ID A0A0M3IHF0_ASCLU Unreviewed; 1914 AA.
AC A0A0M3IHF0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 2.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Myosin motor domain-containing protein {ECO:0000313|WBParaSite:ALUE_0001783301-mRNA-1};
OS Ascaris lumbricoides (Giant roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0001783301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ALUE_0001783301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (MAY-2016) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR WBParaSite; ALUE_0001783301-mRNA-1; ALUE_0001783301-mRNA-1; ALUE_0001783301.
DR Proteomes; UP000036681; Unplaced.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR GO; GO:0030017; C:sarcomere; IEA:UniProt.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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; 1.20.5.340; -; 4.
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; 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; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014751; XRCC4-like_C.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF58; MYOSIN-4; 1.
DR Pfam; PF00063; Myosin_head; 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; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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}; Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT DOMAIN 25..732
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 623..645
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 919..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1860..1914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..978
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1875..1914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1914 AA; 219846 MW; 429292D09EBB40C4 CRC64;
MLQVLYFQIT LKSELVQEMN PPKFEKTEDM SNLTFLNDAS VLHNLRARYS SMLIYTYSGL
FCVVINPYKR LPIYTDSVAS MFMGKRRTEM PPHLFAVSDE AYRNMLQDHE NQSMLITGES
GAGKTENTKK VIAYFAVVGA SQQEAVGVQQ PEGKKKVTLE DQIVQTNPVL EAFGNARTVR
NNNSSRFGKF IRIHFSKKGK VASCDIEHYL LEKSRVIRQA PGERCYHIFY QVYSDFNPTL
KKDLLLDRPL KEYYFCAQAE LTIDGVNDKE EHQLTDEAFD ILHFSPEEKL NCYKLVAAIM
HMGNMKFKQR PREEQAEPDG TDEAEKASAM FGVNHEEFLK ALTRPRVKVG TEWVAKGQNI
DQVTWAVGAM AKGLYSRVFN WLVKKCNITL DQKGIPRDYF IGVLDIAGFE IFDASYLHLY
GDIQLGATKL FNSFEQLWIN FVNEKLQQFF NHHMFVLEQE EYAREGIQWT FIDFGLDLQA
CIELIEKPLG IISILDEECI VPKATDLTLA QKLNDQHLGK HPNFEXPKPP KGKQGEAHFA
MRHYAGTVRY NVMNWLEKNK DPLNDTVVSC MKATQGNNLL NEVWKDYVTQ EEAAIAAKEG
GGGKKHGKSG SFMTVSMLYR ESLNNLMTML NMTHPHFIRC IIPNEKKTSG LIEAGLVLNQ
LTCNGVLEDF RHRYSVLAAD EANSSPDAKK CAEAILGKLV SQQKLTEDNY KMGDTKVFFK
AGVLARLEDI RDEVLKVIMT KFEAYIRWYC GLIDRKRRIE QNAATLLLQR NIHMWCSLRT
WEWFRLYTKV RPMLREGKIA EQMEKLNEKL KSLEDGIEKE AKLRKELEDN SVKTQAEKAD
LLAQLESVKA QLDEAEERVK RESALKGDVD KQLEDLNEQL AQTEDKNEDL MRAKKKVESE
VEALKKQIQD LEMSVRKAES EKQSKDHQVR SIQDEMQMQD ETIAKLNKEK KHQEEMNKKI
MEDLQSEEDK SNHINKIKAK LEQTLDDLEE NLERERRAKA DTEKARRKVE GELKIAQENI
EEATRQKHDL ENNLKRKEAE MNNLSSRLED EQSIVSKLQR QIKEAQSRVG ELEEELEGER
ESRSKADRAK SDLQREIEEL NERLDEQGGA TEAQIEINKK REAELAKLRR DIEEANMNHE
GQLATLRKKH GDAVAELADQ LDMIEKQRQK LEKEKAQIVH DSENLAAQLD SETAAKSNNE
KLAKQLEMQL ADLQGKADEQ SRQLQDFASI RNRLANENAD LNRQLEDLEE QLGALQRVKA
QLSTQLEDTR QAADDEARER QTLAAQAKNF QIEAEQAHNN LDEEIESKNE VMRQLSKANA
EIQQWQSKFE GDGMLRADEI EEVKRKQGLK INELQEALEM ANQKVLSLEK TKSRLMGDLD
DAQVDVERAN SYASQLEKKQ KGFDKVVEEW KKKSDDLSAE LDAAQREARN LSTDLIKMKT
SHEELLETVE GLRRENKGLC NEIKDLSDQL GEGGRSAHET QKIIRRLEVE KEELQHGLDE
AEAALEAEES KVMRAQVEVA QIRSEVEKRI QEKEEEFDST RRNHQRALES MQASLEAESK
GKTELLRVKK KLEADINELE IALDHANKAN ADAQKNLRRY NEQIREIQLQ IEEEQRQRDE
MKEQYYGAEK RAALLQSEKE ELAAACEQAE RARKQAELDA ADGRERANEL IAQTSSLNAT
KRKLEGELQA IHADLDETLN EFRTSEENCK KATADVERLA DEVRQEQEHA THIDRLRQGL
EAQIRELQVQ LDEAEQAALK GGKKVIAKLE QRAHELEGEL DGEQRHYQES IKNVAKAERQ
VRELQFQVDE DKKNFERMQD LVEKLQSKIK TQKKQLEDAE ELANLNLQKY RQIQHQLEDA
EERAENAESA VAKMRAKSRT TTSAAPGGLL VSQSTSAVSR SGSTRPRTTS FVDY
//
