ID A7E700_SCLS1 Unreviewed; 479 AA.
AC A7E700;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Chitin synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SS1G_01076 {ECO:0000313|EMBL:EDN91672.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN91672.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and
CC septum, by transferring the sugar moiety of UDP-GlcNAc to the non-
CC reducing end of the growing chitin polymer.
CC {ECO:0000256|ARBA:ARBA00024009}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CH476621; EDN91672.1; -; Genomic_DNA.
DR RefSeq; XP_001598986.1; XM_001598936.1.
DR AlphaFoldDB; A7E700; -.
DR STRING; 665079.A7E700; -.
DR EnsemblFungi; EDN91672; EDN91672; SS1G_01076.
DR GeneID; 5494803; -.
DR KEGG; ssl:SS1G_01076; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_570065_0_0_1; -.
DR InParanoid; A7E700; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004100; F:chitin synthase activity; IEA:InterPro.
DR InterPro; IPR004835; Chitin_synth.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF45; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 239..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 38..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 53500 MW; 52C8493D139FDB06 CRC64;
MNIQPLAIGN DPIMEDIKAD AANTETLGLR SSVEAELDIT SPVRRPTRGH GAGPEDLTSN
EKAGFASKSR RGKKLQRERV QKMFKKEKAR QEALDTYFPC HAFNQDGSSS PNETIGAYFG
YACYLQVEAR SSFYGLRSAG DVYFTWDDIK NSSRNLMVYS SNVLDLDLLN WFNTIQVSVS
SRFTTLADRT TTANAAVCGR DVTHAFQSSD DKKIAQCFEQ IIKVGSVDTK SVGCIASKVV
LYVSLAFILA IVFVKFILAL IFQWFIASKY AASKTSQSSD PKKRQQQIEE WSDGIYRAPP
RMAEWEPYGF PLAHAILLVT AYSKGELGIR TTLDSIATTD YPNSHKTILV ICDGIIKGEG
EPRTTPDVVL GIMKDFVTSV EEVPAFSYVA VEKGSKRYNI AKVYAGFYNY NADSTINTNK
QLRVPMVCIV KCSTPEESTH RKPGNRGKRD SQIILMSFLQ KVMFDERITE LKFEIFNGF
//
