ID A0A1Y2F1V9_9FUNG Unreviewed; 563 AA.
AC A0A1Y2F1V9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=LY90DRAFT_399348 {ECO:0000313|EMBL:ORY77872.1};
OS Neocallimastix californiae.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Neocallimastix.
OX NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY77872.1, ECO:0000313|Proteomes:UP000193920};
RN [1] {ECO:0000313|EMBL:ORY77872.1, ECO:0000313|Proteomes:UP000193920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:ORY77872.1,
RC ECO:0000313|Proteomes:UP000193920};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:ORY77872.1}.
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DR EMBL; MCOG01000018; ORY77872.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2F1V9; -.
DR STRING; 1754190.A0A1Y2F1V9; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000193920; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000193920};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 389..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 418..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 468..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 563 AA; 64399 MW; 5783C5D7C87653D0 CRC64;
MVRSTSWEDL ESPFTFGRDN DHDDTIINNQ SYASGLDAPS NIYLDEYGDI YTVLLVTCYS
ENESGIRTTL ESLSKTMYDN NYKLLFVVAD GLIKGEGNTK TTPEIIIDMI TLDKRYPPVP
IPQSYIAIAD GTKRHNKAQV YVGWFNRTPI VVVVKCGTES EQKAAKPGNR GKRDSQIIVM
NFFQKVLFND PMVPLEFDLF TKIHTLMGIT PDLFEIILMV DADTKVAPDS LARLVAAMVD
DPMIMGLCGE TRISNKSDSW VTKIQVFEYY ISHHMSKAFE SIFGGVTCLP GCFCMYRIKA
PLDDGYWQPI ISHPNIIQDY SQNVVETLHE KNLLFLGEDR FLTTLMLKTF PSRKLMFVPK
AYCKTMVPDT FPVLLSQRRR WINSTIHNLF ELVFVRQLCG IFCFSMQFVI ALELFGTLTL
PAAIIFTFIL IIVSFIGPVV PIVPLIMLAC ILGLPAVLVA ITSRRLVYIA WMLIYLCALP
IWNFVLPTYA YWHFDDFSWG ETRKVQGDDG AGHGPAEKEE TFDIKQVPLR KWADYEKDRR
RNLTEKWETN IKKWKGQLYP IQE
//