ID A0A085N7I3_9BILA Unreviewed; 419 AA.
AC A0A085N7I3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN ORFNames=M513_03818 {ECO:0000313|EMBL:KFD55177.1}, M514_03818
GN {ECO:0000313|EMBL:KFD65429.1};
OS Trichuris suis (pig whipworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD65429.1};
RN [1] {ECO:0000313|EMBL:KFD65429.1, ECO:0000313|Proteomes:UP000030764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD65429.1}, and DCEP-RM93M
RC {ECO:0000313|EMBL:KFD55177.1};
RX PubMed=24929829; DOI=10.1038/ng.3012;
RA Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL Nat. Genet. 46:701-706(2014).
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; KL363201; KFD55177.1; -; Genomic_DNA.
DR EMBL; KL367538; KFD65429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085N7I3; -.
DR MEROPS; M12.A48; -.
DR Proteomes; UP000030758; Unassembled WGS sequence.
DR Proteomes; UP000030764; 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); 1.
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:SF251; PEPTIDASE M12B DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13688; Reprolysin_5; 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 Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..419
FT /note="Peptidase M12B domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007379470"
FT DOMAIN 240..419
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 397
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 419 AA; 47587 MW; 5BA26F4FE69AAF9D CRC64;
MHAGSSLLLL LFLAAFSINA TEPFVHPFDD QAAFGQHLFT FEPSGKVAPF DLIRLLMPKG
KRQWINASME HRGKIYNFIL TRRADLFDQN FHEWNKKHLP DRSVFYDDFY SCLYDGYALH
DKNMRIAIAG CNSSKRGLLA MADGSFLLIE PIPPTTRAKL QEFGSHVDDL HTLRKRDVGS
IYQPVENKCL HSFDSNKSAP LSFRRYWTVA ASLRKDSRPN RLQTGPLKPD EFASTSASSL
VIETALFVDA RTWQRFAKVY GEKSADKELL SFVVATVHNV NALFRHPTIV PKLRMQIKKY
EVLKKTPPEL ADHMHAHGEA ELLLKAFCNY QEKKNVPYDN DPRHWDHAIL FTGHDIYSNG
LKAVAGFAPV GGMCNPFKSC TINEGVDFGC VFVIAHEMGH RCLTHHDTIQ SNILRLVLE
//
