ID A0A2B7Z3I0_9EURO Unreviewed; 844 AA.
AC A0A2B7Z3I0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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=GX50_06281 {ECO:0000313|EMBL:PGH30924.1};
OS Emmonsia crescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH30924.1, ECO:0000313|Proteomes:UP000226031};
RN [1] {ECO:0000313|EMBL:PGH30924.1, ECO:0000313|Proteomes:UP000226031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH30924.1,
RC ECO:0000313|Proteomes:UP000226031};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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}.
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:PGH30924.1}.
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DR EMBL; PDND01000149; PGH30924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7Z3I0; -.
DR STRING; 73230.A0A2B7Z3I0; -.
DR VEuPathDB; FungiDB:EMCG_08823; -.
DR OrthoDB; 2784803at2759; -.
DR Proteomes; UP000226031; 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:UP000226031};
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 20..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 455..474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 480..501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 508..531
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 675..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 94902 MW; 219D681F7206C2A6 CRC64;
MAAHGNGASD DIPPWAIKDI VYVSILGPVI IAAFLEWFLW LAAFLYCLGK VFVKADHWSI
KVLAVIMMVM FTAFRGTFLP VMMVTLPLPP NITRHFPIQV VSFLQWFAFW TFAVLLIIPW
LFCIYRLVTN SIGRTKRIKE VLDERTAPKT VIVMPVYKEA PHVLIKAVDS VVDCDYPPSC
IHVFLSYDGG QVDESYLTVA AHLGVPITLK SYPASIDVSY KGARITISRF KHGGKRHCQK
QTFKLIDKIY AKYLQRHDNL FVLFIDSDCI LDRVCLQNFM YDMELKPGSK RNMLAMTGVI
TSTTQKNTLI TLLQDMEYIH GQLFERSVES GCGSVTCLPG ALTILRFSAF RKMAKYYFAD
KAEQCEDLFD FGKCHLGEDR WLTHLFMIGA KERYQIQMCT SAFCKTEAVQ SFRSLLKQRR
RWFLGFITNE VCMLTDIRLW YRYPMLCLVR FMQNTIRTTA LLFFIMIISV MTTSNKVENL
PVGFIAVSLG LNYLLMLYFG AKLRRYKAWL YPLMFILNPF FNWLYMVYGI FTAGQRTWGG
PRADAAAADE NTTPEEAAVR AKATGDELNI KVDTFRAVAD GKSSVPIHPA EGVEGRFAAP
DLQPNGYYYT ENDNTSTMTF PDFLPRNPAV SPLPLHPRAS FDSDWTNTSN SMIQLPRTVE
SIMGDEDQRK VQLARQSRAC SSVGAEVGDF DDSRDSMWEA ESTSDSGRRS ISRGKSPARS
STRGERVSSS TAGAFAYDGT NNGGSGNLIP PDTGLFEPAR GRAGRSPLGR NSPVRAVEDD
GADISPSPSP SLSPEGAEGA EVETHQQDDN RDDAAEQAEH SGKKKKRRRQ SRLMKRSRDP
GDMV
//
