ID   CHSC_EMENI              Reviewed;         918 AA.
AC   P30583; C8V7X5; O94165; Q5B4G4;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 3.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=Chitin synthase C;
DE            EC=2.4.1.16;
DE   AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase C;
DE   AltName: Full=Class-I chitin synthase C;
GN   Name=chsC; Synonyms=chs1; ORFNames=AN4566;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FGSC 89;
RX   PubMed=7765719; DOI=10.1271/bbb.58.2254;
RA   Motoyama T., Kojima N., Horiuchi H., Ohta A., Takagi M.;
RT   "Isolation of a chitin synthase gene (chsC) of Aspergillus nidulans.";
RL   Biosci. Biotechnol. Biochem. 58:2254-2257(1994).
RN   [2]
RP   SEQUENCE REVISION.
RA   Horiuchi H.;
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 258-446.
RX   PubMed=1731323; DOI=10.1073/pnas.89.2.519;
RA   Bowen A.R., Chen-Wu J.L.-P., Momany M., Young R., Szaniszlo P.J.,
RA   Robbins P.W.;
RT   "Classification of fungal chitin synthases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:519-523(1992).
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. {ECO:0000305}.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the chitin synthase family. Class I subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA75501.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA60909.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB023911; BAA75501.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AACD01000078; EAA60909.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001303; CBF77244.1; -; Genomic_DNA.
DR   EMBL; M82938; AAA33302.1; -; Genomic_DNA.
DR   PIR; A59054; A59054.
DR   RefSeq; XP_662170.1; XM_657078.1.
DR   AlphaFoldDB; P30583; -.
DR   STRING; 162425.CADANIAP00005872; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblFungi; CBF77244; CBF77244; ANIA_04566.
DR   EnsemblFungi; EAA60909; EAA60909; AN4566.2.
DR   GeneID; 2872365; -.
DR   KEGG; ani:AN4566.2; -.
DR   VEuPathDB; FungiDB:AN4566; -.
DR   eggNOG; KOG2571; Eukaryota.
DR   HOGENOM; CLU_004760_3_1_1; -.
DR   InParanoid; P30583; -.
DR   OMA; AWILHYV; -.
DR   OrthoDB; 256142at2759; -.
DR   BRENDA; 2.4.1.16; 517.
DR   Proteomes; UP000000560; Chromosome III.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR   GO; GO:0030428; C:cell septum; IDA:AspGD.
DR   GO; GO:0001411; C:hyphal tip; IDA:AspGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004100; F:chitin synthase activity; ISS:AspGD.
DR   GO; GO:0090529; P:cell septum assembly; IGI:AspGD.
DR   GO; GO:0006038; P:cell wall chitin biosynthetic process; IBA:GO_Central.
DR   GO; GO:0048315; P:conidium formation; IGI:AspGD.
DR   GO; GO:0000918; P:division septum site selection; IGI:CACAO.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IGI:AspGD.
DR   GO; GO:0030448; P:hyphal growth; IGI:AspGD.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR004834; Chitin_synth_fun.
DR   InterPro; IPR013616; Chitin_synth_N.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22914; PTHR22914; 1.
DR   Pfam; PF01644; Chitin_synth_1; 1.
DR   Pfam; PF08407; Chitin_synth_1N; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..918
FT                   /note="Chitin synthase C"
FT                   /id="PRO_0000193690"
FT   TRANSMEM        605..625
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        637..657
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        672..692
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        715..735
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        745..765
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        845..865
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        890..910
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        281..282
FT                   /note="SK -> RS (in Ref. 1; BAA75501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        675
FT                   /note="L -> F (in Ref. 1; BAA75501)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   918 AA;  104831 MW;  CF13A026D13AEAC4 CRC64;
     MSYNRLGDPY GDDRDARSPI MNPSSLSNRS PSPGRPLDGY QLSDAPYGHH HHIEMPSSDR
     LAEQPTYSVE RIPQSYGHNE AYEAQHQHYP GYEYSVDPEA HHDAYYTQPY QPTVTPGHDD
     YDLGQYPGHQ HSYQDDEPIL QPEDPFQAQN PYSDDYQEDM TIAPTPSPAP LRRWKTVKEV
     QLFQGNLVLD CPIAPKLLNQ IPHAENGQRD EFTHMRYSAA TCDPKDFFEE RFTLRQKLFA
     KPRHTELFIV VTMYNEDDFL FARTMVGVFK NIEHMCSRTR SKTWGKDAWK KIVVCVISDG
     RAKINPRTRA VLAGLGCYQD GIAKQQVNGK DVTAHIYEYT TQVGMELKGN QVHLKPRSGV
     PVQMIFCLKE KNQKKINSHR WFFQAFGRVL DPNICVLLDA GTQPGKDSIY RLWKAFDVEP
     MCGGACGEIK VMLDHGKKLF NPLVAGQNFE YKLSNILDKP LESAFGFISV LPGAFSAYRY
     IALQNDKNGQ GPLERYFLGE KMHGANAGIF TANMYLAEDR ILCFEIVTKR NCRWLLQYVK
     SSTGETDVPD QMAEFILQRR RWLNGSFFAA VYAITHFYQL WRSDHSFIRK FMLLIETIYQ
     TINMLFAWFG IGNFFLVFHI LTTYLGDADL LGTAGKVLGV VFEWLYLATL VTCFVLSLGN
     RPGGSNKLYM TMVYLWVFIM IYLAFAAVFV TVRSIQEEVK DGSFTFSTLF TNSTFFSIIV
     SLGSTYVMWF IASIIFMDPW HMFTCFIQYI LLTPTYINVL NIYAFCNTHD ITWGTKGDDK
     AEKLPSANLK PGGKVDVNIP QDDGDLNAQY EAELMKFAQK PPKEIKTISE EERQADYYKG
     FRSSVVLVWV FCNFALGAVV LSSAGLDRFS DDAEAAETDR NNRAMIYMAV VLWSVAGLSI
     FKFLGAMWFL VVRMFRGV