ID M7B0L2_CHEMY Unreviewed; 733 AA.
AC M7B0L2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Myosin-7 {ECO:0000313|EMBL:EMP30584.1};
GN ORFNames=UY3_12290 {ECO:0000313|EMBL:EMP30584.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP30584.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; KB549018; EMP30584.1; -; Genomic_DNA.
DR AlphaFoldDB; M7B0L2; -.
DR STRING; 8469.M7B0L2; -.
DR Proteomes; UP000031443; 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; 1.20.58.530; -; 1.
DR Gene3D; 1.20.58.60; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
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; 2.
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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR Pfam; PF00063; Myosin_head; 3.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
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};
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:UP000031443}.
FT DOMAIN 32..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 85..733
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 713..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 733 AA; 82736 MW; D8706DFFE68C6EA2 CRC64;
MSDAEMAEFG TAAPYLRQSE KLRLEAQTRP FDLKKDIFVP DVKEEFVKAK LLSREGGKVT
AETEGGQTVT VKEDQIMQQN PPKFDKIEDM AMLTFLHEPA VLYNLKERYA AWMIYTYSGL
FCVTVNPYKW LPVYNAEVVG AYRGKKRSEA PPHIFSISDN AYQNMLTDRE NQSILITGES
GAGKTVNTKR VIQYFAVIAA ISDRSKKEQQ VDKSKGTLED QIIQANPALE AFGNAKTVRN
DNSSRFGKFI RIHFGATGKL ASADIETYLL EKSRVIFQLK SERSYHIYYQ ILSNKKPELL
DMMLVTNNPY DYAFISQGET TVTSIDDAEE LLATDSAFDI LGFTQEEKNS LYKLTGAIMH
FGNMKFKQKQ REEQAEPDGT EEADKSAYLM GLNSSDLLKG LVHPRVKVGN EYVTKGQTVQ
QGTLEDQIIQ ANPALEAFGN AKTVAYAVGA LAKSMYEKMF GWMVTRINNT LETKQPRQYF
IGVLDIAGFE IFDFNSFEQL CINFTNEKLQ QFFNHHMFVL EQEEYKKEGI EWPMGIMSIL
EEECMFPKAT DMTFKAKLYD NHLGKSGNFG KPRNIKGKPE AHFSLMHYAG TVDYNILGWL
QKNKDPLNET VVGLYQKSAL KLLALLFANY AGADSGVMDN PLVMHQLRCN GVLEGIRICR
KGFPNRILYG DFRQRYRILN PAAIPEGQFI DSRKGAEKLL GSLDIDSSQY KFGNTKARGR
RPRGGACGGQ GLS
//
