ID A0A3S1BID5_ELYCH Unreviewed; 1974 AA.
AC A0A3S1BID5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=EGW08_003248 {ECO:0000313|EMBL:RUS89001.1};
OS Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC Plakobranchidae; Elysia.
OX NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS89001.1, ECO:0000313|Proteomes:UP000271974};
RN [1] {ECO:0000313|EMBL:RUS89001.1, ECO:0000313|Proteomes:UP000271974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC2010 {ECO:0000313|EMBL:RUS89001.1};
RC TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS89001.1};
RA Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL Submitted (JAN-2019) 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:RUS89001.1}.
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DR EMBL; RQTK01000069; RUS89001.1; -; Genomic_DNA.
DR STRING; 188477.A0A3S1BID5; -.
DR Proteomes; UP000271974; Unassembled WGS sequence.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
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 CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 3.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.10.250.2420; -; 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:SF71; 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; 3.
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}; Reference proteome {ECO:0000313|Proteomes:UP000271974}.
FT DOMAIN 35..85
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 89..794
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 672..694
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1133..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1339..1372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1421..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1510..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1707..1739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1754..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1893..1974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1707..1728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1778..1792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1893..1933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1939..1959
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 182..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT NON_TER 1974
FT /evidence="ECO:0000313|EMBL:RUS89001.1"
SQ SEQUENCE 1974 AA; 227801 MW; 3E7EB1384486D163 CRC64;
MADFEGASGL TATELSYLAI DRSLINDPSV QAEWASKKLV WVPDDSHGFV AASMRGEKGD
QVECVVDETG RKIVVHRDDI QKMNPPKFNK VEDMAELTCL NEASVLHNLK DRYYSGLIYT
YSGLFCVVVN PYKRLPIYTE KVIELYKGKK RHEVPPHVFA IADTAYRSML QDREDQSILC
TGESGAGKTE NTKKVIQYLA YVAASNRTNR QSITSSAPDA GKGNDQMLKQ GELENQLLQA
NPILEAFGNA KTIKNDNSSR FGKFIRINFD ASGYISGANI ETYLLEKSRS VRQAESERSF
HIFYQFLHGA NAQQRQEFLL EEWGKYSYMT HGKLMVQNID DTAEFKALTE SMSIMGISED
DQTAVLRTIS AVLLLGNMMF KQDRNSDQAT MPDNTVAQKA CHLLSVPVTA LTQAFLKPKI
KVGRDSVTKA QTKAQVEFAV EAISKAMYER LFKWIVMRIN KSLDRTKRQG ASFIGILDIA
GFEIFKMNSF EQLCINYTNE KLQQLFNHTM FILEQEEYQR EGIEWKFIDF GLDLQPTIDL
LEKPMGILAL LDEECWFPKA TDKTFVDKLL GQHTGHPKFE KPDFRADAHF SLIHYADKVD
YSADQWLMKN MDPLNENVVS ILAGSTDNFV SNMWKDADIV GMGAAQAVDT MFGSRTRKGM
FRTVSQLYKE QLAKLMTTLR NTNPNFVRCI IPNHEKKAGK IESGLVLDQL RCNGVLEGIR
ICRQGFPNRI LFQEFRQRYE ILTPGAIPRG FMDGKKAVEK MISVLELDSN LFRIGQSKIF
FRAGVLAHLE EERDLKLTDI IVQFQALARG LLARKNYQKR LQQINAIRVI QRNCAAYLKL
RNWQWWRLFT KVKPLLSVTG QEEKLHVKEE ELKKVKDNYE KQKQETEEME RRYAQIIDEK
NILAEQLQAE TELCAEAEES RARLNKRKEE LEDILHELEL RIEEEEDRNN IVMEEKKAMQ
QNLKDLEDQL EEEEQTRQKL QLEKVAAESK MKKLEEEAAL LEDTNQKLLK EKKLMEERLS
EAQLNMAEEE EKSKQLGKLK NKYEAIIADL EDRLRKEQQA RQELEKIRRR LETELNDLRD
QLSEKRQQVE DLQTQLAKRE EEVQAALQKA DDEQGSKTTT QKQLREVTNQ MQELQEDLEA
EREARTKAEK QKRDLNEEVE ALREELENSL DTTAAVQELR GKREQEVQEL KRMVEQSQKA
HDDAVAEIKQ KYSQQSDQVT EELENTKKAK ANLEKTKAHL EEENKDLGND LKSVQMAKQE
SERKRKQAET QLAEMSLKLA ELERVSGDAG DKSKKLQTEL DQVMNQLEQV ETKALQGQQK
ISSLEAQLAD VQETMQDETR QKLSLQSKLR AVQDEKERLE ERLEEEEETK RAQEKQLLDI
NQKMIEIKKK AEEDMANNEA LEEYKKKAAR DVESLMQQIE EARTAADRAE KSRRKLQAEV
DDMTVELESQ RSSVVNAEKK QRKFDQMLAE EKAVSERLAL ERDQADAESR EKETKILNLQ
RLLDELQERA ESLDRQRQAQ ARELEDLVSS KDDVGKNVHD LEKSKRSLEA TVAEQRQQIE
DLEDELQTAE DMKLRLEVNM QALKAQYERD QAGREDQEEE ARKSLLKQLR EMEAELEDER
KQKAMAVNAR NKLQGDLSGM EQQVEMANKV KEDAVKQYKK LAAQIKDFHR ELDEARAARD
EIANQAKDNE KKVKNLEAEL IRLQEELGAA ERARRNAESE RDEMADEIGS SASGKQALID
EKRRLEAKIS ELEDDLEEEH TNAEMQADKA RKAQLQMEQM ATDLSSERTV SQKLENQRLA
LERQNKEMRE KLQELEGQNR ARTKATIAAL EGKVANLEEQ LDQEAKERAT LARTNRKMDK
RMKELVLQVE DERRGADQYK DQVDKMNNRV KALKRQLDDA EEEVTRSNGQ KRKLQRELDE
QMEANESMSR EMATLRKYRP SASRSSRSVM SSLRGSDTTL DEGGSEDGQD DQQS
//
