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Database: UniProt
Entry: D2V147_NAEGR
LinkDB: D2V147_NAEGR
Original site: D2V147_NAEGR 
ID   D2V147_NAEGR            Unreviewed;      1826 AA.
AC   D2V147;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Myosin {ECO:0000313|EMBL:EFC49629.1};
GN   ORFNames=NAEGRDRAFT_78120 {ECO:0000313|EMBL:EFC49629.1};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN   [1] {ECO:0000313|EMBL:EFC49629.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC49629.1,
RC   ECO:0000313|Proteomes:UP000006671};
RX   PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA   Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA   Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA   Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA   Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT   "The genome of Naegleria gruberi illuminates early eukaryotic
RT   versatility.";
RL   Cell 140:631-642(2010).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; GG738847; EFC49629.1; -; Genomic_DNA.
DR   RefSeq; XP_002682373.1; XM_002682327.1.
DR   SMR; D2V147; -.
DR   STRING; 5762.D2V147; -.
DR   EnsemblProtists; EFC49629; EFC49629; NAEGRDRAFT_78120.
DR   GeneID; 8856442; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_78120; -.
DR   eggNOG; KOG0162; Eukaryota.
DR   InParanoid; D2V147; -.
DR   OrthoDB; 5476192at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
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   CDD; cd00124; MYSc; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR010926; Myosin_TH1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF679; UNCONVENTIONAL MYOSIN IC; 1.
DR   Pfam; PF00063; Myosin_head; 3.
DR   Pfam; PF06017; Myosin_TH1; 4.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51757; TH1; 4.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-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|PROSITE-ProRule:PRU00782};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT   DOMAIN          19..841
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          847..1053
FT                   /note="TH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51757"
FT   DOMAIN          1066..1250
FT                   /note="TH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51757"
FT   DOMAIN          1297..1480
FT                   /note="TH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51757"
FT   DOMAIN          1526..1703
FT                   /note="TH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51757"
FT   REGION          108..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         176..183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1826 AA;  209927 MW;  10AB3662DBEE21D0 CRC64;
     MCDDLTLLLS QSSMKSKKSE QMVVPQKTEI TEIDLTNILA NRYYQNEIYT CVGPAILSIN
     PYKAVKGLYS NETKALFHSH IPYELAPHIY SLAEDAYRTL LEHATANKPT STHVTRARPA
     ITAVSSSSAH SKKMPPPPPP GKPINKEADL DDDTFIINDF SISDGIGVGQ AIIIQGESGS
     GKTLASRIIM EYLAAVSISG LETQRIKDSI LQSNPLLESF GNAKTLRNNN SSRFGKFTNL
     YFNFKGQLMG GELTTILLEK ARVVKRRLGE RNFHIFYQLL SDDYIRKQLN LGFPEEYNYL
     NNNVININEV DDKSEFETTK RAMDLLDMSV PEQMAVFKIV AAILQLGNIT FTAIEDPEER
     KRRNIAPGVE ACDVSNEASL KLVANTLQID AEFLRRSMII RVIKTVGSPM PIEQTQSVEQ
     AEFNRDTLAK NIYERLFLWL VKRVNRALRV PDYEDFVAKK NSETYYNIGI LDIYGFEIYD
     KNIGTGKIVD QDEASNQGKL KNGFEQLCIN FVNEKIQSGV QRSIKKEQED IQKEIYGDDF
     KPTLASTQER NKRFDSDAAI QMIAGKPISV FSLLDEESMF PNGNDVNYVQ KMKTNIKHPY
     FKIPRIAEPT EFELEHFAAL VKYNTADGWV DKNRDTLLAE MLYTMQNTKD HLLMALFPKN
     EQANDVLSKK PANAGTKLQQ TTAEKFLRDV SKLMNQLSSC SLKHHHIRCI IPNYEGRADD
     FQKDVVNHQV RYLGILDTVL SRKADDLGSN VTGYSIKIPY DTFLERYKLL CPETFPYWET
     FITNKYGPVE EFTIEHKKEA VHQILSQEHI GMTNPQDFFL GRGNVLLASP VQLFQLDEMI
     REQKHEMARK IQNSFRRYRK KRAGKMEEMM KKAIKTTEPT KQKEAPEEIR IRHDGFRTSN
     FGETKKRVLI TGSDRRNIFL LDTTSSSSEF EQLRKIAIRD IKKIYISPYS DNYMIFKLDM
     DEGDELVELD NKWEFLEEFN KLIESTASNF KGEHVPRVEV TKDISILNHQ KDKNTGTQNL
     LVRFIPSAYN TKKTVTTECY ADEFDNRLFI VNTFTQADIY NQRKLRRKAS LYAKQDQNRD
     YLRMQNSELM QLLKKDYDDS KVLFSGVVSK YNKRFKKQDR IFMVTDKAIY NIDPSGGYLI
     NRRVPIGQVT SVTVSPYTDN FFVVDHPDQD ILSESAKKTE ILESILESFQ NATNQLLPVK
     VTTNYYINLA KKNTKRVAIS WIIEPENQTQ FSVSTLVPNT AGGADVHVVS EVDNDNDKSM
     NDLAVRQSFQ RRSVRGKMVK NGDMDEVDLN DVFGGLKVRR KDSLLVWFQG DYLNFKDNPK
     FIEMVKKHDP EWNGQVLFSN LMTKVNKRFR TQPRKVVVTP NYIYTLDDEK LHFNRITPIK
     DLSGISLSTM RDAFFVVHCP TDHDLFASCK KKTELVSVIC DAFKDKTGMD LPVHVEDKFV
     YKPSTDVKGV KTIEFRHDPT TKVPILTPTK LGCLIQVNNS DPEKVKQNLP TAKQQKPAAT
     PQLKLYEGSD ERGIQDKMDS IYTGRKGRNR RSLLREYLGD YLRLEGTQRM KKVFDRNGDT
     ELIFSGQVLK YNKNFKKQHR LLVVTDKNVY NIDEQEFKIK RKIPLEEITG VSVSPFDDNV
     FVMHCPTSGD YLLEDEKKTE IISALQNARL RHLKQPLKIN VDDQFNFAPN SSSTMPVTFI
     SDDHCKDTWA ENRANALVVH VKRQEPGVVL EAAYLYLNEE SKPIEVKSTP ILIKLKKRWT
     YKLQIRFYVN EYLAGCEFHE KIDTVSSRLE FVSKVVELEP KEERYVITLP ERKVIYSLLS
     KTRVKCKLVD PSGKVLMAVR FVYDIQ
//
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