GenomeNet

Database: UniProt
Entry: A0A067S954_GALM3
LinkDB: A0A067S954_GALM3
Original site: A0A067S954_GALM3 
ID   A0A067S954_GALM3        Unreviewed;      1915 AA.
AC   A0A067S954;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   31-JUL-2019, entry version 26.
DE   RecName: Full=Myosin motor domain-containing protein {ECO:0000259|PROSITE:PS51456};
GN   ORFNames=GALMADRAFT_259196 {ECO:0000313|EMBL:KDR66437.1};
OS   Galerina marginata (strain CBS 339.88).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Strophariaceae;
OC   Galerina.
OX   NCBI_TaxID=685588 {ECO:0000313|EMBL:KDR66437.1, ECO:0000313|Proteomes:UP000027222};
RN   [1] {ECO:0000313|Proteomes:UP000027222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 339.88 {ECO:0000313|Proteomes:UP000027222};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A.,
RA   Sun H., LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E.,
RA   Pisabarro A.G., Walton J.D., Blanchette R.A., Henrissat B., Martin F.,
RA   Cullen D., Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy
RT   of the white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00782}.
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DR   EMBL; KL142423; KDR66437.1; -; Genomic_DNA.
DR   EnsemblFungi; KDR66437; KDR66437; GALMADRAFT_259196.
DR   OrthoDB; 20724at2759; -.
DR   Proteomes; UP000027222; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of 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:motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IEA:InterPro.
DR   CDD; cd14879; MYSc_Myo17; 1.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR014876; DEK_C.
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; PTHR22914; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF08766; DEK_C; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53448; SSF53448; 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   Complete proteome {ECO:0000313|Proteomes:UP000027222};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Myosin {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027222};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    928    947       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    967    987       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1227   1249       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1625   1646       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1652   1672       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1684   1703       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       16    772       Myosin motor. {ECO:0000259|PROSITE:
FT                                PS51456}.
FT   NP_BIND     116    123       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00782}.
FT   REGION      615    639       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      651    673       Actin-binding. {ECO:0000256|PROSITE-
FT                                ProRule:PRU00782}.
FT   REGION      775    826       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      863    883       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1801   1833       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    615    632       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    775    793       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS   1808   1833       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   1915 AA;  215348 MW;  29D1AC8269C73261 CRC64;
     MNRQSSGTMS AHQRLEAATD LARLSPISDD IIVACLRERF MTDTIYTNIG TSGLVALNPH
     KYVASNADAV LHKYAAEYRD SSEVKDRLPP HIFQIANNAY YHMRRTAQDQ CLVFSGETSS
     GKSENRRLAI KSLLELSVSN PGKKGSKLAN QVPAAEFVLE SFGNARTLFN PNASRFGKYT
     ELQFSDKGRL NGVKTLDYYL ERNRVAAVPS GERNFHIFYY LVAGASPEER QHLHLLEKTA
     YRYLGQRGTS TARPTGGHDD DGQRFDQLKI ALKTIGFSKR HVAQTCQLVA AILHLGNLEF
     TVDRHRNEDA AVVRNTDMLE IVADFLGIQP AALEAALSYK TKLVKKELCT VFLDPDGASD
     NRDDLAKTLY SLLFAWLNEH INQRLCKDDF STFIGLFDLP GPQNMSSRPN SLDQFCINFA
     NERLQNWIQR SLFEKHVNEY NVEGVSRFVP QVPYFDNTEC IRLLQNSPGG LVHIMDDQAR
     RQPKKTDHTM VEAFTKRWGN HSSFKTGTLD RSGFPSFTVN HYNGSVTYSS EGFLDRNLDA
     INPDFVSLLR GVADGLEGTG SINPFVKGLF SAKAIATQAH PRNEDTIVAA QQAVKPMRAP
     STRRKSAVKR MPTLKEGVDV EEKERDDDDT HGAGNLTGSS PCVAGEFKAA LDTLFETIDE
     TQPWYIFCIN PNDSQLPNQL EGRSVKGQVK GVGLTEVARR SVNFFEVGMT PEEFCDRYSE
     GLVAGGVSEG DDREIIGQAR TTFGLGEKDL VLGTLKVFLS QRAFHKFEDQ LRSRDVEEQK
     RNRLRDAEAE AGLDPRGIND PYAPYRSPNE ELEPSPWGNN NYSDAYGASN QQLPLVSNAS
     PFQRADLYDD DYEENKSVRS DDFDARSKFT SQRDDSVSHF GSESYAPSRN MFQNTDKRGL
     MEKEALAGEI QEGETTEILK ESSARRRWVA MCWMLTWWVP TPLLTYVGRM KRMDVRQAWR
     EKLALNLIIW FICGCAVFVI AVLGVVICPT EHIFNSAELA SHSSVLSPNN VLTSIRGEVF
     DLTAVAETHH RVVNVVPVKS ILKYGGQSAD SIFPVQVSAL CNGISGSVSP YIVLDSKNNT
     DVNSVYHDFR VFTNDSRPDW YFERMVEMRY QARVGFVGMT PREIRNHASA GQSIAIYNGL
     IYDVSTYLTS PPAIRTPQGT QAPGGTDVNF MSGDILDLFK FNAGSDITKR LNSLNIDRDI
     LARQKVCLRN LFLVGKVDNR QSPQCLFANY ILLILSIIMV SIIGFKFLAS INFGAARAPE
     DHDKFVICQV PCYTEGDVSL RRTIDSLAQM KYDDKRKLLV VICDGMIVGS GNDRPTPRIV
     LDILGADPNL DPEPLSFMSL GEGAKQHNMG KVYSGLYECS GHVVPYLVIV KIGKPTERAR
     PGNRGKRDSQ MLLMHFLNKV HFNSPMNPLE LEMYHQIKNV IGVNPSFYEY LFMVDADTTV
     DPLSVNRLIS AMIHDKKLLG ACGETELANA KQSLITMMQV YEYFISHHMA KAFESLFGSV
     TCLPGCFTLY RLRTPDTHKP LLIANQLITD YSENRVDTLH MKNLLHLGED RYLTTLLLKH
     FPRFKTQFIR DAHAYTVAPD DWQVLLSQRR RWINSTVHNL GELIFLDQLC GFCCFSMRFV
     VMIDLLSTLI QPVTVAYIAY LIYLVAGLGK SIPTLSLIMI AAVYGIQALV FVMRRKWDMI
     GWMIFYILAI PAFSFFLPLY SFWKMDDFSW GQTRLVLGES GKKMIVHDEG KFDPRSIPLK
     SWSDYENELW DKESNHSIGS WVPPNKIKND GYPESHTASI YGRETFYEPR SFSPAPSQFG
     MHPPPGYQSG RNTPQSPFHV SPETALLQPT PSRPITNYLD IPIPRTHSPE DGDLGGGPSD
     MDIDLAVQQV LRSADLNSIT KREIRRQLED HFGMDLTSRK AVINASIDRI LLNQN
//
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