GenomeNet

Database: UniProt
Entry: A0A2B4RU74_STYPI
LinkDB: A0A2B4RU74_STYPI
Original site: A0A2B4RU74_STYPI 
ID   A0A2B4RU74_STYPI        Unreviewed;       568 AA.
AC   A0A2B4RU74;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN   Name=MEP1B {ECO:0000313|EMBL:PFX20100.1};
GN   ORFNames=AWC38_SpisGene15483 {ECO:0000313|EMBL:PFX20100.1};
OS   Stylophora pistillata (Smooth cauliflower coral).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Pocilloporidae; Stylophora.
OX   NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX20100.1, ECO:0000313|Proteomes:UP000225706};
RN   [1] {ECO:0000313|Proteomes:UP000225706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA   Tambutte S., Allemand D., Aranda M.;
RT   "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT   digitifera provides evidence for extensive differences between species of
RT   corals.";
RL   bioRxiv 0:0-0(2017).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC         ECO:0000256|RuleBase:RU361183};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01211}.
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:PFX20100.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LSMT01000331; PFX20100.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B4RU74; -.
DR   EnsemblMetazoa; XM_022943579.1; XP_022799314.1; LOC111337305.
DR   EnsemblMetazoa; XM_022943580.1; XP_022799315.1; LOC111337305.
DR   OrthoDB; 2900355at2759; -.
DR   Proteomes; UP000225706; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06263; MAM; 1.
DR   CDD; cd04280; ZnMc_astacin_like; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 1.
DR   InterPro; IPR034035; Astacin-like_dom.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000998; MAM_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR10127:SF780; ZINC METALLOPROTEINASE NAS-13; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00629; MAM; 1.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   PRINTS; PR01705; TSP1REPEAT.
DR   SMART; SM00137; MAM; 1.
DR   SMART; SM00209; TSP1; 2.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS50060; MAM_2; 1.
DR   PROSITE; PS50092; TSP1; 1.
PE   4: Predicted;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|PROSITE-
KW   ProRule:PRU01211};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW   Signal {ECO:0000256|RuleBase:RU361183};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT   CHAIN           20..568
FT                   /note="Metalloendopeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT                   /id="PRO_5011812173"
FT   DOMAIN          90..285
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   DOMAIN          407..568
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   ACT_SITE        183
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   568 AA;  64980 MW;  D3A513F23CE47853 CRC64;
     MLVHCRAVLF FVAMYEICGR IVTKREEGWE LEDYLDSEDP NWPSGDYENL SAFDEIWKAN
     EAEDVTDLLE GDIKTDLDSK NATDEEKIND AVRSRQYTWR TKVVPYEISK ELVSSGYMAN
     IRAAFSEFEK YTCIKWKPRG KEKYWVRFIK GKGCWSPVGY RRKSPQLISL GNGCNQKGII
     CHEMMHTLGF YHEQGRPDRD KYVAIYWENI QSGKEHNFKK QSEEDLDPLN APYDTSSIMH
     YGKYTFNKNG RPTIEVIGKP YKMIGQRFGF SKTDIEQLNA LYDCSNDATG GWSSWTSFGP
     CYKHNSKCLH DRQRYCSNKN RDKCPGANMY GVQTQTKPCP HSCSSPVDGH WGRWSSWSPC
     SETCGFGTHT RTRKCNDPPP KYGGEECAGD RTDVGKCLVT VCGLGPYDVS FESEGMHGWK
     LCESHEEKNR PNWYFSRGIT GSPYTGPIKD HTTGSGRYIF FEASAPARNG DVACFHSPKI
     PSTTCQRLTF WYHMYGAQMG TLRVLKKTVD GEATTLWKRS FMQGTNWMFA NVEIYCKEKF
     QIYFEGIRGA GFKGDIGIDD VKIKDCSD
//
DBGET integrated database retrieval system