UniProt: M5EAG8

Database: UniProt
Entry: M5EAG8_MALS4

LinkDB:  M5EAG8_MALS4 
Original site:  M5EAG8_MALS4

All links

Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (7)   
   Pfam (3)   
   PROSITE (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (25)   

Download RDF

ID   M5EAG8_MALS4            Unreviewed;      1824 AA.
AC   M5EAG8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   ORFNames=MSYG_2817 {ECO:0000313|EMBL:SHO78471.1};
OS   Malassezia sympodialis (strain ATCC 42132) (Atopic eczema-associated
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=1230383 {ECO:0000313|EMBL:SHO78471.1, ECO:0000313|Proteomes:UP000186303};
RN   [1] {ECO:0000313|Proteomes:UP000186303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42132 {ECO:0000313|Proteomes:UP000186303};
RX   PubMed=28100699; DOI=10.1093/nar/gkx006;
RA   Zhu Y., Engstroem P.G., Tellgren-Roth C., Baudo C.D., Kennell J.C., Sun S.,
RA   Billmyre R.B., Schroeder M.S., Andersson A., Holm T., Sigurgeirsson B.,
RA   Wu G., Sankaranarayanan S.R., Siddharthan R., Sanyal K., Lundeberg J.,
RA   Nystedt B., Boekhout T., Dawson T.L. Jr., Heitman J., Scheynius A.,
RA   Lehtioe J.;
RT   "Proteogenomics produces comprehensive and highly accurate protein-coding
RT   gene annotation in a complete genome assembly of Malassezia sympodialis.";
RL   Nucleic Acids Res. 45:2629-2643(2017).
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: Cytoplasmic vesicle membrane
CC       {ECO:0000256|ARBA:ARBA00004439}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004439}. 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   ---------------------------------------------------------------------------
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; LT671824; SHO78471.1; -; Genomic_DNA.
DR   RefSeq; XP_018740475.1; XM_018883746.1.
DR   STRING; 1230383.M5EAG8; -.
DR   GeneID; 30056804; -.
DR   KEGG; msym:MSY001_1919; -.
DR   VEuPathDB; FungiDB:MSYG_2817; -.
DR   HOGENOM; CLU_000192_0_2_1; -.
DR   OMA; LEMHHQI; -.
DR   OrthoDB; 1331060at2759; -.
DR   Proteomes; UP000186303; Chromosome 4.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
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   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.58.530; -; 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; 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; 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; PF08766; DEK_C; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
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; 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   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
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:UP000186303};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT   REGION          626..648
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   BINDING         109..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1824 AA;  203859 MW;  8E66902C53DF13A6 CRC64;
     MSGAAPTPVP AAETRAEVED EMLTRVCHRY YQSLYYTQVQ ESVLLVTNPY HAAVDVNSED
     VLRAYTREFR DIRLMVNGPQ LPSHIFRTAC NAYFYMQRTG QDQCLFFLGE TASGKSETRR
     LAMRALASVS SALPGKRGAR LAAQLPAALY VLECMGHAAT EENANASSMV LYTELQFSQN
     GRLIGFKMLP YYLELARVSL LRQPGRAFHL FSLLVAGAAP EDRQRWRLDG AELRLLGVGH
     ARDRDEASRA AAFRQWCDAV TTLGLSTSQR SEMLDVIVAL LHLGDIDFIH EDGPSAAAHV
     VSEEPLYVAA SLLGVGASAL AHALTHLTSV VQGQLCTALL NAEQAAESRD RLVRTLYSLL
     FAWVNEHIRS CFAHEAFDTY IGLLDLPGHR NRIVNHLETF AVNLAADTVQ RHMMHIMRER
     RMGELDHEGL SHLAPLPSTV SGADRLRVLT HYPGGLVHIM DDQARRRPRK NSQTMVEAMQ
     RRWVHHASLQ VERVDRLGAP KFVVTHFHGS VAYEPHGWLA QNDESPALEH MSLLRGAQDG
     LVDGTSGFGS SSAFVRGLFR HASAPGTAVP AKRSPSTKRL GRSGTLRAAA SREPHDDDVY
     GGALHEPAAA ASEGPPCVLG TLQSSLHMLL DVVDEAKAWF VLCVRPNTNV LANQCEPGMM
     RRQLEALDLA QLRVGHESDY SVTLTFTEFC DRYGALPMFD AVDMLAAPAA EAKMRVSDAV
     ARMNWTDTHV AMGLHKVFLS HAVFRELEDH LRATDPEEMQ HQLRKASADD DDAAQAVVDP
     YSPYEARVSR AEHAAPSPPE PATPAWRGWS YDEQQGLLDD ADGEDVLLLD DTKDAGPGEA
     APPAGPQVTE RLRVTFERRL WVVLTWLCTF WVPSPVLGLF PKLRRSDVRM AWREKLAINM
     MIWFVCLCSI FVIVFLGNVV CPRQHLYSVG ELSGHKGSDA FTAIRGEVFD LHKIVGAHLS
     AIPVVSRKSL LQYAGADATS IFPVQVNALC NGPNGPISPW VTLDNSNNTD ANARYHDFRA
     YRGTDVRPDW YYEQMWYMRS QYRVGFVGYT PKEIQNMMED GRTIGVYNSY IYDLTAYVGQ
     GNQGGFRMPE GVAPPANLDR TILDPSVVQL FTQNPGRDVR AMFDALAMPP AKRQDQATCL
     RNLFLIGRVD ERSSPRCTFS SYILLGLSIL MVLTVGVKFF AALQFVRSTP PEDHEKFVVC
     QIPCYTEGAE SMRKTINSIA RLRYDDRRKL IVVICDGNVT GAGNEAPTPQ LVLDVLGAEP
     TEAEPRSFVS LGEGLKQHNM ARVYSGLYEH AGHLLPYLVV AKCGAPSETM RPGNRGKRDS
     QLILMRFFNK VHYGSPMSPL ELEMYHHIKN IIGVNPSFYE YLLQVDADTE VEPSALARMI
     AFFVRDKKVI GLCGETALAN ERQSLTTMLQ VYEYYISHYL VKAFESLFGS ITCLPGCFSM
     FRFRAPDSQR PLFVSHAVLD DYAENRVDTL HLKNLLYLGE DRYLTTLVLK HFPEYKTQFV
     QHARCVTTAP DSWRVLLSQR RRWINSTVHN LVELLKTPQL CGFCLFSMRF VVLIDLLSTV
     VAPVTIGYLV YLLFVVAVEG GTIPVTSIVL LGGIYGLQAI IFLLHRRFDM IGWMVVYILG
     MPLWSLILPL YSFWHMDDFS WGNTRIVTGE KGEKLLVHNE GHFDPQTIPH MTWDEYEREL
     WENRAPPSDE PVGLGPLPHS YADTSPGLSK RYSDMSWPLR DDASLAPLDD ASAKQPWAME
     PPDLLLDPMP PSAEAPGLPR DERLGRLPPN EVLRYDIRQI IAASDLTSIT KRQVRAQLQD
     LYGCPIQEKK AYINAQIEAA LRDL
//

DBGET integrated database retrieval system