ID A7SPX7_NEMVE Unreviewed; 259 AA.
AC A7SPX7;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN ORFNames=NEMVEDRAFT_v1g126434 {ECO:0000313|EMBL:EDO34264.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO34264.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO34264.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; DS469738; EDO34264.1; -; Genomic_DNA.
DR RefSeq; XP_001626364.1; XM_001626314.1.
DR AlphaFoldDB; A7SPX7; -.
DR STRING; 45351.A7SPX7; -.
DR EnsemblMetazoa; EDO34264; EDO34264; NEMVEDRAFT_v1g126434.
DR eggNOG; KOG3538; Eukaryota.
DR HOGENOM; CLU_093979_0_0_1; -.
DR InParanoid; A7SPX7; -.
DR OMA; HDGPPYN; -.
DR PhylomeDB; A7SPX7; -.
DR Proteomes; UP000001593; 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:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR PANTHER; PTHR13723:SF311; 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 Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000001593};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT DOMAIN 5..215
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 155
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 259 AA; 27555 MW; 40EECF0DC42926BD CRC64;
MAGTRYIETL VVADYNMAAF HGTTKLNIYV PTILNVAYSL IGDNSIGADI KYKIKKLQIH
EVENANGLVI STSSSTTLSN FCQWSKGQNV GDDTNQDHFD HATLIASPGT TISYVSQIDV
SVAGLASLKG MCNPDLSCTI NQDMGLGSAF TIAHETGHNL GAKHDGATNT CPSNANIMAT
SASGQSTAFE WSACSCKYVT DFLKDTTLSS CLNDSPVKLA PLPTNTQLPG QIYDRDEQCK
MMIPGSTGFC TSKESVRAG
//
