ID A0A165ESA7_EXIGL Unreviewed; 969 AA.
AC A0A165ESA7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0000259|PROSITE:PS51456};
GN ORFNames=EXIGLDRAFT_200957 {ECO:0000313|EMBL:KZV87568.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV87568.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV87568.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV87568.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV426122; KZV87568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165ESA7; -.
DR STRING; 1314781.A0A165ESA7; -.
DR InParanoid; A0A165ESA7; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
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:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 4.10.270.10; Myosin, subunit A; 1.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45615:SF40; MYOSIN HEAVY CHAIN, MUSCLE-RELATED; 1.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR SMART; SM00242; MYSc; 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|PROSITE-ProRule:PRU00782};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 1..283
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 161..183
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 664..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 331..440
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 772..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..813
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 969 AA; 109626 MW; 03D9953BB37F561E CRC64;
MFVLEQEEYA REGIEWSFVN FGLDLQPTID LIEESGGRPG ILSCLDEECI MPKATDATFT
AKLHGLWTNT DHPGGSKYAP ARFAQGFVVQ HYAGRVEYRT DGWLAKNKDP LNDNLTRVLA
SSSERSVAAM FAEGDGIKRV GGVVVKKGAF RTVTQRHKEQ LASLMGQLSA TQPHFVRCIV
PNTLRRPGRV DVPLVLDQLR CNGVLEGIRI ARLGYPNRLP FVECRARYEL LVPGVLPPGY
MDGRKAAARM LSALELDPAS YRIGTTKVFF KAGVLADLEE QRDGLLYDIF GRLQAVAARR
IQENARLYSA LKDWPWWQLY TKVRPLLAAT RNDEELRRKS VELELAKERA ERDARERQAL
ETLKMELEAD KRRVEEALAA ERVQSSDREA LLERSTRRQA ELEEDVLALQ ADLDTVDGQL
ERVQTQLAEM TERYKSLKAE FLLATEALER WEVEAKEWAS RDEERVKVDG RVVALETEMA
AMAKEMDELR ATLAEREEDK VRLKERMEAA LADLEAKLNA EVTHRDLGRA KADAAEKEAR
QAKEELAEVT RTATDYAAMI QRKEADATRA AADVASMRRE RDAALKQVAE LQAHSDTISN
ELVAQKDDRE RAVAARTKLQ AELDELRVAM DAKSSEETKR SEVERSRELE LADLRSQQAR
LAEELAEARK SGGEAQTALR TVQHERDELL TRRASLLKKA EDGDKKSKDS EAQLANAEKA
RRAAESELQA LRMRQVDLDG QLAEAVKAKE VCYRARRPRP FCLHAVRSRI ANSHPPTRST
RTSRTRYCRS SARRHRGFGR WRQLGRSSRR RLQSAHNSRS LQCKTTPKLR SSRIVTSSSS
ANSRRHKTTF IIASGTCRTF AQSRTRPLSN TSTSSRRPNV LPTSNSQTLR PNFVQRNRNC
ARCSRSRLVC SQTPKTLHAK LKKNVPSTAP RTSRFVRPRR RQTSCAPKSR RSVGLARLLK
RRHAGWTAT
//
