Y1137_DICDI
ID Y1137_DICDI Reviewed; 185 AA.
AC Q54F36;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Lysozyme C-like protein DDB_G0291137;
DE Flags: Precursor;
GN Name=lyC2; ORFNames=DDB_G0291137;
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family. {ECO:0000305}.
CC -!- CAUTION: Although related to the glycosyl hydrolase 22 family, lacks
CC the conserved Asp active site, suggesting it may not have lysozyme
CC activity. {ECO:0000305}.
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DR EMBL; AAFI02000175; EAL61852.1; -; Genomic_DNA.
DR RefSeq; XP_635354.1; XM_630262.1.
DR AlphaFoldDB; Q54F36; -.
DR SMR; Q54F36; -.
DR STRING; 44689.DDB0189256; -.
DR PaxDb; Q54F36; -.
DR EnsemblProtists; EAL61852; EAL61852; DDB_G0291137.
DR GeneID; 8628002; -.
DR KEGG; ddi:DDB_G0291137; -.
DR dictyBase; DDB_G0291137; lyC2.
DR HOGENOM; CLU_118817_0_0_1; -.
DR InParanoid; Q54F36; -.
DR PhylomeDB; Q54F36; -.
DR PRO; PR:Q54F36; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
DR InterPro; IPR001916; Glyco_hydro_22.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR PANTHER; PTHR11407; PTHR11407; 1.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00263; LYZ1; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..185
FT /note="Lysozyme C-like protein DDB_G0291137"
FT /id="PRO_0000389026"
FT REGION 137..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 52
FT /evidence="ECO:0000250"
FT DISULFID 47..126
FT /evidence="ECO:0000250"
FT DISULFID 77..84
FT /evidence="ECO:0000250"
FT DISULFID 81..99
FT /evidence="ECO:0000250"
SQ SEQUENCE 185 AA; 19626 MW; 107437A3C5DF1E96 CRC64;
MFKTLSKSIG FLVAIIALVK GDTYTCSQMQ SLAEGYFRGP TLTTMLCISY YESTYNTQAI
NPTSKAAGLF QILPEHCGEL CKTCTTPSDL LNPTINTECA KSILNSQGFK AWTTYASGDC
KNWNKCVAPS ASTHAASTHG STGPSTHGST THGSTTSTTY TSGASSGLFD FKANNGGGQD
MVKYF