ID A0A445B0I8_ARAHY Unreviewed; 1288 AA.
AC A0A445B0I8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Ahy_A10g046800 {ECO:0000313|EMBL:RYR32205.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR32205.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR32205.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR32205.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) 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:RYR32205.1}.
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DR EMBL; SDMP01000010; RYR32205.1; -; Genomic_DNA.
DR STRING; 3818.A0A445B0I8; -.
DR Proteomes; UP000289738; Chromosome a10.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030048; P:actin filament-based movement; IEA:UniProt.
DR Gene3D; 1.20.5.190; -; 3.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF792; MYOSIN-9; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 5.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
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|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000289738}.
FT DOMAIN 21..70
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 82..613
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1037..1288
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 494..516
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 954..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 748..827
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 963..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 131..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1288 AA; 146240 MW; 79F38CED73719D0A CRC64;
MILSAQHDIT EHNKTAQLSF VVGSHIWIED PDEAWIEGEI LESKGNEITV NCASGTKVIS
KSSHIYPKDP EFPPNGVDDM TRLPHLYSRE TMEKYKGAAF GEKSPNPFAI ADSAYRKMIN
EETSQSILVS GESGAGKTES TKMLMCYLAY MGGRAANEGR SVEQQVLELQ GLDDSKEYLA
TRRAMDVVGI NGNEQDAIFR IVAAVLHLGN IEFVKGDDEE TDSSQPKDDK SRFHLKTAAE
LLMCDEKSLE DSFCKRVMVT RGDKITKSLD PVAASLSRDA LAKIIYSRLF DWIVDKINNS
IGQDPHSKNL IGVLDIYGFE SFKTNSFEQF CINLTNEKLQ QHFNQHVFKM EQEEYTKEEI
NWSYIEFVDN QDVLDLIEKK PGGIIALLDE ACMFPRSTHE TFAEKLYQTF KDNKRFSKPK
LSRTDFTVNH YAGDVTYQTD LFLDKNKDYV VPEHAALLNA SKCNFVSGLF PPLPEETSKS
TKFASVATQF KQQLQSLLET LNATEPHYIR CVKPNNLLKP GIFENSNVLQ QLRCGGVMEA
IRISCAGYPT RKNFDEFIRR FSILEPKVLT SCPDEMTSCK MLLDKVNLKD YQIGKTKVFL
RVGQMAQLDA CRAEVLGRSA TIIQRKVCTY LCQKHYNTLR MSAIQLQRVV RGQLARFHYE
KMRREDASVK IQKNLRMHLS KTAYQALKAS AVFIQTAMRG KTARNQLRYR KLTRAAVIIE
RHGRGYIARS HYKRLKKAAI FAQCSWRRTM ARRELRKLRM AAKEAKALEA AKKELEKQVE
ELSLSLESER RMREAKTQEN EKLQSALHEM ELQLKETQAS LHEMESLLLK ERQAPKTADT
TPMQVIQSNG ADNDIELISK LTAENEQLKG LVNSLEKKST LEIPSNMTEN EVINMLSSER
ELLKDQVSSL EQKINETERK YEECSKLSEE RMNQIIETES KIIELKTSMQ RLEEKVSDME
TENQVLRQKS LSSSSSKKMS EKNPSQSSEN GSNQASTSAS SGQTKTFGTD ADSKVRTSHM
ERHLGFRSSK SLSSGSFDVE HQVDAKYPAL LFKQQLAAYV EKIYGILREN LKKDISPLIS
AFIQAHGKSD DNNHPAASWT AIVQCINRFL NIFKENHVHP VLVQKIFSQV FQHINAEIFN
SLVSQRECCT FNNGQLLKSG LAELEQWSTE ATEEVVEKKD ELSYDGLTNE LCPVLSSHQL
YRICTLYWDG NENDSSQSVS SEVISSLKLL MTDGVEDDSK SYMLEDNSSI PIIVEEISSS
LKDKTTSKVK PPEELLENAG FQFLHDYS
//