UniProt: A0A177WH42

Database: UniProt
Entry: A0A177WH42_BATDL

LinkDB:  A0A177WH42_BATDL 
Original site:  A0A177WH42_BATDL

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (12)   
   InterPro (6)   
   Pfam (3)   
   PROSITE (2)   
   SMART (1)   
All databases (20)   

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ID   A0A177WH42_BATDL        Unreviewed;      2009 AA.
AC   A0A177WH42;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   ORFNames=BDEG_23276 {ECO:0000313|EMBL:OAJ39427.1};
OS   Batrachochytrium dendrobatidis (strain JEL423).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=403673 {ECO:0000313|EMBL:OAJ39427.1, ECO:0000313|Proteomes:UP000077115};
RN   [1] {ECO:0000313|EMBL:OAJ39427.1, ECO:0000313|Proteomes:UP000077115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEL423 {ECO:0000313|EMBL:OAJ39427.1,
RC   ECO:0000313|Proteomes:UP000077115};
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Cuomo C., Devon K., Jaffe D., Butler J.,
RA   Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E., Brockman W.,
RA   Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA   O'Leary S., Kodira C., Zeng Q., Yandava C., Alvarado L., Longcore J.,
RA   James T.;
RT   "The Genome Sequence of Batrachochytrium dendrobatidis JEL423.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OAJ39427.1, ECO:0000313|Proteomes:UP000077115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEL423 {ECO:0000313|EMBL:OAJ39427.1,
RC   ECO:0000313|Proteomes:UP000077115};
RA   Cuomo C.A., Farrer R.A., James T., Longcore J., Birren B.;
RT   "Lineage-specific infection strategies underlie the spectrum of fungal
RT   disease in amphibians.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; DS022303; OAJ39427.1; -; Genomic_DNA.
DR   STRING; 403673.A0A177WH42; -.
DR   VEuPathDB; FungiDB:BDEG_23276; -.
DR   eggNOG; KOG2571; Eukaryota.
DR   eggNOG; KOG4229; Eukaryota.
DR   Proteomes; UP000077115; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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:InterPro.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR   CDD; cd04190; Chitin_synth_C; 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; 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:SF13; CHITIN SYNTHASE; 1.
DR   Pfam; PF03142; Chitin_synth_2; 1.
DR   Pfam; PF08766; DEK_C; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   SMART; SM00242; MYSc; 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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000077115};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1006..1030
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1269..1291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1661..1684
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1696..1715
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1722..1745
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..618
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1951..2006
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
FT   REGION          273..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          671..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          881..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..713
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        881..900
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2009 AA;  222936 MW;  859CBB8BC341E435 CRC64;
     MDWATQSDDL AALLAQETTS AVANNSSPPA AETLIVHTLE QRCLLQRPYT YVGANVLLSV
     GAAAGSNNAV GGVGSLSAQY DRAAETAIST TDDDTLSPLP PHTMQLASTV FYQMLVHQEN
     QSVVFCGMPS AGQSIDRRIF SQQLVDLSKN GKKKSRVLSG AVKMEYALDS FGMAKSPHAV
     DAACYGRYTE YQYSSTGRMV GVKLLDYTLD TARVTAGSSM DDGERTFNIF YQLLAGATKE
     EKETLHISEA ASFAYLKGTK LARANTITRS GTLSRRFPTL GRSGTTSKKD GNTPVASPMA
     ASSTSAHPSS SPEDAIPTAK DAKNFQELRE HLKSLGIGRR TQSQIYQILA AILHLGNIVF
     GVDPNLKEDE STVVRSTETL NIAAALLGLS SKSLADSLTY RSKLVGRELC SIYLQPEGAL
     LQRDALAETL YSLLFSWLVE HLNTRLCKSE EEVNSFVGLV DFPWFRSQYT GSATNFSIFI
     GNYTQERLIQ YTQNCYYDDI DFIFKTDGLS VTLPSYRDNQ WTVDVFRGTS RQKGLLALLD
     EEPESGEDFS LNRNQNLLTH LDNGLKSNPH YIASFQCSTV ATASHSVATT SATVKNMFGI
     RHYNTESVVQ YDLDSFLDQD ICMSDFVALF RGSAGVAESD IPSKEPNVTF IAGLFSNRTG
     LKTIRSGRGA AIGAQKAQGP LRKPSLKRKK KPVTDVTTDS PAETKETGKD NASIAPKSKR
     VSPFTPAAES IDELMDTLKS TRHWSVISFS LSEPCKLLIL LHLISSGSCH NSTFLSCANF
     DLFCDVDASH GLKYNVFTEK YASLLATKGL SHSAGSPRNL VKQFVAAQYW STREVSLGNT
     MVFLSVSRWR WIHAAMKRLE STDENDNLLL NNNKTNSMMT LPSQPVPNAQ PWLTSRQTGP
     LTEDDRSDVE SNYESEYGYN DNDNRFPGKS TDMEMGNMNR TNMASPMSPV LGSKREIVDS
     VTPVTRLRKC WVCCTWTLTW WIPGPFLSCC GKMKRPDIRM AWREKVALCV IIFGLCMFLM
     FFIIGLRYII CPTVPIKSQS EVLQKAFRLG QQTVPWFAAH GRYYFAEDLM SQHIRDYGPG
     TGQGSLALYQ FQQFYGNDVS NLFFKQDRWS VYCPGLAAPQ QGWDYLDPSI PWMKRSDIQA
     ATPMAMHRST DPSGQPQPFS ESLDRFAKGR IGWTEQAVNG MSSNTKRFII IFDNVYYVSP
     IDALQNATFS LTVRNLLSPT PGSDVTAAWK ATRAQSGELQ QELDTALTCL NNIFYVGTVD
     RRDTFQCRLT GGLLLSTSIV LVCVVGFKFL AALQFSSRKE PEAGDKFVIC MVPCYTEGTE
     SLLKTLDSLA TLNYDDKRKL LFVICDGMII GSGNDRPTPR LVLDIFGVDP DIDPEPMAFQ
     SLGEGNRQYN MGKIYSGLYE IRGRSVPFIV VAKVGSPTER VKPGNRGKRD SQLVLMRFLN
     RVHFNAEFAP MELDIYHHMK NIIGVSPSFY EFILMIDADT EVEPNALNRM VSVMVHDVKV
     MGLCGETRIS NEKESWVTMV QVYEYFISHH LSKAFESLFG TVTCLPGCFS MYRIRSASKN
     VPLLVSPALL TEYSENSVDT LHMKNLLHLG EDRYLTTLML KHFPTMRTKF AGEARCSTVV
     PDKWSVLLSQ RRRWINSTVH NLFELVFLDQ LCGLCCFSMR FVVFLDLFAT FVQPAIVIYI
     VYLIYSVSTS TDTFPLLSII LIGCIYGFQV IIFLIKREWQ HIAWMIIYLL AIPVFSFWIP
     CYSFWHFDDF SWGNTRVVVG EGKKTVYVAD AEPFDIRSIP LKRWKDFEGS GGAGSVDSRG
     GVDAWEHGSQ ASGSIVQAGA HRNKAAGYAG SEYSSPGGGV YHRGSAASNY AGSAYGGPAP
     SISGSYHGGL PVIAQSTVPA RYNTHDLTPG QAADPQRFSM ISFGAYPTQT NEMQNARNSS
     ASLVPGPFPS QQTNRYSMLS NTSQQVPVQT GPTDEQILAD IRQILSSGDL MTLTKKQIRD
     DLGQRFGVDL RPRKETINRM IDEVLQGRL
//

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