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Database: UniProt
Entry: A0A261BFT9_9PELO
LinkDB: A0A261BFT9_9PELO
Original site: A0A261BFT9_9PELO 
ID   A0A261BFT9_9PELO        Unreviewed;       513 AA.
AC   A0A261BFT9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Peptidase M12B domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=FL83_16739 {ECO:0000313|EMBL:OZG08545.1};
OS   Caenorhabditis latens.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG08545.1, ECO:0000313|Proteomes:UP000216463};
RN   [1] {ECO:0000313|EMBL:OZG08545.1, ECO:0000313|Proteomes:UP000216463}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX534 {ECO:0000313|EMBL:OZG08545.1,
RC   ECO:0000313|Proteomes:UP000216463};
RA   Fierst J.L.;
RT   "Caenorhabditis latens genome sequence.";
RL   Submitted (JUL-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:OZG08545.1}.
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DR   EMBL; NIPN01000158; OZG08545.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261BFT9; -.
DR   STRING; 1503980.A0A261BFT9; -.
DR   Proteomes; UP000216463; 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:0035262; P:gonad morphogenesis; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR   CDD; cd04267; ZnMc_ADAM_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; IPR033817; MIG-17.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR010909; PLAC.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF243; SOL NARAE, ISOFORM C; 1.
DR   Pfam; PF17771; ADAMTS_CR_2; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50900; PLAC; 1.
PE   4: Predicted;
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   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:UP000216463};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   DOMAIN          225..379
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          469..510
FT                   /note="PLAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50900"
FT   ACT_SITE        310
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         309
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         319
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OZG08545.1"
SQ   SEQUENCE   513 AA;  58091 MW;  E83A815D6DB7F621 CRC64;
     MGQDDRSSHV SLGGHNADVL FDSSSAESAR HEKQLSNNIR LVKKRIHDGL KFSRVIHYTN
     ETIHGMKTNY NSNKTQELSL DVLVVSDFLT YQAFLEMTNG DSHKAVHDLK VYLQAVFDQV
     KIIYDGISFN NETLHMVFAG TYISTQERDC PLWLSWAEDE EERVLNEEIR RLEEDESRWN
     STVEDEEFMN TTTLDSNSTE QLISSERRKK LRKFVDVTLE EMQENNSTEM ALKMDSKKAV
     DKFTIWLKEQ QGLPRHEHAV LITKFDLISI NGNSATQGMA YVGNICENGD SSSVVEDIGA
     GLTSLIVAHE IGHSLGALHD GAYESADCDS NDNYLMAVAV SGSADRQSFL NSRKMSNCSI
     KSIIENLKEP TASCVKKWKT KGSNQKDFMK KPGETVNLAR QCQIAFGPTF KPCLHIGYFH
     GQSICERIWC SDGDSDECQT LNYFPAFDGT DCGYNMWCIE GLCVQNTKKW MDCKDLNAKT
     CSRYSSSKLK HYCKSKDFRE ICCRTCAQKG KVY
//
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