ID A0A2G5SWV4_9PELO Unreviewed; 701 AA.
AC A0A2G5SWV4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=Cni-adm-4 {ECO:0000313|EMBL:PIC19306.1};
GN Synonyms=Cnig_chr_X.g24901 {ECO:0000313|EMBL:PIC19306.1};
GN ORFNames=B9Z55_024901 {ECO:0000313|EMBL:PIC19306.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC19306.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:PIC19306.1}.
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DR EMBL; PDUG01000006; PIC19306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5SWV4; -.
DR Proteomes; UP000230233; Chromosome x.
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 GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd14246; ADAM17_MPD; 1.
DR Gene3D; 4.10.70.30; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR032029; ADAM17_MPD.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR45702; ADAM10/ADAM17 METALLOPEPTIDASE FAMILY MEMBER; 1.
DR PANTHER; PTHR45702:SF6; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 17; 1.
DR Pfam; PF16698; ADAM17_MPD; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF13574; Reprolysin_2; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..701
FT /note="Peptidase M12B domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013680502"
FT TRANSMEM 647..666
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 194..452
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 453..543
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT ACT_SITE 378
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 701 AA; 78214 MW; 7180193519C2D877 CRC64;
MKIHITSIFI FLAVGISQSD AFNTRVKRHA PVIFQKSTRS SIIYFDFLGQ EYVIDLVPNH
SAFHQKFKVY TQNGPQFVAR EEYIGTVREP RKGTGVLTHL ENGEYIGILY FDNDTLHLEP
AYPHGLSEDV GNIVGYFGSD VDLKLDLAAI PHRYQVSFRP SNPLLKHKRA INIASSTSPT
TRTTRSDVHN EKRNRCSLKL VADYSFYSIF GKNNTGIVTK FLVNMIARVN EIYNPVNWDV
GREEGISGRG RFQNMGFSIK EIKVLDRPNA SDAHYNSYSR QWESEKLLKE FAFAEGSKDF
CLVHLVTART FKETSTLGLA YLSHRTWDDT AGGICSKPET FNGKIAYINV LLSTCFANME
QSTYPLITKE IDIVVSHEYG HAWGANHDST MVSDDPDVDE CSPNDQDGGK YLMSPYAQRG
YDQNNVLFSP CSIKSIREVL INKYSGCLEE EMNSFCGNGI VEDGEECDNG VETDEQEVSC
CDKFCRLSVG AKCSPLNHIC CTPTCQFHNS SHVCLPGDPL LCKADALCNG LTGECPPAPP
VADQQECLEG GECSNGVCLP FCEKKSIGQK SCICEDLEIS CRRCCRDQNG TCSPVPGPVY
LRDGIRCSKG TCRDRKCVNE AVDNVRNYFL APFQSTGGLF VFLKTHVVLI AIITISMIFA
AAYSIVKCNE HNISKLREED RAVPLRKVHV SADVFNPGYQ E
//
