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Database: UniProt
Entry: Q588C0_CRYJA
LinkDB: Q588C0_CRYJA
Original site: Q588C0_CRYJA 
ID   Q588C0_CRYJA            Unreviewed;       278 AA.
AC   Q588C0;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Xyloglucan endotransglucosylase/hydrolase {ECO:0000256|RuleBase:RU361120};
DE            EC=2.4.1.207 {ECO:0000256|RuleBase:RU361120};
OS   Cryptomeria japonica (Japanese cedar) (Cupressus japonica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Cupressaceae;
OC   Cryptomeria.
OX   NCBI_TaxID=3369 {ECO:0000313|EMBL:BAD93484.1};
RN   [1] {ECO:0000313|EMBL:BAD93484.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Shigeta S., Fujita Y., Ono K., Aki T., Kawamoto S.;
RT   "Molecular cloning and characterrization of Japanese cedar pollen major
RT   allergen No.121 homologycal with xyloglucan endotransglycosylase(XET).";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes xyloglucan endohydrolysis (XEH) and/or
CC       endotransglycosylation (XET). Cleaves and religates xyloglucan
CC       polymers, an essential constituent of the primary cell wall, and
CC       thereby participates in cell wall construction of growing tissues.
CC       {ECO:0000256|RuleBase:RU361120}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000256|RuleBase:RU361120}. Secreted, extracellular space,
CC       apoplast {ECO:0000256|RuleBase:RU361120}.
CC   -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC       enzymatic activity. {ECO:0000256|RuleBase:RU361120}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC       {ECO:0000256|RuleBase:RU361120}.
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DR   EMBL; AB197670; BAD93484.1; -; mRNA.
DR   AlphaFoldDB; Q588C0; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0016762; F:xyloglucan:xyloglucosyl transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042546; P:cell wall biogenesis; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0010411; P:xyloglucan metabolic process; IEA:InterPro.
DR   CDD; cd02176; GH16_XET; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR044791; Beta-glucanase/XTH.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR008263; GH16_AS.
DR   InterPro; IPR010713; XET_C.
DR   InterPro; IPR016455; XTH.
DR   PANTHER; PTHR31062; XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE PROTEIN 8-RELATED; 1.
DR   PANTHER; PTHR31062:SF304; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE PROTEIN 24; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   Pfam; PF06955; XET_C; 1.
DR   PIRSF; PIRSF005604; XET; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS01034; GH16_1; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   2: Evidence at transcript level;
KW   Apoplast {ECO:0000256|RuleBase:RU361120};
KW   Cell wall {ECO:0000256|RuleBase:RU361120};
KW   Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU361120};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361120};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361120};
KW   Secreted {ECO:0000256|RuleBase:RU361120};
KW   Signal {ECO:0000256|RuleBase:RU361120};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361120}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|RuleBase:RU361120"
FT   CHAIN           23..278
FT                   /note="Xyloglucan endotransglucosylase/hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361120"
FT                   /id="PRO_5005143516"
FT   DOMAIN          14..212
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
FT   ACT_SITE        98
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT   ACT_SITE        102
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-1"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005604-2"
SQ   SEQUENCE   278 AA;  31558 MW;  873E5228CF3864DE CRC64;
     MDLLPCFLLL SLALSFSHLA SANFFNDFDI TWGNDRAKIL DNGQRLQLTL DQSSGSGFQS
     KNEYLFGKID MQIKLVPGNS AGTVTAYYLS SQGDKHDEID FEFLGNLSGD PYIMHTNVFS
     QGKGSREQQF YLWFDPTADF HTYSLLWNPH QIMFSVDGTP VRVFKNSEDL GFAYPKNQAM
     RIYSSLWNAD DWATRGGAVK IDWSKSPFVA SYGNFKAETC SASSDCSVNS WYGAQALELS
     EQEKLEWVRK NYMIYNYCTD SKRFPQGFPA ECTRQTSN
//
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