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Database: UniProt
Entry: I3IYE9_ORENI
LinkDB: I3IYE9_ORENI
Original site: I3IYE9_ORENI 
ID   I3IYE9_ORENI            Unreviewed;      1967 AA.
AC   I3IYE9;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Myosin X, like 1 {ECO:0000313|Ensembl:ENSONIP00000001639.2};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000001639.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000001639.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000256|ARBA:ARBA00004544}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   STRING; 8128.ENSONIP00000001639; -.
DR   Ensembl; ENSONIT00000001638.2; ENSONIP00000001639.2; ENSONIG00000001298.2.
DR   eggNOG; KOG4229; Eukaryota.
DR   GeneTree; ENSGT00940000164909; -.
DR   HOGENOM; CLU_001626_1_0_1; -.
DR   InParanoid; I3IYE9; -.
DR   OMA; NMEFMLA; -.
DR   TreeFam; TF316834; -.
DR   Proteomes; UP000005207; Linkage group LG19.
DR   GO; GO:0044295; C:axonal growth cone; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016459; C:myosin complex; 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   GO; GO:0048675; P:axon extension; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13202; FERM_C_MyoX; 1.
DR   CDD; cd17206; FERM_F1_Myosin-X; 1.
DR   CDD; cd14873; MYSc_Myo10; 1.
DR   CDD; cd13296; PH2_MyoX; 1.
DR   CDD; cd13297; PH3_MyoX-like; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.5.190; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 6.20.240.20; -; 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; 1.25.40.530; MyTH4 domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 4.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR031971; MYO10_CC.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR041797; MyoX_FERM_C.
DR   InterPro; IPR040640; MyoX_N_SH3.
DR   InterPro; IPR036124; MYSc_Myo10.
DR   InterPro; IPR000857; MyTH4_dom.
DR   InterPro; IPR038185; MyTH4_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000159; RA_dom.
DR   PANTHER; PTHR46049; AGAP003327-PA; 1.
DR   PANTHER; PTHR46049:SF9; UNCONVENTIONAL MYOSIN-X; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF16735; MYO10_CC; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF00784; MyTH4; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF18597; SH3_19; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00015; IQ; 2.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00139; MyTH4; 1.
DR   SMART; SM00233; PH; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 4.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51016; MYTH4; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS50200; RA; 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   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:UP000005207};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          56..730
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1134..1232
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1314..1419
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1443..1602
FT                   /note="MyTH4"
FT                   /evidence="ECO:0000259|PROSITE:PS51016"
FT   DOMAIN          1607..1952
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          1611..1721
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   REGION          609..631
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          784..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          914..1080
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        784..800
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..827
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        927..944
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        966..990
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1025..1039
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         150..157
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1967 AA;  224885 MW;  B4841FB38F32BB6C CRC64;
     LRIYFILEKE QLLPATVNSC GDGTLVVTTD YGEVFYLQQA EVTRERVYAM HQSSIDGVED
     MSALAELHEA AIMHNLYQRY QKDSIYTNIG SILAAVNPYK QIPGLYDLER VDLYSKHHLG
     ELPPHIFAVA NECYRCIWKR HDSQCILISG ESGAGKTEST KLLLQFLSVM SQNSAGTPPS
     EKSTRVEQAI VQSSPIMEAF GNAKTVYNNN SSRFGKFIQL HFSESGNIQG GCVIDCILNR
     VVRQNPGERN YHIFYALLAG ASKEQKSLYF LEDPAESYHY LSQSGCLKDK SLNDKELFNS
     VMEALKVLEF TEEEIRDMFK LLSGVLQLGN IEFMTAGGAQ ITTKQVVTNA SELLGLDAFQ
     LSEVMTQRSI ILRGEEICSP LTIEQAIDSR DSVAMALYSQ CFSWIILKIN QKIKGKENFK
     SIGILDIFGF ENFEVNRFEQ FNINYANEKL QEYFNKHIFS LEQLEYNREG VQWEAIDWMD
     NAECLDLIEK KLGLLALVNE ESRFPKGTDF TLLEKLHSRH STNPYYVKPR LADHQFGIKH
     YAGEVLYDVR GILEKNRDTF RDDILNMLKD SRLDFIYDLF EKVGSRNNEE KMGTARRKPT
     VSSQFRDSLH ALMATLSVSN PFFIRCIKPN MEKTPNVFDP EVVLNQLRYS GMLETVKIRR
     AGFPVRRTFK DFFSRYKIIL KEKVPTAGDD KKRTTDLLTK YDKTKKEWQL GKTKVFMKES
     LEQRLEKDRD EVRRQAAMII RAHLLTFSYF KRARASVITL QKHLRRHIQC KRFVKQRKAA
     VVLQKHRRGQ VARAHVRKLR GEKKKKEEEQ KTKEEEEKEK TLGEGETEEA KEEDEARQME
     EILQLEREIE RLQKKREDEV SQLCESSKQE LQLRRDAELK RMKKEASRKA TELIDLLNFG
     GVDPSLGAVG AKPAAEVKAS KGASTTRGAS KEEDVDEGFH AEEECIPLPD FPPPAETDAP
     VDQDIFAQLP PPPPAFAEGT VPPAPPPPKV SMVESLVDGE EPIYSMPADT ESDYDQEEEE
     GSVTAGDDSS VSGSNRGSAA VTDEEHPRKS TCTNASIESY RGSSDSYADS DDEHDGMMDT
     DEEVTNGRVT LLNGNGPPYF HGYLYMKAGL MIPWRRRWCV LKDETFMWFR SKQESLKSGW
     LYKKGGGLST LSRRNWKMRW FVLRDSKLMY YDNDSEEKLK GTIDIRAAKE IVDNHEKENA
     LNIVTDERTY QVFAESPEDA SGWFNVLSKV RVCTPEQLLE MSHEQANPKN AVGTLDVGLI
     DSVCASDNPD RPNSFVIITA NRVIHCNSDT PEEMHHWISL LQKPKGDARI DGQEFLVRGW
     LQKEMKTNAK STSLKLKKRW FVLTHNSLDY YKSSEKNSSK MGTLVLNSLC SVIQPDERVH
     RETGYWNIIV YGRKHSYRLY TKMLNEAMRW TAAIQGLIRD IKENSVNPEI VEQMYRRNPI
     LRYTQHPLHA PLLPLPYGEV TSLQRQQGYA SLQDEAVRVF NSLQEMETLA DTVPIIQGIL
     QTCQDLRPLR DEVYCQVIKQ TNHVPQPNSP ANRAHWHLLT CMSCTFLPSR AILRYLRFHL
     KRIRERYPGA EIERYATFIG ESLKKTKSRE FVPSQEEIAA LLLRQEMSTT VYCHGGGSCK
     ISINSHTTAG EVVEKLIRGL AMEESKNLFS LFEHNGFTDR ALESRVIVAD VLAKFERLAG
     SEEEEEEGEW KLYFKLYCFL DVESMPKEGV EFAFMFEQAH ESLISGHFPA SEETLQHLAA
     LRLQYLHGDG AGRAGWSLGS VYPIGRLRNR ILHSTKPGGV GTGVEKRKTP SFLDGTLRRS
     FKTGSLKKQK MEDEQMLEMW VKEETSATRT SVLEKWTRLQ GMPQHQAMLK YMSIIKEWPG
     YGSTLFDVEC KEGGFPHDLW LGVSADNMSV YKRGEPKPLE TFQYEHITFF GASQPCTYKI
     IVDEREMYFE TPLVGEITKI MRAYINMVVK KRCSIMSVSS VASAWGR
//
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