ID A0A1I7TJD7_9PELO Unreviewed; 462 AA.
AC A0A1I7TJD7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Peptidase M12B domain-containing protein {ECO:0000313|WBParaSite:Csp11.Scaffold626.g6508.t1};
OS Caenorhabditis tropicalis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold626.g6508.t1};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold626.g6508.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) 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 AlphaFoldDB; A0A1I7TJD7; -.
DR STRING; 1561998.A0A1I7TJD7; -.
DR WBParaSite; Csp11.Scaffold626.g6508.t1; Csp11.Scaffold626.g6508.t1; Csp11.Scaffold626.g6508.
DR Proteomes; UP000095282; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT TRANSMEM 266..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..218
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 416..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 162
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 462 AA; 51826 MW; 6C0C27423D0B8517 CRC64;
MKKRVVFSWE QKHIEYGAAV WGAKAPDYSL ASTDPGTTIF IRSLIFVDNK TTAYYEFDMY
RVKLNIMKMV DEANQYLNQL GIGLIVVGIL QTNRGDLSLQ SFHEYRNARL HKIPEHEFAT
LISYKYAGGL AYVNGMCSSH SVSLSGFYPN EPRAMGSIFF HEVAHLVGVP HRDVNESIYV
PNCQCTPIDS RKEDGCLKIP GFDHDCTVQQ FVNTVYKNKC ILKEPIFDES EPVCGNGVLE
DGEDCDCGLP GRCSDLNCQP HTCRFFMHPF FLVLVLVSFI AFLVIATWFI VRRYTGTMLN
CFKMYKSKHD RGNSSPYTNG QIQILAASPY QNRKMSHSSI SGSNTILVSN DSRFATIQRP
KVPPPPPPSR PKTTIQVMAP GVGQPYETNK VFGSYRESFY DDFSDDEFEE QEVPSAYPLP
PGVPTCPSYP PNAPINRVTV DLQSPRTNST ATTSNSTSSF SF
//
