ID E9GBH0_DAPPU Unreviewed; 645 AA.
AC E9GBH0;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN ORFNames=DAPPUDRAFT_316025 {ECO:0000313|EMBL:EFX83156.1};
OS Daphnia pulex (Water flea).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX83156.1, ECO:0000313|Proteomes:UP000000305};
RN [1] {ECO:0000313|EMBL:EFX83156.1, ECO:0000313|Proteomes:UP000000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21292972; DOI=10.1126/science.1197761;
RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT "The ecoresponsive genome of Daphnia pulex.";
RL Science 331:555-561(2011).
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; GL732538; EFX83156.1; -; Genomic_DNA.
DR AlphaFoldDB; E9GBH0; -.
DR EnsemblMetazoa; EFX83156; EFX83156; DAPPUDRAFT_316025.
DR KEGG; dpx:DAPPUDRAFT_316025; -.
DR eggNOG; KOG3538; Eukaryota.
DR HOGENOM; CLU_023955_0_0_1; -.
DR InParanoid; E9GBH0; -.
DR OMA; VESENLC; -.
DR PhylomeDB; E9GBH0; -.
DR Proteomes; UP000000305; 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:UniProtKB-KW.
DR Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR041645; ADAMTS_CR_2.
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:SF275; STALL, ISOFORM C; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000305};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT DOMAIN 82..298
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 44..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 250
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 645 AA; 70468 MW; F6780137FCFB0E3B CRC64;
MIGAHIVRAV DPFPHLKAHQ ESCDVELPVQ IKSNITRQSV VMEPETIEKR KSNKASTDKS
SKNVGKNALE KTIGSKAAAP NKVIELGVFV DSAALSLFMP YLGAREYVKL RELILAFVNA
MQALYHLPSL GQRVDLSIVY MEFHAKPPAN LVNNGERGQL LDSFCSFQTK LNKPSDSDAE
HWDMALLLSG LDFYAVEKGK NNYVTMGLST VTGVCTDIYN CVIGEFGVTN QRGQPYPSTG
FTSVYVMAHE IGHNLGMSHD SSGNVCATEG FIMSPSRGVV GEATWSTCSA KTLASITETC
MNDLPSGNFP DYNHNKYGDR PGQLWSADEQ CRILLRDKAA IAYFATNADI AESCNSMKCR
TPNRDGYYSS GPALPGTVCG NSMWCNGGKC VSAGRALNVE AVRGGWSDWK NKTCSSGCLQ
KSRGAVESER ECNNPKPSDV LHRCEGSSIK ATICDDAQLC GEKSRPTPVE YAGQQCAKFS
KLVPFIDPKG TGIQAAFSEK RPWQSCAIFC QRNDREGFYS PRFELNSLPE VSAHFPDGTW
CGNDGQKDLY CLQRSCASTE VAEGLVRTSG ISSDLDMANN APMTGKVHHQ IPAALEEYFM
LDKDGKPVKE EIDEETVKAA EESLNSHSGY DDQDFITLKP PKSKI
//