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Database: UniProt
Entry: A0A1D6NKQ6_MAIZE
LinkDB: A0A1D6NKQ6_MAIZE
Original site: A0A1D6NKQ6_MAIZE 
ID   A0A1D6NKQ6_MAIZE        Unreviewed;      1019 AA.
AC   A0A1D6NKQ6;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Myosin1 {ECO:0000313|EMBL:ONM40814.1};
GN   ORFNames=ZEAMMB73_Zm00001d044303 {ECO:0000313|EMBL:ONM40814.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM40814.1};
RN   [1] {ECO:0000313|EMBL:ONM40814.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM40814.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; CM007649; ONM40814.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6NKQ6; -.
DR   OMA; CDCDNLE; -.
DR   ExpressionAtlas; A0A1D6NKQ6; baseline and differential.
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:InterPro.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
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   Gene3D; 1.20.5.190; -; 3.
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; 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; IPR037975; MyosinXI_CBD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF772; MYOSIN-5; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 5.
DR   Pfam; PF00063; Myosin_head; 1.
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.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, 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};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}.
FT   REGION          102..124
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          558..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          366..432
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          457..540
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        561..575
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1019 AA;  115938 MW;  3CCD8693EA03BE52 CRC64;
     MFPRSTHETF AQKLYTTFKN NKRFAKPKLS RTDFTVVHYA GDVTYQADYF LDKNKDYVVA
     EHQDLLNASS CLFVAGLFPP LPQETAKSSK FSSIGSRFKL QLQSLMETLS STEPHYIRCV
     KPNNLLKPAI FENTNVIQQL RCGGVLEAIR ISCAGYPTRK TFYEFVNRFG VLAPEVLEGS
     NDDKIACQKI LEKMGLENYQ IGKTKVFLRA GQMADLDARR AEVLGRAARI IQRQIRTYIA
     RKQFAELKRS ATQLQSFVRG TLARKLYECM RQEAAAVKIQ KNMRRHKARE SYLQLQAAAI
     TLQTGLRAMS ARKEFRFRKE TKAAVHIQAQ WRRHRDYSHY KNLQGAALTY QCAWRQRLAR
     RELRKLKMAA RETGALKEAK DKLEKRVEEL TWRLGLEKRL RTDLEEAKAQ EIAKLQETLH
     DMQLQVEESK AMVVKEREAA RKAIEEAPPV IKETPVLVED TEKINSLTTE VEQLKALLLT
     ERQATEAAKR EHAESELRNE ELIKKFESAE KKIEQLQETV HRLEEKATNM ESENKVLRQQ
     AVAISPTSKS LAAYPKSPFQ LKTPENGNAL NGEVKSSPDI TPILPNPKEL EAEEKPQKSL
     NEKQQENQDL LIKCVSQDLG FSSGKPIAAC LIYRCLLHWR SFEVERTGVF DRIIQTIGSA
     IESQDNNDKL AYWLSNSSTL LLLLQRTLKT TGAAGFTPQR RRSSAASFGR VFSGMRASPQ
     SAGRAFMGSR LIGGLGDLRQ VEAKYPALLF KQQLTAFLEK IYGMIRDNLK KEISPLLGLC
     IQAPRTSRAS LIKGSRSQAN ALAQQTLIAH WQSIVKILTN YLNVLKANYV PSVLISKVFT
     QIFSFINVQL FNSLLLRREC CSFSNGEYVK AGLAELEQWC IYATEEYAGS SWEELKHIRQ
     AVGFLVIHQK PKKTLKEITN DLCPVLSIQQ LYRISTMYWD DKYGTHTVSS DVISSMRVMM
     TEDSNNAVSS SFLLDDDSSI PFSVDDISKS MTEIEVTDVD MPPLIRENSG FTFLHQRKD
//
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