ID Q5NTX1_ADICA Unreviewed; 1539 AA.
AC Q5NTX1;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Myosin class 11-1 {ECO:0000313|EMBL:BAD80748.1};
GN Name=myo11-1 {ECO:0000313|EMBL:BAD80748.1};
OS Adiantum capillus-veneris (Maidenhair fern).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC Vittarioideae; Adiantum.
OX NCBI_TaxID=13818 {ECO:0000313|EMBL:BAD80748.1};
RN [1] {ECO:0000313|EMBL:BAD80748.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15574841; DOI=10.1093/pcp/pch186;
RA Kawai-Toyooka H., Kuramoto C., Orui K., Motoyama K., Kikuchi K.,
RA Kanegae T., Wada M.;
RT "DNA interference: a simple and efficient gene-silencing system for high-
RT throughput functional analysis in the fern adiantum.";
RL Plant Cell Physiol. 45:1648-1657(2004).
RN [2] {ECO:0000313|EMBL:BAD80748.1}
RP NUCLEOTIDE SEQUENCE.
RA Takahashi F., Kasahara M., Imai T., Wada M.;
RL Submitted (JUL-2004) 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; AB185287; BAD80748.1; -; mRNA.
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; 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; 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:SF792; MYOSIN-9; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 5.
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; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 2: Evidence at transcript level;
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}.
FT DOMAIN 8..57
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 62..732
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1168..1482
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 1078..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 891..943
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 971..1054
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1078..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 156..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1539 AA; 173795 MW; 7EB1173D4F3CC814 CRC64;
MATEKNITVG SQVWVEDNAL AWVDAEVLEI KGQEVKAQTT SGKLVTTKLS NVHPKDPDAQ
PGGVDDMTKL AYLHEPGVLN NLATRYELND IYTYTGNILI AVNPFAKLPH LYDVHMMEQY
RGAMFGELSP HVFAIADTAY RAMINESKSQ SILVSGESGA GKTETTKLLM QYIAFMGGRA
MTDGRTVEQQ VLESNPLLEA FGNAKTVRND NSSRFGKFVE LQFDGSGRIS GAAVRTYLLE
RSRVVQISDP ERNYHCFYQL CASAEGAERY KLGDPRSFHY LNQSSCYELD HTNSGREYAK
TRRAMDIVGI SLDEQEAIFR VVASILHLGN IDFIQGKEAD SSVLKDEKSK FHLQVAAELL
MCDKQSLLES LSTRIIVTRD ENITKTLDPV SATTNRDTLA KTVYSRLFDW LVDKVNKSIG
QDPDSKTLIG VLDIYGFESF KTNSFEQFCI NLTNEKLQQH FNQHVFKMEQ EEYTKEEINW
SYIEFVDNQD VLDMIEKKPL GIIALLDEAC MFPKATHETF ATKLFQTFKN HKRFIKPKLS
RTDFIISHYA GEVTYQADLF LDKNKDYVVA EHQALLGSSR CPFVASLFPP SPEEPSKSSY
KFSSIGTRFK QQLQALMETL NSTEPHYIRC VKPNPYNKPG RFENSNVLQQ LRCGGVLEAV
RISCAGYPTR RTFDEFVDRF GLLAPELHDE SFDEKAATEQ ILKKVKLSNY QIGKTKVFLR
AGQMAELDSR RAEMLGSAAK VIQRRVRTFL AQRELKALRK AAICVQARWR GKMARKQYER
VEEGSCSHSN SETRSWMASS KILQEGAAAA IVIQAAFRGM KARKEFRFRK ETRAAIKIQT
TWRGYKARSD YKKLRKATLT IQCIWRGRAA RKELKKLKMA AKETGALQEA KTKLEKRCEE
LTLRLQLEKR LRTDLEEAKL QEVSKLQNTI NDMQTQLESA NSLIAKERVL SKQAADQAAT
TIKETQVMQV NEVSNAKLEK LEAENASFKE LMSSLEKRAA EAEEKFLAAK KESDEKIKRA
IESESRIEQL QEAMQRLEEK LSNLESENQV LRQQALNISP AKGLSNRFKS TVLQRSPENG
LLSNGEVKTT PESPVSVPSP EGKEQSEAEQ RRQKVLTADR QQENLDALLK CVTQDVGFSR
DRPVAACIIY KSLLQWRSFE AERTNVFDQI IQTIGTAIES QENNDILSYW LTNTSMLLFL
LQRTLKASGA GGLSQQRRRT SSVTLFGRMT QGFRSSPASG GLSFGNGGVI GGLDSLRQVE
AKYPALLFKQ QLTAYVEKIY GMIRDNLKKE ITPLLGLCIQ APRTSRATLG KAASRSVHAS
STAQQILSSH WHSIIKSLSN LLSTMRANHV SAFFVRKVFT QIFSYINVQL FNSLLLRREC
CSFSNGEYVK AGLAELEHWV YEASEEYAGS AWDELKHIRQ AVGFLVIHQK PKKSLDEITH
DLCPVLSIQQ LYRISTMYWD DKYGTHSLSP EVIANMRVLM TEDSNNAVSN SFLLDDDSSI
PFSVDDISKS MPEADLSDID PPPVLRENPG FFFLQPQAS
//
