ID W5N2N0_LEPOC Unreviewed; 1824 AA.
AC W5N2N0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Myosin-4-like {ECO:0000313|Ensembl:ENSLOCP00000014889.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000014889.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000014889.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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 EMBL; AHAT01000314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01000315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01000316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7918.ENSLOCP00000014889; -.
DR Ensembl; ENSLOCT00000014918.1; ENSLOCP00000014889.1; ENSLOCG00000012091.1.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000164626; -.
DR HOGENOM; CLU_000192_8_1_1; -.
DR InParanoid; W5N2N0; -.
DR OMA; ATENKXD; -.
DR Proteomes; UP000018468; Linkage group LG10.
DR Bgee; ENSLOCG00000012091; Expressed in muscle tissue and 7 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0048731; P:system development; IEA:UniProt.
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; -; 5.
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 InterPro; IPR014751; XRCC4-like_C.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF44; MYOSIN-13; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 2.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 5.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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:UP000018468}.
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 86..780
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 1765..1824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1824 AA; 209626 MW; 6E2F2723AC1ED7DB CRC64;
MSTDAEMAVF GPAAIYLRKP EKERIEAQNK PFDAKTAVFV SEPKELYLKG ILQSKEGGKA
TVKTEGGQTL TVKEDEVFPM NPPKFDKIED MAMMTHLNEA SVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNPEVV AAYRGKKRME APPHIFSVSD NAYQNMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA AIGEKKKEQT SGKMQGTLED QIISANPLLE AFGNAKTVRN
DNSSRFGKFI RIHFGTSGKL ASADIETYLL EKSRVTFQLS DERSYHIFYQ IMTNHKPELI
EMLLITTNPY DFPMISMGQI SVASIDDKEE LVATDTAIDI LGFTPEEKNG IYKLTGAVMH
HGNLKFKQKQ REEQAEPDGT EVADKIAYLM GLNSADLLKA LCYPRVKVGN EFVTKGQTVQ
QVNNAVGALA KSVYEKMFLW MVIRINQMLD TKQPRQFFIG VLDIAGFEIF DFNSLEQLCI
NFTNEKLQQF FNHHMFVLEQ EEYKKEGIEW EFIDFGMDLA ACIELIEKPM GIFSILEEEC
MFPKASDTTF KNKLYDQHLG KTNCFQKPKP AKGKAEAHFS LVHYAGTVDY NVSGWLDKNK
DPLNESVVQL YQKSSVKLLA LLYASFSSTE AESGGKKGGK KKGGSFQTVS ALFRENLGKL
MTNLRSTHPH FVRCLIPNES KTPGLMENFL VIHQLRCNGV LEGIRICRKG FPSRILYGDF
KQRYKVLNAS AIPEGQFIDS KKASEKLLGS IDVDHTQYKF GHTKVFFKAG LLGTLEEMRD
EKLAALITCT QALCRGYLMR KEFVKMMERR ESIYTIQYNI RSFMNVKHWP WMKLYFKIKP
LLKSAEAEKE MANMKEEFAK CKEDLAKAEA KRKELEEKMV SLLQEKNDLQ LQVQSEMEGL
SDAEERCEGL IKNKIQLEAK VKEISERLED EEEMNAELTA KKRKLEDECS ELKKDIDDLE
LTLAKVEKEK HATENKVKNL TEEMASQDES IAKLTKEKKA LQEAHQQTLD DLQAEEDKVN
TLSKAKTKLE QQVDDLEGSL EQEKKLRMDL ERAKRKMEGD LKLSQETVMD LENDKQQSEE
KIKKKDFEIS QFLSKIEDEQ ALGAQLQKKI KELQARIEEL EEEIEAERAA RAKVEKQRSD
LSRELEEISE RLEEAGGATS AQIEMNKKRE AEFQKLRRDL EEATLQHEAT AAALRKKQAD
SVAELGEQID NLQRVKQKLE KEKSEYKMEI DDLSSNMEVV AKAKANLEKM CRTLEDQLSE
LKTKSDENLR QINDISAQKA RLQTENGEFV RQLEEKEALV SQLTRGKQAF TQQTEEMKRQ
LEEEIKAKNA LAHGLQSARH DCDLLREQYE EEQEAKAELQ RCTELFKMKN SYEEALDHLE
TLKRENKNLQ QEISDLTEQI GETGKTIHEL EKAKKQVETE KTEIQTALEE AEASLEHEES
KILRVQLELN QIKSEVDRKI AEKDEEIEQM KRNNQRIVDT MQSSLDAEIR SRNDALRIKK
KMEGDLNEME IQLSHSNRQA AEAQKQLRNV QGQLKDAQLH LDDALRGQED MKEQVAMVER
RNNLMQAEIE ELRVALEQTE RGRKVAEQEL LDASERVQLL HSQNTSLINT KKKLESDIAQ
LQGEVDDTIQ EARNAEEKAK KAITDAAMMA EELKKEQDTS AHLERMKKNL EVTVKDLQHR
LDEAEQLAMK GGKKQLQKLE TRVRDLENEL EAEQRRGVEA IKGVRKYERR VKELTYQAEE
DKKNVNRLQD LVDKLQLKVK AYKRQAEEAE EQANSHLAKF RKVQHELEES EERADIAESQ
VNKLRAKSRD MGSKFRKVQH ELEE
//
