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Database: UniProt
Entry: I1I4X3_BRADI
LinkDB: I1I4X3_BRADI
Original site: I1I4X3_BRADI 
ID   I1I4X3_BRADI            Unreviewed;      1190 AA.
AC   I1I4X3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=100825630 {ECO:0000313|EnsemblPlants:KQJ97208};
GN   ORFNames=BRADI_3g29440v3 {ECO:0000313|EMBL:KQJ97208.1};
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ97208.1};
RN   [1] {ECO:0000313|EMBL:KQJ97208.1, ECO:0000313|EnsemblPlants:KQJ97208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ97208.1,
RC   ECO:0000313|EnsemblPlants:KQJ97208};
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
RN   [2] {ECO:0000313|EMBL:KQJ97208.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ97208.1};
RG   The International Brachypodium Initiative;
RA   Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA   Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA   Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT   "WGS assembly of Brachypodium distachyon.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQJ97208}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ97208};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; CM000882; KQJ97208.1; -; Genomic_DNA.
DR   RefSeq; XP_003574095.1; XM_003574047.3.
DR   AlphaFoldDB; I1I4X3; -.
DR   STRING; 15368.I1I4X3; -.
DR   EnsemblPlants; KQJ97208; KQJ97208; BRADI_3g29440v3.
DR   GeneID; 100825630; -.
DR   Gramene; KQJ97208; KQJ97208; BRADI_3g29440v3.
DR   KEGG; bdi:100825630; -.
DR   eggNOG; KOG0160; Eukaryota.
DR   HOGENOM; CLU_000192_7_2_1; -.
DR   InParanoid; I1I4X3; -.
DR   OMA; PLYGNEY; -.
DR   OrthoDB; 5489458at2759; -.
DR   Proteomes; UP000008810; Chromosome 3.
DR   ExpressionAtlas; I1I4X3; baseline.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR   CDD; cd01383; MYSc_Myo8; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 2.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.20.240.20; -; 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; 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; IPR036022; MYSc_Myo8.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF780; MYOSIN-1; 1.
DR   Pfam; PF00612; IQ; 3.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 4.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50096; IQ; 3.
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:UP000008810}.
FT   DOMAIN          136..185
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          189..860
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          1..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          740..762
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1055..1082
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          984..1032
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1056..1077
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         280..287
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1190 AA;  133869 MW;  C157FF5C1FE6B889 CRC64;
     MASVEVRSVR KSAALRARTM PTKLQPARSM PLDYRYSPTA AASAGVGGKP AANGVGRRAA
     AAPVEEGEVF GVEGDADSPY SSKAGTTEEE EGGGGGGEVD SASSAAATPR KSLPAAAASP
     SQRDTRWGDT SSYGAKQKHR VFCQLPNGDW ALCTVLTTSG DESVLKVSEG KVVRSKTESL
     QPANPEILDG VDDLMQLSYL SEPSVLYNLQ YRYSQDMIYT KAGPVLVAVN PFKKVPLYGN
     EYIYSYKNKT MDSPHVYAIA DSALREMKRD EVNQSIIISG ESGAGKTETA KIAMQYLASL
     GGGSGIEYEI LQTNPILEAF GNAKTLRNDN SSRFGKLIEI HFSTTGRICR AMIQTFLLEK
     SRVVQCAVGE RSYHIFYQLC AGAPTSLREK LNLKKVDEYK YLKQSCCYSI AGVDDAQMFH
     TVTEAMNIVH ISKEDQDNVF AMVSAVLWLG DVSFTVIDDE NHVEIVIEEA AETVARLLGC
     SIEDLNLAFS KRHMKVNNEN IVQKLTLTQA MDTRDALAKA LYASLFEWLV EQINKSLSVG
     KRRTGRSISI LDIYGFESFD KNSFEQFCIN YANERLQQHF NRHLFKLEQE EYVEDGIDWA
     KVEFEDNQDC LNLFEKRPLG LLSLLDEEST FPNATDLTFA NKLKQHLDTN SCFRGERGKA
     FAVRHYAGEV AYDTSGFLEK NRDLLHMDSI QLLAKCKSSI PQIFASKMLT QSDNLESVPY
     RPNAADSQKL SVAMKFKGQL FQLMQRLEST TPHFIRCIKP NNLQLPSIYG QELVLQQLKC
     CGVLEVVRIS RSGYPTRMTH QKFARRYGFL LLEDVASQDP LSVSVAILHQ FNILPEMYQV
     GYTKLFFRTG QIGKLENTRN RTLHGVLRVQ SCFRGHQARR HARERIRGVL ALQSFIRGEN
     ERQSYSSLLR KHRAATVVQR NLRGWLARRY FIKIRKASVV IQSGIRGCLV RRCAGNVDLL
     NVLREFESKK EAEGDQILIK ASFLAELQRR ILRAEATVRE KDEENEMLHQ RLQQYENRWL
     EYEQKMKAME EMWQKQMRSL QSSLSVAKKS LALDETPRMS DSSVEQSWES NGNHVGGGSQ
     LVPRITGREM NASISVIGRL AEEFEQRSQV FADDAKFLVE VKSGQADASL NPDMELRRLK
     QNFDSWKKDF SSRIRETKVI LNKLASGGNE SSPNSAKRKW WGRLNTSKFS
//
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