ID M3B7B9_SPHMS Unreviewed; 974 AA.
AC M3B7B9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=SEPMUDRAFT_131377 {ECO:0000313|EMBL:EMF15757.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF15757.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF15757.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF15757.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-
CC D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) +
CC UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223; EC=2.4.1.16;
CC Evidence={ECO:0000256|ARBA:ARBA00000319};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KB456261; EMF15757.1; -; Genomic_DNA.
DR RefSeq; XP_016763878.1; XM_016902416.1.
DR AlphaFoldDB; M3B7B9; -.
DR STRING; 692275.M3B7B9; -.
DR GeneID; 27899553; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_012773_0_0_1; -.
DR OMA; SIVDCEY; -.
DR OrthoDB; 2784803at2759; -.
DR Proteomes; UP000016931; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF41; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMF15757.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 113..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 543..567
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 579..597
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 666..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..860
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..974
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 974 AA; 110189 MW; 6F62D9E4A9AFC645 CRC64;
MDLLVCGSGH HCIASNRKTH GKRAPATKIQ LTTQAISQRK ARVRTRRPAE VASRHSGAGL
GLRQVTQKLR QSSTRAARNA PSWIKDLNFS MDVALEANDA TFSSSKPWPV KDVVYVAIVG
GVFLAALVEW FLWLIAFLYC LVKVFVKADG KTKWSIRILS AVLMVFFTCM RLVFLPIMVV
TLPLPSQVVQ YFPREMVSIL QWFAFWSFAG LLTVPWLFCV YQLVTHNVGR ERRIKTVLDE
HSAPKVVIVM PCYAEKPEVL LRTVDSIVDC EYPPSCMHIF LSFDGDKENE LFLKTIDCLG
VPITLEHYPK SIDVKYRHCR ITVSRFPHGG KRSCQKRTYR LIDKVYENYL RRNDNLFMLF
IDSDCILDKY CVQNFMYEMN LKPGSKHNML AMTGVITSTT KRNSLITVLQ DMEYIHGQLF
ERSVESGCGA VTCLPGALTI LRFSAFRQMA KYYFAEKAEQ CDDMFDYGKM HLGEDRWLTH
LFMIGATERY QIQMNTSAFC KTEAVETYKS LLKQRRRWFL GFITNEACML TDLRLWKRYP
LLLLIRLAQN TIRTTALLFF IMVISIISTS QKISNLPVGF IAVSLGLNWV LMLYFGAKLG
RYKIMLYPLM FVVNPFFNWL YMVYGICTAY ERTWGGPRAD ALQADEQTTP SQAVANALAS
GDELNIKPET FRPKAESRPP LMPSESLDGR FAPAEQMPGG FYRQGNNHNA TALRSDMTPR
EQEAVSSSDR RRDQSQDSYS SEWSSRDSRY SVPMPRRVES IVGPEITAAY HARQATQRPA
GGAFFETGQF ETEAEVRREL EKPSSSMGEA RRTANRPHSV ESTRSDMSEH SVDMHFAPVQ
RRTPPPPVPS SAPNPPQPGV KAPTRAEEAS SRRSHSPVGL AVPASAHPSR TGRSGSVTRI
GKSPLTRKSY TRLATDDAGS TAGSATDVVV TVPTRSSFDE EWSRRGRRRR SSIGVDGRRR
LSKQPRESRS SSRA
//
