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
//