ID   CHS2_PARBR              Reviewed;        1043 AA.
AC   Q92444;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 2.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Chitin synthase 2;
DE            EC=2.4.1.16;
DE   AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 2;
DE   AltName: Full=Class-II chitin synthase 2;
GN   Name=CHS2;
OS   Paracoccidioides brasiliensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=121759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 32071 / IVIC Pb73 / C81;
RX   PubMed=9483806;
RX   DOI=10.1002/(sici)1097-0061(19980130)14:2<181::aid-yea202>3.0.co;2-d;
RA   Nino-Vega G.A., Buurman E.T., Gooday G.W., San-Blas G., Gow N.A.R.;
RT   "Molecular cloning and sequencing of a chitin synthase gene (CHS2) of
RT   Paracoccidioides brasiliensis.";
RL   Yeast 14:181-187(1998).
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. {ECO:0000305}.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the chitin synthase family. Class II subfamily.
CC       {ECO:0000305}.
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DR   EMBL; Y09231; CAA70433.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q92444; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   VEuPathDB; FungiDB:PABG_07704; -.
DR   VEuPathDB; FungiDB:PADG_08636; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006031; P:chitin biosynthetic process; IEA:InterPro.
DR   GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR004834; Chitin_synth_fun.
DR   InterPro; IPR013616; Chitin_synth_N.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22914; PTHR22914; 1.
DR   Pfam; PF01644; Chitin_synth_1; 1.
DR   Pfam; PF08407; Chitin_synth_1N; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW   Membrane; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1043
FT                   /note="Chitin synthase 2"
FT                   /id="PRO_0000193705"
FT   TRANSMEM        663..683
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        703..723
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        738..758
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        780..800
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        907..927
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        931..951
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1043 AA;  116587 MW;  F63410221B325B73 CRC64;
     MAQESSNMDQ SKSDNVTDNK PNRSLISMAR PSPQRCHPLD QQSASTSSLP TSRPSSSPGQ
     SPNITPSILT SDTLHLPARS VSPTRPWTPS RGSEWSRHMP LSVSSVNYEP PEINCSPRPG
     TPSSKYGGSP RRPLRQPVVC WPPASSAGET SIDIADGGDD SEDPFVVGER TVHQRSNTRS
     SIKLIQFTMQ LSPQLLQMKR TPWVKLTLDD GEDDESDFNV HYGPAPTGRQ ERRGVRKAQM
     TKKEVRLMNG ELVLECKIPR MLHSFLPRRD DREFTHMRYT AVTCDPDDFT VKGFKLRQNI
     GSTMRETELF VCVTMYNENE IDFTRTMHGI MRNISHFCSR TKSRTWGKDG WQKIVVCIIA
     DGRQKVHPRT LNALAAMGVY QDGIAKNVVN QKPVNAHVYE YTTQVSLDPD LKFKGAEKGI
     MPCQVIFCMK ERNEKKLNSH RWFFNAFGRA LNPNICILLD VGTKPEPTAL YHLWKAFDQD
     SNVAGAAGEI KAGKGKGCLG LFNPLVASQN FEYKMSNILD KPLESVFGYI TVLPGALSAY
     RYHALQNDST GHGPLSMYFK GEMLHGKNAD VFTANMYLAE DRILCWELVA KREEQWVLKF
     VKSAVGETDV PDTVPEFISQ RRRWLNGAFF AAVYSLIHFR QIWRTDHTIT RKILLHIEFL
     YQFVSLAFTF FSLANFYLTF YFIAGALSDP TVDPFGHNIG KYIFAILRYT CVLLICLQFV
     LSMGNRPQGA KKMFLSGMII YCIIMMYTVF SALYMVVMQL KTSKEMIKDS LSLGNNTFTY
     IIVSTLSTVG LYFFMSFLYL DPWHMFTSSI QYFALLPSYI CRLQIYAFCN THDVTWGTKG
     DNVIRTDLGT ARITSSSTVE LEMPSEQLDI DSGYDESSAI SATDSKCPRQ SHPRRRCRKT
     TTAVRTYMVS VWFIANAILA MAVSEAFTEK SVGNNAYLAF VLWSVASLAV FRAVGSTAFA
     ILNVVHRVME GKMKFAAAGG TGYGYGSYVG SSSGGGGGSS GVRSSGAGSS LGLSSGMGEK
     VSDWASETGW AVKRTAGKLR FWR