ID W9J7X0_FUSOX Unreviewed; 1880 AA.
AC W9J7X0;
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=FOYG_00638 {ECO:0000313|EMBL:EWZ00922.1};
OS Fusarium oxysporum NRRL 32931.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660029 {ECO:0000313|EMBL:EWZ00922.1, ECO:0000313|Proteomes:UP000030753};
RN [1] {ECO:0000313|EMBL:EWZ00922.1, ECO:0000313|Proteomes:UP000030753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL Submitted (JUN-2011) 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: 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}.
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DR EMBL; JH717839; EWZ00922.1; -; Genomic_DNA.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000030753; 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; 1.20.58.530; -; 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:UP000030753};
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 884..903
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 924..943
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1198..1220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1590..1613
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1625..1644
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1651..1674
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..778
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 947..1009
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 1804..1859
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1880 AA; 208878 MW; 443D6FEAD2E24E37 CRC64;
MAMSLPQLGG AGGPHTQPSL PSLPAHLQSD THLTAHLASR FHVSHPTARL SSHALISLNT
YTNSSKGPDG GKEGSAMAGA EEIADRAFLR LGHRSENQAV VFLGESGAGK STIRAHLLTA
LLNKSSTPLS TKLSLAAYVF DSLTTTKTAT TPTASKSGLF YELQYDTSAT TNPVLIGGKL
LDHRLERSRI ADVPTGERNF HVLYYLLAGT SEAEKSHLGL DGGSATGTTQ KRWKYLGHPT
QLKVGINDAE GFQVFKNALR KLEFPRAEIA EICQILASIL HIGQLEFETT SQTSVTGDDS
GGFSHEGGTT ITAVKNKDVL SIIAAFLGVS AADLQTTLGY KTKMIHRERV TVMLDPNGAR
AHAGELARTL YSLLVAWILE TINQRLCAPE ESIANTVSIV DFPGFCQQTP TGSALDQLLN
NAATECIYNL TLQNFFDRKA DMLESEEVSV AATSYFDNSD AVRGILKPGN GLLSILDDQT
RRNRTDMQFL EALRRRFDGK NAAIEVGSAQ AKLPGSNFMT ENTSAVFTVK HFAGEVDYPV
KGLIEENGEI ISGDLLNMIN GTKSEFVARL FGQDALQTVT HPNERTTVMQ ATVSSKPMRA
PSVMSRKTHR TGRPSTAYKR QQQEAMEELD QQSQAGESKK NAKMTLEQGA SGQFLASLDN
VQKAVTDPGT NSYFVFCLKP NDRRIANQFD SKCVRMQVQT FGIAEISQRL RSADFSLFLP
FGEFLGMTDA ETILVGSERE RAEMVIEEKQ WPQNEVRVGA TGVFLSERCW MEIAQLGEAV
SVSGRYGGLP SSDAGDGLTP AESMAFGASK EHLVSGGNTP LMYGEKAKGG YFTDDTRSEA
GVSAFGGGDM FKNLDTREQM AERGNEKSLE EVEEYRDKPS RKRWVALVFF LTWFIPDFAI
RLIGRMPRKD VRMAWREKVA INMLIWLMCA VAAFFMVGFP MLICPKQYVY SSNELSSYDG
DKGSKGAYVA IRGFVIDLNA FIPNHYPGSN LVSEDTLLNY AGKDISALFP IQVSALCQGK
DGQIPPEVTL DNRNTNITGQ PQLLASRDID VNSVYHDFRY FTNDSRPDWY FEQMYTFKHV
YLKGRMGYSP KYVKKLARDS SWNVVTIHGK VYDMTKYLQG GLRLKAKAGK PTPNIPGATD
FMEDSVVQLF RSAKGQDVSK YWDNIKLSPV KKQRMETCLN NLFYIGDSDT RNSTRCQFAT
YFILAISVML ASILVFKFLA ALQFGGKNVP ENLDKFVMCM IPAYTEDEDS LRRAIDSLSR
MKYDDKRKLL VVVCDGMIIG QGNDRPTPRI VLDILGVSET VDPEPLSFES LGEGMKQHNM
GKIYSGLYEV QGHIVPFMVI VKVGKPSEVS RPGNRGKRDS QMVLMRFLNR VHYNLAMSPM
ELEMYHQIRN IIGVNPTFYE YLFQIDADTV VAADSATRMI SAFIDDTRLI ACCGETALTN
AKGSFITMIQ VYEYWISHNL SKAFESLFGS VTCLPGCFSM YRIRAAETGK PLFVSKEIVE
DYSTIRVDTL HMKNLLHLGE DRYLTTLLLK YHSKYKTKYL FSAQAWTIAP DSWSVFLSQR
RRWINSTVHN LAELIPLAQL CGFCCFSMRF VVFIDLLSTI VQPVIVMYIV YLIYQVATNP
SVVPITAFLL LGAIYGLQAV IFILRRKWEM VGWMIMYIAA IPVFSFGLPL YSFWHMDDFN
WGNTRVIAGE AGKKIVVSDE GKFDPNSIPR KKWEEYQAEL WETQTQTARD DVRSEISGYS
YATKAQGPFS EYGGGYQPSR PGSTAGFGHQ NMSRMSLAHS EMPGNRASQF GGSQFFSPED
LVGMPSDDAL LAEIRDILKT ADLMTVTKKG IKQELERRFN VPLDAKRAYI NSGKSLLSNS
FIRSQANNFS ATEALLSGQL
//
