ID A0A194UQK2_9PEZI Unreviewed; 1217 AA.
AC A0A194UQK2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=VP1G_01319 {ECO:0000313|EMBL:KUI53923.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI53923.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) 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; KN714671; KUI53923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194UQK2; -.
DR STRING; 694573.A0A194UQK2; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000078576; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000078576};
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 237..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 497..524
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1059..1078
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1085..1102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1108..1126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..186
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1217 AA; 135781 MW; C1BC54CC35A9F393 CRC64;
MSLPERPGAR VSYEQRTAYR HSTRRHRPQD IEAGHGYGND DTLHSRGNSS HSFATTVPPS
SNATTDDVPL SPDLEGAAMT GEARLSRKRS LVRPERNRIG KDHPNYYYRK HAANMQTMPS
ATGNDPLYED LEGTTYITTS NREDANSDSI ASKDKRGGGG DGCEAHKARR SRRRANSRRH
SGKITKRKHK EVEQIRPPSL WDIYCAIITF WCPNFVLKCF GKRSKDEARA WREKMGLLSI
IAMIMAFVGF LTFGFTRAVC GAPAQRLQVN HVDSGYMIFH GQAFDLTTSH HPVAEGIPAE
SDGEGANVLY DLPEKEGGKD GSFLFQKVNG KCKGLITLAE GSDVPTNDDD DLAWYFPCNT
FAQDGSTKPN LTIPYYLGYA CHTSADARNA FYDLTPTADV FFSWDDVKNS SRNLVVYSGD
VLDLNLLNWF NTSQVSVPDR FTELADTSTA ANQAVRGRDV THSFMKSGDK VTAECLQQII
KVGSVDSDSV GCIASKIVLY LSLVLILSVV AARFLLAIMF QWFICRRYAA TKTSQSSDRR
KRNQQIEEWS EDIYRAPARL PGDVGSSVAG TSSDHTSKRA STFLPTTSRF SSVYGVDRNS
RRPNMPTTMA SQNSGAALLH PNTMYGQGNS SRNSFPVSDP YGAQPSPSDG PGPAGFIHEA
VVPQPPSDWM PFGYPLAHTI CLITAYSEGE EGIRTTLDSI AMTDYPNSHK CILVICDGII
KGKGEKMSTP DYCIGMMKDF TIHPDDVQPF SYVAVASGSK RHNMAKVYSG FYDYGTKSRI
PLEKQQRVPM ILVSKCGTPA EASKSKPGNR GKRDSQIIMM SFLQKVMFDE RMTELEYEMF
NGMWKVTGIS PDFYEIVLMV DADTKVFPDS LTHMVSAMVK DPEIMGLCGE TKIANKRDSW
VTAIQVFEYF ISHHQAKSFE SVFGGVTCLP GCFCMYRIKA PKGGANYWVP ILANPDVVEH
YSENVVDTLH KKNLLLLGED RYLTTLMLRT FPKRKQVFVP QAVCKTTVPD KFMVLLSQRR
RWINSTIHNL MELVLVRDLC GTFCFSMQFV VFIELMGTLV LPAAIAFTIY VVISSIIGPV
QVIPLVLLGL ILGLPGLLVV ITAHSWTYIV WMIIYLVSLP IWNFVLPSYS FWKFDDFSWG
DTRKTTGDTK KGGHGDAEGE FDSSKITMRR WAEFERERRG RSQYWGSKEN VAGNTHSGGW
AASPAYGYQH DEYFPET
//
