ID A0A0R3RXW7_9BILA Unreviewed; 1993 AA.
AC A0A0R3RXW7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Myosin motor domain-containing protein {ECO:0000313|WBParaSite:EEL_0000709001-mRNA-1};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000709001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000709001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
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; 1147741.A0A0R3RXW7; -.
DR WBParaSite; EEL_0000709001-mRNA-1; EEL_0000709001-mRNA-1; EEL_0000709001.
DR Proteomes; UP000050640; Unplaced.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
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; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 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 Gene3D; 4.10.270.10; Myosin, subunit A; 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; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF47; NON-MUSCLE MYOSIN; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
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 68..793
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 670..692
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1945..1993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 857..1604
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1648..1936
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1945..1961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1972..1993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 162..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1993 AA; 230005 MW; E9C5D88F02B33F74 CRC64;
MGKLRIVNAS NPKQDERVWV PDDTEGFVLG VVIRNVADDR ILLRIEGTGY EKIVCGEELQ
SVNPAKLEKI EDMASLSYLN EASVLHNLRQ RYYSSLIYTY SGLFCVVINP YKWLPHIYST
AVMKSYRGRK RHEVPPHVFA VTDCAYHEML HQREDQSILC TGESGAGKTE NTKKVIQYLA
DIAGAGRHMR SSVARSPGKS LLPTSLSLSP ISESMSSIGQ LEDQLLLANP ILEAFGNSKT
VKNDNSSRFG KFIRINFDQN GCISGANIEH YLLEKSRTIR QAANERSFHF FYQLLLGSSF
SKKSTLLSEC WNMSMFLMDD IDCYRFLTNG NLVIPNVDDA SELSSTLNAM KRMDFSDADI
DAVMRITCAV LLLGNLSFTE DRSSDQAVLV DDRVAQKICC LLGLPVSDLA KAFLKPRVKV
GRDYVHKAQT REQVHYAVEA IAKASYERMF RWLVTRINRS LGRSANSGMA FIGILDIAGF
EIFELNTFEQ LCINYTNEKL QQLFNNTMFI LEQEMYRKEG IEWNFIDFGL DLQPTIDLIE
KPLGILSLLD EQCIFPKSTD KSYVEKLIAN QSKHPKFIIP EFRTKSDFAI IHYAGRVNYA
ADQWLTKNMD PLNDSVVFLL QNSGDQFVSE MWKNAEFASL GMTDQTDYVF GARTKRGMFR
TVGQTYKEQL SRLMKTLQNT SPHFVRCIIP NHEKKAGIIN GPLVLEQLRC NGVLEGIRIC
RQGYPNRMPF HDFRRRYELL VDRETIPPGF LDGKETVRRL LSALEVDASL FRVGQSKVFF
RSGVIAALEE MRDKELQRFV IQFQTYCRGY LARRAFKKLL QKVSAIRIIQ RNGLAWSRLK
DWNWWRLFAK VRPLLEVTAS EEAIAGKESE LKSLRETLLQ KDYTLSDYAT RIEQLTNDRA
ELQKLLEEES VEKTEIEDMK DQLLSMKVQL EKEVESFRQK FEEKETECTF ISAECKKLQD
DAAALRNQLQ VENGKYEQLQ LSYVSIDQKL KNIVIEKDRY FETNEKMTKE KALLEGRLAV
ATQKIVVEEE QNRQNAKLRT KLEAKITDCE QENEKLKKLV EATEAANQKL TVEMRDMRNG
NEELLRKLSE LSVQLQKKNE EIIATLTRCD DEQSQKQNLM KQTKELMLEL QEVKEDLENE
KASRIKSEKG KRDFLEELEA LKHELMESQD KTQANLELRA EREKQYLSIK KELEKTATQH
EQNVAELKAR YLQQLDSVRV ENEELKKQMQ QVIKTKNRIE NELKEKSVVI QQNQTANMEN
ERKRRNAENL LNEWQVKAQG AENNAMELKS SLTKVQSEVE RLTQELENSE NVVLVLHKKV
AAAEAQITDL SDAVNLEKSQ NEALRAKLRT LDDKLENLQE NKDHDEFTIQ KNEKEINSLK
LQLDDTRKKN DEKLLLQAEE LRKKMVKEVE ACKKELDESE QALARSEKAK EKLMQENEDI
LNELNKLRCS AREMEKKQRK FDQVLEEEKL NLAKVVAERD RLSQELRDHE SNALVVAKET
DILRNRIAEL ENIRNTLQLD LDNAVTMKDD TGRSVLELDR MKRQLEAELA NAKETITELE
DNLQLTEDAK LRLDVTLQAT NAELEKVRND KERADDERRK TTLRKLGEME GELESERRSK
LTLLQQKRKL EIDLHHSLEQ IEAITIQKEE FSRQLRKCNL QLKDLQLELD ESKDAKDAAL
LRAQDMEKKL KSLENELATA AETNMQLTAD RRRAERERDD ALEELNIKSG LMSSEDKKRL
ETKIYELEEL LEEEQNNTEL GNDKLKKAQI QLETLTTELA AERSLCEKLE ADKQNSERQC
KELKVALEEL ESDMRTRVRG QIAALEAKLQ ASNEQCAQME QERNMANRQI RRMEKKLSDT
LMMNEEEKRN VEQLKETADR TVARHRQMRR QIEDLEEVVY REQSKCRQLQ RSIDNLNEAN
ETLTRENAQL KSLAALARRP VLNRASTSRL GSETDSTGRG ARSFGGDSAD LLRPNSGSTA
GSYVGDDPDL TTN
//
