ID A0A1X7V0Y1_AMPQE Unreviewed; 550 AA.
AC A0A1X7V0Y1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-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=100635688 {ECO:0000313|EnsemblMetazoa:Aqu2.1.33895_001};
OS Amphimedon queenslandica (Sponge).
OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC Haplosclerida; Niphatidae; Amphimedon.
OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.33895_001, ECO:0000313|Proteomes:UP000007879};
RN [1] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20686567; DOI=10.1038/nature09201;
RA Srivastava M., Simakov O., Chapman J., Fahey B., Gauthier M.E., Mitros T.,
RA Richards G.S., Conaco C., Dacre M., Hellsten U., Larroux C., Putnam N.H.,
RA Stanke M., Adamska M., Darling A., Degnan S.M., Oakley T.H.,
RA Plachetzki D.C., Zhai Y., Adamski M., Calcino A., Cummins S.F.,
RA Goodstein D.M., Harris C., Jackson D.J., Leys S.P., Shu S., Woodcroft B.J.,
RA Vervoort M., Kosik K.S., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The Amphimedon queenslandica genome and the evolution of animal
RT complexity.";
RL Nature 466:720-726(2010).
RN [2] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT evolution of animal complexity.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:Aqu2.1.33895_001}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2017) to UniProtKB.
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:PRU00196}.
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DR RefSeq; XP_003386017.1; XM_003385969.2.
DR AlphaFoldDB; A0A1X7V0Y1; -.
DR EnsemblMetazoa; Aqu2.1.33895_001; Aqu2.1.33895_001; Aqu2.1.33895.
DR GeneID; 100635688; -.
DR KEGG; aqu:100635688; -.
DR eggNOG; KOG3714; Eukaryota.
DR InParanoid; A0A1X7V0Y1; -.
DR OrthoDB; 2876645at2759; -.
DR Proteomes; UP000007879; 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; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 2.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_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; PF00530; SRCR; 2.
DR PRINTS; PR00480; ASTACIN.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 2.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF56487; SRCR-like; 2.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS50287; SRCR_2; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196};
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:UP000007879};
KW Signal {ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 19..550
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5010755666"
FT DOMAIN 145..336
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 340..443
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 446..549
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT REGION 25..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 238
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 411..421
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 474..538
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 487..548
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 518..528
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 550 AA; 62356 MW; EDF89227BB203A02 CRC64;
MNSLTLLVLL FAAIQVQCSP AVPLNGKDGH APEGDKNAQK EVGVNKEERQ LLFGDNKSVM
KKDKDVIDYM EEKERVKKYN KNDTPAKELN DVTKDEESDV PIDDSGEYGS GEDIIEGDIK
VTPEEAAIFK RGGWKELVNS ESWVRGHGKW SRTIPYTVSD SNYPLYTEEY KALEYSIELF
HKFTCLKFVP KKSYHKDYID FASKTGCWSY IGKLPEGYAR PQEISLGRGC RGAIPAHEIM
HALGRGHEQS RFNRDKYVHI INDNIHPNFT HNFDEDYTDN MNIPYDYLSV MHYGSTAFSI
NGQPTIKAVP GPDIVMGQRN TISLYDILNI NIRYCPERAV RLVGGRGSFE GRVEMFWDGR
WGHVDGRPSE FKITNGRVIC KYLGFPDVSE IVQIPNQKHS VGPFFREPFV CNGDEDTPFS
CQYWGEKIFL LPAVVDEAAV ICEKNARLQG GRVTPLFAYG LLEVYVEGRW GAVCDDDFNI
RAANVACRQM GYTRALEYKT TTEYGKNKRP ILMDDVLCEG YEAQITHCPS TPIGEHDCRR
SDAISLFCVI
//
