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Database: UniProt
Entry: A0A2C5YCN6_9HYPO
LinkDB: A0A2C5YCN6_9HYPO
Original site: A0A2C5YCN6_9HYPO 
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}.
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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
//
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