ID A0A066XBR0_COLSU Unreviewed; 1225 AA.
AC A0A066XBR0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=CSUB01_04569 {ECO:0000313|EMBL:KDN63460.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN63460.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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}.
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:KDN63460.1}.
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DR EMBL; JMSE01001224; KDN63460.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XBR0; -.
DR STRING; 1173701.A0A066XBR0; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_002572_1_0_1; -.
DR OMA; SLWNVYC; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000027238; 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:UP000027238};
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 207..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1069..1087
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1094..1114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1120..1143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..193
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1225 AA; 137531 MW; 8E8119BE860194DB CRC64;
MSLPERPGAS SPLENRKPYR NSPSRRNRPG DVDADGYYPV GGRPQHRRGQ SATSFPETIP
SPNINTENQP LSPTYDSPVA GPAAAADEPF QRKRSLVRPE RRRIDKDHPN YYYRQHAANM
NVLPSATGND PIVEDMEGTT DVSGRSQTND NYSDASPPRG SNSRENSREE KKIPTRTKTK
HVSRHKSGKL SKNGKRKQQV EQIRPPSFWN VYCAIITFWM PNFMLKCCGM ASKAQQRAWR
EKMGLISIIL LIMGFVGFIT FGFTQTVCGT PPLRLQVNDV SEGYMIFHGT AYDLSGSRHP
PADGVPMINR THGANVLYDL PEKNGGKDGS FLFQNVNGRC KNLITLAENS DVPTDSNGDL
AWYFPCTVFN QDGSSKPNLT IPYYLGWACH TTRKARDTFY LDLHGAADVY FTWNDIKNSS
RNLIVYSGTV LDLDLLNWFN TTQVKVPARF NELKDRNSAV NRAIRGRDVT RAFQGSSDKQ
IAECFEEIIK VGSVDTDTVG CIASQVVLYC SLVLILAVVL TRFFLAVFFQ WFISRTYGAS
KTSQTGDKRK RNRQIEDWSE DIYRAPPRLP GDIGSSVNGS SDRTSKRQSS FLPTTSRFST
VYGANAMPLV GGKRMPTTMA SSGAGSNMLH PSNMYRHGND SRSSFLRSDP YTSNVSPTEG
PGPAGFIHEA VVPQPPADWM PFGFPLAHTM CLVTAYSEGE LGIRTTLDSI AMTDYPNSHK
VVVIICDGII KGKGENMSTP DYCLAMMKDH TIPPEEVEPF SYVAVASGSK RHNMAKVYSG
FYDYGAKSAI PLEKQQRVPV LLVVKCGTPD EATKSKPGNR GKRDSQIILM SFLQKVMFDE
RMTELEYEMF NGLWKVTGIS PDFYEIVLMV DADTKVFPDS LTHMVSAMVK DPEIMGLCGE
TKIANKRDSW VTAIQVFEYF ISHHLAKSFE SVFGGVTCLP GCFCMYRIKA PKGAQDYWVP
ILANPDIVEH YSENVVDTLH KKNLLLLGED RYLTTLMLRT FPKRKQIFVP QAVCKTTVPD
TFAVLLSQRR RWINSTIHNL MELVLVRDLC GTFCFSMQFV VFVELMGTLV LPAAIAFTFY
VVIISIVHSP PQIIPLVLLG LILGLPAVLI VLTAHSWTYV LWMLIYLVSL PIWNFVLPTY
AFWKFDDFSW GDTRKTAGEK TKKAGLEYEG EFDSSKITMK RWAEFERERR TRTNYWGSKE
NIVGGGNTWS VPPSHQYNDE YFSDA
//
