ID D7G6I0_ECTSI Unreviewed; 1867 AA.
AC D7G6I0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CBJ27565.1};
GN ORFNames=Esi_0075_0035 {ECO:0000313|EMBL:CBJ27565.1};
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:CBJ27565.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ27565.1, 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; FN648981; CBJ27565.1; -; Genomic_DNA.
DR STRING; 2880.D7G6I0; -.
DR EnsemblProtists; CBJ27565; CBJ27565; Esi_0075_0035.
DR eggNOG; KOG0160; Eukaryota.
DR InParanoid; D7G6I0; -.
DR OMA; GKCQSIL; -.
DR OrthoDB; 46994at2759; -.
DR Proteomes; UP000002630; Chromosome LG03.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 CDD; cd14892; MYSc_Myo31; 1.
DR CDD; cd00821; PH; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 2.60.40.150; C2 domain; 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 Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR025939; Aida_C.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR035892; C2_domain_sf.
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 InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF845; MYOSIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51911; C2_AIDA; 1.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW 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 121..959
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1384..1483
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REPEAT 1576..1608
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1751..1867
FT /note="C2 Aida-type"
FT /evidence="ECO:0000259|PROSITE:PS51911"
FT REGION 179..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..853
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1225..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1745..1765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 982..1014
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 192..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 257..264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1867 AA; 206228 MW; AB26CD1676EAD6B8 CRC64;
MGDKFRCYAG NGIDSGGKSG RPSTLSVGLG SGARGGLVIA TDSGDGMDDG TKYRDLVWVP
DGEKVWRAAK KVAGKECSSP SRKRSLTASA GDTVWVHTPT QDTSVEVPKD QTHAYDPSHA
LDLDDASKMN QMHEAPLLDL LLRRFRKDAI YTSVADVLIS INPYKNIPLL YEVPLHQMQD
EPEDEFEESD GEREAPREGR GRNGRAKDAR PKALSDKLGQ PHVFSVADRA FRYMKSPGAE
YTHGKRRGMN QSIIISGESG AGKTEASKHV MRYLITASQL ANGVSQDAAG HESSDGVEAM
AKRIEATLLR SSTLLEAFGN AKTLRNDNSS RFGKYIKLLY DRDSRLMGAS TDHFLLEKSR
LVKVDSGERG YHIFYQMLAG LDEAKAEALS LAPAEEFHMI SQGDCVAISD EVDDRQARHV
NTEFVQTEDA METLGFEAED KAAVFRVLAA LLHLGNVRFE ETESPAQGGA KAKICRADSS
LSSSNDSSSG EGAGLAKAAA LLGLDEDILT RKVMWRAIMA PGKSLHEIAL TARESSDNLS
ALSKHTYGKL FTWIVAFINR CHQQHVRGVT LDKGAAELAG IGDDEDKRSS FIGILDIFGF
EIMATNSFEQ LCINFANEVL QRQFNHHIFV LEQEEYKAEG LDVAAIPFKN NQDIIDLICK
KPLGLMIILE DQVLTGRKAH AMNKLDDRSV LDLYHQEHHR RNPHPNYEKP RMQCDLFTLK
HFAGNVTYDV AGFLEKNNDS LQDDLRALLL DSEDDFVREL ADITPTVPDG QQHLTPQNSP
ARVGVAFRGA DSPPSPPPRG GLGGRYESEG QGGRSPVSDR RQSRRESERQ LDSLVMQLGQ
TEPHYIKCIK PNSAKAPGGW SSPLVIDQLR YSGVLEVVRI RREAYPLRLD YVEMYRNFRV
LAEWKAGGTL SPETCSEEEA RVMCREICSF ALEPDDFQLG RTRVFLKDNA LDKLRWALQA
KYVSAACSIQ AAARSFLARN RLRNALRERA ELRAREAERQ AEETRQRRAS AQVQIAKVAR
GLTQRKRLER QTAGSTVLQA CWRGYNTRKT LESSRAARRT LEGRRATELQ AWARMLLAGQ
ARTRARRAST TLASAWRMRS AVVYKKQTVD NVTTLQAWAR MLLAGQARTR ARRASTTLAS
AWRMRSAVVY KKQTVDNVTT LQGLVRGMLA RRRYAIARGR VVRIQALLRG FTKRSIFLKQ
VAKIITEFPQ LLYVRDRYGS SGVDEMFPHG GGDGDSRDED DTEAGDSNMS ASIKPSRCFS
TLLHAACESG VMDVIALLEA FPEDVTAVDT KGNSSVHVAS SAVDYKLVKY LAKRNNMDVE
KALVEEKDRS EHAERLTRRQ VGTSVNVFRA ARLERARWAA EANAGGSRGV RAANSGPTSL
KAKHCLMSGY LRKRRETDRW LKRWCVLTET SLMYFHKPTD ESPSKIIKLD KAMLKKSEKV
DFAFEIHTPD LLDKRNKEGR LHFSCAGEGE LQQWLVPLRV VVALYQFRND KRREPLVYVD
VERRAQLACL PNNKGETPLH ALAGASLVDF AGTGRRPTGG RQGLPTLSGR TSVVSMQRLA
AWLIESGADP NEPDNSGQTA LHVAMECDNP AVVSTLARKG GDVNLKRPCD GRSVITQVLE
QGQGMDLIEQ VSSAGVTTNN PLLPPPEKLF GFTYVSFFIE KTTFPASKHN AVMDLTTPTP
NVGAFSAMTG TFNFDAPRSV GGRAGGTGVR DTLNKPGYAK STMARWGTRI GHVVGAGGGV
GRGMGEAGVG GPGGEDGPDG AHGPPPPLGT MTIDRVVEQL FFVRVSVYNA KGKLSEAQQD
VTVPIMTNPE YLWWAHTWHM QTPLETLGAG SFVAFELKEK VGMGTRWVKM IARPRLATSK
PEHKTTE
//
