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
//