ID A0A2C5YCN6_9HYPO Unreviewed; 1199 AA.
AC A0A2C5YCN6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=CDD81_3044 {ECO:0000313|EMBL:PHH67275.1};
OS Ophiocordyceps australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1399860 {ECO:0000313|EMBL:PHH67275.1, ECO:0000313|Proteomes:UP000226192};
RN [1] {ECO:0000313|EMBL:PHH67275.1, ECO:0000313|Proteomes:UP000226192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map64 {ECO:0000313|EMBL:PHH67275.1,
RC ECO:0000313|Proteomes:UP000226192};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHH67275.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NJET01000002; PHH67275.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5YCN6; -.
DR STRING; 1399860.A0A2C5YCN6; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000226192; 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 CDD; cd04190; Chitin_synth_C; 1.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF16; CHITIN SYNTHASE 3; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000226192};
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 248..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 511..538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1032..1050
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1057..1077
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1083..1106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..197
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1199 AA; 132623 MW; D640CC2AF6899D8D CRC64;
MSLPERPGGS PRVDGGTWYR QSPSGRTRPG DVEAAGYRGV CKAGRHGRGR SGSSFDESVS
NVNANTDKIP LSPTGAGGSG GDGGSEQAMW RKRSLVRPER KRIGKDHRHY HYHKHASKME
VLPSATGNEV AMEELDSSTE PWARTNESVS SWAGQGSRKG GQVSGEAEKA GAGQASRGKA
GKIGKASKRR GSRWQTGKKK KQGSEEQLGP PSFWNLYCAG VTFWCPDFVL GCFGKTTKAQ
RRAWREKMGL ISIILSIMAV VGFLTFGFTA TVCSAPPLRL QVNKVSEGFM IFHGVAYDLS
NSHHPPAEGI ALRQDGLGAN VLYDLGEKHG GQDGSFLFQN VNGRCKGLIE AAEGSDVPTN
DNGDLAWYFP CTTVKQDGST EPNLTVDYYL GYGCHTTDKS RRAFYVELDK AADVYFTWED
IGNTSRNLMV YSGSVVDLDV LRWFNESQVV VPQRFKELRE RGSAANRAVR GRDVTRMMQA
GPDKAYAQCL EDIAKVGSVD TETVGCMASK VVLYCALTLI LSVVLARFGL ALVFQWFISR
HYGAAKTSQS SDRRKRQRQI EAWSDDIYRA PLRLAGDVGS TVVGSERSRR TASFLPTTSR
FSAVYGAGGR RAPTTMASQR CMAPSSQGAP HQGVVPQPPS DWMPFGFPLA HTMCLVTAYS
EGLDGIRTTL DSIATTDYPN SHKAIVVICD GIIKGKGEAQ STPDVCLAML KDHAVPPELV
QPFSYVAVAS GAKRHNMAQV YCGFYDYGPA SHIPPDRQQR VPMMVIVKCG TPLEALEPKP
GNRGKRDSQI ILMSFLQKVM FDERMTELEY HMFNGLRAVT AISPDYYEIV LMVDADTKVF
PDSLTHMVSA MVKDPEIMGL CGETKIANKR DSWVTAIQVF EYFISHHLAK SFESIFGGVT
CLPGCFCMYR IKAPKGGHNY WVPILANPDI VEHYSENVVE TLHEKNLYLL GEDRFLTTLM
LRTFPKRKQV FVPQAVCKTT VPDKFMVLLS QRRRWINSTI HNLMELVLVR DLCGTFCFSM
QFVIFVELVG TLVLPAAIAF TFYVVITSIV HSPPQIIPLV LLALILGLPG VLIIVTAHSW
SYVVWMLIYL LSLPIWNFVL PTYAFWKFDD FSWGDTRKTA GDEATKGRVE HQGEFDSSKI
TMKRWAEFER DKRSRSSYWG SRENIVGGGG SSNPAATWAL PLGHDHLQSQ DYHHHLAEA
//