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Database: UniProt
Entry: A0A1C7MGP3_GRIFR
LinkDB: A0A1C7MGP3_GRIFR
Original site: A0A1C7MGP3_GRIFR 
ID   A0A1C7MGP3_GRIFR        Unreviewed;      1007 AA.
AC   A0A1C7MGP3;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Chitin synthase 8 {ECO:0000313|EMBL:OBZ76091.1};
GN   Name=CHS8_0 {ECO:0000313|EMBL:OBZ76091.1};
GN   ORFNames=A0H81_03331 {ECO:0000313|EMBL:OBZ76091.1};
OS   Grifola frondosa (Maitake) (Polyporus frondosus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Grifolaceae; Grifola.
OX   NCBI_TaxID=5627 {ECO:0000313|EMBL:OBZ76091.1, ECO:0000313|Proteomes:UP000092993};
RN   [1] {ECO:0000313|EMBL:OBZ76091.1, ECO:0000313|Proteomes:UP000092993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9006-11 {ECO:0000313|EMBL:OBZ76091.1,
RC   ECO:0000313|Proteomes:UP000092993};
RA   Min B., Park H., Kim J.-G., Cho H., Oh Y.-L., Kong W.-S., Choi I.-G.;
RT   "Whole genome sequencing of Grifola frondosa 9006-11.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {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:OBZ76091.1}.
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DR   EMBL; LUGG01000003; OBZ76091.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C7MGP3; -.
DR   STRING; 5627.A0A1C7MGP3; -.
DR   OMA; VAISKVW; -.
DR   OrthoDB; 1331060at2759; -.
DR   Proteomes; UP000092993; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd14879; MYSc_Myo17; 1.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 2.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR036037; MYSc_Myo17.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140:SF860; DILUTE CLASS UNCONVENTIONAL MYOSIN, ISOFORM C; 1.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   Pfam; PF00063; Myosin_head; 2.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Membrane {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:UP000092993};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        792..811
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        832..851
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..641
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          520..542
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          643..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          727..746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..662
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         93..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1007 AA;  111524 MW;  74FFD8C89C1BD26C CRC64;
     MSRQANRQST MSMHQQLESV TDLTTLSPVS EDIIVSCIRE RFMSDNIYTA IGTSALVAIN
     PHNPASPTCL PARQQCLHHM RRTTQDQSIL LSGETGSGKS ESRRLAIKTL LELSVSQPGK
     KGAKLGYQVP AAEFVLEAFG NSRTLFNPNA SHFGKYTELQ FTERGRLSGV KTLDYYLERS
     RVAGAPSGER NFHIFYYLVA GASAEERQHM HLPRRRSIAT SGSAGLPVFV GIKNVGFSKR
     HVAQTCQLIA AILHLGNLEF TIDRHRNEDA AVVRNTDVLD IVADFLGVQS SALEATLSYR
     TKLMKKELCT VFLDPDGASD NRDELAKTLY SLLFAWLNEH INQRLCRDDF TTFIGLFDLP
     GPQNMTSRPN SLDQFCGRLP TFTINHFSGP VTYTSDGFLE KNLDALNPDF VSLLRGSTAS
     SADAPAADGT GSINPFVRGL FSAKAIATQA HPRNEDTIVS AQQPVKPMRA PSTRRKNTIK
     RMPTLKEGDV EEKDRDDEET AIAGSSGGAP CVAGEFRSAL DVLFETLEDT QSWYVFCINP
     NDSQLPNQLE GRSVKAQVRS AGLAEITRRC VTVFEVTMTP DEFVSRYKDL LATSGVPDGD
     SRAQAEQARD ALDLEERDIV LGLHMVFLSQ AAFHRLEDDL RSKDTEEQKR NRLRDAEAEA
     GLDPRGLSDP YAPYQVPGGE SPYEGGNDDY GQSSQALPLV SNASPFQRGD AFDDYDERKS
     LRSEDFDGRS AYTSARDGES VSNFGTESYA PSRNMFQNAD KKGLLDKEAL AGEIQEGEVA
     EVLKESSARR RWVALCWMLT FWCPTFLLRY VGRMKRIDIQ QAWREKLALN MIIWFVCGCA
     VFVIAIISPI ICPTEHVFNA AELASHSFNL NPNNVYTSIR GEVFDLTAIA ETHERIVSVV
     PSKSILKYGG TSSDNIFPVQ VSALCNGING TVSPYVVLSS ANVTDPNAQY HDFRAWTNDP
     RPDWYFEQMV QMRWNNRVGF VGYSPKQIKS MASGGSSVAI SKVWSTT
//
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