ID   MYSH_ACACA              Reviewed;        1577 AA.
AC   P47808;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=High molecular weight form of myosin-1;
DE   AltName: Full=High molecular weight form of myosin I;
DE            Short=HMWMI;
OS   Acanthamoeba castellanii (Amoeba).
OC   Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida;
OC   Acanthamoebidae; Acanthamoeba.
OX   NCBI_TaxID=5755;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2243110; DOI=10.1016/s0021-9258(17)30552-5;
RA   Horowitz J.A., Hammer J.A. III;
RT   "A new Acanthamoeba myosin heavy chain. Cloning of the gene and
RT   immunological identification of the polypeptide.";
RL   J. Biol. Chem. 265:20646-20652(1990).
CC   -!- SUBUNIT: Myosin I heavy chain is single-headed.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000305}.
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DR   EMBL; M60954; AAA27709.1; -; Genomic_DNA.
DR   VEuPathDB; AmoebaDB:ACA1_024380; -.
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-KW.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR   GO; GO:0022607; P:cellular component assembly; IEA:UniProt.
DR   Gene3D; 1.25.40.530; -; 1.
DR   Gene3D; 3.40.850.10; -; 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; IPR000857; MyTH4_dom.
DR   InterPro; IPR038185; MyTH4_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF00784; MyTH4; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00139; MyTH4; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51016; MYTH4; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Actin-binding; ATP-binding; Methylation; Motor protein; Myosin;
KW   Nucleotide-binding; SH3 domain.
FT   CHAIN           1..1577
FT                   /note="High molecular weight form of myosin-1"
FT                   /id="PRO_0000123363"
FT   DOMAIN          75..751
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          755..782
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1261..1401
FT                   /note="MyTH4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT   DOMAIN          1519..1577
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          628..650
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          730..744
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          1435..1466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1483..1520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1483..1516
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         168..175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         119
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1577 AA;  177531 MW;  BAF2E8EBABB7438C CRC64;
     MHFLFFFANR QFLSLKCPQA EFVWIPHPVH GYITGKFIQE DYGGTSYCQT EEGESLSVAC
     APSQLAKVAK SVLDKSVDDL VQMDDINEAM IVHNLRKRFK NDQIYTNIGT ILISVNPFKR
     LPLYTPTVMD QYMHKVPKEM PPHTYNIADD AYRAMIDNRM NQSILISGES GAGKTECTKQ
     CLTYFAELAG STNGVEQNIL LANPILESFG NAKTLRNNSS RFGKWVEIHF DQKGSICGAS
     TINHLLEKSR VVYQIKGERN FRIVATELVK APPRSRGGGG SSPARPESFK FLSQSGCIDV
     EGVDDVKEFE ERVLCHGQAR VRVQFSEDDI NNCMELISAI LHLGNFEFVS GQGKNVETST
     VANREEVKIV ATLLKVDPAT LEQNVTSKLM EIKGCDPTRI PLTPVQATDA TNALAKAIYS
     KLFDWLVKKI NESMEPQKGA KTTTIGVLDI FGFEIFDKNS FEQLCINFTN EKLQQHFNQY
     TFKLEEKLYQ SEEVKYEHIT FIDNQPVLDL IEKKQPQGLM LVLDEQISIP KSSDATFFIK
     ANQTQAARST QLRGGEDSRT DFIIKHYAGD VIYDSTGMLE KNKDTLQKDL LVLSESSKQK
     LMKLLFPPSE GDQKTSKVTL GGQFRKQLDS LMTALNATEP HYIRCIKPNS EKQADLFHGF
     MSLQQLRYAG VFEAVRIRQT GYPFRYSHEN FLKRYGFLVK DIHKRYGPNL KQNCDLLLKS
     MKGDCXSKVQ VGKTRVLYRA PEQRGLELQR NIAVERVTIQ IQAGVRRMFA RRLYKRMRAI
     KPVLLNAIKS RSLSVLEQAI DAAKDIEFDM KLIRDCKELR SVILKEMEIT KKLTDYIGAP
     PNHKTYLQVE PLYAQLCAVL TEAESINYST PLVETGQQIK YMIAQRVETR EQLKQAVDGA
     VRVDLEAAIA RAEQIGLEES EPTLAAGRQE LQRIYREEEL VAELLNALAV GMAMRTSETT
     WDHAAIDAHT LGSAIYAAES FGFRTEQGRL TLDEAKVIVE VRQHLAADDY ESLSMTLKKA
     TTTLNKNSMS QSTKTEIDEA YEELSHNTAV NDLIEKVVQA IQDHDQEMLD YGVQQADSLR
     ITDRPEMMQA TELLNRIVNA RALLREGITN VDQAQLETAL ADAASFAYTR EEVPTAQQLL
     DRIYVINHDA DVGLYYMEKE PLERAWAGAQ EINLKTAQID EVRNVLANDE QKFIQEQLKT
     ANRLGDQARA IRLNIKLKEI FFGQFGKMFV FEQFGGLRKP EDFAKAKLLG REALKLGMFK
     WTKSPIPTSL TTLDQLAVKS ATRLFKNVLG FMGDRPLPYP NALAQDLLEQ CLAAPELRNE
     VYCQIIKQLT ENPSPQSVTK GWQLMRCCLQ TFPPSEEFAN CLEMFLAAKG KDDKYIEMLH
     DTQYGDKRTS APNVEQILAA KQYVTRIDLN QSTQVDTSVV PQGFVPEKLI ADDTEGVIRA
     GSRPAQARAQ PGQQAQPAGA ARQQAAAPVQ AAAATASYDY GQQQQQQQQG YDQQQQAYGG
     GADYGQQQQQ QDLPAEPTEE YKQVEVVYDY DGGGDAQRLV LVKGAIITVI KEYEGWAYGS
     TDDGQVGLYP INYTRPI