ID A0A2B4SN00_STYPI Unreviewed; 1062 AA.
AC A0A2B4SN00;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN Name=nas-6 {ECO:0000313|EMBL:PFX30250.1};
GN ORFNames=AWC38_SpisGene4925 {ECO:0000313|EMBL:PFX30250.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX30250.1, 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:PRU00059}.
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:PFX30250.1}.
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; LSMT01000053; PFX30250.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4SN00; -.
DR EnsemblMetazoa; XM_022927252.1; XP_022782987.1; LOC111323816.
DR OrthoDB; 2911813at2759; -.
DR Proteomes; UP000225706; Unassembled WGS sequence.
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; cd03590; CLECT_DC-SIGN_like; 1.
DR CDD; cd00041; CUB; 2.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 2.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033989; CD209-like_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR10127:SF887; ASTACIN-LIKE METALLOENDOPEPTIDASE; 1.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00090; TSP_1; 2.
DR PRINTS; PR00480; ASTACIN.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00209; TSP1; 2.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 2.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS50092; TSP1; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
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..23
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 24..1062
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5011809533"
FT DOMAIN 73..267
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 663..773
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 784..898
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 929..1043
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT ACT_SITE 166
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 1062 AA; 122528 MW; D1645C395D7DB9B9 CRC64;
MALAPNGLLC FVLMTILINR SLMSPVAKQH TAAFDEIARV NKNYAKYQAG TVWQVDMKLP
KRNLGRKGVD GSAPIRDRTS LWPKGVIPYT IAYSIPGNSK IRQLLSDAMA EWEKHTCIKF
VERENQADYV EFYYGEGCNS DVGRVGGRQT TSLGRGCAHH GIVVHELGHL IGFWHEQNRP
DRDNYIIIKE ENIIPKFKFA FDKYSSRKID SLGVEYDYKS VMHYGEKAFT KNGLPTIVAR
QSSITTFGNS HLSSLDIQQA NLLYRCPDYP NFPKDFVWSS NGPMRKNATY NIYARCIRIS
HHRSTSWSDN YLCYRRDKKS LSLSFSGRGP VPGKKCIQLR IPTKSHYESW ARSYFCWPHD
GIYKFKWLTH APTAEERPNC LELCEPRDPT WGRNKYFLCA TKDRQPIDGN WTRWRPWTTC
TRKCGGGVQS RLRSCTNPQP SFGGRYCVGK ASEARMCNTQ ECAEWPKFPE DFSFVRKPRA
GSNETCIRIF ERLDYFAFKD FLLCSAADKR QPEMRWSDKG DVKYMECTRI LVPKDARRGR
WDDNYLCIAA NSGFPYRFVW SYSNQIPGLP CMRWYAKNGR SGWNETYLCA EDRFKSTAIP
ERIINGGWSL WTSWNTCSKS CDGGKQRRVR LCDNPKPNRN GRPCQGKHLD ERRCNEQKCP
SACGTEFRAV SGRFNSPNYP KPYPGKMKCE WIIRVPDGQR IQLKFLFFNI YGPKCDDSVV
VYDGQTVSSR RFGKYCGSKL PPVLHSSSNV LLVKFHSNLQ RGYYGFNAKW EAKKVEVMET
ANECGRQITG SSGTLSSPGF PGSYPPNLDC VWVITVPRGN HIELKFKVFD IHKVVRRGCR
YDYIEVRDGN SRNSPSLGRH CGKSVDEKFQ TVSNHVRIRL HSDGSHERQG FVLTWRSLRR
LVVTQEPTTK PLCPRGWVSH LMNGTDMVYC YLVRHNMHTW YMARNDCIGS RSDLLSISNA
KEQEFVTKHL LAESFMWIGY NDIQREGQWA WSDRTHQSYK NWATGDPNNG GQYRKKDEDC
AVLKSNGKWN DYPCTTRFKY ICKARASRLS VEGLHSRRRD QR
//
