ID D8LTS1_ECTSI Unreviewed; 1949 AA.
AC D8LTS1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=Myosin D {ECO:0000313|EMBL:CBN73968.1};
GN ORFNames=Esi_0009_0126 {ECO:0000313|EMBL:CBN73968.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBN73968.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBN73968.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; FN649137; CBN73968.1; -; Genomic_DNA.
DR STRING; 2880.D8LTS1; -.
DR EnsemblProtists; CBN73968; CBN73968; Esi_0009_0126.
DR eggNOG; KOG0160; Eukaryota.
DR InParanoid; D8LTS1; -.
DR OMA; DQLADNE; -.
DR OrthoDB; 36097at2759; -.
DR Proteomes; UP000002630; Chromosome LG07.
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:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
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; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF845; MYOSIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Coiled coil {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|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630}.
FT DOMAIN 71..812
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 635..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..692
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1127..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1243..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1437..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1479..1519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1665..1774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1898..1949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 964..1024
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1049..1122
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1778..1886
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1129..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1370..1389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1497..1519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1708..1732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1934..1949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 184..191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1949 AA; 212575 MW; 9368213D7D5E05BF CRC64;
MEVGAAVWVK DKEGEEAWVA GTVLEKSAGK PCKVEIEVDE EFSEEPLTFT LREEDGYELE
DLKLANEEDM DHVEDLIALP HLHEAAILHS LCRRFDRGDI YTFTANAILL AVNPFKRLPL
YSKELLTEYF NMGYMRQQGI EPPQALGPHV FAIADSAYRD MMKGIHAGKS AGMGPVNQSI
LISGESGAGK TESTKFVMRY LTTVGNGEDG VELEKGSIMD RVLQSNPILE AFGNARTIRN
DNSSRFGKFI ELMFNKRGNL LGAGIETYLL EKVRIPTQAE NERNFHIFYQ MCKGGDDEER
ERWELQGPEE YHFVNQGDCY DLRKVEDEDE FVQTKAALTT MGFEASSIQT IFDIMAGLIH
LGELEFEANE EDEAAMLSDE EENQECMARV CRLCYLPEDG LLRALTSKTI EVGPRKEKTT
IKLKDHQAYD ARDALAKAFY GQLFNWLVAT INSHINCDRK EVKASVGVLD IFGFECFEHN
SFEQLCINYT NETLQQQFNQ FVFKMEQKEY SKEGIEWSFV EFPDNQDCLD LIEGKKKGLL
TMLDDECRMG IRGTDANYAS RLYKEHAETE RFESDSAMRT KLCFAVKHYA GQVEYHVETF
CDKNKDELPK ESDELFASST NDFVVNLFAP AGAKKAKTKG KKPAAPKPKK DASGVAGLKP
TVGTQFKDQL HNLMDMIKDT RPHYIRCIKP NDNAEPDEVS RVRVMEQLRY GGVLEAVRVA
RSGYPVRLPH KDFYTRYRCL ISLDPKVKKS KYPMRLQGTS TVAQKMCKDL VKNVLSPAMV
SMKNIPEDTM QFGKSKVFLR KNAHDFLEMI RSQRITSAAV TLQRVARGFV YRRVFFATKH
ALLLIQRMSR GMIARRKVEH MRRMRAALRT QTAYRRHFAR KNFLSIKGAA LALQCATRWR
KAAKVHIELR RQHRSTKIQS WYRMLAPWRA HRKLRSATLA LQCRMRQKIA YGELRDLRIK
AKDVGNLKGD NERLKAEILV LREAASNAAA AAGDERLTSA MKEADSLREE VEKLKAKVLN
TISLHLARTK SISDDSAASG AAAAAADETG SLRAKIAELE ATVEEEKQAA ATAVAASTNT
TTAAAAASPG NSAELESMRA SIADLETALA EEKEKSAAAA AAAAAANADA SSVSRSAPAA
ATESGGSSEE ASALRARVAE LEEEVERKKE EMANMPPPPA APAAPASTGS QGELEQRVAE
LEAELAEEKK AKAMALRATV AKLEKELAAE KSALKAAVAK AAGTAGGASK AEAEAERQAE
IEEEKESAFL RKQLGELEAA LSRERQERER AVLDRDRSEE LAKRMSKSLK NRGMSAAASA
GEDGEDGGSL KGTTNGSAVL GSENGDEDGD DLLVGMNNED MMISNLSQVL DEEREARRTA
EEENARLQTE ADAATDAQRA QAKAVQTLTL ELEDARKAQQ KAEQSAAQAA ASAAALVASS
DSGRPRVNLE GNALRTPTTA WRGAVHGFDN GGGGGAGGGF GGSGGGGGGG GGGGGGNSGS
HASSPGSTSN SVPGSSRSNQ LHTNAVLEFE ERLEAIKVGL SQGVDCWVWE DKTRQVEAIM
KVEEGEAGSS KLTFAAKGSY LIWRAPVRPM QMDSRLKVSL GHGDLHGLGS QDDSTYLTMR
CGGSSADEAR MVIVQVADKE MRNDLVSSVR RLLTQAKVGA MAAQMRGPDA GGSGGCGGGG
RPGINRRVSS VFELGGGSGG GRANPGISSP PRRQSTRPSL STAASFSVGS SGGPGFSPRI
PSGGGGGKSP AKAGSGVTSA TPPLHRKNQN QGEDPEMLDL LKNQLEQLAM AKEAELNAKE
VELQESRLTS ERTMVQMMEL TNEVNTKQDE IRMLKRQAME AVEDMEEMRR THKDNAHVSM
QLLKKMEGLQ FDNEELRHET EFLRNKVAMF YNEARMREDE GGHGGGEGFS REEMPPPSSV
SSSRDGGGPG MPASPSGSMS SFASCDATS
//
