UniProt: A0A059BYT9

Database: UniProt
Entry: A0A059BYT9_EUCGR

LinkDB:  A0A059BYT9_EUCGR 
Original site:  A0A059BYT9_EUCGR

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (1)   
All databases (20)   

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ID   A0A059BYT9_EUCGR        Unreviewed;      1092 AA.
AC   A0A059BYT9;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Cellulose synthase {ECO:0000256|RuleBase:RU361116};
DE            EC=2.4.1.12 {ECO:0000256|RuleBase:RU361116};
GN   ORFNames=EUGRSUZ_F04216 {ECO:0000313|EMBL:KCW71116.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW71116.1};
RN   [1] {ECO:0000313|EMBL:KCW71116.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW71116.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC         beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19929, Rhea:RHEA-
CC         COMP:10033, Rhea:RHEA-COMP:10034, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18246, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00000122,
CC         ECO:0000256|RuleBase:RU361116};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361116};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|RuleBase:RU361116};
CC   -!- PATHWAY: Glycan metabolism; plant cellulose biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004768, ECO:0000256|RuleBase:RU361116}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC       ECO:0000256|RuleBase:RU361116}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361116}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC       cellulose synthase subfamily. {ECO:0000256|ARBA:ARBA00007548,
CC       ECO:0000256|RuleBase:RU361116}.
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DR   EMBL; KK198758; KCW71116.1; -; Genomic_DNA.
DR   RefSeq; XP_010063847.1; XM_010065545.2.
DR   AlphaFoldDB; A0A059BYT9; -.
DR   STRING; 71139.A0A059BYT9; -.
DR   EnsemblPlants; KCW71116; KCW71116; EUGRSUZ_F04216.
DR   GeneID; 104450842; -.
DR   Gramene; KCW71116; KCW71116; EUGRSUZ_F04216.
DR   KEGG; egr:104450842; -.
DR   eggNOG; ENOG502QQGG; Eukaryota.
DR   InParanoid; A0A059BYT9; -.
DR   OMA; DMWRNEQ; -.
DR   OrthoDB; 1210919at2759; -.
DR   UniPathway; UPA00695; -.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0016759; F:cellulose synthase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009833; P:plant-type primary cell wall biogenesis; IBA:GO_Central.
DR   CDD; cd16617; mRING-HC-C4C4_CesA; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR005150; Cellulose_synth.
DR   InterPro; IPR027934; CES_Znf_RING.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13301:SF27; CELLULOSE SYNTHASE; 1.
DR   PANTHER; PTHR13301; X-BOX TRANSCRIPTION FACTOR-RELATED; 1.
DR   Pfam; PF03552; Cellulose_synt; 1.
DR   Pfam; PF14569; zf-UDP; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU361116};
KW   Cell wall biogenesis/degradation {ECO:0000256|RuleBase:RU361116};
KW   Cellulose biosynthesis {ECO:0000256|ARBA:ARBA00022916,
KW   ECO:0000256|RuleBase:RU361116};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU361116}; Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361116};
KW   Metal-binding {ECO:0000256|RuleBase:RU361116};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361116};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361116};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361116};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361116};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361116"
FT   TRANSMEM        311..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361116"
FT   TRANSMEM        870..891
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361116"
FT   TRANSMEM        903..921
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361116"
FT   TRANSMEM        941..963
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361116"
FT   TRANSMEM        984..1008
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361116"
FT   TRANSMEM        1020..1041
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361116"
FT   TRANSMEM        1053..1073
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361116"
FT   DOMAIN          38..84
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          243..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..263
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1092 AA;  123633 MW;  92406EBCC02FFD0A CRC64;
     MDTGRLVTGS HNRNEIILIN ADEVGRVTCV KHLSGKICQI CADEIEITGD GEPFVACNEC
     AFPVCRHCYE YERSEGTQAC PHCKTRYKRI KGSPRVEGDE EEENTDDLER EFDIGESGRG
     NLHCMAEGMP STHLNFGPNL QTHASGFTTP SELDASSVVP EIPLLTYGQE NVGISFNKHA
     LIIPPLMGQG RRIHPMPNSD SSVPLPPRTL DPNKDSAVYG YGTVAWKERM EEWKKKQNER
     IQVVKHDRGS DGQEPDDADL PTMDEGRQPL SRKLPIPSSK ISPYRLIIIL RLVILGLFFH
     YRILHPVNDA YGLWLTSVIC EIWFAMSWIL DQFPKWYPIK RETYLDRLSL RYEKEERPSK
     LADIDIFVST VDPMKEPPLI TANTVLSILA VDYPVDKVAC YVSDDGAAML TFEALSETSE
     FAMKWVPFCK RFNIEPRAPE WYFSQKVDYL KDKVNPEFVR ERRDMKREYE EFKVRINGLV
     AMAQKVPEEG WTMQDGTPWP GNNVRDHPGM IQVFLGQNGD RDVEGNELPR LVYVSREKRP
     GFDHHKKAGA MNALVRVSAV ITNAPYLLNV DCDHYINNSK ALREAMCFMM DPISGKKICY
     VQFPQRFDGI DRHDRYSNRN VVFFDINMKG LDGIQGPIYV GTGCVFRRQA LYGYDAPIKK
     KPPGKTCNCW PKWCCLCCGS RKRGRKMKSN EQKKTLRNRE ASKQIHALEN IEEGIEGIDN
     EKSSLMSRVK FEKKFGQSPV FIATTLMEEG GVPKGATTAS LLKEAIHVIS CGYEDKTEWG
     KEVGWIYGSV TEDILTGFKM HCHGWRSVYC IPKRPAFKGS APINLSDRLH QVLRWALGSV
     EILLSRHCPI WYGYGCGLKW LERFSYINSV VYPLTSIPLI AYCTLPAVCL LTGKFIVPEI
     SNYASLIFMA LFISIAATGI LEMQWGGVGI HDWWRNEQFW VIGGVSCHLF ALFQGLLKVL
     AGVNTNFTVT SKAGDDGEFS ELYLFKWTSL LIPPLTLLIL NIIGVIVGVS DAINNGYETW
     GPLFGKLLFA LWVIVHLYPF LKGFMGKQDR LPTIIIVWAI LLASILTLLW VRINPFISKD
     GIVLEVCGLD CN
//

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