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Database: UniProt
Entry: W5N1X9_LEPOC
LinkDB: W5N1X9_LEPOC
Original site: W5N1X9_LEPOC 
ID   W5N1X9_LEPOC            Unreviewed;      1936 AA.
AC   W5N1X9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLOCP00000014638.1};
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:ENSLOCP00000014638.1, 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:ENSLOCP00000014638.1}
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; AHAT01000310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7918.ENSLOCP00000014638; -.
DR   Ensembl; ENSLOCT00000014667.1; ENSLOCP00000014638.1; ENSLOCG00000011877.1.
DR   eggNOG; KOG0161; Eukaryota.
DR   GeneTree; ENSGT00940000163461; -.
DR   HOGENOM; CLU_000192_8_1_1; -.
DR   InParanoid; W5N1X9; -.
DR   OMA; TIQYNFR; -.
DR   Proteomes; UP000018468; Linkage group LG10.
DR   Bgee; ENSLOCG00000011877; Expressed in embryo and 6 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; -; 5.
DR   Gene3D; 1.20.5.370; -; 4.
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; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 6.
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          1887..1936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         181..188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1936 AA;  222831 MW;  8408E967D15DD5A7 CRC64;
     MSGDSEMSIF GEAAKYLRKS EKERLEAQSR AFDARTACFV DDDKELYVKG VIQSKEGGKV
     TVKTEDNRTV TVKDNQVYPL NPPKFDKIED MAMMTHLNEP CVLYNLKERY AAWMIYTYSG
     LFCVTVNPYK WLPVYNPEVV AAYRGKKRME VPPHIFALSD NAYQFMLTDA DRENQSILIT
     GESGAGKTVN TKRVIQYFAS IATSGDKKKA EYTSKMKGTL EDQIIQANPL LEAFGNAKTV
     RNDNSSRFGK FIRIHFAASG KLSSADIETY LLEKSRVTFQ LSSERNYHIF YQLTCNKKPE
     LIEMLLISSN PYDFTYISQG EVAVKSIDDA AELMATDEAI DILGFSADEK NGIYKLTGAV
     MHYGNLRFKQ KQREEQAEPD GTEVADKAAY LMGLNSSEFL KCLCYPRVKV GNEYVTKGQS
     VQQVYNSVGA LGKSVYEKMF LWMVIRINQQ LDTKQARQQF IGVLDIAGFE IFDFNTLEQL
     CINFTNEKLQ QFFNHHMFVL EQEEYKKEGI DWEFIDFGMD LAACIELIEK PMGIFSILEE
     ECMFPKSTDT SFKNKLYDQH LGKSASFLKP KHVKGKAEAH FSLGHYAGTV DYNISGWLEK
     NKDPLNESVV QLYQKSSLKL LSFLYSSYAG DDAGAKKGGK KKGSSFQTVS ALFRENLNKL
     MSNLKTTHPH FVRCLIPNET KTPGAMENHL VVHQLRCNGV LEGIRICRKG FPSRIQYGDF
     KQRYRVLNAS AVPEGQFMDN KKASEKLLGS IDIDHTQYKF GHTKVFFKAG LLGVLEEMRD
     ERLAQLVTCI QSVCRGNLMR NEFKKMMERR ESLFTIQYNI RSFMNVKHWP WMKLYFKIKP
     LLMSAEAEKE MANMKEEFAK CKEDLAKSEA RRKELEEKMV SIIQEKNDLF IQVQAEADNL
     TDAEERCEGL IKSKIQLEAK LKEITERLED EEEMNAEMTA KKRKLEDECS ELKKDIDDLE
     LTLAKVEKEK HATENKVKNL TEEMGSLDEN ISKLSKEKKA LQEAHQQTLD DLQVEEDKVN
     TLNKAKTKLE QQVDDLEGSL EQEKKIRLDL ERAKRKLEGD LKLAQESIMD LENEKQQMEE
     KLKKKDFEVT QLQGRIEDEQ VLGSQLQKKI KELQARIEEL EEEIEAERAA RAKVEKQRAD
     LSRELEDISE RLEEAGGATS AQIEMNKKRE AELQKLRRDL EEATLQHEAT AAALRKKHAD
     TVADLGEQID NLQRVKQKLE KEKSELKMEV DDLSSNMEAV SKSKANLEKL CHSLEDQLLE
     VKVKEDENHR LISDLTAQKS RLQTENGELY RQLEERESLV SQMTRVKQAF SQQIEELKRQ
     NEEDTKAKNA LAHALQSSRH DCDLLREQFE EEQEAKAELQ RSMSKANSEV AQWRTKYETD
     AIQRTEELEE AKKKLAQRLQ EAEEAIEATN SKCSSLEKTK QRLQGEVEDL MMDVEKANAA
     AAILDKKQRN FDKILAEWKQ KYEETQAELE SALKEVRSIG TENFKMKNAY EESLEHLETL
     KRENKNLQQE ITDLTEQLGE NGKSIHELEK ARKQAEQERG EIQSALEEAE ASLEHEEGKI
     LRVQLELNQV KSEIDRKIAE KDEEIEQLKR NNQRVIDTLQ STLDAEVRSR NDALRMKKKM
     EGDLNEMEIQ LSHANRQASE SQKQLRNIQA QLKDAQLHLD DALRGHEDMK EQVAMVERRN
     NLMQAEIEEM RAALEQTERG RKVAEQELLD SSERVQLLHS QNTSLINSKK KLESDLTQCQ
     GEIEDAIQEA RNAEEKAKKA ITDAAMMAEE LKKEQDTSAH LERMKKNLEV TVKDLQHRLD
     EAEQLAMKGG KKQLQKLETR VRELENELEA EQKHGADAIK GVRKYERRVK ELTYQCEEDK
     KTVARLQDLV DKLQLKVKAY KRQAEEAEEQ ANSHLSKFRK VQHELEEAEE RADIAESQVN
     KLRAKSRDIG AKGKED
//
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