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Database: UniProt
Entry: A0A182T4N0_9DIPT
LinkDB: A0A182T4N0_9DIPT
Original site: A0A182T4N0_9DIPT 
ID   A0A182T4N0_9DIPT        Unreviewed;       595 AA.
AC   A0A182T4N0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=GH18 domain-containing protein {ECO:0000259|PROSITE:PS51910};
OS   Anopheles maculatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles; Anopheles maculatus group.
OX   NCBI_TaxID=74869 {ECO:0000313|EnsemblMetazoa:AMAM019547-PA, ECO:0000313|Proteomes:UP000075901};
RN   [1] {ECO:0000313|Proteomes:UP000075901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=maculatus3 {ECO:0000313|Proteomes:UP000075901};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles maculatus species B.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMAM019547-PA}
RP   IDENTIFICATION.
RC   STRAIN=maculatus3 {ECO:0000313|EnsemblMetazoa:AMAM019547-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC       {ECO:0000256|RuleBase:RU004453}.
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DR   AlphaFoldDB; A0A182T4N0; -.
DR   EnsemblMetazoa; AMAM019547-RA; AMAM019547-PA; AMAM019547.
DR   VEuPathDB; VectorBase:AMAM019547; -.
DR   OrthoDB; 2663738at2759; -.
DR   Proteomes; UP000075901; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          175..558
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   REGION          561..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..587
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   595 AA;  67650 MW;  C72028C5B58A4FC5 CRC64;
     MSKQQGKYEL LKEDTKLRRQ HTYIQSCLLI ALCGMSSLTV YATWTMIYRQ NLIIPPALLD
     VSHHWRNRLV LYEEALRQTL KQQQNTLPNY PDNPASGRDS KGTIVKSIYA NNGSAMLPDN
     IFRATNPAAN DDKYQSSKSV EPLHVKELDS ERIFPSRFGN YIYSKEAMNG QPPSPKIVCY
     YTTPVMNAAR QQGVIGRGHN LRHILQPEHI DPYLCTHLNI GIIDIVNHTL YIDNNVREAL
     VSTKQLRRVN PSLRILLWVG GASVGGFAEM VENHATRKLF IQSLKAALEL YHLDGVDLDW
     EFPDNGGKRR MHFSQLLHEI RREYQREHRT YILSVAVAPQ ETIAYMAYDV TEINNYADYV
     NLMTYDYHFY SPDLPQTGLN APLYRRANEH SLLGTLNINE SVHYWLSAGL EKNKLILGLP
     TYGHSFTLVN PFNTRIGAPA SNFGRVGTLG FASYSEICWF RRYNIYVHQV YDVDSCSPYL
     YSGSEWISYE DERSLECKAK YIKSHGFGGA MIFSLNTDDF GSYCAENALY RDVTEAGASK
     NQASFPLLRK VRSVLVEPDA NRTATNHHQQ KQLELLSGAS SASLGATDSK EEDTR
//
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