ID A0A443S2P6_9ACAR Unreviewed; 277 AA.
AC A0A443S2P6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
DE Flags: Fragment;
GN ORFNames=B4U80_11778 {ECO:0000313|EMBL:RWS21753.1};
OS Leptotrombidium deliense.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombiculoidea; Trombiculidae; Leptotrombidium.
OX NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS21753.1, ECO:0000313|Proteomes:UP000288716};
RN [1] {ECO:0000313|EMBL:RWS21753.1, ECO:0000313|Proteomes:UP000288716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-UT {ECO:0000313|EMBL:RWS21753.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
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:RWS21753.1}.
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DR EMBL; NCKV01010999; RWS21753.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443S2P6; -.
DR STRING; 299467.A0A443S2P6; -.
DR EnsemblMetazoa; LDEU010287-RA; LDEU010287-PA; LDEU010287.
DR VEuPathDB; VectorBase:LDEU010287; -.
DR Proteomes; UP000288716; 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 CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF250; ADAM METALLOPROTEASE; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00023049};
KW Reference proteome {ECO:0000313|Proteomes:UP000288716};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT DOMAIN 77..273
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 228..252
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RWS21753.1"
SQ SEQUENCE 277 AA; 31485 MW; 2DA5A2EEB29F0AB9 CRC64;
GLKEPLHFCG NVLLGEFHYE NKTFKISFNQ TDRIQRIQKI GISGRAMTMH YHTCGVPLFV
NKSAKITTRA MQKYGPYFIP ILVVVDHANY LRFKKNKKSI ISNVKKYFKS ASEMMKPLGV
TLSVADVVIW DKKDEIKIVR SGDATLNNLQ VYFESKLMAK YQNCVRIAHL LINVKDLDMA
GRGFVGSACT LDHAVSFTWT KYTNYDNVQY TAHELSHNLG MAHDTPACKC GKEKMCTMAM
GNKGLGKKWS DCSLNEYNTV INNQDLDCLK EKLKQCK
//
