ID A0A2K3QHH0_9HYPO Unreviewed; 794 AA.
AC A0A2K3QHH0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein B {ECO:0000313|EMBL:PNY26998.1};
GN ORFNames=TCAP_03071 {ECO:0000313|EMBL:PNY26998.1};
OS Tolypocladium capitatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY26998.1, ECO:0000313|Proteomes:UP000236621};
RN [1] {ECO:0000313|EMBL:PNY26998.1, ECO:0000313|Proteomes:UP000236621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY26998.1,
RC ECO:0000313|Proteomes:UP000236621};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
RL Submitted (AUG-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PNY26998.1}.
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DR EMBL; NRSZ01000472; PNY26998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3QHH0; -.
DR STRING; 45235.A0A2K3QHH0; -.
DR OrthoDB; 2961161at2759; -.
DR Proteomes; UP000236621; 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:InterPro.
DR CDD; cd04271; ZnMc_ADAM_fungal; 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 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; 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 Integrin {ECO:0000313|EMBL:PNY26998.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000236621};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..794
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014451897"
FT TRANSMEM 704..728
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 273..489
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 514..604
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 736..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 429
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 794 AA; 85607 MW; 0B7A355D167BB0C5 CRC64;
MVTLRSVVSA VAAAAALLAP SSLAYSTRRN PVSRISLIDD PVIKTPSHRV HSHSKFDLTF
TLHHGRQRIR LALNPNHDLI HDDFAVTYLA GDGTVRVVEK VARTEHRVYR GDAFIERLGH
GGWSKAGWAR IMVHRDGERP VFDGAFRIDG DNHHIQTGDQ YQKLRRDEDP VVAGSQDAEE
LMVVWRDSDV VDFSDDPAEL RRRGLDHESL CNADALDFNS RFRQQESQSP NLLRAIEFRS
LFGRQSIDDG AGNDAGLNLL NSIGSVDGCP GTRKVALVGI ATDCTYWDGF DSKDDLRKNV
IGMVNKASEV YESTFKISLG IQNLTVSDRA CPGTASALTP WNVGCGAQTT INDRLNTFSK
WRGRFQDNNA YWTLLTRCAT ESAVGLAWRG QLCRSGSGDS ADGSGKNETV AATNVVVRTD
TEWQVFAHET GHTFGAVHDC TEGTCPLNAA KQACCPLSRS SCDAGGKFMM NPSTGRAITQ
FSACSIGNIC SGLKSNMIKG SCLSDNKNVQ TITGSQCGNG IVESGEDCDC GGDAGCKGNK
CCDAKTCKFI NGAVCDASNE DCCTGQCQFA SNGTVCRAST GVCDMTEVCP GDRASCPYDK
HRSDGTSCGD GLNCASGQCT SRDMQCRSMA NSLTGANNTT ACPDGGCVLA CQSPEMSPGQ
CVAYNQNFLD GTNCGAGGKC SNGSCQGTST LKEIGKWIQD HKSIFIPVVS IVGGLILIAI
MSCIVSSIRR RMRRRKLPKG PEMNSWSSYN VQGGQQGQWN QQRQWTESSG AIVSPPPADA
SGRWMTRQRD MRYA
//
