ID   Q17042_ARGIR            Unreviewed;      1951 AA.
AC   Q17042;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   SubName: Full=Myosin heavy chain {ECO:0000313|EMBL:AAC46490.1};
OS   Argopecten irradians (Bay scallop) (Aequipecten irradians).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC   Argopecten.
OX   NCBI_TaxID=31199 {ECO:0000313|EMBL:AAC46490.1};
RN   [1] {ECO:0000313|EMBL:AAC46490.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Muscle {ECO:0000313|EMBL:AAC46490.1};
RX   PubMed=7809102; DOI=10.1073/pnas.91.26.12686;
RA   Nyitray L., Jancso A., Ochiai Y., Graf L., Szent-Gyorgyi A.G.;
RT   "Scallop striated and smooth muscle myosin heavy-chain isoforms are
RT   produced by alternative RNA splicing from a single gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:12686-12690(1994).
RN   [2] {ECO:0007829|PDB:1NKN}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 838-888.
RX   PubMed=12867988; DOI=10.1038/nature01801;
RA   Li Y., Brown J.H., Reshetnikova L., Blazsek A., Farkas L., Nyitray L.,
RA   Cohen C.;
RT   "Visualization of an unstable coiled coil from the scallop myosin rod.";
RL   Nature 424:341-345(2003).
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; U09782; AAC46490.1; -; mRNA.
DR   PDB; 1NKN; X-ray; 2.50 A; A/B/C/D=838-890.
DR   PDBsum; 1NKN; -.
DR   SMR; Q17042; -.
DR   EvolutionaryTrace; Q17042; -.
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; 1.10.287.1490; -; 1.
DR   Gene3D; 1.20.5.340; -; 5.
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; 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; 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; 6.
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:1NKN};
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          29..79
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          83..778
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          656..678
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1044..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1190..1228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1260..1335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1347..1366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1902..1951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1209..1227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1260..1285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1286..1302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1309..1335
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1902..1918
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1919..1941
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         176..183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1951 AA;  224254 MW;  1FDC3D7D691C1410 CRC64;
     MNIDFSDPDF QYLAVDRKKL MKEQTAAFDG KKNCWVPDEK EGFASAEIQS SKGDEITVKI
     VADSSTRTVK KDDIQSMNPP KFEKLEDMAN MTYLNEASVL YNLRSRYTSG LIYTYSGLFC
     IAVNPYRRLP IYTDSVIAKY RGKRKTEIPP HLFSVADNAY QNMVTDRENQ SCLITGESGA
     GKTESTKKVI MYFARVAANL YKQKQEEPTT THARASNLED QIIEANPVLE AFGNAKTVRN
     NNSSRFGKFI RIHFGPTGKI AGADIETYLL EKSRVTYQQS AERNYHIFYQ ICSNAIPELN
     DVMLVTPDSG LYSFINQGCL TVDNIDDVEE FKLCDEAFDI LGFTKEEKQS MFKCTASILH
     MGEMKFKQRP REEQAESDGT AEAEKVAFLC GINAGDLLKA LLKPKVKVGT EMVTKGQNMN
     QVVNSVGALA KSLYDRMFNW LVRRVNKTLD TKAKRNYYIG VLDIAGFEIF DFNSFEQLCI
     NYTNERLQQF FNHHMFILEQ EEYKKEGIAW EFIDFGMDLQ MCIDLIEKPM GILSILEEEC
     MFPKADDKSF QDKLYQNHMG KNRMFTKPGK PTRPNQGPAH FELHHYAGNV PYSITGWLEK
     NKDPINENVV ALLGASKEPL VAELFKAPEE PAGGGKKKKG KSSAFQTISA VHRESLNKLM
     KNLYSTHPHF VRCIIPNELK QPGLVDAELV LHQLQCNGVL EGIRICRKGF PSRLIYSEFK
     QRYSILAPNA IPQGFVDGKT VSEKILAGLQ MDPAEYRLGT TKVFFKAGVL GNLEEMRDER
     LSKIISMFQA HIRGYLIRKA YKKLQDQRIG LSVIQRNIRK WLVLRNWQWW KLYSKVKPLL
     SIARQEEEMK EQLKQMDKMK EDLAKTERIK KELEEQNVTL LEQKNDLFLQ LQTLEDSMGD
     QEERVEKLIM QKADFESQIK ELEERLLDEE DAAADLEGIK KKMEADNANL KKDIGDLENT
     LQKAEQDKAH KDNQISTLQG EISQQDEHIG KLNKEKKALE EANKKTSDSL QAEEDKCNHL
     NKLKAKLEQA LDELEDNLER EKKVRGDVEK AKRKVEQDLK STQENVEDLE RVKRELEENV
     RRKEAEISSL NSKLEDEQNL VSQLQRKIKE LQARIEELEE ELEAERNARA KVEKQRAELN
     RELEELGERL DEAGGATSAQ IELNKKREAE LLKIRRDLEE ASLQHEAQIS ALRKKHQDAA
     NEMADQVDQL QKVKSKSEKE KQQLRSEVED LQAQIQHISK NKGCSEKVMK QFESQMSDLN
     ARLEDSQRSI NELQSQKSRL QAENSDLTRQ LEDAEHRVSV LSKEKSQLSS QLEDARRSLE
     EETRARSKLQ NEVRNMHADM DAIREQLEEE QESKSDVQRQ LSKANNEIQQ WRSKFESEGA
     NRTEELEDQK RKLLGKLSEA EQTTEAANAK CSALEKAKSR LQQELEDMSI EVDRANASVN
     QMEKKQRAFD KTTAEWQAKV NSLQSELENS QKESRGYSAE LYRIKASIEE YQDSIGALRR
     ENKNLADEIH DLTDQLSEGG RSTHELDKAR RRLEMEKEEL QAALEEAEGA LEQEEAKVMR
     AQLEIATVRN EIDKRIQEKE EEFDNTRRNH QRALESMQAS LEAEAKGKAD AMRIKKKLEQ
     DINELEVALD ASNRGKAEME KTVKRYQQQI REMQTSIEEE QRQRDEARES YNMAERRCTL
     MSGEVEELRA ALEQAERARK ASDNELADAN DRVNELTSQV SSVQGQKRKL EGDINAMQTD
     LDEMHGELKG ADERCKKAMA DAARLADELR AEQDHSNQVE KVRKNLESQV KEFQIRLDEA
     EASSLKGGKK MIQKLESRVH ELEAELDNEQ RRHAETQKNM RKADRRLKEL AFQADEDRKN
     QERLQELIDK LNAKIKTFKR QVEEAEEIAA INLAKYRKAQ HELEEAEERA DTADSTLQKF
     RAKSRSSVSV QRSSVSVSAS NAAHVAHHHV E
//