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Database: UniProt
Entry: A0A3Q0SSY2_AMPCI
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Original site: A0A3Q0SSY2_AMPCI 
ID   A0A3Q0SSY2_AMPCI        Unreviewed;      1722 AA.
AC   A0A3Q0SSY2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Myosin-11 {ECO:0000256|ARBA:ARBA00040393};
DE   AltName: Full=Myosin heavy chain 11 {ECO:0000256|ARBA:ARBA00042406};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000023290.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000023290.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Muscle contraction. {ECO:0000256|ARBA:ARBA00037488}.
CC   -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy
CC       chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
CC       regulatory light chain subunits (MLC-2).
CC       {ECO:0000256|ARBA:ARBA00038612}.
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   STRING; 61819.ENSACIP00000023290; -.
DR   Ensembl; ENSACIT00000023903.1; ENSACIP00000023290.1; ENSACIG00000018028.1.
DR   GeneTree; ENSGT00940000155421; -.
DR   OMA; NCACYLR; -.
DR   Proteomes; UP000261340; Unplaced.
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   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd01377; MYSc_class_II; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 5.
DR   Gene3D; 1.20.5.4820; -; 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   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF23; MYOSIN-11; 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; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 5.
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   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          27..76
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          80..784
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          662..684
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1002..1032
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1116..1199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1556..1676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1116..1143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1155..1199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1560..1676
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         173..180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1722 AA;  198353 MW;  2E447F212BB329C6 CRC64;
     MADTDDNKYL FLENDFXNSG VAQADWAAKK MVWVPSEREG FEPASIKEEK GDQVLVELSN
     GQKVTVNKDD IQKMNPPKFS KVEDMAALTF LNEASVLHNL RERYFSSLIY TYSGLFCVVV
     NPYKMLPIYS EKIIEMYKGK KRHEVPPHIY SITDNAYRNM MQDREDQSIL CTGESGAGKT
     ENTKKVIQYL AVVASSHKGK NPANPVSRNS FIGELEKQLL QANPILEAFG NAKTIKNDNS
     SRFGKFIKLN FDVTGYLVGA NIDTYLLEKS RCIRQAHTER AFHIFYYMVA GAKDKVREEL
     LLEDFSSYRF LIEGHVEIPG QEDDEMFDET LEAMEIMGFN EEERLGMLKV VSSVLQLGNI
     KFEKERNNEQ ATMPDNTAAQ KVCHLQGINV TDFTRAILTP RIKVGREVVQ KAQTKQQADF
     AIEALAKAMY ERLFRWILAR VNKTLDKSKR QSSSFLGILD IAGFEIFEDN SFEQLCINYT
     NERLQQLFNH TMFILEQEEY KREGIEWNFI DFGLDLQPCI ELIERPNNPP GILALLDEEC
     WFPKATDVSF VEKLLNTHTG HVKFSKPKQH KDKLMFSVLH YAGKVDYNAA NWLTKNMDPL
     NDNVTALLNN SSSTFVQDLW KDVDRVVGLE TMTKMSESSV PSSTKSKKGM FRTVGQLYKE
     SLGKLMTTLH NTQPNFVRCI IPNHEKRSGK MDSHLVLEQL RCNGVLEGIR ICRQGFPNRI
     VFQEFRQRYE ILAANSIPKG FMDGKQACCL MVKHLDLDPN LYRIGQSKMF FRTGVLAQLE
     EERDLKLTVV IIAFQAQARG FLGRKAFSKR QQQLSAMKVI QRNCACYLKL KNWQWWRLFT
     KVKPLLQVTR QEEEMGQKEE ELKAAKEVAA KTEAELKDIT QKHSQLMEER AQLELKLQAE
     TELCAEAEEM RVRLEAKKQE LEEVLHEMEA RLEEEEDRSN ALQQEKKEME QQLQLMEAHI
     AKEEDAKQNL QLEKAAVEGK VKKLEEDILL MEDQNNKLQK ERKLLEERMA DMSSNLAEEE
     EKSKNLTKLK AKHESMISEL EVRMKKEEKG RQDMEKAKRK VEAELAELQE QHADLQAQLA
     ELQALTRTDD PFSQRGAAVK RIRELEALLS ELQEDLEAER AARGKAEAAR RDLGEELNAL
     RTELEDSLDT TAAQQELRAK REQEVAMLKK AMEEEGRNHE AQIQELRQKH SQAVEELNEQ
     LEQAKRVRAG LEKAKQALEK ESADLSSDLR SLASAKQDVE HKKKKVEGQL NELNSRFNES
     ERQRNELSER VSKMTLELDS VTGLLNEAEG KNIKLSKDVS GLSSQLQDAQ ELLSEETRQK
     LNLSGRLRQM EEDRNSLMEQ LEEETEAKRA VERQVSSLNM QLSDYKKKLD EMSGTVEMLE
     EGKKRLQREL EAVNTEYEEK ASAYDKLEKS RSRMQQELED VLMDLDSQRQ LVSNLEKKQK
     KFDQMLAEER SVSCKYAEER DRAEAEVREK ETKVLALTRA LEERHEALEE AEKMVKALRA
     EMEDLISSKD DVGKNVHDLE KAKRGLEAIV EEMRTQMEEL EDELQVAEDA KLRLEVNSQA
     LKAQHERELQ ARDELGEEKR KQLLKQVREL ESELEEERKQ RGQASAGKKK LEGELKDMED
     QLEATSRGRD EALKQLRKIQ GQAKDLQREL EDSRAAQKEV LASARESERR SKAMEADIIH
     LHEVLAAAER ARKQAETERD ELSEELASNS SGKWVSRVIN AF
//
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