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Database: UniProt
Entry: V7C718_PHAVU
LinkDB: V7C718_PHAVU
Original site: V7C718_PHAVU 
ID   V7C718_PHAVU            Unreviewed;      1532 AA.
AC   V7C718;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESW25075.1};
GN   ORFNames=PHAVU_003G005200g {ECO:0000313|EMBL:ESW25075.1};
OS   Phaseolus vulgaris (Kidney bean) (French bean).
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; Phaseolus.
OX   NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW25075.1, ECO:0000313|Proteomes:UP000000226};
RN   [1] {ECO:0000313|Proteomes:UP000000226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX   PubMed=24908249; DOI=10.1038/ng.3008;
RA   Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA   Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA   Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA   Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA   Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA   Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA   Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT   "A reference genome for common bean and genome-wide analysis of dual
RT   domestications.";
RL   Nat. Genet. 46:707-713(2014).
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; CM002290; ESW25075.1; -; Genomic_DNA.
DR   RefSeq; XP_007153081.1; XM_007153019.1.
DR   EnsemblPlants; ESW25075; ESW25075; PHAVU_003G005200g.
DR   GeneID; 18633469; -.
DR   Gramene; ESW25075; ESW25075; PHAVU_003G005200g.
DR   KEGG; pvu:PHAVU_003G005200g; -.
DR   eggNOG; KOG0160; Eukaryota.
DR   OMA; SIMERHQ; -.
DR   OrthoDB; 942984at2759; -.
DR   Proteomes; UP000000226; Chromosome 3.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR   GO; GO:0030048; P:actin filament-based movement; IEA:UniProt.
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:SF751; MYOSIN HEAVY CHAIN; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 2.
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; 5.
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:UP000000226}.
FT   DOMAIN          27..76
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          81..753
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1193..1477
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          634..656
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   COILED          891..1127
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         175..182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1532 AA;  175063 MW;  798CFAB4A2A80D5E CRC64;
     MWEQSVSMST IDANINSNEI AGQLSYVAGS LVWVEDPESA WIDGEIQDSK KDDITIIFES
     GTRVVSKSAN MYPKDPEFPP NGVEDMTRLA YLHEPGVLQN LKVRYSENEI YTYTGNILIA
     VNPFQRLPHL SETSTMAKYK GAAFGEQSPH PFAIASSAYS KMINEERSQS ILVSGESGAG
     KTESTKMLMH YLAFLGGRAA TEGRSVEQQV LESNPVLEAF GNAKTVRNNN SSRFGKFVEI
     QFDQKGRISG AAIRTYLLER SRVCQVSDPE RNYHCFYMLC AAPKEDSGKY KLGDPRKFHY
     LNQSNCIELD GLDDSKEYLA TKRAMEVVGI SSDEQDAIFR IVAAVLHLGN IEFIKGAEEE
     LDSSQPKDEK SFYHLKIAAE LLMCDEKSLE DSFCKRVMVT RGDTITKSLD PNSAALSRDA
     LAKIVYSRLF DWIVCKINNT IGQDPESNKL IGVLDIYGFE SFKTNSFEQF CINLTNEKLQ
     QHFNQHVFKM EQEEYTKEEI DWSYIEFVDN QDVLDLIEKK PGGVIALLDE ACMFPRSTHE
     TFAEKLYQTF RDNKRFSKPK LSRTDFTINH YAGDVTYQTD FFLDKNKDYV VPEHAALLSA
     SKCPFVSGLF PPLPEETTKS TKFSSIATQF KLQLQSLLET LNATEPHYIR CVKPNNLLKP
     GIFENSNVLQ QLRCGGVMEA IRISCAGYPT RKNFDEFVQR FTILEPLVLK ACPDEMTACK
     RLLDRASLKD YQIGKTKVFL RAGQMAELDA CRAEVLGKSA SVIQRKVRTF LCRKRYVILQ
     LSAIELQRVA KGQLARHQFE CLRREAASMK IQKDFRMYIS RNAYKTTYAS AICIQTGMRG
     MAARNDLRFR RRTKAAIIIQ GRYRCHSAST YFRKLKKAAI FAQCSWRRTI ARRELRKLKM
     AAKEAKVLEE AKNNLEKQVK ELTSCLEEEK TMREAKTREN EKLQNALQEK ELQFQELKEV
     KEKETEKLQH DLKEMELQFE EIKEAKIQET EKLQCALKEM ELQFQETKEA LIQEQEAKEA
     LIQEHEAAMK VAEQTPSIQE NSVNDVDNEL VNKLTAENDQ LKGQVSSLEI KIDETERKYE
     ETNRISEDRM SQIIETESKM IEIKTNMQRL EEKVSDMETE NQVLRQQTLL SSSSRRMSGK
     FSPGAVPESV DILFKCVTKD LGFSEGKPVA AFTLYNCLLH WKSFEAEKTS IFDRLIQIIG
     SEIEDPDKND CMAYWLSNTS CLFFHLHRCL RVPTARKPPT PTSFFGRMAQ GFRSSNSLSS
     SAFDVVHQVD AKYPALLFKQ QLAAYVEKIY GIVRENFKTD LLPVLSSCIK ADRASDENSQ
     QAGSWLSIME CLNKYLKILK ENYVPTVLVQ KLFNQVFQYI NVELFNSILL HEECCTFKHG
     EYLKSGLAEL EQWCTEATEE YIGSSWDELK HASQAVRFLV AEKKDELSYD DLTNDICPVL
     SAQQLTRICT LYSDEDDDKK QSVSTDVTTR LKLLMTDDED EGSKTYSLED NTSHPIIVEE
     IPASSQDKNI PKVKPPDELL ENANFQFLHD YC
//
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