ID A0A0B1P012_UNCNE Unreviewed; 1882 AA.
AC A0A0B1P012;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=EV44_g2609 {ECO:0000313|EMBL:KHJ30164.1};
OS Uncinula necator (Grape powdery mildew).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=52586 {ECO:0000313|EMBL:KHJ30164.1, ECO:0000313|Proteomes:UP000030854};
RN [1] {ECO:0000313|EMBL:KHJ30164.1, ECO:0000313|Proteomes:UP000030854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=c {ECO:0000313|Proteomes:UP000030854};
RX PubMed=25487071;
RA Jones L., Riaz S., Morales-Cruz A., Amrine K.C., McGuire B., Gubler W.D.,
RA Walker M.A., Cantu D.;
RT "Adaptive genomic structural variation in the grape powdery mildew
RT pathogen, Erysiphe necator.";
RL BMC Genomics 15:1081-1081(2014).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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:KHJ30164.1}.
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DR EMBL; JNVN01004914; KHJ30164.1; -; Genomic_DNA.
DR STRING; 52586.A0A0B1P012; -.
DR HOGENOM; CLU_000192_0_2_1; -.
DR OMA; LEMHHQI; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000030854; 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 PRINTS; PR00193; MYOSINHEAVY.
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:UP000030854};
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 893..912
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 933..952
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1203..1222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1602..1620
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1625..1647
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1653..1674
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..785
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 956..1015
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 1825..1880
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT BINDING 99..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1882 AA; 209331 MW; A4A45B8EC8BD13F8 CRC64;
MALNQGGGPH SQPSLVALPQ HLQSDTHLTA HLASRFHVSL STAQLSSHAL ICLNTYTSSA
KGPNGGKEGS AMWGVEDLAD RAYARLGARS ENQAIVFLGE SGAGKTTVRS HLLSAFLNKY
STPLSTKLSL AAYIFDTLTT TKTATTPTAS KAGLFFELQY DTASTVNPIL IGGKILDHRL
ERSRVASVPI GERNFHVLYY LLAGTSVAEK THLGLDSPGT LSNAVHSPSQ AVHGDITGNQ
KRWRYLGHPT QLKVGINDAE GFQLFKTALR KLEFPRSEIA EICQVLASIL HLGQLEFEIT
AGNMALGDEG GYSHEASQST TAVKNKDVLS IVAAFLGVSA QDLQTTLGYK TKILQRERVT
VMLDPKGARS NANELARTLY SLLVAYVIES INQRICATED TVANTIAIID FPGFAQQSST
DSVLDQLLSN AATESLYNFT LQTFFEAKAE MLENEEVSVA ATSYFDNSDA VKGLLKPSNG
LLSILDDQAK RNKTDMQLLE CLRKRFEGKN PAISVSSATA KLPGSNFATH NLAASFSVKH
FAGEVDYLIA GLIEENEESV SGDLMNLIAS TKNDFVSQLF GQEALRTVVH PQEKKTIMQA
QVSSKPLRKP SVMRRKGDGV SGISGRDIKD PFDSIDELPE SRDGVKGRRG RNIDHGAAGQ
FLSGLDDVIK SLTAPNTNPY FVFCLKPNDR RIANQFDSKC VRTQIQTFGI AEISQRLRNA
DFSIFLPFAE FLGLAEAESI LVGSEREKAE TVVDERRWPA NEARIGSTGV FLSERCWAEI
ARLGERGFTM GRYPIPSDDG EDGVSPGTVH ITSKERLLGG PSASPGGILY GIDKKSGYFN
NEVDTRSEAG ISALGQGDMF RNLDTRQQMA EKGNEKTMVE VEEVKTSASR KRWVSLVYIL
TWFIPDFMVR WLGRMPRKDV RMAWREKFAI NMLIWLSCLF AAFVVVVFPM LICPKQHVFS
ASELSSFDGK KGRHAYVAIR GQVFDLTEFA PSHFPNIIPQ KSILAYAGLD ATSLFPVQVS
ALCQGVNGTI DPSIQLDYTS TNTSGSASVI SSTDSNYRYH DFRAFTNDSR PDWFFEQMML
LRANYHKGNI GYTPNYVRKL AEKQVSMAIL NDRIYDLTKY LQGGRAVKVK PGEDVPTDVN
TNFMSLPVVD LFQQKAGQDV TKFWATLPID EEMRHRMLLC LDNLFYVGNV DTRNSAQCKF
AEYLLLIISI LLCSVIGFKF FAALQFGGKN IPENLDKFVI CQVPAYTEDE DSLRRAIDSA
ARMRYDDKRK LLVVICDGMI IGQGNDRPTP RIVLDILGVS DSIDPEPLSF ESLGEGMKQH
NMGKVYSGLY EVQGHIVPFL VIVKVGKPSE VSRPGNRGKR DSQMVLMRFL NRVHYNAPMS
PLELEMYHQI RNIIGVNPTF YEYMLQIDAD TVVGADSASR MVSAFLDDTR LIGVCGETAL
SNAKSSFITM IQVYEYYISH NLSKAFESLF GSVTCLPGCF TMYRIRAVDS GKPLFVSREV
VEQYANIRVD TLHMKNLLHL GEDRYLTTLL MKHHPKYKTK YIRTAHAWTI APDSWQVFLS
QRRRWINSTV HNLIELIPLS QLCGFCCFSM RFIVFLDLLS TLVQPVTLAY IVYLIFLIVW
DNKSLIPTTA FILLGAIYGL QAVIFILHRK WEMIGWMILY ILAIPVFSFG LPLYSFWHMD
DFSWGNTRVV TGEKGKKIVI TDEGKFDPNS IPHKKWEEYQ TELWEAQTGK DDHSEVSGYS
YGTKYPGAVS EYNYTPSRPM SRVEGAIGSN LPYDTKNLNL HSSGLSLSHS EGFGLGALGD
QRQSQYGGSQ FFGQQELEMS NLTGLPNDDA ILAVIRDILK TADLMTVTKK SIKLELERRF
GVALDARRAY INSGMLRIIF KC
//
