DTML1_DICDI
ID DTML1_DICDI Reviewed; 592 AA.
AC Q54J86;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Dictomallein-1;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=dtmlA; ORFNames=DDB_G0288219;
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; AAFI02000109; EAL63340.1; -; Genomic_DNA.
DR RefSeq; XP_636850.1; XM_631758.1.
DR AlphaFoldDB; Q54J86; -.
DR SMR; Q54J86; -.
DR PaxDb; Q54J86; -.
DR EnsemblProtists; EAL63340; EAL63340; DDB_G0288219.
DR GeneID; 8626518; -.
DR KEGG; ddi:DDB_G0288219; -.
DR dictyBase; DDB_G0288219; -.
DR eggNOG; ENOG502SN3T; Eukaryota.
DR HOGENOM; CLU_451780_0_0_1; -.
DR InParanoid; Q54J86; -.
DR PhylomeDB; Q54J86; -.
DR PRO; PR:Q54J86; -.
DR Proteomes; UP000002195; Chromosome 5.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..592
FT /note="Dictomallein-1"
FT /id="PRO_0000322646"
FT DOMAIN 140..402
FT /note="Peptidase M66"
FT ACT_SITE 295
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 592 AA; 65793 MW; D256499FDB53A2AA CRC64;
MKILIILLVF LNLITNINCA VCSSRLQVSD IKFANTHVLP IEGKSWKNNT VTLKILPNRE
SLLLAKFQDQ TLSYTVKVWV DDSLMGKLTL NDPSKLPPTE SNGTKYSTVH HSIRIPKDWM
KPKMKIQFST MLLKSEFFFP NIGHETNLNM WLLPFYLFGA NDTNTQPLSV TGSISKDVSD
ELIQKWSLSS LNALNHPISR IDWSYLILPA GRNNLPGLRI TNSDQKRDGY EIMSVVLGIL
SGIRGANGEG PSSVLYYAPL IHLGANGKYA DPWGGLGGGS VGTGDYSYTG IFIHEAGHSY
GLPHAGDSYK SGNYPYVDGS LLGSEWGFDM NHNEFLSVNI PSNIGAYKNC NKSFILDQNK
NCVKQSVMQG GAGNQAQGYR YSMFADYEEV TIQNYFKDSI IYDKSFSTGY KKWNTTTLKY
ETYTPSTKSN GLYGINDGLP IERNVDVYTI IITHSFVGPA NLSQIYPIFK SKGNLMPFFD
PTNSTQLVDI RPNVSKYAWY CHANGCDYTI KITYTDGTTK YMLLQRGKRS WFSPSGAIGS
GFTDPLSGES SLSVIFNIKA DKTPSKIELF ETLLGFNGFN STTATLLVSQ SF