ID V8P5L3_OPHHA Unreviewed; 1409 AA.
AC V8P5L3;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 22-FEB-2023, entry version 40.
DE SubName: Full=Myosin-X {ECO:0000313|EMBL:ETE69172.1};
GN Name=MYO10 {ECO:0000313|EMBL:ETE69172.1};
GN ORFNames=L345_05024 {ECO:0000313|EMBL:ETE69172.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE69172.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE69172.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE69172.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
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}.
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:ETE69172.1}.
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 EMBL; AZIM01000833; ETE69172.1; -; Genomic_DNA.
DR Proteomes; UP000018936; 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:InterPro.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
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; cd13296; PH2_MyoX; 1.
DR CDD; cd13297; PH3_MyoX-like; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 6.20.240.20; -; 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; 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:SF2; UNCONVENTIONAL MYOSIN-X; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00612; IQ; 2.
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 SMART; SM00295; B41; 1.
DR SMART; SM00015; IQ; 3.
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 Motor protein {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Myosin {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936}.
FT DOMAIN 1..96
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 559..657
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 739..844
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 882..1042
FT /note="MyTH4"
FT /evidence="ECO:0000259|PROSITE:PS51016"
FT DOMAIN 1047..1392
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 1051..1093
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 175..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1409 AA; 162716 MW; D43931F312C98D3B CRC64;
MPDQFDQNVV LNQLCYSGML ETVRIRRAGF PVRRPFQDFH KRYKILMRNL TLPEDLKGKC
TALLYLYDST KTEWQLGKSK VFLRESLEHM LEKQREIEVG KAAMIIRAHV LGYMARKHYK
KVLYYVVIIQ KNYRAFYLRR RYLLLKKAAI TFQKQVRGLI ARRIYKQLLE EKKQQEEGKR
QREEEKRKQQ KMEAERLAQQ AKEALVVIPK PPKELKQELE RQKENKQVEE ILRLEKEIED
LQRMKEQQEL TLTEASLQRL QQLRDDELKR LEDEACRAAQ EFLESLNFDE IDECVRNIER
TLSVSSSFCA ELSGTTGTEK PNFNFSQPYP EEEVDEGFEA DDDAFKDSPN PSEHGHSDQR
TSGIRTSDDS SEEDPYMNDT VVPASPATGN NTIIPSILDS LSLHNSSSGE STYCMPENVS
RQPPNASELI SPEADYDYDQ DDYEDGAITS GSSVTFSNSH SSQWSPDYRC SIGTYNSSGA
YRFSSEGAQS SFEDSEEDFD SRFDTDDELS YRRDSVYSCV SLPYFHSFLY MKGGLINTWK
RRWCVLKDET FLWFRSKQEA LKQGWLHKKG GGSSTLSRRN WKKRWFVLRQ SRLMYFENDG
EEKLKGTLEI RSAKDIIDNT CKENGIDIVM TDRTYHLIAE SPEDASQWFS VLSQVLTSTE
QEIREMHDEQ ANPQNAMGTL DVGLIDSVCA SDSPDRPNSF VIITANRVLH CNADTPEEMH
HWITLLQRSK GDTRVEGQEF IVRGWLHKEV KNSPKMSSLK LKKRWFVLTH NSLDYYKSSE
KNALKLGTLV LNSLCSAVPP DEKIFKETGY WNVTVYGRKH CYRLYTKLLN EATRWSSAIQ
NVIDTKAAID TPTQQLIQDI KENCLNPEVV EQIYKRNPIL RYTQHPLHSP LLPLPYGDIN
LNILRDKGYT TLQDEAIKIF NSLQQLESVP DPIPIIQGIL QTGHDLRPLR DELYCQLIKQ
TCKVPNTGSL GNLYSWQILT CMSCMFLPSR SILKYLKFHL KRIHDQFPGT EMAKYALFIY
ESLKKTKGRE FVPSRDEIET LINRQEMTST VYCHGGGSCK ITINSHTTAG EVVEKLIRGL
GMEDSRNMFA LFEYNGITDK AIESRTVVAD VLAKFEKIGA TSEGDHAAWK FYFKLYCFLD
IEHVPKDSVE FAFMFEQAHE AMIQGHFPAP EETLQVLAAL RLQYLQGDYS SSNVTVPEME
DVYPLQRLKS RIVQSTKIFV PTERFERKRN NFLEGTLRRS FRSSSVTKQK MEEDQMLNMW
VREEISAART SMLDKWKKMQ GMTQEQAMAK YMNLIKEWPG YGSTLFDVEC KEGGFPQELW
LGVSAEAVSV YKRGEGRPLE VFQYEHILSF GAPLANVYKI VVDERELLFG TTEVIDIAKL
MKAYISMIVK KRYSTSRSVS SHGSQSSCR
//