ID A0A139IHP6_9PEZI Unreviewed; 1053 AA.
AC A0A139IHP6;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=AC579_771 {ECO:0000313|EMBL:KXT14102.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT14102.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT14102.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT14102.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-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: 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:KXT14102.1}.
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DR EMBL; LFZO01000094; KXT14102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139IHP6; -.
DR STRING; 113226.A0A139IHP6; -.
DR Proteomes; UP000073492; 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:UP000073492};
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 892..920
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 940..962
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 974..996
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1002..1025
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1053 AA; 118977 MW; B575B088A5C4B8FD CRC64;
MDEELDAVAE DTTDTADRHS RDPSLNASRR WADFQEAAAA RNFSLPSGQQ PPRQEQVVPE
DNRRCRGEGH LLEPTNFSRR LGWSNDQAQV GRLDSQLRSF SRPFERSDDR ARNDAFGLSF
RSFSRPFERS DDGPKGDRRE ARPSSFSRPF QRTGEGAQDD RLNSGSRRFN GSVGQIDDGP
QDDRLSSRST SFSRPFDHRD VSTARRPSSD SEARNVTSRG PEEWSRHSIS FSHVSYAPLE
TPRTARTRPI SWYAPNFIPP TIFEHASQAS EIAPDDVASS RRTSMVLHPA NRTSSSTQNL
SVPVSPLQTN FSRPRQGSRR ERPISAPMGL DWQWTTKSET NAQGRKRWTW DPSTPSQARN
RDNSLRSEGI EQHDFAFDHD SEHRKSGADQ DLPRHDPRRM RGASIFEEHG PRRASTWTVR
PHRRQSLRTH SFDPGVRRRF SNAAEMVFGS ERRQSVVAKA VEDVIAPQTE GALRFYHTPS
VAAFDVDIEK GPDDPDEGPV NPARNLTKKE LLHQRLFFGS IVVSLNIACI VASGMGYSGT
WVLVIILFFK SKDFLSVWIQ IFCRIYYKLK PLFRRIQVEK KAAWILSLIP AYSESEEQIV
KTLFSLRDNG MGEHKQVMCV ILDGKPRPIK DHMTKVVASF SRQYVSLKWK VGTLQIDAGF
VDDIPTLCIE KTPNAGKKDS LILCHDLFNF PRSNMDQTIK DLREELWSTI IPELTKRPDL
SKFDLVFCTD ADSTIHHGAL AKLADACLAD PKAIAACGFV FVEYEPGLEW SVWNLYQQFQ
YSFGQIVRRG AEHYVGKVTC LPGCITMIVV RPEMAGAIEK YAKPVTTFPV LRHQVQYLGT
DRRLTYSMLS QGNYLHTLFV PEAGSETVAP QSLKHYLSQR RRWGSNAYFN NYFYFAGANM
ILITRIAALI EISRLTMVYY RVFNTGLFLY GVATHFDALS LLPLLIVSFT PSFWFAFAVA
FLNDHLRANW KKLLCGFCIN RCISPFMSIT VFSLVAKNLG SQVWGISGVT AGTNVTPAAA
VGVLAERRAS MTEQVEAAKA ESSDRTMEGI MEG
//