ID A0A2T7Q1F1_POMCA Unreviewed; 497 AA.
AC A0A2T7Q1F1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PVD39470.1};
GN ORFNames=C0Q70_02101 {ECO:0000313|EMBL:PVD39470.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD39470.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD39470.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD39470.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD39470.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVD39470.1}.
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DR EMBL; PZQS01000001; PVD39470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7Q1F1; -.
DR STRING; 400727.A0A2T7Q1F1; -.
DR EnsemblMetazoa; XM_025250068.1; XP_025105853.1; LOC112571211.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg1.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProt.
DR CDD; cd02872; GH18_chitolectin_chitotriosidase; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 2.170.140.10; Chitin binding domain; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
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; PF01607; CBM_14; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00494; ChtBD2; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
DR PROSITE; PS50940; CHIT_BIND_II; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119}.
FT DOMAIN 1..366
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 436..491
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
SQ SEQUENCE 497 AA; 53973 MW; CCC854CB3DE18141 CRC64;
MCYYTNWSQY RTGRGRFVPS NIDVNYCSHL IFAFAQVSDN QLNTVEWNDV LSYGDGGLYT
QFNNLKQQKP SLSTLLAVGG WNAGSSEFTR MVSTAATRAQ FVTSSISLLR TNNFDGLDLD
WEYPGQRGSP PEDKQRFALL VQELRQAFDN EARSTGRQRL LLTAAVPASL SAVDIGYDVP
TLNQYLDYFN LMEYDFFVGS EPQTGLNAPL NTQNPSSLSI VSSVNYWIQK GAARAKINLG
FPSYGHTFAL SSPSNAGIGA PAVGQGVPGT ITGQAGFLSY YEICDSVLSR YNIQRDPAGT
ELYGSLGTQW IAFDDVFSYQ SKLTWLNNNG LAGAIVWSVD LDDFTGGSCG TRYPLISVLG
SCLINGVNCS PTGSTAITQA PPPVTPAPTF APTAPPLVTR APTFAPTAPP TVFVPPTTPR
PVTFSPTTTA PSATGDAQCP SRSGLYRDVQ DCSAFWFCYL PLRWRFTCPP GTSFNQRTLV
CDFTSYVDCT AGFLFQG
//
