ID   A0A3B0JP32_DROGU        Unreviewed;       501 AA.
AC   A0A3B0JP32;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=C-type lectin domain-containing protein {ECO:0000259|PROSITE:PS50041};
GN   ORFNames=DGUA_6G003133 {ECO:0000313|EMBL:SPP75339.1};
OS   Drosophila guanche (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP75339.1, ECO:0000313|Proteomes:UP000268350};
RN   [1] {ECO:0000313|Proteomes:UP000268350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Alioto T., Alioto T.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; OUUW01000001; SPP75339.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B0JP32; -.
DR   STRING; 7266.A0A3B0JP32; -.
DR   OrthoDB; 3660997at2759; -.
DR   Proteomes; UP000268350; Unassembled WGS sequence.
DR   CDD; cd00037; CLECT; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..501
FT                   /note="C-type lectin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017263730"
FT   DOMAIN          26..175
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   REGION          126..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..144
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..402
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..459
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   501 AA;  55094 MW;  1C3C9A5632ADB0C5 CRC64;
     MAKIILFCVL SLLACAAGQR ITTIHLDGVQ YFISRMNPYS PELNYFLAYQ YCRSLGLQLA
     SFETKEKAES MTTYLKNAGY GNYDFWTSGN RLGTGMFLWM STGLPFNATF DFFENSADAI
     QAGLLDPVDH NSNTSPQRTA RDSSSGAEKG CVILKQPTLK WMPEDCSAVK DFICEQTRCY
     YYNYGSIPVS SAQGRPITST TPRPPAALMH LHAATTTTPL PLLMSTTGGL YTAAKAKSSP
     AIAHRLAEEA SSPSFHSFKL NQDRSLTDKD AIDVEVDDQD ADMDAEEHDE HDHEHEHEVE
     SDGDVEGDDH DGDSDNFSEH ARELVGDGEG DDIKEHVFPL HDNELHHEMH SIEEVQQQLQ
     HHDEDAAPAA AAAAEESVSA EHEPEAEGDS DPEAEAEAET DSEAESQAPG QASEALPSST
     ESPAAAAIEE RIKQIAQDFQ KMASSQEMQT PSNEENLPKQ SLSLNDLIRT LRPNEQQIIP
     QIDSDYSNAM RVLGKTLVPH N
//