ID A0A2T7PTZ3_POMCA Unreviewed; 460 AA.
AC A0A2T7PTZ3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=C0Q70_03887 {ECO:0000313|EMBL:PVD36896.1};
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:PVD36896.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD36896.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD36896.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD36896.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000966,
CC ECO:0000256|RuleBase:RU361166};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000256|ARBA:ARBA00007072, ECO:0000256|PROSITE-ProRule:PRU10060,
CC ECO:0000256|RuleBase:RU361166}.
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:PVD36896.1}.
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DR EMBL; PZQS01000002; PVD36896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7PTZ3; -.
DR STRING; 400727.A0A2T7PTZ3; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg2.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF00759; Glyco_hydro_9; 2.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS00698; GH9_3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PROSITE-ProRule:PRU10060};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW ECO:0000256|RuleBase:RU361166};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW ProRule:PRU10060};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU10060};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10060};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 23..460
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5015374394"
FT DOMAIN 49..278
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT DOMAIN 295..450
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT REGION 26..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 428
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 437
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 460 AA; 51103 MW; 6A14B03F04801591 CRC64;
MMAPMLVFVL TVVLLRIEPI RGLESGASDT RRRAPEASST PAGPPPKRYN EALRLSNLFY
YAQRSGKLPA NNPVPWRKDS ALLDCVVGGF YDAGDHVKFG FPFGAAMTML LWGVVRFRDG
YVYAGQLDDV YTISKWGLDY MVNSWDPFRE ELVIQVGDGD IDHQFWGRPE DMTMPRPCLK
IGVNRDGSDV AADYAAALAA GSIVFREKGD VQYARELLLT AESIYDFAVN NRGLYSNTLS
AAQQQYYRST NDKDEMCVAG VWLFKATGDD KYLYQAELAA VRGHREAHVR GGYRSFLKGW
QPGGFVQYTP CGLAWSEQTY WGSNRHAANV AFAALVAAED GIAPEVNRKW AAEQINYILG
DNPHDGGCFS YEIGYGNKYP LRPHHRAASC PDPPATCDQR NLNTDNPSPH ILYGGLVGGP
ILNDGYNDTR PDYVHNEVAL DYNSGFQSAL AGRWRCNTLL
//
