ID C6JVY2_PHATR Unreviewed; 2303 AA.
AC C6JVY2;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=Myosin 29 {ECO:0000313|EMBL:ACS35536.1};
OS Phaeodactylum tricornutum (Diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC Phaeodactylum.
OX NCBI_TaxID=2850 {ECO:0000313|EMBL:ACS35536.1};
RN [1] {ECO:0000313|EMBL:ACS35536.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UTEX 646 {ECO:0000313|EMBL:ACS35536.1};
RX PubMed=20217677;
RA Heintzelman M.B., Enriquez M.E.;
RT "Myosin diversity in the diatom Phaeodactylum tricornutum.";
RL Cytoskeleton 67:142-151(2010).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; GQ141540; ACS35536.1; -; mRNA.
DR SMR; C6JVY2; -.
DR HOGENOM; CLU_230138_0_0_1; -.
DR GO; GO:0016020; C:membrane; 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; cd17781; CBS_pair_MUG70_1; 2.
DR CDD; cd14890; MYSc_Myo29; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 4.
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 InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000270; PB1_dom.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF845; MYOSIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00571; CBS; 7.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF00564; PB1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00116; CBS; 8.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00666; PB1; 1.
DR SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 4.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51371; CBS; 6.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51745; PB1; 1.
PE 2: Evidence at transcript level;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2279..2298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 149..909
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1445..1503
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 1512..1568
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 1688..1747
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 1797..1855
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 1864..1920
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 2039..2097
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 2187..2268
FT /note="PB1"
FT /evidence="ECO:0000259|PROSITE:PS51745"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..805
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1378..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1231..1265
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..37
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 277..284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2303 AA; 251990 MW; 0DF20099E6B147F4 CRC64;
MTTTPATVDP QGHQFSPTTR KNKKKGHTNK KKSGSPGKNT KSKAVDMVTG KTTVEYFFDP
TLLINGTSGS ETPFKTAKDS QDPLFFTSKH LFMPCTIIKP LNDENSQNAG KLNTQPFAGP
TLVKTSDGTL HKIKDSSCLT SLQAPDDYIG MDDVLHLPQI TEASLLHTLR LRYRRDDIYT
LAGPILISIN PYQSVCLPGG ESIYSEEQML VYRSSTLAVD DKTPHLFQIA DRAYTALMDS
VHPSAAADHL EDEDAVMLRD HHQPPGMVRN QSIIISGESG AGKTEATKII MKYLARITRK
SEKPSATEGT ALLSPNGKRI AALEDRVLSS NPLLETFGNA QTLRNDNSSR FGKFIHIYFD
TIKGGITGAS ISNYLLEKTR ITTQVDGERN YHIFYQLLSG VDSTLMEDLG LQEGVQGFAY
LGNRSAEKSE ADAEAFRETI VCLERIGLDT EDQRAVFGMT AAVLHLGNIQ FEATDQEENC
EAIISAATLP SLRKACELLG LDEAKLSEAI LTKVLVVNGK TIKKPQNVAL AEDKRDALAK
MTYSCLFLWL VQCINETLQQ KSTSKAFNSD KLGFIGVLDI YGFECFEQNG LEQLLINYCN
EKLQRHFNRH LFEVEQELYA NEGVDWSYIT FNDNRPCLEL IEGGSGIVGI LNTLDDAWGG
MGTASEKDGK FVTHLHKLFG TGSGDSKKGD TESGHPNFVT PKFGNDRQFI VLHYAGEVRY
TAEGFVEKNM ETMSNEIREL GEQSSLDLSQ KVYSCGQSDI SGKDPLRSSI RGISVGSQFR
SSLQSLVTDL DRTQPHYIRC IKPNLSKAPG SFLAGEVLKQ LRYSGMMEAI RIRREGYALR
EEHESFFSRF SVLLNQDEVD TDETGIEQLV KVLSKRLNVT EADWQIGHSK IFLRRELSDK
LERLAKLRVH AAARTLGRFG RRVTYRRLSA FLVAWVRFRL TMLTRYRETR AASKLAAVVR
RYRQVHQFRL IKRGVVLIQS QQRRLLAMQR VRKFRDPFCD MEFRECKKLL GAEQVRLDEA
VKLKDFRAAA KLEEKIATIQ DAVERKRPLT RQIVEARIVQ VQKELDDSLS RKAFAECGPL
QDRLDELLAK RAELPTVDEL REEVRSAEAA MALAVKNRDF AGAAAGQAHI DEARGRLADV
LAAQNEDEDS EDGEGKENKA LGFESRAQLE FDITEISVQV KVAIDSKDFK KASLLQVAMD
ERESLRQFFP SVRDLQAALK AGKADLDEAV SKKAFARAEK ITNKISELEK QLEKEKEKMA
ELQIPEETSK AATTLHDGQV RVFQSRMDLE SEITKLSDLV SKAVKAKDFK KANMIQADAD
ALAKLRDLLP SVAELQMQLL AKKEEMEAAI SEKRFADADE INVAIDEIET TLKKEKSLAP
LKPGGPHLSV KAKDKGDASV KTAPAVANVP TNKSVRSNAT APVWKTPSKP AAVVAKTVSK
PVSKLRPAKP VTVEPSSSID SVAQLLAMKR ANATVVVSSD GSLSGILTDT DITRRVVAKF
VDTALSTVDE VMTPFPTCVA MEDSAMDALT IMLENHFRHL PVVDDRGIVV GLLDIAKCLD
DAIGKLEKTN KQSSRAGEDA VKNILVNKSG SIDSQAVALQ ALLGNLMAKA FGDKTVPTLR
ALLGGKPGTI VHPSASIREA GILMAETRKA ALVVDNDVLV GVFTFKDMLS RAVAKGLDLD
ATSVADVMTP EPESVSPDMN ALEALQTMHD NRFLTLPVCE SDGTIVGLVE VLDVIYGCGG
PEGWRSMFDS AMDVDDDFSD VTSINSAGKS TLIAGRQDRS TLQALEESTN ERPVSKLRPS
KPITSRIDDT ILRVSQTLSS KRGAASLVVS TDGSLAGIMT DTDITRRVVA KHIDTSATSV
SEVMTPNPTC VAMSDSAMDA LTTMVENHFR HLPVVDDQGS VVGLLDIAKC LNDAISKLER
TSEKTNSAAE DAVKQMVAQQ GAGGAQAAAL KALLGNLMSQ AFGGKQMPTL RSLLAGKPGT
LVDPSTSIRN CGLRMADSRK AALVVDDGEL VGVFTFKDMM SRAVAKELDL DVTPVSQVMT
PSPEFVSPDM TVLEALQSMH DNKFLTLPVC ESDGRVVGLV DVMDVIHGCG GAEGWKSIFS
NVMELDDISD VHSLSKSRVS GRRLGSPSHI KAPPETPYVT KLPGNIPATL EFEEPDDHAS
FNGSTIGDER GVSKLLSPDE GSLAAVVGVF KVTEPNGRTH RIRCETLVTE LLEAVAEKVD
IPRSRLQIQY VDDEGDTVVI TTDHDVAESW SFARKANQKV AKLNAVSIEP KSSGPNSKVM
AGAGIALTLV GVLAFVIMKP KKA
//