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Database: UniProt
Entry: E9GBI1_DAPPU
LinkDB: E9GBI1_DAPPU
Original site: E9GBI1_DAPPU 
ID   E9GBI1_DAPPU            Unreviewed;       541 AA.
AC   E9GBI1;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN   ORFNames=DAPPUDRAFT_100864 {ECO:0000313|EMBL:EFX82961.1};
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:EFX82961.1, ECO:0000313|Proteomes:UP000000305};
RN   [1] {ECO:0000313|EMBL:EFX82961.1, 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; EFX82961.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9GBI1; -.
DR   EnsemblMetazoa; EFX82961; EFX82961; DAPPUDRAFT_100864.
DR   KEGG; dpx:DAPPUDRAFT_100864; -.
DR   eggNOG; KOG3538; Eukaryota.
DR   HOGENOM; CLU_037555_0_0_1; -.
DR   InParanoid; E9GBI1; -.
DR   OMA; QCKTPHR; -.
DR   PhylomeDB; E9GBI1; -.
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:InterPro.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF251; PEPTIDASE M12B DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:ARBA00023049};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000305};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..541
FT                   /note="Peptidase M12B domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012022718"
FT   DOMAIN          247..463
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   REGION          66..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        415
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         414
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         418
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         424
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   541 AA;  60090 MW;  10431508355BD5D7 CRC64;
     MRWILFLSAI GLASAGVLPE PSELLRSLHT LMNVDELGRT FGVDNSSQVD DYEVVYIRRH
     RSFMPEDPLQ RNASPKTKRS GPRENHAHYS FAANGKNYNL KVRPNNFLMA PNMKTVVRSS
     GEQVKEIVEE HRRECHFLNI DGGIVAALSH CTKNDIRGYV IDEGRSLEIL PIAMRLRQML
     RSPVENDNSV VGAHILRSVD PYERLRAHQV EVNLIDKEVT IGEKSKTISD AKGNSRNANN
     DRTAPNKIIE LGIFVDYMAV SLFMPYLGAK QYGKLRELIL TFVNAMQALY HLPSLGQRID
     FTIVYMEFQE KAPINLINSG DRGKLLDSFC AFQTKLNEPS DSDAEHWDIA FLLSGLDFYS
     VEGGKNNYVT MGLSTVTGVC TNNYNCVIGE FGVTNQQGQP YPSTGFTSVY VMAHEIGHNL
     GMSHDSSGNT CTTEGFIMSP SRGVVGEATW STCSASTLAK VTETCMNDLP TANHPEYNDD
     KYGDRPGQSW PADEQCRLLL RDPVAFAYFA TSADIAASCN SLKCKTPNRD GFFTSGPALF
     S
//
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