ID A0A3P9NHF1_POERE Unreviewed; 2070 AA.
AC A0A3P9NHF1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Unconventional myosin-X-like {ECO:0000313|Ensembl:ENSPREP00000009015.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000009015.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000009015.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000009015.1};
RG Ensembl;
RL Submitted (SEP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_008397965.1; XM_008399743.2.
DR STRING; 8081.ENSPREP00000009015; -.
DR Ensembl; ENSPRET00000009124.1; ENSPREP00000009015.1; ENSPREG00000006160.1.
DR GeneID; 103458733; -.
DR CTD; 566674; -.
DR GeneTree; ENSGT00940000164909; -.
DR OMA; NMEFMLA; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000006160; Expressed in head.
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; PF00788; RA; 1.
DR Pfam; PF18597; SH3_19; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00295; B41; 1.
DR SMART; SM00015; IQ; 3.
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; 2.
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:UP000242638};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 63..739
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1197..1296
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1378..1483
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1521..1680
FT /note="MyTH4"
FT /evidence="ECO:0000259|PROSITE:PS51016"
FT DOMAIN 1685..2055
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 1689..1732
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 618..640
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 804..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1871..1913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..850
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..958
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1036
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1891..1913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 157..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2070 AA; 235123 MW; BC86B84AD6B3213F CRC64;
MESFFTEGAR VWVREKEQLL PATVNSCGDG TLVVTTDYGE VFYLQQAEVT RERVYAMHQS
SIDGVEDMSA LAELHEAAIM HNLYQRYQKD NIYTNIGSIL AAVNPYKQIP GLYDLDRVDL
YSKHHLGELP PHIFAVANEC YRCIWKRHDS QCVLISGESG AGKTESTKLL LQFLSVMSQN
SIAAPQSERT THVEQAIVQS SPIMEAFGNA KTVYNNNSSR FGKFIQLHFS ECGNIQGGCV
IDYLLEKNRV VRQNPGERNY HIFYALLAGA SNEDKSLYFL EEPAESFHYL SQSGCLKDKS
LNDKELYNSV MEALKVLGFT EEEIRDMFKL LSGVLQLGNM EFMLAGGAQI TTKQVVSNAS
ELLGLDAFQL SEVLTQRSII LRGEEICSPL TIEQAIDSRD SVSMALYSQC FSWIILKINQ
KIKGKENFKS IGILDIFGFE NFEVNRFEQF NINYANEKLQ AYFNKHIFSL EQLEYNREGV
QWDAIDWMDN AECLDLIEKK LGLLALVNEE SRFPKGTDFT LLEKLHSRHS TNPYYVKPRV
ADHQFGIKHY AGEVLYDVRG ILEKNRDTFR DDILNMLKDS RLDFIYDLFE KVGSRNNEEK
MGTARRKPTV SSQFRDSLHA LMATLSASNP FFIRCIKPNM EKNPNVFDPE TVLNQLRYSG
MLETVKIRRA GFPVRRTFKD FFSRYKIIIN DKVPAAGDDK KRSTDLLTKY DKTKKEWQLG
KTKVFMKESL EQRLEKDRDE IRRQAAMIIR AHLLTFSAKK RFKQVRSSIV VLQKHLRRHV
QRRQFVKKRR AALVLQKHRR GQVARTRVRK LREEKKKREE EQRKEEEEEK KKSGGEENEE
VNEDDKKDEA RQMEEILQLE KEIERLQKKR EDEVSQLCES SKQELQLRRD AELKRMKKEA
SRKATELIDL LNFGGVDPSA EAVGAKPAAE AKTAKAVSTA GGASKEEDVD EGFHAEEECI
PLPDFPPPAE SDAPIDQDIF VHLPPPPPAF AEGTVPPAPP PLPADSDPAA GIPPPPPLPP
PGDGATIPPP SSLPPPAEGE KTEETKTDSE RKVSMVESLV DGEEPIYSMP ADTESDYDQE
DEEGSVNAGD DSSVSGSNRG SATVTDEEHP RKSTCTNTSV ESYRGSSDSY ADSEDEHDGM
MDTDEEVTNG RVTLLNGNGP PYFHGYLYMK AGLMIPWKRR WCVLKDETFM WFRSKQESLK
SGWLYKKGGG LSTLSRRLNW KMRWFVLRDS KLMYYENDSE EKLKGTIDIR AAKEIVDNHE
KENALNIVTD ERTYQVFAES PEDASGWFNV LSKVRVCTPE QLLDMSHEQA NPKNAVGTLD
VGLIDSVCAS DNPDRPNSFV IITANRVIHC NSDTPEEMHH WISLLQKPKG DARIDGQEFL
VRGWLHKEMK TNAKSTSLKL KKRWFVLTHN SLDYYKSAEK NSSKMGTLVL NSLCSVIQPD
ERVHKETGYW NIIVYGRKHC YRLYTKMLNE AMRWTAAILG VIESKTPIET PTLQLIRDIK
ENSVNAEIVE QMYRRNPILR YTQHPLHSPL LPLPYGEVTS LHRQQGYASL QDEAVRVFNS
LQEMETLADT VPIIQGILQT CQDLRPLRDE VYCQVIKQTN HVPQPNSPAN LAHWHLLTCM
SCTFLPSRAI LRYLRFHLKR VRERYPGTEI ERYASFIGES LKKTKTREFV PSQEEIAALL
LRQEMSTTVY CHGGGSCKIS INSHTTAGEV VEKLIRGLAM EDSKNLFSLF EHNTFTDRAL
ESRVIVADVL AKFERLAGSE EDEEEGEWKL YFKLYCFLDV ESMPKEGVEF AFMFEQAHES
LISGHFPASE ETLQHLAALR LQYLHGDGAG RAGWSLGSVY PIGRLRNRIL QSTKPGVSAA
GGAGSRGSGG IGDVIGTIGG QGGTGASTEK RKTPTFRDSS LRKSKTGSLK KQKVEGEQRL
EMWVKEETSA TRTSILEKWA RLQGMPQHQA MLKYMSIIKE WPGYGSTLFD VECKEGGFPN
DLWLGVSADN VSVYKRGDPK PLETFQYEHI TFFGASQPCT YKIIVDEREM YFETPQVGEI
TKIMKAYINM MVKKRCSIMS VSSVSSSWAR
//
