ID A0A2T7PVV4_POMCA Unreviewed; 1237 AA.
AC A0A2T7PVV4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PVD37548.1};
GN ORFNames=C0Q70_00142 {ECO:0000313|EMBL:PVD37548.1};
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:PVD37548.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD37548.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD37548.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD37548.1};
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:PVD37548.1}.
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DR EMBL; PZQS01000001; PVD37548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7PVV4; -.
DR STRING; 400727.A0A2T7PVV4; -.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02872; GH18_chitolectin_chitotriosidase; 2.
DR Gene3D; 3.10.50.10; -; 3.
DR Gene3D; 2.170.140.10; Chitin binding domain; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 3.
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; 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; 3.
DR SMART; SM00494; ChtBD2; 1.
DR SMART; SM00636; Glyco_18; 3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 3.
DR SUPFAM; SSF54556; Chitinase insertion domain; 3.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
DR PROSITE; PS50940; CHIT_BIND_II; 1.
DR PROSITE; PS51910; GH18_2; 3.
PE 3: Inferred from homology;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119}.
FT DOMAIN 1..316
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 387..746
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 788..1147
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 1184..1237
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT REGION 316..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1237 AA; 139807 MW; 6C527BD9C426276B CRC64;
METHTGGVDA GYKQFTDLKK NNPTIRILLS ISNWKEVSPF FSRMVKTEAD RSQFIKHSIS
VLRKHEFDGL DIFWKYSASQ GSKLEHRRLI TELVTELKHA YDEESKISGK PRLLLTAAVG
AGKAIIDSVY DIPEISKHLD FISLMTYNFH GFWEKVTGHH SPLYSTDTLN TDWAARYWVE
QGAPRDKLVI GVSYNGRSFT LKNPSENQVG AVSVRPGQPG PFTKTAGLLS YFEICGLLQK
DATRHFTEDQ KVPYLHSGDQ WVGYDDQHSL RHKVELAASY GGVMLWSLDL DDFSGDHCNE
GPYPLTKAVN TYCIEGGPSE PVNESEPDST PEPTSTSVPE KPNVEDIEEE KWNGTNLSEP
NSTPDPIVTP GPNPISDPGP HGAQTCERTV CYVTWWSQNR AGMASFKPEY VDTSLCTHLM
YAYAKVQNNQ IRQFYSNDEE RYKQFTDLKK NNPTIRILLA VGGWNHDNAG FTEMVKTGDD
RSQFIKNSIT VLRKHEFDGL TLDWRYPANR GSPPEDRRLF TELVKELKHA YDEESKISGK
PRLLLTAAVS VKKSIIDSAY EIPEISEHLD FMNLVTFYFD GPGENVTGHH SPLYSQDTRN
MDWAARYWVE QGAPRDKLVI GVSFYGKSFT LENPSEHQVG AVSVRPGQPG PITKRRGFLA
YYEVCDLLQK GTTRHFIEDQ KVPYLHKGDQ WIAYDDKDSL KYKVELAASY GGVMLWTLDL
DDFSGNHCDE GPYPLTKAVN EYCKVEDVEE EKWNGTNQSE PNSTPYPIVT PGPNPISDPG
PHGAQTCERI VCYVTRLSQY NAGMASFKPE YVDTSLCTHL IFAFAKVQGN QLLEYERNDE
EQYKQFTDLK KNNPTIRTLL AVGGWDQGSR GFSRMVKTEA DRSQFIKHSI TVLRKHEFDG
LDLDWMYPAT RGSPPEDRRL FTELVKELKH AYDEESKISG KPRLLLTAAV GVGKSVIDSA
YDIPEISEHL DFISLMTYDF HGSWEKVTGH HSPLYSTDTL NMDWAARYWV EKGAPRDKLV
IGVSFYGRSF TLKNPSEHQV GAVSVRPGQP GLFTKSAGLL SYFEICDLLQ NGATRHFIED
QKVPYLHKGD QWVGYDDKDS LKFKVDLSVS YGGVMLWNLD VDDSTGHHCN EGAYPLTKAV
NTYCKRGIES GPPGPVDQSD PDSTPAPTST SVPEITDDDD KEIKEFCKGK PNDMYSDPKN
STYFIYCSEG IPYRRPCPAG LVFSPMFRLC DWPRHWR
//
