ID E4YVS7_OIKDI Unreviewed; 1910 AA.
AC E4YVS7;
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_T00020134001 {ECO:0000313|EMBL:CBY39562.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY39562.1};
RN [1] {ECO:0000313|EMBL:CBY39562.1}
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; FN655573; CBY39562.1; -; Genomic_DNA.
DR Proteomes; UP000011014; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
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; -; 5.
DR Gene3D; 1.20.5.370; -; 5.
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; 2.30.30.360; Myosin S1 fragment, N-terminal; 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; IPR008989; Myosin_S1_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|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW 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}.
FT DOMAIN 32..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 86..761
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 637..659
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1110..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1863..1910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1880..1899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1910 AA; 219752 MW; 846B76FFE04DE18C CRC64;
MALWDPEAAG NAANYLRLPN LQLIDIRNAP FEAKTAVWVP YSETGYSKGY KMGEKDGKIE
VKRLADDKVK LYKPDDVEPQ NPPKYELLED MANLTYLSEA AVVHNLNTRY NIFLIYTYSG
LFCVTVNPYK WLPVYDNHVV LCYYNKRRTE MPPHVYSIAD NAYQDMLRAS ENQSMLITGE
SGAGKTVNTK RVIQYFAVVC ALGSEKDKKD QIVAANPAME AFGNAKTIRN DNSSRFGKFI
RIHFQVTGKL ASGDIDTYLL EKSRVTFQLK AERCFHIFYQ ILTGHKPQIN EMCMLSTDPY
DYKWCSLGEI KVKSIDDNEE LDATDESFDI LGFTEDEKAG IYKITASLMH SGNAAFKEKP
REEQAEPDGT EAAEKIAYLL GVNAQDWLKA VCTPKVKVGT EYVVKGQTVQ QVYYSIGAIV
KASFNRLFEW LVTVVNRALS TDLPRNNFIG ILDIAGFEIF EFNTFEQLCI NYTNERLQQF
FNHHMFILEQ EEYKREGIEW TFIDFGMDLQ ATIELIEKPL GIMSLLEEEC IVPKATDMTY
KDKLFQQHLG KTKSIGKVKK QGKFEAHFEI YHYAGTVAYN VIDWLLKNKD PLNNSLVQLF
KVSTLTTCKA IWESYVSAED APKGGGGKKG GKRQESLLRL MTNLHATQPH FVRCIIPNEQ
KKPGYMDNNL VLHQLRCNGV LEGIRICRKG FPSRVEYSDW KQRYAILNPN AVPKAGFIDP
KKACEKILAG ITSIDVQVYR FGHTKLFFKA GIIGALEDLR DDKIAEILTK LQTRMRFNLS
RAVFLKTLKE RDGAVVIQSN WRAYTTLKDW EWQKLLFKIR PLLNTAEKKA EFDELLKEYE
EMKKELEIES KRRKQLEQEY SKFIQLKNRL ISEFAGETDA LQDAEDRYES LMKSKIDLDG
KIKELHERLE DEEEINVDLS NKRRKLETEC KELRKDIDDL EGTLSKVEKE KSTVEADVRT
KTDELSALED TIAKLQKEKK ALQEAHQQAL DDLQAEEDKV NSLSKAKNKL EQQVDDLEQS
VETEKRSRLD LERLKRKLEG DLRLAQETIM DLENDKQRLE EKLKKAEFEY NQLSTRFEDE
QALVAQLQKK IKELMARIEE LEEELEAERA AKAKSEKSRS DLSRELEELS ERLEEANAQT
QGQIEVNKRR EAELAKLQRD LEEHNIAHES TLSAMRKKHA DTSSELTETI DNLSRVKTKL
DKEKSELKME ADDLISNVES LTKSKISYEK SCRHLEDQYA ELKMKHEEQE KAISDSAATK
ARLTTEMNEL RRTFEEKEQI NSQLSRQKNS VSQANDELRR SLDEEVKGKN ALVHQVQAAK
HDHELLREAY DEEVEAKNEL QRQLSKSNSE SSQWRTKYET DAVQRTEELE DAKKKLSGRL
SEAEESVEAA LAKCSSLEKS KGRLQSEIED LTVELERANA AAGALEKKQR SFDKILEENK
IKQEEINAEL EKAQKDSREA SNEVFKMRNA YEEAVDCLES AKRENKQVQE EIADLTDQVA
EGAKSISELE KAKRNIEVER NELAASLEET EAAVESEEAK TLRITVELQQ IKSESDRRLQ
EKDEEMDNNR RNASRTVETI QSQLDTEIRS RSEAVRIKKK LEGDISDIEI QLAHANRQLN
DAQRQNKDIM GQIKDAQMAL DESERIYDEV KEQTAVTDRR VNLLQAEIDE LRSAVEQAEK
GRKAAEQELM EANERANLLH TQNTALANQK RKLEQELLAV ANEVEEAIQE AKNAEDKAKK
SILDASIMAE DLKKEQDASS HLERMKKNQE IQLKELQARL DDAEQVALKG GKKHVQKLEG
RLRELESELD NERRRGVDSQ KAVRKMERKV KETVYAGEED KKNLGRLQDQ ADKLQLKVKQ
FKRMAEEQEE ASTQNMSRYR KVQHELDEAE ERADMAESTL SKMRSKSSAF
//
