ID W9XIZ4_9EURO Unreviewed; 1878 AA.
AC W9XIZ4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=A1O3_10078 {ECO:0000313|EMBL:EXJ76921.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ76921.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ76921.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ76921.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) 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 -!- 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:EXJ76921.1}.
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DR EMBL; AMGY01000011; EXJ76921.1; -; Genomic_DNA.
DR RefSeq; XP_007738359.1; XM_007740169.1.
DR STRING; 1182542.W9XIZ4; -.
DR GeneID; 19174159; -.
DR eggNOG; KOG2571; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR HOGENOM; CLU_000192_0_2_1; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000019478; Unassembled WGS sequence.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000019478};
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..786
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 1820..1875
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 601..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..816
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 COMPBIAS 801..816
FT /note="Polar 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 1878 AA; 207872 MW; AF18D75289489E17 CRC64;
MASRGNVPAH LQPSLPALPA HLQSDTHLTA HLASRFHISL PTAKLSSQGL ICLNTFTSST
RGPNGDKEGS AMGEAEDLAR RAWARLGNRA EDQAIIFFGE SGSGKTTVRS HLLSSFLSFS
STPLSSKLSL AAFVFDTLTT TKTTTTQTAS KAGLFYELQY DASSTIPTLI GGKLLDHRLE
RSRISHVPTG ERSFHVLYYL LAGTSAAEKS HLGLDGHVNV TTTGTGLSRS ASVAQKRWRY
LGHPTQLKVG INDAEGFQHF KNALRKLEFP RTEIAEICQV LAAILHIGQL EFGTGQATLT
AAEESGGYSH EGGETVTVVK NTDTLAIVAA FLGLSLPDLE ESLRYKTKTI HRERVTVMLD
PKGARENADE LATTLYSLLV AYIIESINQR TCAAEDSVAN TISIVDFPGF ADHSSTGSVL
DQLLNNAANE SLFNTCLHSF FENTAEMLES EEVSVPATSY FDNSDAVRGL LKHGNGLLAI
LDDQTRRGRT DLQFLESLRK RFDNRNKAIT VSSSTSTIPG SNFVSTNLAA SFTVRHYAGE
VDYPVHSLVD ENGDVVSGDL MNMIKATKSD FVASLFGQEA LNTVSHPAEK TAIVQAQVSS
KPLRMPSVSR KKHDQLRRMA SRRADRSPAL QEDEPVPGAE ESRLRRTKPT ATGLTQGAAA
QFLSALDNIT KSLTAPNVNN YFVFCLKPND RRIANQFDSK CVRQQVQMFG IAEISQRLRT
ADFSIFLPFG EFLGLADTDT GVVGSDREKS QLVLDSKHWP ANEARVGNTG VFLSERCWAS
IALIGSHSSA YFGGEAGSPS RPLTPGQNPF SDSKAGLLSS ADGTPGSFYG DETKGGGYFG
SRELDAKSDA GVSAFHSGDM FRNLETKEEL AEKGNKKKME EVDVVPVSSS RKRWLAIVYF
LTWYLPDFAV KWVGGMKRKD VRTAWREKFA INLLIWLSCG FVVFFIIIFP ELICPKQHVY
SAAELSSHDG KGKHSAYVAI RGEVFDLGAF MPNHYPSIIP SSSLKKYAGV DATGLFPIQV
SALCQGKDGR VDPTVQLDYT ATNISGTASV ISSADPNRRY HDFRYFTNDS RPDWFFEQMI
MLKANFRKGS VGYTPQYVKT LAKKSKSIAI LNDRVYDFTT YNQGGRSVRA PPGEKVPSGV
DTDFMDSLVV DLFTQRAGHD VTKYWNALPI DSTLRNQMQT CLDNLFFVGV TDTRNSAQCL
FARYILLAIS ILLCSVIGFK FFAALQFGGK NVPENLDKFV ICQVPAYTED EESLRRAIDS
AARMRYDDKR KLLIVVCDGM IIGQGNDRPT PRIVLDILGV SETVDPEPLS FESLGEGMKQ
HNMGKVYSGL YEVQGHIVPF MVVVKIGKPS EVSRPGNRGK RDSQMVIMRF LHRTHYNLPM
SPLELEMHHQ IRNIIGVNPT FYEFMLQIDA DTVVAPDSAT RMVSAFLRDT RLIGVCGETS
LSNAKSSFIT MIQVYEYYIS HNLTKAFESL FGSVTCLPGC FTMYRIRAAE TGKPLFVSKE
IIQDYSEIRV DTLHMKNLLH LGEDRYLTTL LMKHHSKYKT KYIFHAHAWT VAPDSWKVFM
SQRRRWINST VHNLIELIPL QQLCGFCCFS MRFVVFLDLL STVVAPVTVA YIVYLIVILA
TSSDVIPLTA FILLGAIYGL QAIIFILRRK WEMIGWMIVY ILAMPVFSFG LPLYAFWHMD
DFSWGNTRLV TGEHGKQILL SDEGKFDPDS IPKKKWEEYQ AELWDAQTQR DDAKSEVSGY
SYGTKSYLPT GSVYGGGYTE SQHLMPPSRS VSQLGIHLPV YDGGHSQSRL SLAPSEMLGS
GMVPSGRSVA DMEMSDLTGL PTDDLLLNEI RDILRTADLM TVTKKGIKQE LERRFNVNLD
AKRAYIGSAT EAILSGQL
//
