ID A0A016WEY4_9BILA Unreviewed; 613 AA.
AC A0A016WEY4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN Name=Acey_s0719.g1807 {ECO:0000313|EMBL:EYC38399.1};
GN ORFNames=Y032_0719g1807 {ECO:0000313|EMBL:EYC38399.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC38399.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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:EYC38399.1}.
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DR EMBL; JARK01000319; EYC38399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016WEY4; -.
DR MEROPS; M12.302; -.
DR Proteomes; UP000024635; 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 CDD; cd04273; ZnMc_ADAMTS_like; 1.
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 InterPro; IPR002870; Peptidase_M12B_N.
DR PANTHER; PTHR13723:SF318; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS ADT-1; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF01562; Pep_M12B_propep; 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:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT DOMAIN 264..466
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 420
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 436..441
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 613 AA; 68920 MW; 777584DC0BAA39FD CRC64;
MISVLYCNQK QPRKRVQSAE NQVRLNLGNH LASREKDAFS AACSTKVFPM SRSFHHKLTK
RELKYVFGVD EVHQVPEYEL IKTQRHRKKD GGLRLQFSAW GDDFVLDLKP NSRLISPHIV
SVTRNGTQVT EQKGLPMDYN CHFQGTVSSH GHVPVAISDC RHLMGTLVMN DHFLILQSIP
RRVQRHSIDG EHFVFKRSPS LLTHFEQHNI EEEMIGLNEI HEPFCDTIES RDDPNSAEIL
SLNYTIPSSA KLDSAFVFPN MDPITLEIGL FLDSQLFEHF QREYIQDAEQ HLLDFSLALI
NNVHVLYQQP TLSPNLEIVI VRYEMWKSQP SNLATFVHKN GQAQSLLDAF CRHQAHINPG
TDLTDSGHWD HGVLLTGYDI YHTTASVAGV APVARMCDQL FACSLVEGLH LGRSFVLAHE
MGHNMGMVHD GVQNQCSKSC CLMSAVNGAG KTTWSECSVR EFNAFLLQLD ESGKGNCLRD
GSPGLLERNH LQDGRSPGQR FTADQQCAYF WGRDYQVEIP SGRSIEDICR ILWCGNGGST
ISTAHPALEG SYCGNNKWCH EGRCQPWPSG PPPAVVHGGW SRWSNDDRCP IQQCHVTGSI
AVKPQHRDCV NPA
//
