ID Q8TGV2_EXODE Unreviewed; 1885 AA. AC Q8TGV2; DT 01-JUN-2002, integrated into UniProtKB/TrEMBL. DT 26-APR-2005, sequence version 2. DT 28-JUN-2023, entry version 85. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; PS51998; DEK_C; 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 DOMAIN 1827..1882 FT /note="DEK-C" FT /evidence="ECO:0000259|PROSITE:PS51998" 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 //