ID F2SXA2_TRIRC Unreviewed; 669 AA.
AC F2SXA2;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 2.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein B {ECO:0000313|EMBL:EGD90974.2};
GN ORFNames=TERG_07197 {ECO:0000313|EMBL:EGD90974.2};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD90974.2, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; GG700656; EGD90974.2; -; Genomic_DNA.
DR AlphaFoldDB; F2SXA2; -.
DR STRING; 559305.F2SXA2; -.
DR VEuPathDB; FungiDB:TERG_07197; -.
DR eggNOG; KOG3607; Eukaryota.
DR InParanoid; F2SXA2; -.
DR OMA; YGLQQNF; -.
DR OrthoDB; 2961161at2759; -.
DR Proteomes; UP000008864; 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:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04271; ZnMc_ADAM_fungal; 1.
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; 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 PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF159; MIND-MELD, ISOFORM J; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF13688; Reprolysin_5; 1.
DR SMART; SM00608; ACR; 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 Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Integrin {ECO:0000313|EMBL:EGD90974.2}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000008864};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT TRANSMEM 578..600
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 141..365
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 390..479
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 624..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..663
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 303
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 669 AA; 71572 MW; 1C79FB048488EF60 CRC64;
MHRDGEDPLF EGVFTVMHDH HQVIAKSKYV RKRHQQDPPL DNTPGEYMLL FRGSDIAQTQ
STGNVERSIM SSPSCDADTL AYDSNTNFMF PPLPEENNTS IWNYFTTSIG KRQMTDTGGV
VPGSRDLKET IGSTSGCPNT RKVALIGVVA DCTYTNTFAS EMDARADIIS VVNAASVVYE
HSFNISLTLG EINILPKNCP ATASSATPFN QQCDDRAGGG SFTLADRLNT FSAWRGKKTD
DFAFWTLMTD CTTENQVGLA WAAQLCVKGV QGNPDSRNSS SQAVAGANVV SKTDNTWQVF
AHEAGHIFGA VHDCDSMLCQ NSANPDNSRC CPATASTCDA GGRFMMNPTS GSQITNFSPC
SIGQICSRMA RRTILTNCLT TNRGVDTISG QQCGNGIVED GEDCDCGDEE SCKGNTCCDS
KTCKYTSGSQ CDDTNEECCK GCKFASSSTI CRTSSGPCDP EEKCSGNSGD CPHDIHSKDG
ETCGTDLQCA SGQCTSRDLQ CQMHLGNQVA GSRTVAFDSY GCEVACKDPD RPNVRYEGSL
TFLDGTPCGG GGTCKNGQCS GSTFGNEVSD WVSRHKPIVI GVAVGAGCLL LLAIASCICG
RSRRQRPRNR KMPPINMRPM APVYNGWNGA PPNAQQSSPG GHPPYNNIPP PINAPPPAYP
GHMPPTRYA
//
