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Database: UniProt
Entry: H6U2P4_9STRA
LinkDB: H6U2P4_9STRA
Original site: H6U2P4_9STRA 
ID   H6U2P4_9STRA            Unreviewed;      1146 AA.
AC   H6U2P4;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Cellulose synthase 3 {ECO:0000313|EMBL:AFB20350.1};
GN   Name=CesA3 {ECO:0000313|EMBL:AFB20350.1};
OS   Aphanomyces euteiches.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=100861 {ECO:0000313|EMBL:AFB20350.1};
RN   [1] {ECO:0000313|EMBL:AFB20350.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 154.73 {ECO:0000313|EMBL:AFB20350.1};
RX   PubMed=22483051;
RA   Blum M., Gamper H.A., Waldner M., Sierotzki H., Gisi U.;
RT   "The cellulose synthase 3 (CesA3) gene of oomycetes: structure, phylogeny
RT   and influence on sensitivity to carboxylic acid amide (CAA) fungicides.";
RL   Fungal Biol. 116:529-542(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; JN561770; AFB20350.1; -; Genomic_DNA.
DR   AlphaFoldDB; H6U2P4; -.
DR   VEuPathDB; FungiDB:AeMF1_011370; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:InterPro.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IEA:InterPro.
DR   InterPro; IPR005150; Cellulose_synth.
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; PF03552; Cellulose_synt; 2.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        37..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        154..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        214..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        421..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        497..519
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        925..945
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        960..981
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        993..1012
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1032..1051
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1063..1080
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1100..1120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   1146 AA;  126806 MW;  9760851355997513 CRC64;
     MVVLGNLVSG IIGVVGGFSL SLAGWSPLSI GSRPLFMVTQ CLSSFAMLYT LVYVCFEYAS
     LSTGETTRLI IALCVGAAAA IVTAFLSSIG CMLLTICTGL IIAPWLLTLD TVAGKLFVGE
     SSFAKQEFVI GFGLLFTLLF LSSSKTGDLE CHRFKYILFS AVTGGFIFSD GLFRIALDPT
     PPPSEASFGI MGFKTATGDV LSNFSSGIAS SDQLTMVAIW AGVAVVGLLN QLSMRWGLIC
     YNKVGSHAGM GMTSMHEETL ELPSGAAASA PFMHERTRLV CENCFATVPA GTAFCTECGE
     AMPGDDHVPS VSVSQAQPPS IAMGADGKTP ANWQQIPNRA YLSTTSFVDP KKMTEHNAES
     RSIRFMDQGD KPYASSMGGG RNYYEPSFRS FAMSTYSIAN RAAEPVETPN IRKYKMSGGG
     FFHVIYFLSA ITGVLWLVFL ITFYPRETPC NEAQPLLPCS LIEESIKTAR KCYTSTNEMS
     KDTVTGNFYC IKPTPGGVWF CYAIFVGSEY LNFFLGLLFN FSMWRPIRRG ARYLNDFKPP
     LPKEQWPTVD VFLCHYSEPV ADTMATMKNI LAMQYPPELL HVWVCDDGYA SSSWDANNHF
     KVTVNTKNIN FCGDLRGDLA RMMHERVVGP VTDDASLKAW RRQHSSVREL RKDGSKGVQR
     RDCAVGSLSD DYDYRDRGLP RVTFVGRMKP ETHHAKAGNI NNILFNEGAD GKYILILDND
     MKPHPKFLLA VLPFFFSEGE AVDGGGRQYS DDISWNQVAY VQTPQYFEDT PQLTEMGDPC
     GHKNTIFFDA VQCGRDGFDS AAFAGTNAVF RRQAFDSIGG IQYGTQTEDA YTGNILHQAG
     WDSVYFRKDF EGEAKDRIRL CEGAIPETVA TSLGQKKRWA MGAVQILLMK GDSEVDPDWR
     PPRVPTPDPK PSLTFPRKMF FYDSVLYPFG SIPALCYVFI AIYYLCTGSA PIYTPGNRML
     WTFLPVMLAR WMLNLLANRT VDNNDVWRAQ QTWFSYSFIT ALAILEAIRW RLTGVISAWT
     NTGAGQKTSW TEIPNVMILF SLFVSQFVAL ARFFSYENAT SPWNYISAMF FGFWIMSNFY
     PMAKMSISEY AGWDHTKATF TANVFGSLLL VGIVVFVQVW QSTYVNNQYV AQGTIVGSTS
     GSGSGA
//
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