ID A0A1S4DIN4_TOBAC Unreviewed; 1157 AA.
AC A0A1S4DIN4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Myosin-2-like isoform X1 {ECO:0000313|RefSeq:XP_016513144.1};
GN Name=LOC107830177 {ECO:0000313|RefSeq:XP_016513144.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016513144.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016513144.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_016513144.1; XM_016657658.1.
DR AlphaFoldDB; A0A1S4DIN4; -.
DR SMR; A0A1S4DIN4; -.
DR STRING; 4097.A0A1S4DIN4; -.
DR PaxDb; 4097-A0A1S4DIN4; -.
DR GeneID; 107830177; -.
DR KEGG; nta:107830177; -.
DR OrthoDB; 5489458at2759; -.
DR Proteomes; UP000084051; Unplaced.
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; -; 1.
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:SF706; MYOSIN-11; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 3.
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:UP000084051}.
FT DOMAIN 106..155
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 159..830
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..732
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1013..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 946..980
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 16..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 250..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1157 AA; 130916 MW; B13209FF07104BC5 CRC64;
MLSVSPNSMA RSSLEEMLET LRKRDENEKP KDLPPALPAR PKLKSKTRPP SPKRMLPNSL
GIKGDVELEK NSSKKLQESK GLQRNANFGA YKKVKGMEPN INYFINKKLR IWCCLRNGQW
VSGQVQSSSG DKATVLLSDR SVVTVPVGEL LPANPDVLEG VDDLMQLSYL NEPSVLHNLQ
HRYARDTIYS TAGPVLIAIN PFKDIQLYGD EFVTAYRQKF LNDPHVYSIA DTAYDRMMED
EISQSIIISG ESGSGKTETA KIAMEYLAMI GGGRNAIERE VLQTSYILEA FGNAKTSKNN
NSSRFGKLIE IHFSATGRIC SAKIQTLLLE KSRVVQLVNG ERSYHIFYQL CAGAPPTLRD
KLKLKGASEY KYLNQSDCLV IHDIDDAEEF RKLMEALNTF RISERDQEHV FQMIASVLWL
GNITFEVIDN ASHVEVVQNE AVTNAASLIG CRVNDLMLAL STRQIQVGKD KVAKSLTMEQ
ATDRRDTLAK FIYANLFDWI VDQMNRKLAM GKEQKGRSIN ILDIYGFESF KRNSFEQFCI
NYANERLRQH VNRHLLKLEQ EEYELDGIDW TKVDFEDNQE CLDLFEKKPI GLISLLNEES
NSLKATDLTF ASKLQQQIKS DPCFKGERGE FHIRHYAGEV TYDATGFLEK NRDALHSDII
QLLSSSNGQL PQLFASVSAN EDTEFSSPST YTGVPDFQKQ SVATKFKDHL FKLMQQLENT
TPHFICCIKP NNKQVPGMCD KDLIIQQLRS CGVLEVVRIS RSGYPTRLTH QEFTSRYGFL
LVKDNACQDP LSMSVSILQQ FDILPELYQV GYTKLYFRAG QIAALEDVRN QVLQGTLEVQ
KCFRGHRARC YFHELKGGVI TLQSFIRGEI ARNRYNTSVG SKAKVAHKSD EQLVAVVQIQ
SAIRGWLARK DLNKLQSAKT LNVDIPKTGR KMEAKELPRE ILPSVVEDLE RRLLKAEATL
GEKEMENVAL KEQLNLFEAR CLEYEVKMRS MEEMWQKQMA SLQQASLAAA KNSLGAGDTT
GRPGKPEGSP SPRYYDSDDA TSMDTPAGCT PVKFTNSLGV GANREVNGGL AIVSHLTLEF
EQRKQNFDDE ALAIVHLKPG QLHSTNPADE YRRLKCRFEE WKKDYKVRLK ETKAKVHKLG
CSKAGKNRRK WWGKKSK
//
