ID A0A2T4AN30_TRIHA Unreviewed; 754 AA.
AC A0A2T4AN30;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539};
DE EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539};
GN ORFNames=M431DRAFT_362610 {ECO:0000313|EMBL:PTB58318.1};
OS Trichoderma harzianum CBS 226.95.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983964 {ECO:0000313|EMBL:PTB58318.1, ECO:0000313|Proteomes:UP000241690};
RN [1] {ECO:0000313|EMBL:PTB58318.1, ECO:0000313|Proteomes:UP000241690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB58318.1,
RC ECO:0000313|Proteomes:UP000241690};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) 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; KZ679677; PTB58318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4AN30; -.
DR STRING; 983964.A0A2T4AN30; -.
DR OrthoDB; 352133at2759; -.
DR Proteomes; UP000241690; 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:UP000241690};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PTB58318.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 149..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 494..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 623..651
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 663..687
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 737..753
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 331..520
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF13632"
FT REGION 20..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 85011 MW; 812A9F40239BBF74 CRC64;
MMRGHQEEYE EMVDIGNFRR HHQTGSDDSH PRLLSDNMRS NRSSAAHPDD FTAPQWPPSI
AGTGSSPSLT LRSGATTPYD QLSSTKHLIY ADSRSSTPMN PSHISLTTLL PQNGRSPSKE
VSSDNDDHNG VAILHDRDDS DIWKGWRRYL YTLTPFLTIL NTGVYLTYLG LRIACVILAQ
KASGTTFAAA WVFIAVELVV AVPSLMHNIW TMWSLKKRHR PKMRLTGNDV PTVDCFVTCC
GEDDELVMDT VRGACDQDYP IDRFRVIVLD DGKSAGLERS CAILSHTYPN LYYMARVKIP
GQPHHFKAGN LNYGLDQVHM LPGGASQYMA ALDADMIPER DWLRALLPHA VMDPKMALVC
PPQLFYNTPP SDPLAQSLDF FVHVIEPIKD AMGVAWCTGS GYVARREALE QIGNFPLGSL
AEDVATSTLM LGKGWKTAYV HEPLQFGTVP EDYGSHLKQR TRWAIGTVDT SFKLNFCLWG
EKVRQMTFAQ RFSGFLYASL SLYTILLSIS LFAIPIILIM GKPLVAYAND TQLRWLIRAC
FANTIVNRLC EFVLFIPAGY HTGQRGSRYQ LWMSPYIALC IIRAFALPKW LGGEAQAFKP
TGSLSSALNE RDPKLKKNMF RRLWTILINY MALFHLAFVY LTLVAVCLVS YRCFFQESNR
VRDILLCLVT HAFWPPLTFI FICSSLWTPV AYAIDPPQMP DREDLLVRDP ETKVAHPTTQ
SKKIAFGGQA AWFEFEYTFS TLYTCLIFVA SFLF
//
