ID S3BPM5_OPHP1 Unreviewed; 824 AA.
AC S3BPM5;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=F503_06537 {ECO:0000313|EMBL:EPE02337.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE02337.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE02337.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE02337.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
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; KE148181; EPE02337.1; -; Genomic_DNA.
DR AlphaFoldDB; S3BPM5; -.
DR STRING; 1262450.S3BPM5; -.
DR VEuPathDB; FungiDB:F503_06537; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_012773_0_0_1; -.
DR OMA; NCIHVFL; -.
DR OrthoDB; 2784803at2759; -.
DR Proteomes; UP000016923; 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:UP000016923};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPE02337.1};
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 603..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 93071 MW; 17D34FEE0CDBD366 CRC64;
MAPDLESPWP VHDIVYTSIV GLLMIAACLE WFLWIAAFLY CLCKVFRKAE HWTVNVLAIL
VGVAFTLLRL IFLPIMIVTL PLPGAVVRMW PADMVAVLQW FAFWSFAGLL TVPWLFCVYQ
IVTHQLGRTK RIKQVLDEVS APKVVIVMPC YREEPAILIT AINSVVDCDY PPSCIHVFLS
FDGDQEDELY LNTIEKLGVP LTLESYPKSI DVTYRAARVT VSRFPHGGKR HCQKSTFQLI
DRVYQQYLRR NDNLFILFID SDCLLDRVCL QNFVYDMELS PGNRRDMLAM TGVITSTTKR
HSLITLLQDM EYVHGQLFER TVESGCGAVT CLPGALTMLR FSAFRRMAKY YFADKAEQCE
DLFDFAKCHL GEDRWLTHLF MIGAKKRYQI QMCTSAFCKT EAVQTVRSLI KQRRRWFLGF
LTNEVCMLTD WRLWKRYPIL ILVRFMQNTI RTTGLLFFIL VLALLTTSKR VSDLPVGFIA
VSLGLNWVMM IYFGFKLRRF KIMLYPLMFV LSPFFNWYYM VYGIFTAGQR TWGGPRADAA
AADGDKTTVQ DAIEQAEKTG DDLNIVPESF MPAAEVQRQK SGNAGHSVLP TAMALSLVEE
PTELAADNES PSRLSNPIPY TDNPAHERGC DSWQPGFSLG RSKSGRTMLQ PPDKIDGMFS
APQRTDAGWY HYPDDSMASL HLAGGPSQQH NARPKQQQQP HQSFAGRHPR HSSESSLSSR
TNAGGREGGP SNAGGHSSVY MPRRVESLMS DEDRRKYEMA QASQLSFNHG GVLSGLAGPS
RLSGPSVSPG RVYEYQSEAE MHQAGFFANE PSPNLPQSPK APEQ
//
