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Database: UniProt
Entry: A0A0N1HTE8_LEPSE
LinkDB: A0A0N1HTE8_LEPSE
Original site: A0A0N1HTE8_LEPSE 
ID   A0A0N1HTE8_LEPSE        Unreviewed;      1376 AA.
AC   A0A0N1HTE8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Putative myosin IB heavy chain {ECO:0000313|EMBL:KPI83118.1};
GN   ORFNames=ABL78_7859 {ECO:0000313|EMBL:KPI83118.1};
OS   Leptomonas seymouri.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX   NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI83118.1, ECO:0000313|Proteomes:UP000038009};
RN   [1] {ECO:0000313|EMBL:KPI83118.1, ECO:0000313|Proteomes:UP000038009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI83118.1,
RC   ECO:0000313|Proteomes:UP000038009};
RX   PubMed=26317207;
RA   Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA   Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA   Yurchenko V.;
RT   "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT   Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT   donovani.";
RL   PLoS Pathog. 11:E1005127-E1005127(2015).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {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:KPI83118.1}.
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DR   EMBL; LJSK01000435; KPI83118.1; -; Genomic_DNA.
DR   EnsemblProtists; KPI83118; KPI83118; ABL78_7859.
DR   VEuPathDB; TriTrypDB:Lsey_0435_0030; -.
DR   OMA; AHMQFYR; -.
DR   OrthoDB; 1094820at2759; -.
DR   Proteomes; UP000038009; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00065; FYVE_like_SF; 1.
DR   CDD; cd00201; WW; 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; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13140:SF729; HEAVY CHAIN, UNCONVENTIONAL MYOSIN; 1.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          11..790
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          886..925
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          1053..1115
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          237..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          661..683
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1235..1269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1281..1376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1254..1268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1292..1376
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         122..129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1376 AA;  152587 MW;  AECACC3CC4D42C77 CRC64;
     MTSEYKLRET VGVEDLVLLP QITEKAITDD LAVRYRSDLI YTNIGSVLLV VNPFKQIPGL
     YNEAHMQFYR HSGRLGGAQD ALLEAQEPGD AAIGGPHIFA LAEDTYRRMV SEEENQCVII
     SGESGAGKTE ASKQIMQYIS AVSGNTSDMQ KVKRIILESN PLLEAFGNAK TLRNDNSSRF
     GKFLEVYFDI RGGPVGGHLS HFLLEKSRVS SQQEGECNFH ILYQLCVGAA MALEESATAS
     HKTHPGKGTK DYVEEGESDL EDDSPIAWAE LFTEMHMQGL SDTAGYTRLG PASNVYPWKY
     LRPTIASGRH ADNFTPRTGI DDAQGWKETL LAMEAMGMTK GDQISVIKVL CLVLHFGELE
     FVAPAEGGEL AAGQQPCTLA NPEVLDLIAQ HLGVDAKALF KALTWRKLQV GATEVVFSPL
     DAQQCRNTRD AIARALYEGV FEFIVSSVNI AFGDAPHALM LGVLDIYGFE IFAKNGFEQF
     CINYVNEKLQ QIFIELTLRV EQEEYVRENI PWEAIKYFDN QIVCDLIESN RPPGMFAIID
     DVCITMAKEE ESVADRKLLD KLDMNYHSHP NFVRSERGFI IKHYAGDVEY STDGFIGRNK
     DRLGADVVEA LTQCKNSFVL EILTEVLADG MAAGSPTGAS AGAGATMRRT TTAGFKIRQQ
     AADLMRTLKQ CTPHYVRTIK SNDMKRGNFF DEARVLHQVK YLGLLENVRV RRAGYSYRQY
     FDKFLKRFKY TCPSTYPRPF RGTDKAACET ILSYLQNDHA VLPPQSYAIG TNKVFIRQPE
     HVLALEQSRE AAFHSLSVTI QRAWRRYTQR KQLLRLKAKL DRSYQRRGKV RRADSVFRAY
     EGLYVDLDSV VAAAGLQTAL GAAGGTLPRA LSSRLAVAAD AMFHFDPIAR AWHAFWSSSV
     EAGQPRRKFF VNALTQETVW ERPREVDPPR LVFSCVAERL VNWATAKTVR EFIFVTSHDV
     LYVVRERPRM EDVPADGTES SKKKRKEAKA KAVANQGAGG EVALEPCFTL QKRLDLRLLT
     QVAVTAMADT VLVLRMLPVL APYRPVLDTV KTKTGPVQCE TCGRKATPAM RRANCPSCGR
     LCCVRHCLIH ARPLPTMNGH TKPVHVCPAC VVGEPLEAVS DMVLLTPFKT ELAGTLCTHY
     QERMGNPLPL LVSSSIPFSV WTPAPPLVGK RKAPSSAGKA KGRKGAAVAT AGEAEELPGV
     LGGSYEVTLT CVASDDALTA DTVLVPAISC AALEAQPEAD KRSSRKSAVV VKPTKKRTKQ
     DEDDLSAVPA DTPKVLTVVS PHGITASQIQ RMEAAREERR KAAAARRRQE EEEERKRESQ
     REAERAAEHR RLVQERKKAK AAETARMEAE RAAHAKAAAD RREEAARLVA ERARRR
//
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