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}.
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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
//