ID A0A1L9UXU0_ASPBC Unreviewed; 1854 AA.
AC A0A1L9UXU0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=ASPBRDRAFT_411472 {ECO:0000313|EMBL:OJJ76503.1};
OS Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ76503.1, ECO:0000313|Proteomes:UP000184499};
RN [1] {ECO:0000313|Proteomes:UP000184499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101740 / IMI 381727 / IBT 21946
RC {ECO:0000313|Proteomes:UP000184499};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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 ---------------------------------------------------------------------------
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; KV878680; OJJ76503.1; -; Genomic_DNA.
DR SMR; A0A1L9UXU0; -.
DR STRING; 767769.A0A1L9UXU0; -.
DR VEuPathDB; FungiDB:ASPBRDRAFT_411472; -.
DR OMA; LEMHHQI; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000184499; 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; 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:UP000184499};
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 895..914
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 934..954
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1202..1224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1600..1621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1627..1648
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1655..1678
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 958..1017
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 1796..1851
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1854 AA; 206266 MW; 94A9C43BB975D29E CRC64;
MAGTTPAGRT PSHAQSSLPS LPAHLQSDTH LTAHLASRFH VGLPTARLSS QALISLNTYT
TSSRGPDGDK EGSAMGEAED LAKRAFTRLG ARGENQAIVF LGESGSGKTT IRSHLLSSFL
SFSSTPLSSK LSYAAFVFDT LTTTKSVTTP TASKAGLFLE LQYDGSSSVN PTLIGGKIID
HRLERSRIAS VPTGERSFHV LYYLLAGTSA AEKEHLGFDG SIHVSTSGGK LSGASIGHKR
WRYLGHPTQL KVGINDADGF QHFKTALRKL EFPRSEIAEF CQILAAILHL GQLDFVSGQA
TTTTAEESGG YSHEGGETVT VVKNKDVLSV IAAFLGLGVE ELETSFGYRT KTIRRERVTV
MLDPKGARQN ADGLARTLYS LLVAYIFEGI NQRICAAEDS VANTISIIDF PGFSQASATG
STLDQLLSNA ATESLYNFCL QSFFDRKAEM LDREEVTVPA TSYFDNSDAT RGLLKSGNGL
LSILDDQTKR GRTETQFLES VKKRFENKNP AITVGGTGQG TTLISQGART AFTVKHFAGE
VDYPVHGLLE ENGDVISGDL MNLMRSTSSD FVRDLFGQEA LQTVTHPQER TAIMQAQVSS
KPMRMPSMAR RKAGPSRLAF DAPVADDQDD YESQAGSTTK SSGRRKSTML AHGIQGAAGQ
FLSSLDIVTK CLGSPDLNPY FVFCLKPNDR RIANQFDSKC VRAQVQTFGI AEISQRLRNA
DFSIFLPFAE FLGLAEIGNV VVGSDKEKSE VVLDEKRWPG NEARVGSTGV FLSERCWADL
AKLGERVVPV YPAEGSDEGG DNLLHARAGG YTDSKVRLLG PTDQSPGGFI YGEEGKQGYS
SSREFDGRSD AGASAFNSGD MFRNLDTREQ MLEKGNEKKM EEVDEAPVSG SRKRWMAIVY
LLTFYIPDFM IKMFGRMSRK DVRVAWREKL AINLIIWFSC AFAIFFIVAF PGLICPTQHV
YSTAELSSHN GKDGHNSFVA IRGVVFNLGK FMPSHYPDIV PEKQLKKYAG TDATGLFPVQ
VSALCPGKDG SVDPTVLLDY SSTNVSGSAT TVSTSDTNWV YHDFRYFTND SRPDWFQEQM
IMLKANYFKG WIGYTPTYMK TLGEKSQYIG SINGRVYDLT TYVAGGRRVQ APVGKSVPAN
VDRDFMDDLV VQLFQRLPGQ DLTKYWEDLQ ISDVMRERMQ LCLDNLFFVG HVDTRNSPRC
QFARYFILAI SIFICLIVVF KFLAALQFSR KNLPENLDKF IICQVPAYTE DEESLRRAID
SMARMRYDDK RKLLVVICDG MIIGQGNDRP TPRIVLDILG VPESVDPEPL SFESLGEGMK
QHNMGKIYSG LYEVMGHIVP FMVVVKVGKP SEVARPGNRG KRDSQMVLMR FLNRVHYNLP
MSPMELEMYH QIRNIIGVNP TFYEFILQVD ADTVVAPDAA TRMVSTLLAD TRILGLCGET
ALSNAKTSMV TMIQVYEYYI SHNLVKAFES LFGSITCLPG CFTMYRIRSA ESGKPLFVSK
EIVEAYSEIR VDTLHMKNLL HLGEDRYLTT LLIKHHPKYK TKYISAAKAY TIAPESFAVF
LSQRRRWINS TVHNLIELIP LNQLCGFCCF SMRFIVFVDL ISTIIQPVTV AYIVYLIYWL
VHDTSTIPWT AFVLLAAIYG LQALIFIFRR KWEMIGWMII YILGIPISSL ALPLYSFWHM
DDFSWGNTRV ITGEKGRKVV ISDEGKFDPA SIPKKTWEEY QAELWEAQTS RDDRSEVSGF
SYGTKSYHPM QSEYGFPASR PVSQFNLPRY SSRMSLAPSE MMSRNMEMEM EDLSHLPGDD
VLLSEIREIL RTADLMTVTK KSIKLELERR FGVNLDAKRP YINSATEAIL AGNL
//
