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Database: UniProt
Entry: Q6GVM1_9VIRI
LinkDB: Q6GVM1_9VIRI
Original site: Q6GVM1_9VIRI 
ID   Q6GVM1_9VIRI            Unreviewed;      1072 AA.
AC   Q6GVM1;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Cellulose synthase {ECO:0000256|RuleBase:RU361116};
DE            EC=2.4.1.12 {ECO:0000256|RuleBase:RU361116};
GN   Name=CesA2 {ECO:0000313|EMBL:AAT48369.1};
OS   Mesotaenium caldariorum.
OC   Eukaryota; Viridiplantae; Streptophyta; Zygnemophyceae; Zygnematophycidae;
OC   Zygnematales; Mesotaeniaceae; Mesotaenium.
OX   NCBI_TaxID=31321 {ECO:0000313|EMBL:AAT48369.1};
RN   [1] {ECO:0000313|EMBL:AAT48369.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UTEX 41 {ECO:0000313|EMBL:AAT48369.1};
RA   Roberts A.W., Roberts E.M.;
RT   "Cellulose synthase (CesA) genes in algae and seedless plants.";
RL   Submitted (MAY-2004) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU361116}.
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DR   EMBL; AY633542; AAT48369.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6GVM1; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   UniPathway; UPA00695; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:UniProtKB-EC.
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; IEA:UniProtKB-KW.
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:SF261; CELLULOSE SYNTHASE FAMILY PROTEIN; 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        849..870
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361116"
FT   TRANSMEM        882..900
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361116"
FT   TRANSMEM        920..942
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361116"
FT   TRANSMEM        963..990
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361116"
FT   TRANSMEM        1002..1021
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361116"
FT   TRANSMEM        1033..1051
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361116"
FT   DOMAIN          37..84
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   1072 AA;  119888 MW;  8E804CD76E80CDD9 CRC64;
     MESTTGLVAG SHNRKELVVI SVDEEREPLP SHAAGICQIC SDDVGPSHES SQLFIACIEC
     GYPVCRSCYE YERKEGSRAC PRCKTVYMRH KGSPRVDTDP EEEEIDDIDN ELRDIVQQPQ
     SDNNWNSKTL GFDAESVNSS LMKRHLYLNS GYGHAYFGSP NHSDAVSDLG SNTIQPSVPA
     SETGKKSFSS SIDGSECRML DSYKDNGYGN VAWKVKCDRD GEANAVSVNM GGMEAMQLRG
     GGHDYFPEEL PSPLDDARQP LSRKVHFAMG LIQPYRLLIV LRLLVLAFFL RYRFLNPADS
     RPLWLASVVC EVWFAVSWIL DQFPKWNPIN RETNLGRLQL RYGEALDAVD LFVSTVDPGK
     EPPLTTANTL LSILAMDYPV EKLNCYLSDD GASKLTFDAV NETSEFAKKW VPFCKKFAVE
     PRAPEAYFAQ KTDFLKGQVQ SSFVNERRNM KKEYEEFKVR INHLVSDFQN VPEDGWTMAD
     GSYWPGNNAR DHPGMIQVFL GPSGGKDVEG NALPRLVYVS REKRPGFNHH KKAGAMNALI
     RVSALLTNAP HILNLDCDHY VNASSALRHA MCFLMEPSTG QKTAFVQFPQ RFDGVDRSDR
     YANHNTVFFD INLRGLDGIQ GPVYVGTGCC FRRHALYGFS PLKDKKIGGR QPWFGELSRT
     NSSLKQKVSP STSPLFTMDA GDVEMNENES LLNLKRFERR FGGSPTLVLS TFQEDSSSPA
     PYSSSSSSWD ASCLPEAIQV ISCGYETDTE WGTEIGWIYG SVTEDILTGF KMHCRGWRSV
     YCHLALPHRP AFKGRAPINL SDRLEQILRW ALGSVEILFS RYSPLWYGWM GGNGGGLKLL
     QRMAYVNTVV YPFTAFPLIV YCTLPALCLL SDQFIIPSIS TVSAIWFVLL FISIFASAFL
     EMRWSGVSME EWWRNEQFWV IGGVSAHLYA VFQGLLKVVV GIDTNFTVTA KTADEEEEFE
     ELYLFKWTTL LIPPTTLIAL NAIGIAAGIA NAINNGYAEW SALIGKVFFA FWVLVHLYPF
     LKGMMGKNTR MPTLVIVWSV LLASILSLIW VKTSPFGLTT TGPSAEDCGV RC
//
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