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Database: UniProt
Entry: A0A226DZT7_FOLCA
LinkDB: A0A226DZT7_FOLCA
Original site: A0A226DZT7_FOLCA 
ID   A0A226DZT7_FOLCA        Unreviewed;      1940 AA.
AC   A0A226DZT7;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Myosin heavy chain, muscle {ECO:0000313|EMBL:OXA50729.1};
GN   ORFNames=Fcan01_14082 {ECO:0000313|EMBL:OXA50729.1};
OS   Folsomia candida (Springtail).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC   Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX   NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA50729.1, ECO:0000313|Proteomes:UP000198287};
RN   [1] {ECO:0000313|EMBL:OXA50729.1, ECO:0000313|Proteomes:UP000198287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VU population {ECO:0000313|EMBL:OXA50729.1,
RC   ECO:0000313|Proteomes:UP000198287};
RC   TISSUE=Whole body {ECO:0000313|EMBL:OXA50729.1};
RA   Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT   "The genome of Folsomia candida.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OXA50729.1}.
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DR   EMBL; LNIX01000008; OXA50729.1; -; Genomic_DNA.
DR   STRING; 158441.A0A226DZT7; -.
DR   OMA; CERMAKQ; -.
DR   OrthoDB; 640507at2759; -.
DR   Proteomes; UP000198287; Unassembled WGS sequence.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0030017; C:sarcomere; IEA:UniProt.
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; -; 3.
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; 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; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 5.
DR   SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 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   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Muscle protein {ECO:0000256|ARBA:ARBA00023179};
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:UP000198287};
KW   Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT   DOMAIN          35..83
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          87..778
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          657..679
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          927..947
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1918..1940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1263..1297
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1333..1916
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        927..945
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         180..187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1940 AA;  221909 MW;  EABFBC4D6B6C978B CRC64;
     MVIEQKFKPG EEPDPTEFLF VSMEMKRQDQ SKPYDAKKAC WVPDEKEGFV VGEIAGTKGD
     IIIVKVDGAD KNFKKDLVGQ VNPPKYEKCE DMSNLTFLND ASVLHNLRQR YYARLIYTYS
     GLFCIAVNPY VRFPIYTPRA MKIYQGKRRN EVPPHIFAIA EGAYQNMLQD HENQSILITG
     ESGAGKTENT KKVIAYFANV ASSGKASDSK KVSLEDQIVQ TNPVLESFGN AKTTRNDNSS
     RFGKFIRIHF GPSGKLAGAD IESYLLEKAR VISQMSQERC YHIFYQLMSP NCNKAGVKSM
     CLLGDDIYKY HYCSQGKVTV PSIDDSEEFA ATHEAFEILL FTDEERANIY RITAAVMHMG
     ELKFEQKGRD EQAMQAEEEE GAATGKLLGI DGEILYINIC KPRIKVGTEF VTKGQNVQQC
     NATCGALAKS MFDRLFKFLV KKCNETLDTK QNRASFSAVL DIAGFEIFEE NGFDQLCINF
     TNEKLQQFFN HHMFVLEQEE YKKEGLDWIF EDFGMDLQAT ITLFEQPMGV FSILEEESMF
     PKATDQTFIE KLKSNHLGKS NCFLKPKPPK PGFKEGHFAV AHYAGTVTYN ITGWLEKNKD
     PLNDTVVDQY KKGGNALICE LYSDHPGQSE EAGGKGGGGG KKKGGFKTVS SGYREQLGNL
     MATLKATHPH FIRCIVPNEI KKPGLVDAAL VMHQLTCNGV LEGIRICRKG FPNRMLYPDF
     KHRYAILASA QMAAEKEDKK IAVACFETIG LNADKYRVGH TKVFFRAGVL GEMEEIRDDK
     LGKIITWLQA QVRKYNVAKA YRTLEKQRKA LEVVQRSLKS YVNLRCWPWW GLWKLIKPNL
     QTCKIEENMK KAEVKIAKFE AILVEEEKAR AEAEKKAKHT IHEKDKLLKE LDEEKNAGSN
     FQERFNKINA QKNELDAQLN DLTNRVQSEE DQKNQIQQQL RKQQQDLANT KKELEENAKS
     LEKLDADKVA KEGQIKNLNE ELAHQEELIS KLQKEKKQVQ EAAQHTSEDV QALEDKVNGL
     NKIKTKLERS LDELEDSLER EKKLRGDIEK AKRKVEGDLK IAQEAVADLE RNKKDVEQTV
     QRKDKEISSL TAKLEEEQGL IAKLQRQIKE LQARIEELDE ELEAERIARA KAESQRSNLA
     RELEELGSRL EEAGSATSGQ IELNKKREAE LAKLRRELEE TNVQHEASMA GLRKKHNDAV
     AEMAEQIDNL NKMKAKAEKD RSQIATELND SRAAMDHLVN DKAGQEKLGK HLQHQMAEIQ
     GRYEEVARNV NEVDQTKKRL ALENTDMARQ IEEAESNLSA LGKLKVSLAT QLEDTKRLAD
     EEGRERATLL GKYRNVEHDL DLLREQLDEE AEAKSEIQKQ LSRANAEAQL WRTKYENEGV
     ARIEELEEAK RKLLARLQEA EETIESLNVK SIALEKTKQR LSSQLEDMTS EVDRSRALVI
     QLEKKQKYFD KIIDEWKAKV GDLQSEVDAS QKEARSYATE VFRIRAAYEQ EQEQLDAVKR
     ENKNLADEIK DLFDQIGEGG RNVHEIEKAR NRLQIEKEEL QSALEEAEAA FEQEENKVLR
     VQLELSQVRQ EIDRRIQEKE EEFENTRKNQ QRALDSMQAS LEAESKGKQE ALRVKKKLET
     DINELEIALD HANKTNAEAS KTIKRYLQQL KETQSLLEEE QRARDEAREA YGIAERRANA
     FSNELDESRT LLEQADRARR CAEQELHDAR DQINELGNQT SILGGIKRQL DSQLQTMHAD
     LEAILNEAKN SEEKAKKAMV DAARLADELR MEQEHAQSQE RARKGLEVTM KDLQGRLEEA
     EQSILKGGRK QIAKLEERVR LIETELDSEQ RRHSEAQKNM RRAERRCKEL SFQAEEDRKN
     HEKMQDLVEK LQQKIKTYKR QIEEAEEVAA LNLAKFRKAQ QEYEEVEERN DLAEAALSKV
     RPGPLPRGRP ASMARGMSPF
//
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