ID A0A0D1XRU3_EXOME Unreviewed; 783 AA.
AC A0A0D1XRU3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539};
DE EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539};
GN ORFNames=PV10_05444 {ECO:0000313|EMBL:KIV90836.1};
OS Exophiala mesophila (Black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV90836.1, ECO:0000313|Proteomes:UP000054302};
RN [1] {ECO:0000313|EMBL:KIV90836.1, ECO:0000313|Proteomes:UP000054302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV90836.1,
RC ECO:0000313|Proteomes:UP000054302};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala mesophila CBS40295.";
RL Submitted (JAN-2015) 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; KN847523; KIV90836.1; -; Genomic_DNA.
DR RefSeq; XP_016222410.1; XM_016370117.1.
DR AlphaFoldDB; A0A0D1XRU3; -.
DR STRING; 212818.A0A0D1XRU3; -.
DR GeneID; 27323289; -.
DR VEuPathDB; FungiDB:PV10_05444; -.
DR HOGENOM; CLU_016061_0_1_1; -.
DR OMA; RWLIRAC; -.
DR OrthoDB; 352133at2759; -.
DR Proteomes; UP000054302; 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:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0043934; P:sporulation; IEA:UniProt.
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:UP000054302};
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 179..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 525..550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 653..681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 693..719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 764..782
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 362..547
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF13632"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 88572 MW; 7914FB20F79271A1 CRC64;
MPLRKNDRRS SPHEEPMTEI RMSAASTTTS LNNTPRDSEF QVSNTPHPVY GYYSEQIPLQ
PPSSFRRPAP YDNHNRTLSD LITAESLSSS PIDGANGSPI PPFAPRANSS YSEPGTRNSS
PYPSPYPAST PFRSQETLRP LVPDASATYL HRDWVKEGSI AQLHHRDDKE LLAGKRRKLY
TWFAPTLGLA TLALYWLYFG LRIKFVVAAQ QSFGSPFPLA WIFIAVEISV AIPIFLQTFW
SLFILKKRNR PKLRLMGNNV PTVDVLITCC GEDFDVIMDT VRAACDLDYP QDRYRVLLLD
DGKSDALKNA VEEMRETFPN LYYKRRPKFP GVPHHFKAGN LNYGLDEVHT LPGGAGEFMA
ALDADMIPEQ HWLRAILPHL LVDPKMALAC PPQLFYNVPR DDPLCQSLDF FVSVSETVKD
ALGVAWCTGS GYAIRRSALD EIGLFPKGSL AEDVATSTLL LGKGWKTAYV HEKLQFGTVP
EDYGSHLKQR TRWAIGTVDT AFKLRFCLWG DAVKRMKFAA RVSSFLYAFL SLFNIFLTLS
IFALPIVLIS GKPLVAYATE NQLRWLIRAC FATVFCNRLC EFVLYIPSGY ATGQRGSRSQ
LWMSPYIALT LIRSFVLPTW LGGQAQAFKP TGSLKSALNE RFPKQRAPMY RRIWTICVNY
LAGFHVAYVY WVLVAVCLSS YRCFVTKYTT RDILICLVTH AFWPPLPWVI VCSSFWIPFT
YAVDPPSMPD REELLTRDPK TGVAHPTKEA KKIGLGKQSW LFEFEYSFTT IFTATVFVAT
FFF
//
