UniProt: A0A251TBT5

Database: UniProt
Entry: A0A251TBT5_HELAN

LinkDB:  A0A251TBT5_HELAN 
Original site:  A0A251TBT5_HELAN

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Ontology (11)   
   GO (11)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (18)   
   InterPro (7)   
   Pfam (4)   
   PROSITE (4)   
   SMART (3)   
Literature (1)   
   PubMed (1)   
All databases (33)   

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ID   A0A251TBT5_HELAN        Unreviewed;      1636 AA.
AC   A0A251TBT5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Myosin ATPase {ECO:0000313|EMBL:KAF5783043.1};
DE            EC=5.6.1.8 {ECO:0000313|EMBL:KAF5783043.1};
DE   SubName: Full=Putative myosin XI A {ECO:0000313|EMBL:OTG08528.1};
GN   Name=XIA {ECO:0000313|EMBL:OTG08528.1};
GN   ORFNames=HannXRQ_Chr11g0342761 {ECO:0000313|EMBL:OTG08528.1},
GN   HanXRQr2_Chr11g0503321 {ECO:0000313|EMBL:KAF5783043.1};
OS   Helianthus annuus (Common sunflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG08528.1, ECO:0000313|Proteomes:UP000215914};
RN   [1] {ECO:0000313|EMBL:KAF5783043.1, ECO:0000313|Proteomes:UP000215914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5783043.1};
RX   PubMed=28538728; DOI=10.1038/nature22380;
RA   Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA   Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA   Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA   Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA   Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA   Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA   Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA   Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA   Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA   Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA   Vincourt P., Rieseberg L.H., Langlade N.B.;
RT   "The sunflower genome provides insights into oil metabolism, flowering and
RT   Asterid evolution.";
RL   Nature 546:148-152(2017).
RN   [2] {ECO:0000313|EMBL:OTG08528.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaves {ECO:0000313|EMBL:OTG08528.1};
RA   Langlade N., Munos S.;
RT   "Sunflower complete genome.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAF5783043.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5783043.1};
RA   Gouzy J., Langlade N., Munos S.;
RT   "Helianthus annuus Genome sequencing and assembly Release 2.";
RL   Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. Plant myosin class XI subfamily.
CC       {ECO:0000256|ARBA:ARBA00008049}.
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DR   EMBL; MNCJ02000326; KAF5783043.1; -; Genomic_DNA.
DR   EMBL; CM007900; OTG08528.1; -; Genomic_DNA.
DR   EnsemblPlants; mRNA:HanXRQr2_Chr11g0503321; mRNA:HanXRQr2_Chr11g0503321; HanXRQr2_Chr11g0503321.
DR   Gramene; mRNA:HanXRQr2_Chr11g0503321; mRNA:HanXRQr2_Chr11g0503321; HanXRQr2_Chr11g0503321.
DR   InParanoid; A0A251TBT5; -.
DR   Proteomes; UP000215914; Chromosome 11.
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:0016853; F:isomerase activity; 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; cd01384; MYSc_Myo11; 1.
DR   Gene3D; 1.10.10.820; -; 1.
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; 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; IPR036018; MYSc_Myo11.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140:SF806; IQ MOTIF, EF-HAND BINDING SITE-RELATED; 1.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 4.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM01132; DIL; 1.
DR   SMART; SM00015; IQ; 5.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 6.
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   Isomerase {ECO:0000313|EMBL:KAF5783043.1};
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:UP000215914}.
FT   DOMAIN          8..57
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          62..731
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1304..1581
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          613..635
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1578..1597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          876..1234
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         156..163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1636 AA;  186421 MW;  0FEB188B14E2F791 CRC64;
     MSTSANIIVG SQVWVEDNEV SWIDGEVLEI NDKEIKVQCS SGKEVVAVLS SVYPKDPEFP
     EGGVDDMTKL AYLHEPGVLR NLKSRFDMDE IYTYTGNILI AVNPFKRIPN LYDKSVMEKY
     KGIALGELNP HPYAIADMAY RQMVNEGISQ SILVSGESGA GKTESTKNLM QYLAYMGGRH
     GADERSVEQQ VLESNPVLEA FGNAKTVRNN NSSRFGKFVE LQFNEIGKIS GAAIRTYLLE
     RSRVCQVSDP ERSYHCFYML CAAPPEVSEK YKLGDPRTFH YLNQSNCYQL TGVDESKEYL
     ETIHAMGVVG INSDEQEAIF RVVAAILHLG NIEFSRGSEP DSSQPKDDKS RFHLKTAAEL
     FMCDETALQE SFCQRVMVTR GESIKKSLDP NSAAISRDAM AKIVYSKLFD WIVTRINNSI
     GQDANSKLLI GVLDIYGFES FKTNSFEQFC INLTNEKLQQ HFNQHVFKME QEEYSKEEIN
     WSYIEFVDNQ DILDLIEKKP GGILALLDEA CMFPRSTHAT FADKLYQTFK DHKRFSKPKL
     SNTDFTICHY AGDVTYQSDF FLDKNKDYVV AEHQALMNAS KCFFVSSLFP PLAQDSSKAS
     KFISIGSQFK QQLQALLETL SHTEPHYVRC VKPNNLLKPA IFDNPNILQQ LRCGGVMEAI
     RISCAGFPTR KPFHEFIDRF KILSPNVLTM SDEIEASKIL LQKANLEGYQ IGKTKVFLRA
     GQMAEIDARR SEVLGRSAIK IQKRFRGYST CNKYTLLRSS AIVIQTICRG EVARVCYERR
     RKERACLRIQ KNARMHRERT RYKSMSSSVI FIQNGMRGMA ARNAYNYKRK TKAAIGIQSR
     CRRHLALRRY VKMRKVAVYA QSVLRKDLAR IELKRLKKIA SDTSALQDAK NKLEQEAKEL
     AMRLQEEERN RADMEEAKKK ETLKLQSTVK QMEVQLAEME EAKNNENAKL QSAIKELEVQ
     LADMEQAKNM EKEKLESALK EMEVQLANME EAKNEEKARL ESTIKGMEAE LADMEEAKKK
     ETAELQSAIT EMENKLADME ETKNKENAKL QSTIEEMEVQ FQEIKELLEA AKREMEQVRV
     ADNEKIETLT REMEQVRAAD NEKIETLTRE MEQVRADDNE KIETLTREME QVRAADNEKI
     ETLTREMEQL RAADNEKIET LTTDNEKLKD VVNSLESEIN ETQKKYEETS KLSEDRLKEA
     MDAEAKIIDL KLDMQCLQEK IADMEAEDQI LRQKEHQSGS PSNKFNSNLT QSTIGREREL
     VDNVMKAATE DLGFSQGKPV ATYVIYKSLL HCKAFEPDIT TVFDRIIQMM GSAIEKSEEI
     KHMAYWLSVT STLLFLIQRT LSPSPPKPEQ PTSLFGRMTK GFRSASIISI VCHVEVKYPA
     LLFKKQLAAY VEKLYGFIRN DLKKDMSQLL ASCIQAPITS DGKVFPVEFW DSIIERLDGL
     LDTLKECNVP LGIIQKIFSQ VFSFTDVQLF NSLLLHKECC TFANGEYVKA GLSKLEVWCS
     KVTAEYAGSS SDELNRVRQA IGFMVSKEKS KISYDEFTTK LCPVLSIQQL HRLCTFYSNN
     KDDTDSAAPD LISKLKGLMS EDSSDPDSDS YLVDDNTSSM AFPVEEIGKS INEKDFSNMK
     PSPELLEKPE FQFLLE
//

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