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Database: UniProt
Entry: E4XU70_OIKDI
LinkDB: E4XU70_OIKDI
Original site: E4XU70_OIKDI 
ID   E4XU70_OIKDI            Unreviewed;      1941 AA.
AC   E4XU70;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GSOID_T00004047001 {ECO:0000313|EMBL:CBY13267.1};
OS   Oikopleura dioica (Tunicate).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC   Oikopleuridae; Oikopleura.
OX   NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY13267.1};
RN   [1] {ECO:0000313|EMBL:CBY13267.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21097902; DOI=10.1126/science.1194167;
RA   Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA   Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA   Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA   Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA   Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA   Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA   Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA   Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA   Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA   Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA   Roest Crollius H., Wincker P., Chourrout D.;
RT   "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT   pelagic tunicate.";
RL   Science 330:1381-1385(2010).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC       ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; FN653173; CBY13267.1; -; Genomic_DNA.
DR   InParanoid; E4XU70; -.
DR   Proteomes; UP000001307; Unassembled WGS sequence.
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; cd01377; MYSc_class_II; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 4.
DR   Gene3D; 1.20.5.370; -; 3.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 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; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014751; XRCC4-like_C.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF67; MYOSIN-6; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 5.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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:UP000001307}.
FT   DOMAIN          32..83
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          87..791
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          663..685
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1124..1182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1191..1210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1867..1915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1124..1164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1875..1896
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         180..187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1941 AA;  223677 MW;  AE072848C5E77186 CRC64;
     MSLWDADAAG NAAQWLRLPQ ETMLEIQNRP YTGRNAVWVP NSSTQYCKGE LVGDGKKPGH
     KLIKREDGKE KEYHEDHIEF QNPPKYELLE DLANLTYLSE ASVVYNLSER YRRFMIYTYS
     GLFCITVNPY KWLTVYDNHV VGIYKGKRKS EMPPHIFAIS DNAYNDMLRE RHNQSMLITG
     ESGAGKTVNT KRVIQYFAVV AALGQSAKGN DDGGGTLEDQ IVAANPAMEA FGNAKTTRND
     NSSRFGKFIR IHFGMTGKLA SGDIDTYLLE KSRVVFQLPS ERGFHVFYQI CSGGRPDLNE
     MTLTTTDPYD FHFCSMGEIK VKSINDVEEL EATDGSFDIL GFEPAEKSGI WQVTAGLMHS
     GNMKFKNKQR EEQAEADGTE ASEKAGFMFG ISGADFVKAL CYPRVKVGAD FVTKGQTCPQ
     VSYGLGAICK SVFERLFNWI VTTVNRALST DAPRNFFIGI LDIAGFEIFD FNTFEQLCIN
     YTNEKLQQFF NHHMFVLEQE EYRKEGIEWS MMDFGMDLAA TLELIERPLG IMSILEEECM
     FPKATDMTFK EKLFQTHMGK NDKFGKVVKT KPKDKSIDEP HFEIHHYAGT VGYNVTDWLQ
     KNKDPLNTTV VDLFKKSSSK IMQSLWADFA SADETAKKSS GKGGKRQKGG SFQTVSALHR
     ESLNRLMTNL RSTQPHFVRC IVPNEIKKPG EMDWNLVLHQ LRCNGVLEGI RICRKGFPSR
     VQYDEFTQRY LILAPSVEKG SGEFSDPKKA AQNVLASLAE SGAMDQDKYR LGHTKLFFRA
     GAIGDLEDLR DEKISSILTS LQCFFRYKLA AIKFNELNKR RNAIERIQTN IRCFQYLKDW
     EWMKIMFKIK PLISQAEEGK KLQELEKNYA ECKTALEKET KRRKELEEAQ VSLVQEKNEL
     EQKMNGQLTL LEDAETRCEE LIEQKIDLDA KCRDMQEKLE DEEELNNDLV AKKRKLEDEC
     SELKKDIDDL ELTLAKIEKE KHATENKVKN VTEELGSVDE AIVKLEKEKK ALQEAQKQTL
     ADLQNEEEKV GTLQKTKGKL ETQVDDLEIT LEAEKKNRMD LERAKRKLEG DIRLTQENVM
     DLENDKAGEE EKLKKSEFDF SQMNAKLEDE QALCSQLNKK IKELQSRTEE VEEELESERA
     SRGRSEKTRT DLSRELEELA ERLEESASNT QTEVEASKRR DAEMAKIRRE LEETTLNHES
     TLSNTRKKQS DQICALSGSV DQFSRQKQKL EKEKSEMKME VDDLQQNVEQ LTKSKLNYEK
     QNRNTEDQII EYKQKLEEAD STLNTLMTNK SKNANEINEL RRLIEEKEAS FNQVQRARNS
     LTQTNEEIKR QLEEETKFKN AYSHQLQQTK HDIDMLREHY EEEQEGKQEV QRNLAKGQGE
     VVFWRNKYET DAIQRTEELE EAKKKLVNRL QDAEEQMEAA QGRCGSLDKT KTRLQGEVED
     LSSDLERSNA AAVQLDKKQR NFDKLLAETK QKQEELQVEL EVSQKDARHQ QSELFTLKNA
     VEESNDQLES INRENRNLAE EVLECQESLA EGAKTIHDLE KSKRELETLR SEIQSTLEES
     ESAIEAEEAK SMRVQVELQQ IKQEIDRKLA EKDEELDNNR RNHTRALEQI QASLDNEMRA
     RGEAVRSRKK MESDLNDLEV QCRHIRKQAD DAIKTGKELL NSHKELNINL DEHQRESEDI
     KEQSQVAERR VNLMSGEIEE LRGGLEQAER QRKQAENDLM EANERANMLH TQNTAFINQK
     RKIENELGTV RNEVEEAITE ARSAEEAAKK ALTTAALLAE DLKKEQDTSH HMERMKKNHE
     NSVKDLQMRL DEAEQVALKG GKKQVQKLET KIREIEGELE SEHRRNAEHT KVVRKLERKI
     KESNYTNTES KKNLTRVTDQ TDKLQSKVRN FKKQSEEATE SAQMSASRYR KLQHELDEAQ
     ERAELAEAAV AKARNRQREQ I
//
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