ID A0A3Q7J033_SOLLC Unreviewed; 1028 AA.
AC A0A3Q7J033;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=alpha-L-fucosidase {ECO:0000256|ARBA:ARBA00012662};
DE EC=3.2.1.51 {ECO:0000256|ARBA:ARBA00012662};
DE AltName: Full=CCT-beta {ECO:0000256|ARBA:ARBA00033237};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc11g069000.2.1};
RN [1] {ECO:0000313|EnsemblPlants:Solyc11g069000.2.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc11g069000.2.1};
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2] {ECO:0000313|EnsemblPlants:Solyc11g069000.2.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc11g069000.2.1};
RG EnsemblPlants;
RL Submitted (JAN-2019) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC {ECO:0000256|ARBA:ARBA00008020, ECO:0000256|RuleBase:RU004187}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family.
CC {ECO:0000256|ARBA:ARBA00007951}.
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DR AlphaFoldDB; A0A3Q7J033; -.
DR STRING; 4081.A0A3Q7J033; -.
DR PaxDb; 4081-Solyc11g069000-1-1; -.
DR EnsemblPlants; Solyc11g069000.2.1; Solyc11g069000.2.1; Solyc11g069000.2.
DR Gramene; Solyc11g069000.2.1; Solyc11g069000.2.1; Solyc11g069000.2.
DR InParanoid; A0A3Q7J033; -.
DR Proteomes; UP000004994; Chromosome 11.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IBA:GO_Central.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR CDD; cd03336; TCP1_beta; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 3.50.7.10; GroEL; 1.
DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1.
DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 1.
DR InterPro; IPR012716; Chap_CCT_beta.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000933; Glyco_hydro_29.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR NCBIfam; TIGR02341; chap_CCT_beta; 1.
DR NCBIfam; NF041083; thermosome_beta; 1.
DR PANTHER; PTHR11353; CHAPERONIN; 1.
DR PANTHER; PTHR11353:SF23; T-COMPLEX PROTEIN 1 SUBUNIT BETA; 1.
DR Pfam; PF01120; Alpha_L_fucos; 1.
DR Pfam; PF00118; Cpn60_TCP1; 2.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1.
DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004187};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004187};
KW Reference proteome {ECO:0000313|Proteomes:UP000004994};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1028
FT /note="alpha-L-fucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018691402"
SQ SEQUENCE 1028 AA; 113772 MW; C69EA236CD9A5004 CRC64;
MIKKKPITQF LKTIIILLLF QLSTSSHRKP PPLPILPIPK SRQISWQIAE MALFLHFGTN
TFTDSEWGTG HVDPSIFNPK LLNATQWVTV AKDFGFKRVV LTAKHHDGFC LWPSKYTDYS
VKSSPWRNGV GDIVADLAEA ARNGGLELGL YLSPWDRHEH CYGETLEYNE YYMGQMTELL
TRETSNNKHS QISTPAEKNL LSRYGEIKYV FLDGAKGDGE KDMEYFFDDW FSLIHQLQPG
ASIFSDVGPD TRWVGNENGV AGSTCWSLFN GSNVKIGGYS DARYSAEGDA FGQDWVPAEC
DVSIRSGWFW HASEKPKSAM TLLDLYYKSV GRNCPLLLNV PPNSSGLISD EDIHVLKEFS
ELRNSIFSHN LAKSALLSAS SIRGDSNDTQ FSPKNVIEEG LHTYWAPDQG QQSDWTLYLQ
FQQVITFNVL GLQEPIQMGQ RIIEFHLDML DENGKWQHVV NGTTVGYRRL LLFPTVKSHL
LSSQIDKLFK DEATEEKGER ARMASFIGAM AIADLVKTTL GPKGMDKILQ STGRGHSVTV
TNDGATILKS LHIDNPAAKV LVGKVGSYPK TNPLNIMFNR FIWTNGKQDE EVGDGTTSVV
VLAGELLREA EKLVNAKIHP MTIIAGFRMA SECARNVLEQ KVVDNKQDAE KFRSDLMNIA
RTTLSSKILS QDKEHFAKLA VDAVMRLKGS TNLEAIQIIK KPGGSLKDSF LDEGFILDKK
IGVGQPKRIE NAKILVANTA MDTDKVKIYG ARVRVDSMAK VADLEAAEKE KMREKVQKII
SHGINCFVNR QLIYNFPEEL FADAGILAIE HADFDGIERL GLVTGGEIAS TFDNPESVKL
GHCKLIEEIM IGEDKLIHFS GVAMGQACTI VLRGASPHVL DEAERSLHDA LCVLSQTVND
SRVLLGGGWP EMVMAKAVDE LAKKTPGKRS HAIEAFTRAL LAIPTTIADN AGLDSAELIA
QLRAEHHKDE SNAGIDVISG SVGDMSELGI SESFKVKQAV LLSATEAAEM ILRVDEIITC
APRRREGM
//
