ID A0A0F4G704_9PEZI Unreviewed; 957 AA.
AC A0A0F4G704;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=TI39_contig4384g00003 {ECO:0000313|EMBL:KJX93148.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX93148.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX93148.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX93148.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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:KJX93148.1}.
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DR EMBL; LAFY01004343; KJX93148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4G704; -.
DR STRING; 1047168.A0A0F4G704; -.
DR OrthoDB; 2784803at2759; -.
DR Proteomes; UP000033647; 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:UP000033647};
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 23..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 461..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 486..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 514..537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 609..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 107300 MW; 1A8C6CFAB3653840 CRC64;
MLKPRDASNG VPPITDPWPV RDILYVAIVG GVMLAALLEW ILWLLAFIYC LVKVFQKADG
ESKWTIRILC VINMVFFVGM RLIFLPIMMV TLPLPSQVVQ YFPEEMVSVL QWFAFWSFAG
LLTIPWLFCI YQLVTHNVGR ERKIKTVLDE NSAPKVVIIM PCYNEEPEIL LRTVDSMVDC
DYPPSCLHIF LSFDGDKENE LYLNTLDKLG VPLTLESYPK SIDVTYRSCR VTVSRFPHGG
KRSCQKRTYK LIDKVYAEYL RRNDNLFLLF IDSDCILDKV CIQNFVYEME LKPGSKKNML
AMTGVITSTS VKNTLITILQ DMEYIHGQLF ERSVESGCGA VTCLPGALTI LRFSAFRKMA
KFYFADKAEQ CDDLFDYGKC HLGEDRWLTH LFMIGAQERY QIQMNTGAFC KTEAVQSFKS
LLKQRRRWFL GFITNEVCML TDPRLWTRYP LLLLIRLGQN TIRTTGLLFF IMVISILSTS
QKIANLPIGF IAVSLGLNWV LMLYFGYRLG RYKIMLYPLM FVVNPFFNWI YMVYGIFTAG
QRTWGGPRAD AGVVDEKMTA AEVVAHAEAT GNELNVVPET FTHRTAHTTA PLMPSSHLEG
RFAKPEHLPG GYYRHTNDSG ALHSDMTPRH PLDVESRLAG PARPSGTRES STDSFLSSTN
SIHTPRRVES IFAPDDALAY FARQADQAPS GGAYFESERR EAREVRKRRS VPTMRAPSQP
SQPRLRRRSI SVDSFDRRSM RSEDSVELHF AVPRGRRRTA VSPPPGISSS TTDPAPTAAA
VESTPSDPNG QAPVVRAASL PGATSRPQTT SPSVSRSPTR RTSPTTTTQY LPLLHPQRRH
RSESANQGRS PLARKSFERI ASPPKEVQSG TTASTSAPPR ASADAGPSSS SRTGIRISES
DSETLESQRR GRGRRGRFSH DGVFGRGRAG TSVGSDGRRR LSRQSGRREG SGGASGR
//
