ID O44934_DORPE Unreviewed; 1935 AA.
AC O44934;
DT 01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1998, sequence version 2.
DT 27-MAR-2024, entry version 137.
DE SubName: Full=Myosin heavy chain isoform A {ECO:0000313|EMBL:AAC24207.1};
OS Doryteuthis pealeii (Longfin inshore squid) (Loligo pealeii).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Myopsida; Loliginidae; Doryteuthis.
OX NCBI_TaxID=1051067 {ECO:0000313|EMBL:AAC24207.1};
RN [1] {ECO:0000313|EMBL:AAC24207.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Ventral siphon muscle {ECO:0000313|EMBL:AAC24207.1};
RX PubMed=9742454; DOI=10.1023/A:1005341416989;
RA Matulef K., Sirokman K., Perreault-Micale C.L., Szent-Gyorgyi A.G.;
RT "Amino-acid sequence of squid myosin heavy chain.";
RL J. Muscle Res. Cell Motil. 19:705-712(1998).
RN [2] {ECO:0007829|PDB:3I5F, ECO:0007829|PDB:3I5G}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-839 IN COMPLEX WITH ADP AND
RP MG(2+).
RX PubMed=17502101; DOI=10.1016/j.str.2007.03.010;
RA Yang Y., Gourinath S., Kovacs M., Nyitray L., Reutzel R., Himmel D.M.,
RA O'Neall-Hennessey E., Reshetnikova L., Szent-Gyorgyi A.G., Brown J.H.,
RA Cohen C.;
RT "Rigor-like structures from muscle myosins reveal key mechanical elements
RT in the transduction pathways of this allosteric motor.";
RL Structure 15:553-564(2007).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril
CC {ECO:0000256|ARBA:ARBA00004657}.
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; AF042349; AAC24207.1; -; mRNA.
DR PDB; 3I5F; X-ray; 3.10 A; A=1-839.
DR PDB; 3I5G; X-ray; 2.60 A; A=1-839.
DR PDB; 3I5H; X-ray; 3.40 A; A=1-839.
DR PDB; 3I5I; X-ray; 3.30 A; A=1-839.
DR PDBsum; 3I5F; -.
DR PDBsum; 3I5G; -.
DR PDBsum; 3I5H; -.
DR PDBsum; 3I5I; -.
DR SMR; O44934; -.
DR EvolutionaryTrace; O44934; -.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
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; -; 6.
DR Gene3D; 1.20.5.370; -; 4.
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; IPR000048; IQ_motif_EF-hand-BS.
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:SF40; MYOSIN HEAVY CHAIN, MUSCLE-RELATED; 1.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 7.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3I5F, ECO:0007829|PDB:3I5G};
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 Metal-binding {ECO:0007829|PDB:3I5F};
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 29..79
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 83..777
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 655..677
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1226..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1901..1935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1901..1917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1918..1935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3I5F"
FT BINDING 132
