ID A0A2C9JTX8_BIOGL Unreviewed; 470 AA.
AC A0A2C9JTX8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN Name=106068164 {ECO:0000313|EnsemblMetazoa:BGLB008038-PB};
OS Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Planorbidae; Biomphalaria.
OX NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB008038-PB, ECO:0000313|Proteomes:UP000076420};
RN [1] {ECO:0000313|EnsemblMetazoa:BGLB008038-PB}
RP IDENTIFICATION.
RC STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB008038-PB};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR RefSeq; XP_013082929.1; XM_013227475.1.
DR AlphaFoldDB; A0A2C9JTX8; -.
DR EnsemblMetazoa; BGLB008038-RB; BGLB008038-PB; BGLB008038.
DR VEuPathDB; VectorBase:BGLB008038; -.
DR OrthoDB; 2940912at2759; -.
DR Proteomes; UP000076420; 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:UniProtKB-KW.
DR Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF243; SOL NARAE, ISOFORM C; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT DOMAIN 161..386
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 329
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 470 AA; 53848 MW; 406A76D873DB0664 CRC64;
MHFGVPKSNR SGNRFLEDVT RKADDAKRDL GHESDDDSSE DYIEVPAEFE DKKNWEKDGD
GIAQRRADDR EDRGKRKDWR RKFRRNSNGK LKDRDLDQKY QFGENYFYPD DQMNVDFMSL
MTSRSGSTRH RRQTLTEWAA FDLPSLFHWN SSNLYRSNHD YVVEVMVVVD ARAYQEFQYD
WSTLQVYLLH FWQSVNTRFK ELVNPSVTLK IKSINKIIFS GFQPFIENNR IEPGSELVDV
NGVLMDFMTY TGQHYESNPS LPDHDIAILL TGEDLCKKKS DGTWSQKTKG IAFIRGGCIS
SRRFLNQSYD LGVAEVGPGF RGVLTAAHEV GHLLGAFHDG EKNSSDCPST SGYIMSSTWT
DPYVYNRFSN CSKQNLKHFL ESSDSNYTSG YNVPTRLPGQ LYTLADQCQH FIEGTPCKNV
ALDSQCGQLC CEKWSQPFTS KEPAADGTVC GDRKMCYNGE CLHQALIPFQ
//
