ID A0A087XKQ2_POEFO Unreviewed; 1831 AA.
AC A0A087XKQ2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Myosin X, like 1 {ECO:0008006|Google:ProtNLM};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000006355.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000006355.2}
RP IDENTIFICATION.
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; AYCK01013440; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 48698.ENSPFOP00000006355; -.
DR Ensembl; ENSPFOT00000006366.2; ENSPFOP00000006355.2; ENSPFOG00000005639.2.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000164909; -.
DR Proteomes; UP000028760; 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-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13202; FERM_C_MyoX; 1.
DR CDD; cd17206; FERM_F1_Myosin-X; 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; 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:SF4; UNCONVENTIONAL MYOSIN-X ISOFORM X1; 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 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};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..1831
FT /note="Myosin X, like 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012587885"
FT DOMAIN 1..476
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 982..1080
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1162..1267
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1305..1465
FT /note="MyTH4"
FT /evidence="ECO:0000259|PROSITE:PS51016"
FT DOMAIN 1470..1816
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 1474..1523
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 356..378
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 551..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..753
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1831 AA; 211124 MW; DBE0400490D048C1 CRC64;
MFYFIYMLCL HTCVADMYLL SEGPESYHYL SQAGCVQDSS LDDKQLFNSV MEALKVMEFS
EEEIRDVFKL LSAVLQMGNI EFMTAGGAQI TSNGVVSNVS ELLGLDSFQL SEVLTQRSMI
LRGEEICSPL TVEQAVDSRD SVAMALYSQC FSWIIMRINQ KIKGKDNFKS IGILDIFGFE
NFEVNRFEQF NINYANEKLQ EYFNKHIFSL EQLEYNREGI QWEAIDWMDN AECLDLIEKK
LGMLALINEE SRFPKGTDYT LLEKLHSRHA TNPYYVKPRV TDHQFGIKHY AGEVLYDVRG
ILEKNRDTFR DDILFILKDS RLDFIYDLGS RSGDETLKMG TARRKPTVSS QFRDSLHSLM
ATLSASNPFF VRCIKPNMDK KANRFDPDVV LNQLRYSGML ETVKIRKAGF PVRRTFKDFF
SRYKMIHKNK TASAEEKSCC LEVLTLHDNT KKEWQLGKTK VFLKEALEQR LEKEREEVRR
RAGMVIRAHI LSYVARKQYK RVLYSVVTIQ KNYRAHFWRR AFVRLRLAAV ILQKHRRGQL
ARSVCHKLRE EKRRREEEEK KRREEEEERR RLEDERERME EEERRKEEER LKEEEEGKRR
AEEEEEQRLM KEKEEQQKLA AKGDTTRNSL VNGACPKQDL TQTPSYNHTS EEESRQMEEI
LRLEREIERL QKQQEDGVSL LGDVSREELR QMRDAEIYRL EKEASRVATE FLELLDFGGL
EPSLSSEENL HEVNESAAPL AEEEVDEGFP AEDECVPLPD FPPPAAVPLD TDVFQSIPPP
PPAFAEGVTV SSSSGPHSGP EKLPPATTNG LNHTPIVTDS QTRPPPPSPL IVTNGERQPC
QTTTRTLDFV PLNDVPSQSN LPDAESDYDQ EEFEEAHGSS GASINDGHIT DEEVLRESSC
TQNSLDSFRG SSDSFIDSDE ENDGYVDTDE EISNGRVSLL NGTGPPYFHG YLYMKGGLMI
PWRRRWCVLK DETFMWFRAK QDSLKSGWLY KKGGGMSTLS RRNWKMRWFV LREAKLMYFE
NDSEEKLKGT IDIRAAKEIV DNHEKENALN IVTEERTYQI YAESPEDASG WFNVLSRVHS
ASPEQLLEMH HEQANPKNAV GTLDVGLIDS VCASDNPDRP NSFVIITANR VIHCNTDTPE
EMHHWIGLLQ KSKGDTKVDG QEFLVRGWLH KEMKSGAKST SLKLKKRWFV LTTNSLDYYK
SSERNTTKLG TLVLNSLCSV VQPDEKVFKD SGYWNIIVYG RKHSYRLYTK MLNEAMRWAN
AIQGVIDNKV PIETPTQQLI RDIKESSLNV EAVEQTYWRN PILRYTQHPL HSPLLPLPYG
DVSVHLQKEK GYTSLQDEAV KIFNSLQEME AVSDPVPIIQ GILQTCQDLR PLRDEVYCQL
IKQTNHVPHP NSPANRAHWH LLTCMSCTFL PSRGILRYLK FHLKRIKELF PGTEIEMFAH
FIGESLKKTK MREFVPSQEE IVALLTRQEM TTTVYCHGGG SCKISINSNT TAGEVVEKLI
RGLAMEDSRN MFALFEHNNT VDKAVESRVL VADVLAKFER LAGSEEARDE GQWRLYFKLY
CFLDVESMPK EGVEFAFMFE QAHESLTRGH FPAREETLQH LAALRLQFLF GDKTRIAWNL
ENVYPVGRLR NRILQFTKAG GASGSGQTLE RRRTSFLDGT LRRGLKTGSM KKQRMEEEQM
LEMWIKEEMS ATRASIVEKW SHLKGLDQHQ AMLKYMSIIK EWPGYGSTLF DVECKEGGFP
HDLWLSVSAE NVSVYKRGEP KPLETFPYEH IVFFGAPQPC TYKITVDERE MFFETPEVGE
ITKIMKAYIN MIVKKRCSVK SVSSYGTNWI R
//
