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Database: UniProt
Entry: X0CUV5_FUSOX
LinkDB: X0CUV5_FUSOX
Original site: X0CUV5_FUSOX 
ID   X0CUV5_FUSOX            Unreviewed;       811 AA.
AC   X0CUV5;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539};
DE            EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539};
GN   ORFNames=FOQG_02962 {ECO:0000313|EMBL:EXK97946.1};
OS   Fusarium oxysporum f. sp. raphani 54005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK97946.1, ECO:0000313|Proteomes:UP000030663};
RN   [1] {ECO:0000313|EMBL:EXK97946.1, ECO:0000313|Proteomes:UP000030663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54005 {ECO:0000313|EMBL:EXK97946.1,
RC   ECO:0000313|Proteomes:UP000030663};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW815.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; JH658364; EXK97946.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0CUV5; -.
DR   eggNOG; ENOG502QVIM; Eukaryota.
DR   HOGENOM; CLU_016061_0_1_1; -.
DR   Proteomes; UP000030663; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd06421; CESA_CelA_like; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43867; CELLULOSE SYNTHASE CATALYTIC SUBUNIT A [UDP-FORMING]; 1.
DR   PANTHER; PTHR43867:SF2; CELLULOSE SYNTHASE CATALYTIC SUBUNIT A [UDP-FORMING]; 1.
DR   Pfam; PF13632; Glyco_trans_2_3; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   4: Predicted;
KW   Cellulose biosynthesis {ECO:0000256|ARBA:ARBA00022916};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        214..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        249..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        552..578
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        629..649
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        681..709
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        729..751
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          390..578
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF13632"
FT   REGION          1..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   811 AA;  91693 MW;  5F96850242AF1D2B CRC64;
     MNGHHGYAEG EQEREYREMV EIDVQRQHQQ QHEQRQYQQQ EYFQQDLHSP YGPPEQQYTP
     YSPYHSSTEE FQGRSVTEQG RPARPSPAHF DDYSPAPEWP PHIANSPGQY FNDTPGGSRS
     ASPTLRSGRE TPARLHHHPG NSSVDWRPSS LMNQSHLSLA ALLPGGGSPQ SSSANTLYNK
     DYIVDSSTIQ HVHKRDDAEI WGGWKRWVFR LVPFLTFANT GLYMAYLALR IACVIWAQNA
     ADTTYAGAWI FIGVEIATAI PSLMHNTWTM WSMKKRNRPK LRLTGNDVPT VDAFITCCGE
     DDDLVMDTVR AACDLDYPRD RYRVILLDDG KSSGLEEACA KLSMTYQNLY YMARVKIPGQ
     PHHFKAGNLN YGLDEVHKLP GGAGQFMAAL DADMIPERDW LRAILPHMLI DPKMALACPP
     QLFYNTPPSD PLAQSLDFFV HVIEPIKDAL GVAWCTGSGY VARREALDEI GNFPLGSLAE
     DVATSTLMLG KGWKTAFIHE PLQFGTVPED YGGHLKQRTR WAIGTVDTSF KLNFCLWGDK
     VRQMTTAQRF SGFLYASLSM YTILLTISLF AIPIILIMQK PLVAYATDEQ LRWLIRACFA
     SVISNRLCEF ALFIPAGYHT GQRGSRYQLW MSPYIALCLI RSFILPTWLG GQTQAFKPTG
     SLGSALNERD AKLRKNMFRR LWGILINYMA LFHFAFVYLT LVAVVLTSFR SFVTTHTVRD
     TLTALLTHAF WPPLTFLFIC SSLWTPVSYA IDPPAMPDRE DLLNRDPKTQ VAHPTTQSKK
     IAFGGQAAWF ELEYTTTTIY TCLVFVCSFI F
//
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