ID   Q8TGV2_EXODE            Unreviewed;      1885 AA.
AC   Q8TGV2;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 2.
DT   22-FEB-2023, entry version 84.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   Name=CHS5 {ECO:0000313|EMBL:AAL79830.2};
OS   Exophiala dermatitidis (Black yeast) (Wangiella dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=5970 {ECO:0000313|EMBL:AAL79830.2};
RN   [1] {ECO:0000313|EMBL:AAL79830.2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=14871935; DOI=10.1128/EC.3.1.40-51.2004;
RA   Liu H., Kauffman S., Becker J.M., Szaniszlo P.J.;
RT   "Wangiella (Exophiala) dermatitidis WdChs5p, a class V chitin synthase, is
RT   essential for sustained cell growth at temperature of infection.";
RL   Eukaryot. Cell 3:40-51(2004).
RN   [2] {ECO:0000313|EMBL:AAL79830.2}
RP   NUCLEOTIDE SEQUENCE.
RA   Liu H., Szaniszlo P.J.;
RL   Submitted (MAR-2005) 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   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; AF469116; AAL79830.2; -; Genomic_DNA.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   VEuPathDB; FungiDB:HMPREF1120_08776; -.
DR   BRENDA; 2.4.1.16; 6682.
DR   PHI-base; PHI:390; -.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR   CDD; cd14879; MYSc_Myo17; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR014876; DEK_C.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR036037; MYSc_Myo17.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR   PANTHER; PTHR22914:SF45; CHITIN SYNTHASE; 1.
DR   Pfam; PF03142; Chitin_synth_2; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF08766; DEK_C; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   SMART; SM01117; Cyt-b5; 2.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   SUPFAM; SSF109715; DEK C-terminal domain; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
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        894..913
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        933..953
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1201..1223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1599..1620
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1626..1647
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1654..1677
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..789
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          957..1016
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   REGION          601..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..647
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         99..106
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1885 AA;  208884 MW;  455A842ED0D426F3 CRC64;
     MATRGNVPAH MQASLPALPA HLQSDTHITA HLASRFHVSL PTARLSSQGL ICLNTFTSST
     RGPNGDKEGS AMGEPEDLAR RAWARLGNRA EDQAFGFFGE SGSGKTTVRS HLLSSFLSFS
     STPLSSKLSL AAFVFDTLTT TKTTTTQTAS KAGLFYELQY DASSNNPTLI GGKLLDHRFE
     RSRISHVPTG ERSFHVLYYL LAGTSAAEKS HLGLDGHVNI TTAGTGLSRS ASVSHKRWRY
     LGHPTQMKVG INDAEGFQHF KNALRKLEFP RTEIAEICQV LAAILHIGQL EFGTGQATLT
     AAEESGGYSH EGGETVTVVK NRDTLAIVAA FLGLGVQDLE ESLRYKTRTI HRERVTVMLD
     TKGARENADE LATTLYSLLV TYIIESINQR VCAAEDSVAN TISIVDFPGF ADHSSTGSVL
     DQLLNNAANE SLYNTCLHSI FEKTAEMLES EEVSVPATSY FDNSDAVRGL LKHGNGLLAI
     LDDQTRRGRT DVQFLESLRK RFENKNKAIT VGSATSTMPG SNFATTNLAA SFTVRHYAGE
     VDYPVHSLVE ENGDVVSGDL MNMIKATKSD FVANLFGQEA LNTVSHPAEK TAIVQAQVSS
     KPLRMPSVSR KKHDQLRRMA SRRADRSPAP QEEEPLPGTE EAKVRRTKPT ATGLTQGAAA
     QFLSALDNIT KSLTAPNVNN YFVFCLKPND RRIANQFDSK CVRQQVQMFG IAEISQRLRT
     ADFTIFLPFG EFLGLTNADG GVVGSDREKA QLVLDSKHWP PNEARIGNTG VFLSERCWAS
     IALTGSQAAA YFGGDIGSPS RPDTPGHNPF SDSKARLVGS ADGTPGSFYG DEAKGGGYFG
     SRELDAKSDA GASAFHSGDM FRNLETKEEL AEKGNKKKVE EVDVVPVSSS RKRWLAIVYF
     LTWYLPDFAI KWIGGMKRKD VRTAWREKFA INLLIWLSCG LVVFFIIVFP ELICPKQNVY
     SAAELSAHDG KGKHSAYVAI RGQVFDLGAF MPNHYPKIIP QSSLKKYAGV DATGLFPVQV
     SALCQGKDGR VDPTVQLDYT ATNISGTAAV ISSTDANRKY HDFRYFTNDS RPDWFYEQMI
     MLKANYRKGS IGYTPQYVKT LAKKSKSIAI LNDRVYDFTT YNEGGRSVRA PPGEEVPSGV
     DTDFMDSLVV DLFTQRAGHD VTKYWNALPL DPGLRSRMQL CLDNLFFVGV TDTRNSPRCL
     FARYILLAVS ILLCSVIGFK FFAALQFGGK NVPENLDKFV ICQVPAYTED EDSLRRAIDS
     AARMRYDDKR KLLIVVCDGM IIGQGNDRPT PRIVLDILGV SETVDPEPLS FESLGEGMKQ
     HNMGKVYSGL YEVQGHIVPF MVVVKVGKPS EVSRPGNRGK RDSQMVIMRF LHRVHYNLPM
     SPLELEMHHQ IRNIIGVNPT FYEFMLQIDA DTVVAPDSAT RMVSAFLRDT RLIGVCGETS
     LSNAKSSFIT MMQVYEYYIS HNLTKAFESL FGSVTCVPGC FTMYRIRAAE TGKPLFVSKE
     IIQDYSEIRV DTLHMKNLLH LGEDRYLTTL LLKYHSKYKT KYIFHAHAWT IAPDSWKVFM
     SQRRRWINST VHNLIELIPL QQLCGFCCFS MRFVVFLDLL STVVAPVTVA YIAYLIVLLA
     TESDVVPLTA FILLGAIYGL QAIIFILRRK WEMIGWMIVY ILAMPVFSLG LPLYAFWHMD
     DFSWGNTRLV RGEHGKQILL SDEGKFGPDS IPKKKWEEYQ AELWDAQTQR DDARSELSGY
     SYGTKSYLPT GSVYGGGYND TQHLMMAPSR SASQLDMHPT PMYGGGGGHN QSRMSLAPSE
     MLGSQSNLMM PSGRSVADME MSDLTGLPTD DMLLNEIRDI LRTADLMTVT KKGIKQELER
     RFNVNLDMKR AYIGSATEAI LSGQL
//