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; 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; 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; Signal; Transmembrane; Transmembrane helix;
KW Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..798
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein B"
FT /id="PRO_0000397721"
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..798
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 734..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..792
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 32
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 227
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 798 AA; 86572 MW; BD27A9326ACFE42A CRC64;
MKAFSCLLAV IATAASLFQH VDASHARDKL NNISRVERPV IHTPSRRVHA HSHFDLTFDL
YPRRNRIKLQ LEPNHDVLSH NARVTFLDTE GNVDRIERIE RRDHSVFKGW AWTQAKSGVW
ERVGWARIIM HRDGEDPLFE GVFTVMHDHH QVIAKSKYVR KRHQQDPPLD NTPGEYMLLF
RGSDIAQTQS TGNVERSIMS SPSCDADTLA YDSNSNFMFP PLPEENNTSI WNYFMTSIGK
RQMTDTGGVV PGSRDLKETI GSTSGCPNTR KVALIGVVAD CTYTNTFASE MDARADIISV
VNAASVVYEH SFNISLTLGE INILPKNCPA TASSATPFNQ QCDDRAGGGS FTLADRLNTF
SAWRGKKTDD FAFWTLMTDC TTENQVGLAW AAQLCVKGVQ GNPDSRNSSS QAVAGANVVS
KTDNTWQVFA HEAGHIFGAV HDCDSMLCQN PANPDNSRCC PATASTCDAR GRFMMNPTSG
SQITNFSPCS IGQICSRMAR RTILTNCLTT NRGVDTISGQ QCGNGIVEDG EDCDCGDEES
CKGNTCCDPK TCKYTSGSQC DDANEECCKG CKFASSSTIC RTSSGPCDPE EKCSGNSGDC
PHDIHSKDGG TCGTDLQCAS GQCTSRDLQC QMHLGNQVAG SRTVAFDSYG CEVACKDPDR
PNVRYEGSLT FLDGTPCGGG GTCKNGQCSG STFGNEVSDW VSRHKPIVIG VAVGAGCLLL
LAIASCICGR SRRQRPRNRK MPPINMRPMA PAYNGWNGAP PNAQQSSPGG HPPYNNIPPP
INAPPPAYPG HMPPTRYA
