ID I1LF91_SOYBN Unreviewed; 1176 AA.
AC I1LF91;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=100801124 {ECO:0000313|EnsemblPlants:KRH36145};
GN ORFNames=GLYMA_10G286300 {ECO:0000313|EMBL:KRH36145.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH36145.1};
RN [1] {ECO:0000313|EMBL:KRH36145.1, ECO:0000313|EnsemblPlants:KRH36145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH36145};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH36145.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH36145}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH36145};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH36145.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH36145.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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}.
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DR EMBL; CM000843; KRH36145.1; -; Genomic_DNA.
DR RefSeq; XP_003536741.2; XM_003536693.3.
DR AlphaFoldDB; I1LF91; -.
DR SMR; I1LF91; -.
DR STRING; 3847.I1LF91; -.
DR PaxDb; 3847-GLYMA10G43230-1; -.
DR EnsemblPlants; KRH36145; KRH36145; GLYMA_10G286300.
DR GeneID; 100801124; -.
DR Gramene; KRH36145; KRH36145; GLYMA_10G286300.
DR KEGG; gmx:100801124; -.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_7_2_1; -.
DR InParanoid; I1LF91; -.
DR OMA; PHFITHA; -.
DR OrthoDB; 5489458at2759; -.
DR Proteomes; UP000008827; Chromosome 10.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; 1.
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:UP000008827}.
FT DOMAIN 126..175
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 179..851
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 66..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..753
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1038..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 971..1019
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 78..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 270..277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1176 AA; 133002 MW; E3CA93F5F0C4B676 CRC64;
MSQTSTVLPA FHSIKSLPPE YKFANNPNPV LVEKHGDVKF RRNNPIGSNG LENGAQVGEV
SEEVNGRAGG MDLSDEDSPY GAKGRSLKDR PSNADEDSVS VSLPPLPLLT SSRESRWNDT
NPYGSKKKLQ SWLQLPNGDW ELVKIITTSG DESVISLPNG KVFKVKEESL VPANPDILDG
VDDLMQLSYL NEPSVLFNLQ YRYNHNMIYT KAGPVLVAVN PFKKVPLYGN DYIEAYKCKS
IESPHVYAIT DTAIREMIRD EVNQSIIISG ESGAGKTETA KIAMQYLAAL GGGSGIENEI
LKTNPILEAF GNGKTLRNDN SSRFGKLIEI HFSETGKISG ANIQTFLLEK SRVVQCNEGE
RSYHIFYQLC AGAPSSLREK LNLLSAEDYK YLRQSNCYSI TGVDDAEEFR IVKEALDVVH
ISKGDQENVF AMLAAVLWLG NISFTVVDNE NHVQAVEDEG LLTVAKLIGC EIEDLKLTLS
TRKMKVGNDI IVQKLTLSQA IDARDALAKS IYACLFDWLV EQINKSLAVG KRRTGRSISI
LDIYGFESFN RNSFEQFCIN YANERLQQHF NRHLFKLEQE EYIQDGIDWA KVEFEDNQDC
LNLFEKKPLG LLSLLDEEST FPNGTDLTFA NKLKQHLNSN SCFKGEREKA FTVRHYAGEV
TYDTSGFLEK NRDLLHLDSI QLLSSSICHL PKLFASHMLT QSEKPVVGPL HKSGGADSQK
LSVATKFKGQ LFQLMQRLES TTPHFIRCIK PNNLQSPGSY EQSLVLQQLR CCGVLEVVRI
SRSGFPTRVS HQKFARRYGF LLLENVASQD PLSVSVAILH QFNILPEMYQ VGYTKLFFRT
GQIGVLEDTR NRTLHGVLRV QSCFRGYRAR CYRKELWRGI TTLQSFIRGE KSRKEYAASL
QRHRAAVIIQ KRMKTVFSRN RMKNINDAAV VIQSFIRGWL VRRCSGDIGL SKSQGIKTNE
SDEVLVKASF LAELQRRVLK AEAALREKEE ENDILHQRLQ QYENRWSEYE LKMKSMEEVW
QKQMRSLQSS LSIAKKSLAM DDSERNSDAS VNASDDRDFS WDVGTNHRRQ ESNGAKSMSA
GLSVISRLAE EFEQRSQVFG DDSKFLVEVK SGQVEASLNP DRELRRLKQM FEAWKKDYGA
RLRETKVILH KLGSEDGSIE KVKKSWWGRR NSTRIS
//
