ID A0A0D1YR80_9EURO Unreviewed; 699 AA.
AC A0A0D1YR80;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=PV11_05884 {ECO:0000313|EMBL:KIV83899.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV83899.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV83899.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV83899.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN846952; KIV83899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1YR80; -.
DR STRING; 1016849.A0A0D1YR80; -.
DR HOGENOM; CLU_012773_1_1_1; -.
DR OrthoDB; 2784803at2759; -.
DR Proteomes; UP000053599; 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:UP000053599};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..699
FT /note="chitin synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002252122"
FT TRANSMEM 41..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 524..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 699 AA; 79654 MW; C14A32328EAB26F4 CRC64;
MTIAFFLLRG IFVPVMLATL PLPARVTQYF PGPFVNFLQQ FAFYSFAAML IVPWLFCVYR
LVVIPLGRQK LIKYPLNERT APKVVVVMPV YKEPPESLLK ALNSVVDCDY PAACIHVFMS
FDGDNIDELY LKTIDRLGIP VTLKEFPKSI DVAYNGARVT VSRFPHGGKR HCQKATFLLI
DKIYKRYLQH KDDLFILFID SDCILDSVCI QNFMYDMELR PGNKHNMLAM TGVITACTEK
NSFLTILQDM EYVHGQLFER SVESGCGAVT CLPGALTLLR FSAFRNMAKY YFSDRAEECE
DLFDYAKTHL GEDRWLTHLF MLGAKERYQI QLSTSAFCKT EAVQTLRSLL KQRRRWFLGF
ITNEVCMMTD ARLWRKYPLL CLLRFMTVTV RTTALLFLIT IVSVATTSSR VDRLPWEFMC
ISCGLNWLLM FYFAIKLHRW KALLYPLMFT INPFMNWIYM VYGIFTAGQR TWGGPRADAG
AADAKVTPQE AIEHAIATGD DLNIVPETFK PAMEVRRRRT RPSLLLPSPS IEGRFAPPEH
EWSPKDSISP SPSEDKFEKS FSTHPRRTKQ DSLDLSDSEG ISIHTPRRMT SLSGLNETTV
AAITQHLPIA LSCDHDAQSA TIMNANQHAN GSGPERRIHL YDRSPLGRIS PVIAMPVEED
VPSLYGGSME HSNDAQQVRN KVSEQKRLRK RSPSVANMV
//
