ID A0A0D2D9H7_9EURO Unreviewed; 706 AA.
AC A0A0D2D9H7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=Z517_12186 {ECO:0000313|EMBL:KIW74246.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW74246.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW74246.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW74246.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) 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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KN846977; KIW74246.1; -; Genomic_DNA.
DR RefSeq; XP_013278054.1; XM_013422600.1.
DR AlphaFoldDB; A0A0D2D9H7; -.
DR STRING; 1442368.A0A0D2D9H7; -.
DR GeneID; 25311676; -.
DR VEuPathDB; FungiDB:Z517_12186; -.
DR HOGENOM; CLU_012773_1_1_1; -.
DR OrthoDB; 2784803at2759; -.
DR Proteomes; UP000053029; 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:UP000053029};
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 26..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 504..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..706
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 706 AA; 80641 MW; 4F74C371DD923852 CRC64;
MIATLPLPQH LTQYFPTLMT SILQEFAFYS FAAMLVIPWL FCVYQLVVVP LGRQKRVKYT
LNEQTAPKVV VVMPVYKEPP DSLWTALNSV VSCDYPAACI HVFVSFDGDD IDELYLKTID
RLGVPVTLKD FPKSIDVAYN GARVTVSRFP HGGKRHCQKA TFLLIDKIYK RYLQEKDDLF
ILFIDSDCIL DPVCIQNFMY DMELRPGSKH NMLAMTGIIT SSTKKHSFIT LLQDMEYVHG
QLFERSVESG CGAVTCLPGA LTLLRFSAFR NMARFYFSDK AEECEDLFDY AKTHLGEDRW
LTHLFMLGAK QRYQIQLSTS AFCKTEAVQS FRSLLKQRRR WFLGFITNEV CMLTDGRLWR
KYPMLCFLRF ATVSIRTTAL LLLITIIAIS STSTRVDSLP WEFMCISCGL NWLLMFYFAI
RLHRWKAALY PMMFMLNPFL NWVYMVYGVF TAGQRTWGGP RADAGAADAK VTPQQAIEHA
IATGDDLNIV PETFKPAIEF RRRRTRPSAL QPSSSVEGRF FSAEQEPGPM PDHEMASPTP
SHVNFNTQQH RYEHESLDMS DSDSLSVHTP KWINSFSEDN EKRHRPSRAV DMESRPRSMV
ADTRRFLGEG HLATRNMAGA IPALQGSRDM FTCAEHGNSR QEAARNHESD NRSPLGRNSP
MMAASVEEDF SGLDGKEDME DIGKAKRQSL KRQRLRKRSP SPGRMV
//
