ID A0A1Y3BTI6_EURMA Unreviewed; 374 AA.
AC A0A1Y3BTI6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN ORFNames=BLA29_003334 {ECO:0000313|EMBL:OTF82916.1};
OS Euroglyphus maynei (Mayne's house dust mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC Pyroglyphidae; Pyroglyphinae; Euroglyphus.
OX NCBI_TaxID=6958 {ECO:0000313|EMBL:OTF82916.1, ECO:0000313|Proteomes:UP000194236};
RN [1] {ECO:0000313|EMBL:OTF82916.1, ECO:0000313|Proteomes:UP000194236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:OTF82916.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:OTF82916.1};
RA Arlian L.G., Morgan M.S., Rider S.D.;
RT "Genome Survey of Euroglyphus maynei.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:OTF82916.1}.
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DR EMBL; MUJZ01006147; OTF82916.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3BTI6; -.
DR OrthoDB; 5395001at2759; -.
DR Proteomes; UP000194236; Unassembled WGS sequence.
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:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 2.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR45702; ADAM10/ADAM17 METALLOPEPTIDASE FAMILY MEMBER; 1.
DR PANTHER; PTHR45702:SF3; KUZBANIAN-LIKE, ISOFORM A; 1.
DR Pfam; PF13574; Reprolysin_2; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000194236};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT DOMAIN 193..362
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 113..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 306
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 374 AA; 42821 MW; 192BA3336145D42B CRC64;
MTDDEDSTFV GIITKDGLLD GHLQTRQEEF YIEPAERYFD LNFDQHDFHS VIYVTGDVNF
PSNAMHGAIS MANNNNNFFT NNDSTTLFVR YIPLFNPFQT TTNIMADHWF DQTKTKRPRR
STNISKNQMM NNNNGNNKSS SNENETSEIN IEMTTTSSYN VANKLINNDD HNKQRQIMKE
NKQQQSSNNH GIYWRDMDSL HYTESEPYGI KAVHPRTHWI DDQRHHDRHV VVDPKKTTCM
LYLQADHLFY EKMGSEEACI ESMTRHVQKV NNIYKNTGHL NTGIVTLLNY GKHVPPIVSH
VTLAHEIGHN FGSPHDPEDD HACTPGGENG NYIMFARATS GDKRNNNKFS PCSLRSINAV
LNTKAKSLKG CFQG
//
