DTML2_DICDI
ID DTML2_DICDI Reviewed; 599 AA.
AC Q54CQ0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Dictomallein-2;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=dtmlB; ORFNames=DDB_G0292822;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the dictomallein family. {ECO:0000305}.
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DR EMBL; AAFI02000197; EAL60960.1; -; Genomic_DNA.
DR RefSeq; XP_629366.1; XM_629364.1.
DR AlphaFoldDB; Q54CQ0; -.
DR STRING; 44689.DDB0252868; -.
DR PaxDb; Q54CQ0; -.
DR EnsemblProtists; EAL60960; EAL60960; DDB_G0292822.
DR GeneID; 8628883; -.
DR KEGG; ddi:DDB_G0292822; -.
DR dictyBase; DDB_G0292822; -.
DR eggNOG; ENOG502SN3T; Eukaryota.
DR HOGENOM; CLU_451780_0_0_1; -.
DR InParanoid; Q54CQ0; -.
DR OMA; HAGEAYD; -.
DR PhylomeDB; Q54CQ0; -.
DR PRO; PR:Q54CQ0; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 InterPro; IPR019503; Peptidase_M66_dom.
DR PROSITE; PS51694; PEPTIDASE_M66; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..599
FT /note="Dictomallein-2"
FT /id="PRO_0000322647"
FT DOMAIN 145..407
FT /note="Peptidase M66"
FT ACT_SITE 299
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 599 AA; 67712 MW; F35FD52A67249CDC CRC64;
MKLILIYLIL VFNLFNFINC QNILKVSNVR FAQTHVIPIE GKSWNIQGST KHMSIVGKRR
ALLLASFQDQ NLSYFATIWY DGGKVGMIQL NDPSQLPLTE DNGEKYSKVH HSGMIPKEWV
RVGMKIQFSS FGGINGTEVS DILSPDVGQD YTLKMWILPF YLFGANDTNT QPFSKTKGID
SGISKELIEK WSCSDLQADN HPIQKIDWPY FVMEPRSGNP AMVITNSDQK KDGYAIMNGV
LSILWLLRGM FGESSSSIQI YSPLLHLDAK GRYADTYGGL GGSSAGTGNH RFTGIFIHEQ
GHAMGLPHAG EAYDNKRKYP YKQGSLSGSE WGFDANHNEF LGTFIPPTAE LYKTCKKNSI
IDSKGRCVKQ SVMQSGAGDQ SSKYRYSMFA DFEMTTIQNY FKNSIYYDET NGKYKKWNDT
SKSYYAYKPI TKEKGFEGVD ENTPIERNVD IYSIIFTYST VEKPKVGKIS QIYPLLKSKG
NLIRQFDPTN KKEMDSVNPK LNGEFKWYCN SSGCDYTIRV TFYDSSLKHV LLQQGKRKYK
LPTGSFRDNI NDPKSSDSFM LGGVNIKANK KIKKVELLET PFAWNGIPKN PTVLVSKSF