ID A0A1J7IXA6_9PEZI Unreviewed; 843 AA.
AC A0A1J7IXA6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=CONLIGDRAFT_641883 {ECO:0000313|EMBL:OIW32134.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW32134.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW32134.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW32134.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
RL Submitted (OCT-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; KV875095; OIW32134.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7IXA6; -.
DR STRING; 1408157.A0A1J7IXA6; -.
DR InParanoid; A0A1J7IXA6; -.
DR OrthoDB; 2784803at2759; -.
DR Proteomes; UP000182658; 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 InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF41; CHITIN SYNTHASE; 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:UP000182658};
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 14..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 54..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 449..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 474..495
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 502..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 576..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 95079 MW; B8B4C1EEA2779621 CRC64;
MLGEVSPAWP VKDIVYTAIV GLVMLAAVLE WFLWIAAFMY CLVKVFQKAE HWTVRILSVV
VGGAFLLLRF IFLPIMIVTL PLPSQIVKVW PPEMVRFLQW FAFWSFAGLL TVPWLFCVYQ
IVTHQLGRTK RIKQILDEVS APKVVIVMPC YREEPEVLIT AINSVVDCDY PPSCIHVFLS
FDGDQEDELY LNTIENLGVP LTLETYPKSI DVAYRGARVT VSRFPHGGKR HCQKMTFKLI
DKVYQEYLRR NDNLFILFID SDCILDRVCL QNFVYDMELS PGNRRDMLAM TGVITSTTKK
HSLITLLQDM EYIHGQLFER TVESGCGAVT CLPGALTMLR FSAFRRMAKY YFADKAEQCE
DLFDFAKGHL GEDRWLTHLF MIGAKKRYQI QMCTSAFCKT EAVQTMASLI KQRRRWFLGF
ITNEVCMLTD WRLWKKYPIL ILVRFMQNTI RTTALLFFVM ILALLSTTKS INDLPVGFIA
ISLGLNWLMM IYFGAKLRRY KIWLYPLMFI LNPFFNWYYM VYGIFTAGQR TWGGPRADAA
AADSTTTAQQ AIEQAEKAGD DLNIVPESFI PAAEAQALGG GSGETKSRKS KRVSDGGGVA
RSRSILQPPD RIAGKFSAPE RTPSGWYQHP DDSMASVSIL AGGSSSAYYG RNKLLHRDSF
ESAETGGSYS VYMPRRVESI MGEEDRRKYE LAQASQVSTF MGNSRLYQGP PPGQVYEFSE
SELRRAGFAD ATADGVGSAR PSQHRRLASN DSVHSGVSAE QQQQQQHPQA STADANRAAR
QPLVPPPSVN SRTGRSPLGR ASWVRTSTMD EVEGQIEGSH DVEASEHGQR GWSRPDQRNG
GLS
//
