UniProt: A0A165DD77

Database: UniProt
Entry: A0A165DD77_9APHY

LinkDB:  A0A165DD77_9APHY 
Original site:  A0A165DD77_9APHY

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (3)   
   InterPro (2)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (8)   

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ID   A0A165DD77_9APHY        Unreviewed;      1119 AA.
AC   A0A165DD77;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-JUN-2023, entry version 20.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   ORFNames=LAESUDRAFT_703243 {ECO:0000313|EMBL:KZT04611.1};
OS   Laetiporus sulphureus 93-53.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Laetiporus.
OX   NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT04611.1, ECO:0000313|Proteomes:UP000076871};
RN   [1] {ECO:0000313|EMBL:KZT04611.1, ECO:0000313|Proteomes:UP000076871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-53 {ECO:0000313|EMBL:KZT04611.1,
RC   ECO:0000313|Proteomes:UP000076871};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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; KV427635; KZT04611.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165DD77; -.
DR   STRING; 1314785.A0A165DD77; -.
DR   InParanoid; A0A165DD77; -.
DR   OrthoDB; 1331060at2759; -.
DR   Proteomes; UP000076871; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW   Transferase {ECO:0000313|EMBL:KZT04611.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        332..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        801..820
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        832..851
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        858..882
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   COILED          925..952
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1119 AA;  123786 MW;  C6960DEE32EE1D53 CRC64;
     MATRVRLNDV DTRPLKTTTL TSATLRRAKT LTRPERSVAP VPLINPRSAH LPSGSRIEDE
     DEALDSWRIF SRLVTFWAPA ALLRSVGGLH DKHTIQAWRE KMALCFIILC LCGVIGFITV
     GFQKVLCPSS DQINSGRYVR IGSVADTLGV RGWMMNLTSL TPAVMFGVNF TELLKYPGQD
     ITTYFKRDAS DYPACVGIPF HAAADVVCTH NASCPLDALN TSMTFDSLGL VNTSYIVGYD
     WDDVAALDNY LVIDGAVLNM NAYIARHPDA LEDDAVDSAL RTVLYGPGNS GRDGTRLFSF
     RADIRSAIPC LMQRYYAGNI DKISPGCLLS NLVLYAGLVV ILGLVLIRFA MACVFSWFVS
     ERLCSPPDST DLNKSAISHA VMPDGANISI RNKNGTAPWA GRVGPKKLPK SGLTPRSLTS
     STSTLVNSTE GPVAPVMSLA EIGAELFAVC LVTCYSEGEE SLRTTLDAIS RTTYADSRKL
     LFIVADGMIT GAGEKRSTPD ICVGLLEPDL RFGNPTPMSY IAVGAGAKAE NRAFVYAGHY
     IVAGRRTPTV IVVKCGTEAE IATEKKPGNR GKRDSQLILM NFFSRVTYND RMTPLDFDLF
     RKIHILMGVT PDFFEVCLMV DADTKVYPDS LSYLVNCMHH DNMIMGVCGE TRIANKRQSW
     VTAIQVFEYF ISHHLAKAFE SVFGGARRAT GDDWVPLITK PEIVQQYSQS VVTTLHQKNL
     LLLGEDRFLT TILYRTFPNR KMIFLPQARC RTIVPDTFSV LLSQRRRWIN STIHNLMELV
     LVRNTCGTFC FSSQFAVFMD LLGTVVLPIA IVLTYILIIS MAMDPPRSFE EAIPLILLVA
     ILGLPGLLIM LTTRKMVYVF WMLIYLIALP IWNLILPVYA FWHFDDFSWG ETRKVEGEAK
     GRGHDGLNSS TAGMSVPLRR WEDWERSRLR KLRRAERRLR DLERLQGSYV NANGPFAMRT
     ELSSYYSSDS NSIASSDDDQ WGPQIGGYNE HSAAFPPPPV GLIQHTFSSA ESVAGADLKA
     MLDVGFDDRP SPPHSRVATQ IPKFQLSDVR APPHDPRGYT PLGSTSPGYL CYNHACPPIA
     PSTPPLVMGA TSRGDWRSRA TNMHAYGPLG PLDPSARRY
//

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