ID   A0A1L0BWL6_9ASCO        Unreviewed;      1165 AA.
AC   A0A1L0BWL6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   22-FEB-2023, entry version 21.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   ORFNames=SAMEA4029010_CIC11G00000002195 {ECO:0000313|EMBL:SGZ55635.1};
OS   [Candida] intermedia.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ55635.1, ECO:0000313|Proteomes:UP000182334};
RN   [1] {ECO:0000313|EMBL:SGZ55635.1, ECO:0000313|Proteomes:UP000182334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ55635.1,
RC   ECO:0000313|Proteomes:UP000182334};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; LT635760; SGZ55635.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L0BWL6; -.
DR   STRING; 45354.A0A1L0BWL6; -.
DR   OrthoDB; 1331060at2759; -.
DR   Proteomes; UP000182334; Chromosome v.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182334};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        431..454
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1011..1029
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1036..1056
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1062..1085
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1165 AA;  130611 MW;  EAECE1D12791A90F CRC64;
     MSGFRNSGGS NKYQEFDPES GDLNRKRSLV RPERQRIDQS HPMYHYAQVV NQESDHLKVQ
     PSLTGLEPTN STSASRKSFQ LGVQNISEDD EEGIPLMNIE SPQKAGREVY GLNDEVHDVP
     TQNVTRNVHR KPVHAKPENN DNDIYFWKVY CYVITFWAPG PLLKLFGLKT KSRQFAWREK
     IGLITCILYI GAFVAYITFG FTKTVCDPGR IKMRTNTING GYLIINGRAY DLTSSQHPGA
     AGISPGTNIL YPPINAGGMD GSFLFQNVNG HCQDLIVPRE NCSIPTNGNE LAWYMPCRLF
     NQDGSSSVNK TSVYYDGWAC HTSSSARDAY YGLEVNGDVY FTWDDIKNSS RNLVVYSGVV
     LDLDLINWIL TDDVTYPQLF NDLRDDDTFK GHDISLILSN SEERRAAKCL TEIIKVGVVD
     SDSIGCIASK IVLVVSLVFI LSVVILKFLI ACYFRWYVSR KQGATEIDNK SMAAREREIE
     DWVETPAASG PISTVPVKAR ANYKTQKTNR QSVFFKSGNG LTLIPNSDLN NYYAGGNEKL
     SKAFKYTTMT TQAATLGKSK RNLRATNTRS MLFNQSRNLS VDLLSRPQSV FNPFDGSEEF
     NVNGLSPDLI HPDVVPQPPV EYQPFGYPLA HMITLVTCYS EDEEGLRLTL DSIATTDYPN
     SHKLVIIVCD GLIKGSGNDR TTPEIALDLM TDFCVPPEDV QAHSYVAVAQ GSKRHNMAKV
     YAGFYKYNDE TVPPEKQQRV PVLTVVKCGT PEEAGGAKPG NRGKRDSQII LMSFFQKVTF
     DERMTELEYA LLESIWRVTG LMSEFYEIIL MVDADTKVYP DCLTHMCAEM IKDPTIMGLC
     GETKITNKSQ SWVTAIQVFE YYISHHQAKA FESVFGSVTC LPGCFCMYRI KAPKGDNGYW
     VPILANPDIV ERYSDNVTNT LHKKNLLLLG EDRYLTALML RTFPKRKQIF VPKAACTTLV
     PDTFKVLLSQ RRRWINSTVH NLMELVLVRD LCGTFCFSMQ FVIFIELVGT VVLPAAITFT
     IYVVVYAIVS RPTPVMSLVL LGVIFGLPGL LIVITVSSLK YLIYFFIYIL ALPIWNFVLP
     CYAFWKFDDF SWGETRTVAG GDKGAHGDKE GIFDSSSIVM KRWREWERDR RAYVTGGLTV
     PGAAWDPASA EKDMGYSGGS LGSLP
//