ID R7SS04_DICSQ Unreviewed; 1139 AA.
AC R7SS04;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 22-FEB-2023, entry version 47.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=DICSQDRAFT_111238 {ECO:0000313|EMBL:EJF57737.1};
OS Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Dichomitus.
OX NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF57737.1, ECO:0000313|Proteomes:UP000053319};
RN [1] {ECO:0000313|EMBL:EJF57737.1, ECO:0000313|Proteomes:UP000053319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF57737.1,
RC ECO:0000313|Proteomes:UP000053319};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; JH719445; EJF57737.1; -; Genomic_DNA.
DR RefSeq; XP_007369488.1; XM_007369426.1.
DR AlphaFoldDB; R7SS04; -.
DR GeneID; 18833966; -.
DR KEGG; dsq:DICSQDRAFT_111238; -.
DR HOGENOM; CLU_002572_0_0_1; -.
DR OMA; KYLVNCM; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000053319; 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:SF26; CHITIN SYNTHASE 7; 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:UP000053319};
KW Transferase {ECO:0000313|EMBL:EJF57737.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 824..844
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 851..871
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 877..903
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 125097 MW; 172D14EDC7D2A904 CRC64;
MSAQFRPKFD PSDVPIPTSR TLQPSATTVR RAKTLTRPER TVAPVPLINA QVAHSAAGPR
AAASDDGPPL DAWRIFSRVV SFWAPDFLLE SLGGLRDKQK RQAWREKIAL CFIIIILCGG
VGFVTVGFQK VLCPDTTQFV SRFAPKGSVG GVLGVQGWQM NITKFPTAQG VNFTDLLKSP
GQDITTLFQR NASQYPACSG LSFRAAAEAP CPQADKCPIG QLDTTSLEKD GFINTTLVVG
YDWDQVAALQ NYLVIDGAVL NMNSYMALHP TPIPSDNVDA AIRTVLQNMP GGSGRDATRL
FYYRSELRQA VPCLVQRYYA GNIDKITPGC VVSQLVLYAG LIVVLSLVMV RFAMACVFNW
FMSSRLAGPP DNLTLNRSAI SPAVMPEGAN VSIDNLNGTA PWAGPGGTKR LMKPNSKTVR
SMVSSSSTLV NNRDSGAAAP VMSLAQIGAE LFAVCLVTCY SEGEDSLRTT LDSISTTSYA
DQRKLLFVVA DGMITGAGEK RSTPDICVSL LEADPRFGNP VPMSYAAVGS GAKSENRAMV
YAGHYTVAGR RTPTVVVVKC GTEQEAATDK KPGNRGKRDS QLILMNFFSR VTYNDRMSPL
DFDLFRKIHV LMGVTPDFFE VCLMVDADTK VYPDSLKYLV NCMHHDQMIM GVCGETRIAN
KRQSWVTAIQ VFEYFISHHN AKAFESVFGG VSCLPGCFSM FRLKARKATG DDWVPLIIKP
EIVKEYSQSV VTTLHEKNLL LLGEDRFLTT ILLRTFPNRK MMFLPQAKCR TVVPDTFSVL
LSQRRRWINS TIHNLMELVL VRNLCGTFCF SMQFVVFMDL LGTVVLPIAI SLTYMLIVGM
ILAPPHNFEE AIPLVLLIAV LGLPAILILI TTRKVVYIFW MLIYLAALPV WNFVLPVYAF
WHFDDFSWGE TRKVEGERKG EAHGEGAGVI GAASVPMRRW EDWERSRLRK IRREERRRRE
FERQHGAYIG SNGELVARSE VYSQYDGSDT VSVASSDDDH WGAQIGGYNE NSVQYPPPPV
TLMPQALASA ETIAGSDLEA MLEVGFDERS SGRARGHETR FQLSDRGNGY TPLSRATSPG
VQTAQAAPLL QPISPTTPGD SIGTGSSADW QAHGKESSGG RSGKQDYGPL GPLDPRSKF
//