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Database: UniProt
Entry: A0A0E0DH14_9ORYZ
LinkDB: A0A0E0DH14_9ORYZ
Original site: A0A0E0DH14_9ORYZ 
ID   A0A0E0DH14_9ORYZ        Unreviewed;      1654 AA.
AC   A0A0E0DH14;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=alpha-L-fucosidase {ECO:0000256|ARBA:ARBA00012662};
DE            EC=3.2.1.51 {ECO:0000256|ARBA:ARBA00012662};
OS   Oryza meridionalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI04G17980.1};
RN   [1] {ECO:0000313|EnsemblPlants:OMERI04G17980.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI04G17980.1};
RA   Wing R.A., Panaud O., Henry R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OMERI04G17980.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family.
CC       {ECO:0000256|ARBA:ARBA00007951}.
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DR   STRING; 40149.A0A0E0DH14; -.
DR   EnsemblPlants; OMERI04G17980.1; OMERI04G17980.1; OMERI04G17980.
DR   Gramene; OMERI04G17980.1; OMERI04G17980.1; OMERI04G17980.
DR   HOGENOM; CLU_003188_1_0_1; -.
DR   Proteomes; UP000008021; Chromosome 4.
DR   GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00051; EFh; 2.
DR   CDD; cd05117; STKc_CAMK; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000933; Glyco_hydro_29.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24349:SF570; CALCIUM-DEPENDENT PROTEIN KINASE 12; 1.
DR   PANTHER; PTHR24349; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF01120; Alpha_L_fucos; 1.
DR   Pfam; PF13499; EF-hand_7; 4.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00812; Alpha_L_fucos; 1.
DR   SMART; SM00054; EFh; 6.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS00018; EF_HAND_1; 6.
DR   PROSITE; PS50222; EF_HAND_2; 6.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          93..352
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          411..446
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          447..482
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          483..518
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          1162..1431
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1473..1508
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          1509..1544
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          1545..1580
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          1..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1084..1152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1122..1137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1191
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1654 AA;  183169 MW;  C1E0BC008C6C8EC3 CRC64;
     MGNCFTKTYE IPITSGTMRR PASTAERSKA RGGDEPGTWR RPSFPRHGAP PHRPPTSSST
     SSSAAGALSR RASGGGEMGP VLQRPMVSVR SLYQLDRKLG SGQFGTTYLC TERATGNWYA
     CKSVSKRKLV RRTDVDDVRR EITILQHLSG QPNIAEFRGA YEDNDHVHLV MEFCSGGELF
     DRITAKGSYS ERQAAAVCRD ILTVVHVCHF MGVIHRDLKP ENFLLASADD DAPLKAIDFG
     LSVFIEEGKV YKDIVGSAYY VAPEVLQRNY GKEADIWSAG VILYILLCGT PPFWAETEKG
     IFDAILVNQV DFSTSPWPSI SESAKDLIRQ MLHRDPQKRI TASQALGSTP EFVANSLNGC
     LHAAEHRWLK EGGASDRPID SAVLSRMKQF KAMNKLKQLA LKVIAENLSP EEIKGLKQMF
     NNMDTDRSGT ITVEELKVGL TKLGSRISEA EVQKLMEAVD VDKSGSIDYS EFLTAMINKH
     KLEKEEDLLR AFQHFDKDNS GYITRDELEQ AMAEYGMGDE ANIKQVLDEV DKDKLKLTMA
     TILLLLLGLL VGLLLLRAHG VTGSPAPTPP PLPVLPVPSY AQLRWQLSEM ALFIHFGPNT
     FTDSEWGSGR ADPAVFAPSA LDAGQWARAA AAGGFGRVVL TAKHHDGFCL WPSALTNYSV
     AASPWKGGAG DVVGELAAAA RAEGIGLGLY LSPWDRHEPV YGDTVAYNEH YLGQMTELLT
     RYGDVEEVWL DGAKGEGKDM DYMFDAWFAL IHQLQQRVVI FSDAGPDTRW VGDEAGVAGY
     TCWSPFNKST VTIGHIIPEY SRCGDPFGQD WVPAECDVSI RPGWFWHASE KPKNATTLLD
     IYYKSVGRNC LLILNVPPNS SGLISTEDMQ VLQEFTEILQ TIFSQNFAAN ATVAASTVRG
     GLGNQQFAPS NVLQESIYSY WAPEEGESSW EMLFDLGQSA SFNVIQLQEP IQMGQRVIKF
     RVEILVDELW QTIVEGTTIG YKRLLQFPVV EGQFLKLSID GARADPLISF FGVFMDSFSV
     TYSLENHEKP SVVNSSEVIM LRTDHSIGNK SIATMRRKGK EKGNEEAFAM GNCFTKTYEI
     PITSGTMRRP ASTAERSKAR GGDEPGTWRR PSFPRHGAPP HRPPTSSSTS SSAAGALSRR
     ASGGGEMGPV LQRPMVSVRS LYQLDRKLGS GQFGTTYLCT ERATGNWYAC KSVSKRKLVR
     RTDVDDVRRE ITILQHLSGQ PNIAEFRGAY EDNDHVHLVM EFCSGGELFD RITAKGSYSE
     RQAAAVCRDI LTVVHVCHFM GVIHRDLKPE NFLLASADDD APLKAIDFGL SVFIEEGKVY
     KDIVGSAYYV APEVLQRNYG KEADIWSAGV ILYILLCGTP PFWAETEKGI FDAILVNQVD
     FSTSPWPSIS ESAKDLIRQM LHRDPQKRIT ASQALANSLN GCLHAAEHRW LKEGGASDRP
     IDSAVLSRMK QFKAMNKLKQ LALKVIAENL SPEEIKGLKQ MFNNMDTDRS GTITVEELKV
     GLTKLGSRIS EAEVQKLMEA VDVDKSGSID YSEFLTAMIN KHKLEKEEDL LRAFQHFDKD
     NSGYITRDEL EQAMAEYGMG DEANIKQVLD EVDKDKVFRR GKKDSVSCKL KAEENFTSET
     NLLGWAALGP QKRDLPLATT ETIEQSTLRH AELN
//
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