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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//