ID A0A2L2SQ11_9HYPO Unreviewed; 847 AA.
AC A0A2L2SQ11;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539};
DE EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539};
OS Fusarium venenatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI40044.1, ECO:0000313|Proteomes:UP000245910};
RN [1] {ECO:0000313|Proteomes:UP000245910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3/5 {ECO:0000313|Proteomes:UP000245910};
RA King R.;
RL Submitted (OCT-2014) 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; LN649232; CEI40044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L2SQ11; -.
DR STRING; 56646.A0A2L2SQ11; -.
DR OrthoDB; 352133at2759; -.
DR Proteomes; UP000245910; Chromosome iiii.
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:UP000245910};
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 247..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 588..614
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 717..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 765..787
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 426..614
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF13632"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 847 AA; 95745 MW; 647BD0979CCC7988 CRC64;
MNGNGNRDYG DEHDREYREM VEIDVQRQHQ QQHEQRQQLQ HDQQQQEYFQ QDLRSPYGPP
EQLQHQPAYT PYSPYQSEFE DMQQGRSITE QGRPSRPSPA HLEDHSPAPE WPPHIASSPG
QYFHDTPGGS RSGTPSLLSG QETPARLHYH AGDSSVDWRP SSLMVPSPSV RTLVNKSSNV
TDQTFSRDKQ NQSHLSLAAL LPNGSPQNSS DNTLAKEYIV DSSAIQTVHK RDDVDIWKGW
KRWVFKLVPV LTFMNTGLYM AYLALRIACV IWAQNAAGQT YEGAWVFIAV EIAVAIPSLM
HNIWTMWSMK KRQRPKLRVT GNDVPTVDAF VTCCGEEDDL VMDTVRAACD LDYPRDRFRV
IILDDGKSAG LEDQCNKLAM TYPNLYYMAR PKIPGQPHHF KAGNLNYGLD AVHKLPGGAG
QFMAALDADM IPERDWLRAI IPHMLIDPKM ALACPPQLFY NTPPSDPLAQ SLDFFVHVIE
PIKDALGVAW CTGSGYVARR EALDQIGNFP LGSLAEDVAT STLMLGKGWR TAFIHEPLQF
GTVPEDYGGH LKQRTRWAIG TVDTSFKLNF CLWGDKVRQM TTAQRFSGFL YASLSLYTVL
LTISMFAIPI ILIMQKPLVA YATDEQLRWL IRACFASVIS NRLCEFALFI PAGYHTGQRG
SRYQLWMSPY IALCIIRSFV LPTWLGGQTQ AFKPTGSLGS ALNERDAKLR KNMFRRLWGI
LINYMAIFHL FFVYLTLVAV VLTSFRSFVT TDTVRDTLTA LLTHAFWPPL TFLFICSSLW
TPISYAIDPP AMPDREDLLN RDPKTQVAHP TPQSKKIAFG GQAAWFELEY TVTTAYTCLV
FVASFIF
//
