UniProt: A0A251V324

Database: UniProt
Entry: A0A251V324_HELAN

LinkDB:  A0A251V324_HELAN 
Original site:  A0A251V324_HELAN

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Ontology (11)   
   GO (11)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (19)   
   InterPro (8)   
   Pfam (4)   
   PROSITE (4)   
   SMART (3)   
Literature (1)   
   PubMed (1)   
All databases (34)   

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ID   A0A251V324_HELAN        Unreviewed;      1563 AA.
AC   A0A251V324;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Myosin ATPase {ECO:0000313|EMBL:KAF5811339.1};
DE            EC=5.6.1.8 {ECO:0000313|EMBL:KAF5811339.1};
DE   SubName: Full=Putative myosin-like protein XIF {ECO:0000313|EMBL:OTG29011.1};
GN   Name=XIF {ECO:0000313|EMBL:OTG29011.1};
GN   ORFNames=HannXRQ_Chr04g0117591 {ECO:0000313|EMBL:OTG29011.1},
GN   HanXRQr2_Chr04g0180291 {ECO:0000313|EMBL:KAF5811339.1};
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:OTG29011.1, ECO:0000313|Proteomes:UP000215914};
RN   [1] {ECO:0000313|EMBL:KAF5811339.1, 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:KAF5811339.1};
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:OTG29011.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaves {ECO:0000313|EMBL:OTG29011.1};
RA   Langlade N., Munos S.;
RT   "Sunflower complete genome.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAF5811339.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5811339.1};
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; MNCJ02000319; KAF5811339.1; -; Genomic_DNA.
DR   EMBL; CM007893; OTG29011.1; -; Genomic_DNA.
DR   STRING; 4232.A0A251V324; -.
DR   EnsemblPlants; mRNA:HanXRQr2_Chr04g0180291; mRNA:HanXRQr2_Chr04g0180291; HanXRQr2_Chr04g0180291.
DR   Gramene; mRNA:HanXRQr2_Chr04g0180291; mRNA:HanXRQr2_Chr04g0180291; HanXRQr2_Chr04g0180291.
DR   InParanoid; A0A251V324; -.
DR   OMA; QSSCYEV; -.
DR   OrthoDB; 5489458at2759; -.
DR   Proteomes; UP000215914; Chromosome 4.
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; cd15475; MyosinXI_CBD; 1.
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; IPR037975; MyosinXI_CBD.
DR   InterPro; IPR036018; MYSc_Myo11.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF270; MYOSIN-12; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 3.
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; 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; 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:KAF5811339.1};
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..730
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1193..1506
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          612..634
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   COILED          875..1088
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   1563 AA;  178440 MW;  EC1A5D5ACC7A04F3 CRC64;
     MGTPVNIIVG SHVWVEDPEL AWIDGEVIDI KGKDATIVTT NGKTIKADIS NIYPKDTEAP
     AAGVDDMTKL AYLHEPGVLY NLATRFGLNE IYTYTGNILI AVNPFRRLPH LYDVHMMQQY
     KGAAFGELSP HLFAIADDCY RAMINEHGSQ SILVSGESGA GKTETTKMLM RYLAFMGGRS
     GTEGRTVEQQ VLESNPVLEA FGNAKTVKNN NSSRFGKFVE IQFDKQGKIS GAAVRTYLLE
     RSRVCQVSDP ERNYHCFYML CAAPPEDVKR FKLGDPRTFH YLNQTNCYEV ANIDDGREYL
     ETRNAMDVVG INQDEQDAIF RVVAAILHLG NVDFIKGKEF DSSKVKDEKS LYHLRTAAEL
     LMCDAKALEQ SLCERVIVTP DGNITKPLDP AAAVLSRDAL AKTVYSRLFD WIVDKINNSI
     GQDPDAKSII GVLDIYGFES FKVNSFEQLC INLTNEKLQQ HFNQHVFKME QEEYTKEEIN
     WSYVEFVDNQ DVLDLIEKKP GGIIALLDEA CMFPKSTHET FAQKMYQTYK SHKRFSKPKL
     SRTNFTINHY AGDVTYQADQ FLDKNKDYVV AEFQALLNNS KCSFVANLFP PLEDSSKQSK
     FSSIGTRFKQ QLQSLMETLS TTEPHYIRCV KPNTVLKPGI FENDNVLNQL RCGGVLEAIR
     ISCAGYPTKR AFDEFLERFG MLAPDVLDGS DEKSACVAIC DRFGLKGYQI GKTKVFLRAG
     QMAELDTRRA EVLATAARRI QRQIRTYLTR KEFIILRKST INMQKNWRAR LARKLYDYLR
     KEAASIRIQK HTRGGAARTS YKLLQKSAIA IQTGLRAMAA RDEFRRRRRN KAATILQTEW
     RRYHACSEYK NKKKATLTLQ CLWRSKVARK ELRMLKMAAR DAGALREAKD KLEKRVEELT
     WRLDFEKHLR VDLEEAKGQE ITKLQNALQE MQEKLEEAHN QIIHEKEAAK IAIEQAPPVI
     KEVPVVDNTK VEELENHNHE LEDEIIELKK RVEEFEHKYN EVETESKNRF RELEESQAKI
     SGLQETIERL DANLSNMESE NQVLRQQALV ASTNEELSEE TELLKSKIKE LESENEILRN
     RKVVVEQITT PMSTPEKLLP QLQHLDNGHE TKDDFETPHV EQEKIKELDN GMLSPLTKQK
     SLTDRQQENH DVLIKCLLED KRFDKTRPVS ACIVYKTLVQ WRSFEAEKTH IFDRIIHTIR
     ASIEDNIKDL AYWLSTTSTL LFLLQSTIKA SGSPYKSPHR NRASPSTLFG RMTQGFRTSP
     VGMGISSGYS GMEGKPNTQS KIEAKYPALL FKQHLTACVE KLYGMIRDSL KKEISPFLNS
     CIQAPRSTRV RPTRGASRNI LSNIVAKQQA SMIHWQSIVN SLDNTLGILS ENYVPSIITR
     KIFSQVFSFI DVQFFNSLLL RRECCSFSNG EYVKSGLHEL EQWCKKATDQ FTGSSWDELQ
     HIRQAVALLV SHQKTQKSME EITNELCPAL SVPQIYRIGT MFWDDKYGTQ GLSKEVIGKM
     RALMAEDSVS MPNNSFLLDV DSSIPFSLEE ISQSFLDVDL SDIDPPPLLR QRSDFHFLLQ
     QID
//

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