ID A0A084Q834_STAC4 Unreviewed; 794 AA.
AC A0A084Q834;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=cellulose synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012539};
DE EC=2.4.1.12 {ECO:0000256|ARBA:ARBA00012539};
GN ORFNames=S40285_09505 {ECO:0000313|EMBL:KFA60119.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA60119.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA60119.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA60119.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KL661913; KFA60119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084Q834; -.
DR STRING; 1283841.A0A084Q834; -.
DR HOGENOM; CLU_016061_0_1_1; -.
DR InParanoid; A0A084Q834; -.
DR OMA; RWLIRAC; -.
DR OrthoDB; 352133at2759; -.
DR Proteomes; UP000028524; 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:UP000028524};
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 191..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 535..561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 674..696
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 705..727
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 775..793
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 373..561
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF13632"
FT REGION 16..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 794 AA; 88980 MW; 2516E49F7E4B5E62 CRC64;
MKGRNEHVDE FEIDELHSRQ HTPGYGPPLH QQHQQHQQPP PGFNFGFVEH SNESHDVLPR
DITRPPRLAQ HSAGHHSPGL ASPMMHWDPS QQTLTNNPYD SRPSSPGASP WVESGRSTPV
GMSPSYSKPA WDSRPNSFLT QNTSGAASRT NLLARPPSPV LNSAPLKDGF AITSLHERDD
SDIWKGWRRN VFFLVPLMTF LQAGCYLLYL GYRIACVIFA QQAGNEVYIQ AWVFIGIEVV
VAIPPLLHNM WTMWAIKKRG RPKLRLIGEN VPTVDVFVTC CGEDVDVIMD TVRAACYLDY
PLDRFRVLLL DDGKDPELEE AMAKLSVLFP NVIYVARPKF PGVPHHFKAG NLNYGLDHVH
TLPGGAGQFM AALDADMIPE PTWLRAILPH MLRDQKVALA CPPQLFYNVP RGDPLSQSLD
FFVHVIEPIK DALGVAWCTG SGYVARRDAL DQIGNFPLGS LAEDVATSTH LLGCGWKTAY
IHEPLQFGTV PEDYGGHLKQ RTRWAIGTVD TSFKLKFCLW GDKVRQMTVA QRFSGFLYAS
LNLYTILLSV SLFAIPIILI MGRPLVAYAT YDQLRWLIRA CFATLVSNRL CEFVLSMPAG
YHTGRRGARY EMWMSPYIAL CVVRSFILPK WLGGQSQAFK PTGSLGSALN ERDAKSRKGL
FRRLSAILFG YMGWYHLTFV YVTLVGVVLT SFRCIVLQTS LQDQLFALVT HAFWPPLTFV
FICSSLWTPI AYAIDPPTVP EREALLDRDP KTGVAHPTPK SKKIAFSGDD AYYEVEYTLT
TAFTCLVFVA SFIF
//
