ID E9FQX7_DAPPU Unreviewed; 848 AA.
AC E9FQX7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
DE Flags: Fragment;
GN ORFNames=DAPPUDRAFT_39648 {ECO:0000313|EMBL:EFX90290.1};
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:EFX90290.1, ECO:0000313|Proteomes:UP000000305};
RN [1] {ECO:0000313|EMBL:EFX90290.1, 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
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; GL732523; EFX90290.1; -; Genomic_DNA.
DR AlphaFoldDB; E9FQX7; -.
DR MEROPS; M12.231; -.
DR KEGG; dpx:DAPPUDRAFT_39648; -.
DR eggNOG; KOG3538; Eukaryota.
DR HOGENOM; CLU_000660_1_1_1; -.
DR InParanoid; E9FQX7; -.
DR OMA; HYDGICY; -.
DR PhylomeDB; E9FQX7; -.
DR Proteomes; UP000000305; Unassembled WGS sequence.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 4.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF200; ADAM METALLOPEPTIDASE WITH THROMBOSPONDIN TYPE 1 MOTIF B, ISOFORM B; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 3.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 4.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 4.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 4.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000305};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT DOMAIN 92..304
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 43..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 241
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 170..224
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 199..206
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 218..299
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 257..283
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 326..349
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 337..356
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 344..375
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 369..380
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 403..440
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 407..445
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 418..430
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT NON_TER 848
FT /evidence="ECO:0000313|EMBL:EFX90290.1"
SQ SEQUENCE 848 AA; 94319 MW; CBCA8344854DA139 CRC64;
QTGYVAIGGE EYIIEPIKGH PNASADQQQR EHPHLIYKRS ALSAAANDQE TSHGDGHGTC
GNDEKWQETQ SELAGERGQR HSIRKRSVSL ERNVETLVVA DQKMTEFYSN EDIETYILTV
MNMVSALYRD ASIGNAINIV MVRLMLLENE ALEEGLDISH HADNTLKSFC KWQATINPET
DDHPNHHDVA ILLTRYNICT RVNEPCSTLG LAEVAGMCQS YRSCSVNEDT GLSLAYTVAH
ELGHNFGAHH DGPTNGCEPL SGDQHVMSPQ LSSDAGPLVW SNCSRKDITR FLDRNWGTCL
EDSPSDHEFH YPELPPGAMY NIDHQCRLQY GPETMHCAGM DEVCQTLWCK LPDNRCVSRL
EPAAPGTSCA KHKWCSNGHC VQMGDRPQVI DGEWGEWGPW SDCTRTCGAG LASSARLCDN
PAPAHGGKYC VGERRRYRVC NLDPCPADGP SYRAVQCSAF DATPYKGENH TWLPVQMKSA
PCQLHCKPEG QFFSVMLSDS VVDGTPCNPG TRDMCINGVC RRVACDWGID SKAQEDRCGV
CHGDGTQCNT IRGNYTEPDG IDYIEMVVIP KGARNIRFVE ADEAANYIAI QSVETNEYYL
NGQWTVQWSG EYRAGVTLIY YRREEELDEI HIPGPSMEDL RFLLLYRVPN PGVSYEYTVA
NENITRTPEF RWEYMDWSVC TATCGGGTQV SQPKCMEKEA GLVEETYCAA LAKPEEKSRS
CNKQSCPPRW WVGPWQHCSI TCGKGRGLRK RTVICVRSLS DDEQMALHDA DCPVTDRPTE
EDACEPLAPC PGEASWETGT WSKCSVRCDG GTRVRDVSCY ETTTSTLVDD ALCTDFKPDD
VESCNEVG
//
