ID A0A1X7S9C7_ZYMTR Unreviewed; 673 AA.
AC A0A1X7S9C7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=ZT3D7_G11275 {ECO:0000313|EMBL:SMQ56120.1};
OS Zymoseptoria tritici ST99CH_3D7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ56120.1, ECO:0000313|Proteomes:UP000215127};
RN [1] {ECO:0000313|EMBL:SMQ56120.1, ECO:0000313|Proteomes:UP000215127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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}.
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DR EMBL; LT853704; SMQ56120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7S9C7; -.
DR STRING; 1276538.A0A1X7S9C7; -.
DR Proteomes; UP000215127; Chromosome 13.
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:SF45; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 2.
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:UP000215127};
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 112..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 517..544
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 550..568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 580..600
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 76796 MW; EC71ED70DA19A8AA CRC64;
MIPTRFDMRI TNPERKWQHP TPTPRPVIPD VDEITEVQES EQAQATPAQA LPSTQPATEM
INSHVLQQAS EIAQSPRFTF QTTQLPAKPR QVDVDGTLAK RGRRKIVLHK RIFQGTQLSL
NGFFIFFTWY FAQYWYVILP IISAAIALNV VMIISLICKR TWTAIRPEEK ITPETPESLV
YIVPCYNETK EELTRSLDSL IAQQKVDDHK QAIVIICDGK VRGPGMEKTT ADYLLDDILK
DRTLRKRIPG GYTAWDSRPM DVTVQSGRYK SLPYFCIVKE QNQGKRDGLI AVRSFLYNFN
RRQEKPATIM NQEYFDTMAS WMLQDASIEH VDDLIGMDAD TVFADECAYE LVQTSRFKGT
MGVAGYVAVD WKNKLWGFWR LYQNTEYTIT QCLRRLHQGR VTHKVSCLPG ACQLLKICEE
TCGDRVLVEL FGRCPDFKDG LLKHIQASAS EDRNHVCHML TARPESKTRQ ALRAKAYTDV
PVTWAVYLSQ RRRWSLGATG NDWLLCWAPG MQWFERILSI VSALTWFLTP FVFAAYGSFI
YAIVVHPSTT LLAITSIMLV PIVYYICIPA WHAQSWKEVF QFWTGLLIYI FFGPFCRMIV
LCYSVKNIDS FGWGKTRQVI AEDGEKSGKL APAGLPDQTK STESLPERSP SVGDDHLNET
ARDIGDEEKT VGT
//
