ID A0A100I6D3_ASPNG Unreviewed; 1854 AA.
AC A0A100I6D3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=ABL_00984 {ECO:0000313|EMBL:GAQ34975.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ34975.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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 -!- 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:GAQ34975.1}.
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DR EMBL; BCMY01000001; GAQ34975.1; -; Genomic_DNA.
DR PaxDb; 5061-CADANGAP00001697; -.
DR VEuPathDB; FungiDB:An02g02360; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1174618; -.
DR VEuPathDB; FungiDB:ATCC64974_60860; -.
DR VEuPathDB; FungiDB:M747DRAFT_336951; -.
DR OMA; LEMHHQI; -.
DR Proteomes; UP000068243; 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 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..911
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 932..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 597..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..653
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; 206247 MW; 3222805FBD8E547D CRC64;
MAGPAPSGRT PSHAQSSLPS LPAHLQSDTH LTAHLASRFH VGLPTARLSS QALISLNTYT
TSSRGPDGDK EGSAMGEAED LAKRAFTRLG ARGENQAIVF LGESGSGKTT IRSHLLSSFL
SFSSTPLSSK LSYAAFVFDT LTTTKSVTTP TASKAGLFLE LQYDGSSSVN PTLIGGKIID
HRLERSRIAS VPTGERSFHV LYYLLAGTSA AEKEHLGFDS SIHVSTSGGK LSGASISHKR
WRYLGHPTQL KVGINDADGF QHFKTALRKL EFPRSEIAEF CQILATILHL GQLDFVSGQA
TTTTAEESGG YSHEGGETVT VVKNKDVLSV IAAFLGLGVE ELETSFGYRT KTIRRERVTV
MLDPKGARQN ADGLARTLYS LLVAYIFEGI NQRICAAEDS VANTVSILDF PGFSQASATG
STLDQLLSNA ATESLYNFCL QSFFERKAEM LDREEVTVPA TSYFDNSDAT RGLLKSGNGL
LSILDDQTKR GRTDSQFLES VKKRFENKNP AITVGSTGQG TTLISQGARS AFTVKHFAGE
VDYPVHGLLE ENGDVVSGDL MNLMRSTSSD FVRDLFGQEA LQTVTHPQER TAIMQAQVSS
KPMRMPSMAR RKAGPSRLAF DAPEADDQDE YESQAGSMSK SSGRRKSTMP GNGMQGAAGQ
FLSSLDIVSK CLNSANLNPY FVFCLKPNDR RIANQFDSKC VRAQVQTFGI AEISQRLRNA
DFSIFLPFAE FLGLAEIGNV VVGSDREKSE VVLDEKRWPG NEARVGSTGV FLSERCWADL
AKLGERVVPV YPAEGSDEGG DNLLHARAGG YADSKVRLLG PSDQSPGGFI YGEDGKQGYS
SSREFDGRSD AGASAFNSGD MFRNLDTREQ MLEKGNEKKM EEVDEAPVSG SRKRWMAIVY
LLTFYIPDFM IKTFGRMSRK DVRTAWREKL AINLIIWFSC AFAIFFIVAF PGLICPTQHV
YSSGELSTHN GKDGHNSFVA IRGIVFNLGK FMPSHYPDIV PEKQLKNYAG TDATGLFPVQ
VSALCPGKTG SIDPTVLLDY SSTNVSGSAT TVSTTDTNWV YHDFRYFTND SRPDWFQEQM
IMLKANYFKG WVGYTPTYLR TLGDKSQYIG SINGRVYDLT TYVAGGRRVQ APVGESVPTN
VDRDFMDDLV VQLFQRLPGQ DLTKYWEDLA ISDVMRERMQ LCLDNLFFVG HVDTRNSPRC
QFARYFILAI SIFICLIVVF KFLAALQFSR KNLPENLDKF IICQVPAYTE DEESLRRAID
SMARMRYDDK RKLLVVICDG MIIGQGNDRP TPRIVLDILG VPESVDPEPL SFESLGEGMK
QHNMGKIYSG LYEVMGHIVP FLVVVKVGKP SEVARPGNRG KRDSQMVLMR FLNRVHYNLP
MSPMELEIYH QIRNIIGVNP TFYEFILQVD ADTVVAPDAA TRMVSTLLAD TRILGICGET
ALSNAKTSMV TMIQVYEYYI SHNLVKAFES LFGSITCLPG CFTMYRIRSA ESGKPLFVSK
EIVEAYAEIR VDTLHMKNLL HLGEDRYLTT LLIKHHPKYK TKYISAAKAF TIAPESFAVF
LSQRRRWINS TVHNLIELIP LNQLCGFCCF SMRFIVFVDL ISTIIQPVTV AYIVYLIYWL
IHDTSTIPWT AFVLLAAIYG LQALIFIFRR KWDMIGWMFI YILGIPISSL ALPLYSFWHM
DDFSWGNTRV ITGEKGRKVV ISDEGKFDPS SIPKKTWEEY QAELWEAQTS RDDRSEVSGF
SYGTKSYHPM QSEYGFPASR PVSQFNLPRY SSRMSLAPSE MMSRNMEMEM EDLSHLPADD
VLLSEIREIL RTADLMTVTK KSIKLELERR FGVNLDAKRP YINSATEAIL AGNL
//
