ID A0A368G1B3_ANCCA Unreviewed; 297 AA.
AC A0A368G1B3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Reprolysin family zinc metalloprotease {ECO:0000313|EMBL:RCN38214.1};
GN ORFNames=ANCCAN_15880 {ECO:0000313|EMBL:RCN38214.1};
OS Ancylostoma caninum (Dog hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN38214.1, ECO:0000313|Proteomes:UP000252519};
RN [1] {ECO:0000313|EMBL:RCN38214.1, ECO:0000313|Proteomes:UP000252519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baltimore {ECO:0000313|EMBL:RCN38214.1,
RC ECO:0000313|Proteomes:UP000252519};
RA Mitreva M.;
RT "Draft genome of the hookworm Ancylostoma caninum.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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:RCN38214.1}.
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DR EMBL; JOJR01000415; RCN38214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368G1B3; -.
DR STRING; 29170.A0A368G1B3; -.
DR Proteomes; UP000252519; 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; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR036436; Disintegrin_dom_sf.
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:SF249; PEPTIDASE M12B DOMAIN-CONTAINING PROTEIN; 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:0000313|EMBL:RCN38214.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Metalloprotease {ECO:0000313|EMBL:RCN38214.1};
KW Protease {ECO:0000313|EMBL:RCN38214.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000252519};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..297
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016960330"
FT DOMAIN 52..225
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 297 AA; 33788 MW; F026DBD924703974 CRC64;
MNLLLLYGLV IRFWYCHATE EKFQRRLKRA PAVWGDAAPD YSIATFGSAP YRYLYTLLFV
DDKITGYYEY DMVRVKTNIL KVVEEANTYF NQLRLGIVVV DVMQTMRSNL SLYGFQEYRR
QRLHKLPPHD FAALISFRYA GGLAFVGGLC SDKAVMLCGF YPSSPSAMGS IFFHEVAHLV
GVPHRPANYS LYVSNCACKR STSNPNGCLR IPGFDHDCTA QQFVNVMYQK KCIRTKPIES
ISEPICGNGV TEQGEQCDCG LPAQCERWNC RPETCTYRVH PSILVRLLAC TFSRIDI
//