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3I5F"
FT BINDING 176..183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT BINDING 179
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3I5F"
FT BINDING 180
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3I5F"
FT BINDING 181
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3I5F"
FT BINDING 182
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3I5F"
FT BINDING 183
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3I5F"
FT BINDING 184
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3I5F"
FT BINDING 242
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0007829|PDB:3I5F"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:3I5F"
SQ SEQUENCE 1935 AA; 221531 MW; 7C4245EA440DB124 CRC64;
MTMDFSDPDM EFLCLTRQKL MEATSIPFDG KKNCWVPDPD FGFVGAEIQS TKGDEVTVKT
DKTQETRVVK KDDIGQRNPP KFEMNMDMAN LTFLNEASIL HNLRSRYESG FIYTYSGLFC
IAINPYRRLP IYTQGLVDKY RGKRRAEMPP HLFSIADNAY QYMLQDRENQ SMLITGESGA
GKTENTKKVI QYFALVAASL AGKKDKKEEE KKKDEKKGTL EDQIVQCNPV LEAYGNAETT
RNNNSSRFGK FIRIHFGTQG KIAGADIETY LLEKSRVTYQ QSAERNYHIF YQLLSPAFPE
NIEKILAVPD PGLYGFINQG TLTVDGIDDE EEMGLTDTAF DVLGFTDEEK LSMYKCTGCI
LHLGEMKWKQ RGEQAEADGT AEAEKVAFLL GVNAGDLLKC LLKPKIKVGT EYVTQGRNKD
QVTNSIAALA KSLYDRMFNW LVRRVNQTLD TKAKRQFFIG VLDIAGFEIF DFNSFEQLCI
NYTNERLQQF FNHHMFVLEQ EEYKKEGIVW EFIDFGLDLQ ACIELIEKPM GILSILEEEC
MFPKASDTSF KNKLYDNHLG KNPMFGKPKP PKAGCAEAHF CLHHYAGSVS YSIAGWLDKN
KDPINENVVE LLQNSKEPIV KMLFTPPRIL TPGGKKKKGK SAAFQTISSV HKESLNKLMK
NLYSTHPHFV RCIIPNELKT PGLIDAALVL HQLRCNGVLE GIRICRKGFP NRIIYSEFKQ
RYSILAPNAV PSGFADGKVV TDKVLSALQL DPNEYRLGNT KVFFKAGVLG MLEDMRDERL
SKIISMFQAH IRGYLMRKAY KKLQDQRIGL TLIQRNVRKW LVLRNWEWWR LFNKVKPLLN
IARQEDENKK AQEEFAKMKE EFASCEQMRK ELEEQNTVLM QQKNDLVIAM SSGEDAIGDA
EEKIEQLIKQ KSDFETQIKE LEDKLMDEED AATELSAQKK KSDAEIGELK KDVEDLEAGL
AKAEQEKTTK DNQIKTLQDE MAQQDEHLSK LNKEKKNLEE VQKKTLEDLQ AEEDKVNHLS
KLKTKLEQTL DELEDNLERE KKIPGDVDKA KRKVEQDLKT TQETVEDLER VKRDLEDAGR
KKDMEINGLN SKLEDEQNLV AQLQKKIKEL QARIEELEEE LEAERQARTK VEKQRTELSR
ELEELGERLD EAGGATAAQM ELNKKREQEL LRLRRDLEEA TMQHESQIAT LRKKNQEATN
ELGDQIDQLQ KVKSRLEKEK TQLRAEMDDV QSQVEHAGKN RGCSEKMSKQ MEAQLSELNA
KIDDQARSVS ELTSQKSRLQ TEAADLTRQL EEAEHNVGQL TKLKSSLGAS LEDAKRSLED
EGRLRAKLQA EVRNLNSDID GIRESLEEEA ESKSDLQRAL SRANAEVQQW RSKFESEGAA
RADELEDAKR KLQAKLSEAE QTADTLHSKC AGLEKAKSRL QGELEDLAID VERSSAHANN
LEKKQRNFDK VVSEWQHKCN DLQAELENAQ KEARSYSAEL FRVRAQCEEV GDTVASLRRE
NKNLADEIHD LTDQLGEGGR NTHELEKARK HLALEKEELQ AALEEAEGAL EQEEAKVMRA
TLEISQIRQE IDRRLQEKEE EFDNTRRNHQ RAIESMQASL EAEAKGKAEA LRIKKKLEGD
INELEIALDA TNRGKAELEK NVKKYQGQIR ELQSQVEEEQ AQRDEAKEHY QMAERRCAAI
NGELEELRTI LEQAERARKA AENELADASD RVNELQAQVS TVGSQKRKLE GDVTAMQSDL
DELNNELKDA DERAKHAMAD ATRLADELRQ EQDHGLSVEK MRKSLESQVK ELQVRLDESE
AAALKGGKKM IQKLESRVRE LEAELDSEQR RHAETQKSMR KVDRRVKELS FQQEEDRKNY
ERMQELVDKL QNKIKTYKRQ VEEAEEIAAI NLAKFRKVQQ ELEDAEERAD QSEGALQKLR
AKNRSSVSAA RTSPM
//
