ID A0A094AJS2_9PEZI Unreviewed; 1212 AA.
AC A0A094AJS2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, 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=V493_05885 {ECO:0000313|EMBL:KFY23395.1};
OS Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY23395.1, ECO:0000313|Proteomes:UP000029327};
RN [1] {ECO:0000313|EMBL:KFY23395.1, ECO:0000313|Proteomes:UP000029327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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}.
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:KFY23395.1}.
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DR EMBL; JPJV01002260; KFY23395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094AJS2; -.
DR STRING; 1420906.A0A094AJS2; -.
DR HOGENOM; CLU_002572_1_0_1; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000029327; 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:UP000029327};
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 240..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 497..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1066..1084
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1091..1111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1117..1140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1212 AA; 135747 MW; 125FD9998493B045 CRC64;
MSLPQRPGRS DLPPQERRSS YRTSTSRSQP SHDAEEEYAG QNAQSPTSRR TRQHRVESTA
SPANTRPPHN PNPANPAAHD FQRKRSLVRP ERNRIDRDHP NYYYRQHAAN MTVLPSTTGN
DPILEDRGDV NGGRVEPDQR SSRDGPYGSP SPLESQGTIQ GSETGGFEKD PKSSKLTRTT
NKSRKQTREE RRRQRDADVI KPPSLWNVYC SIITFWCPDF ILRCFGKPAK EQQRAWREKM
GLISIILMVM AFVGFITFGF TATVCGNPPT RLRVNEVDKG FMIFHGKAYN LLESHHTAAT
GISENGNVLY EPEDSGGRDG SFLFQNVNGK CKGLISKSEG SDVPSDDKGN LGWYFPCNIV
NQDGSSDPKN KTFGAYLGHQ CHTTAKGRDL FYALQSSGDV YYTWDDIKNG TRNLAVYSGT
VLDLDLLKWF NGSQVTVPRV FVDLSNKATT LNQGVRGRDI THKFQASGDK GLAECLEQII
KVGSVDTDTI GCIASQVVLY VALAFIISIV GAKFVLALYF QWFLSRKYAA SKTSQSSDPK
KRNKHIEEWS NDIYRAPPRI AGDPGSTVAG SSDRNSRRAS SMFLPTTSRF TSPYTLNGEK
SGPRPAPTTM ASQNSTAQLF PPNPMYRGQN ESRMSFINST PDDRSIGGVM SDVSGDGPGP
AGFIHEAVVP QPPPEWQPFG YPLAHAICLV TTYSEGEQGI RTTLDSIATT DYPNSHKMIL
VICDGIIKGA GELQSTPDIV LGMMKDHSIL PEDVPAFSYV AVASGSKRHN MAKVYSGFYD
YSANSTVPLD RQQRVPMMCL VKCGTPDEAS KSKPGNRGKR DSQIILMSFL QKVMFDERMT
ELEFEMFNGL WKITGMSPDF FEVVLMVDAD TKVFPDSLTH MISAMVKDPE IMGLCGETKI
ANKRISWVTA IQVFEYFISH HLSKSFESVF GGVTCLPGCF SMYRIKAPKG GQNYWVPILA
NPDVVEHYSE NVVDTLHKKN LLLLGEDRYL STLMLRTFPK RKQVFVPQAV CKTTVPEEFL
VLLSQRRRWI NSTIHNLMEL VLVRDLCGTF CFSMQFVVFI DLIGTLVLPA AIAFTLYVVI
VSIVKKPVQV IPLVLLALIL GLPAVLIVLT AHRWSYVAWM LIYLISLPIW NFVLPVYAYW
KFDDFSWGDT RKTAGEKTKK AGIEYEGEFD SSKITMKRWA EFEKERRQRQ AGQWNAHSNT
SSYRDDYYDN NN
//
