ID M4B5D7_HYAAE Unreviewed; 1382 AA.
AC M4B5D7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Myosin-like protein {ECO:0008006|Google:ProtNLM};
OS Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS (Peronospora arabidopsidis).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Hyaloperonospora.
OX NCBI_TaxID=559515 {ECO:0000313|EnsemblProtists:HpaP801487, ECO:0000313|Proteomes:UP000011713};
RN [1] {ECO:0000313|Proteomes:UP000011713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Emoy2 {ECO:0000313|Proteomes:UP000011713};
RX PubMed=21148394; DOI=10.1126/science.1195203;
RA Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA Tyler B.M.;
RT "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT arabidopsidis genome.";
RL Science 330:1549-1551(2010).
RN [2] {ECO:0000313|EnsemblProtists:HpaP801487}
RP IDENTIFICATION.
RC STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP801487};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
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; JH598388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 559515.M4B5D7; -.
DR EnsemblProtists; HpaT801487; HpaP801487; HpaG801487.
DR VEuPathDB; FungiDB:HpaG801487; -.
DR eggNOG; KOG0160; Eukaryota.
DR eggNOG; KOG0504; Eukaryota.
DR HOGENOM; CLU_000192_7_15_1; -.
DR InParanoid; M4B5D7; -.
DR OMA; HEPGICH; -.
DR Proteomes; UP000011713; 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; cd00124; MYSc; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
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; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF845; MYOSIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00248; ANK; 8.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00015; IQ; 2.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 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}; ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW 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 Reference proteome {ECO:0000313|Proteomes:UP000011713};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 77..813
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REPEAT 981..1013
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1014..1046
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1077..1109
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1147..1182
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1219..1251
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1281..1354
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 660..682
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 908..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 186..193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1382 AA; 155981 MW; 92F796D8CE4D625B CRC64;
MEKGVGVWLH DQETDEWHRA TVVRLEEPQN DSDARAVTLR VSEGPHAKTD RTMVIDVQAL
ENEEVDGVLL ANSSDMDVVE DLIQLPHLHE PGICHTLSER FKINEIYTLT GEILLAINPF
QPLGIYTDKI TRKYIRNGDK RVLGQDVPDM PPHVYSIADK AYRSLMSPIG HGARGSAVNQ
SILVSGESGA GKTETTKFVM NYLATISQHK NTSAESSVMK QVLSSNPILE SFGNARTIRN
DNSSRFGKFI KMEFSAEGSL IGASIQTYLL EKVRLAYQAE SERNYHIFYE IVAGATAEEK
KRWNLKALNT FHYLNQSTCV KRKDGVNDAE QFVVLKTAMQ TMGFNEDDME SIFVTISALL
HIGNLEFDEI HQASGTEGSE ISSTCNDSMK VVLDYLETDK QGLEQAICNR NIQTKDEHYS
IGLLPRAAEN VRDALARFLY GKLFDWLVCR INDIVENDTR GVPFIGLLDI FGFEDLEHNS
FEQLCINYAN ETLQQHFNLT VLRMEQETYE KEEIQWSFIN FPDNGPCIDL IQSKPFGILP
ALDEECIVPQ GNDRNFSRKL YRQHGVNPHF SASKTEMANH LFVVHHYAGA VTYDTFGFCE
KNKDILYPEI TAIIERSSKP FVRGLLQASL ESKVSVRKPK GRASSNATRV SLGSQFRNQL
KTLLETINVT DCHYVRCLKP NDKAEANLLV PKRVCDQLKA GGVLEAVRVN RAGYPVRITH
QQFIKRYRPL ANGEYLQRIP AESAEDFFDI DEQKKAASLL VEFLAKAHAE RYPELSGAAS
ENKQETAVNG IQVGLTRVFF RRSAIQFVEA QLAKRYGEFV VLIQAAVRGL IARRHYARMR
VSAVVVQKMI RGFNTRCRFY VLRENHRKKQ AEILRQKVLA EKKQLDEERR ASEEQRLMDE
NRKAAELEEQ NRLTAQSASS DPVSDDSSEG DRGSSMKLPN FSGGSNEEVG NRAVSRFRFT
KDYTDDDQSM PSTSRQVAMD PGDTVLHVAA NCCNEQDVLK LLQNGSDINA CNRRGRTPLH
TASLYQNMEV VGILLDWGAD YIVQDDDGNT PLHLTKEPRI ARMLLEAGCT PNIVNADGRT
TLIDAVDRGD AKTVKLLLHF RADVLFRELK HHQTALHLAV RKGHYQIVME LCKSDEIQNL
ILLTDRNDNN ALHFAVSRDR KNGYRLVDYL IKHGGEVDKV NARFQTPLVV HIMTTRQTDP
AITELFLVRG ADANVQLADG STLLHVAVER ELIDIACVLI KHGGSLNVPD AKGRMVVEVA
NKKYLKKLFS AITQPPTWID EKERRSCMLC GSNFKFGSRR HHCRHCGRVC CSDCSAFTVE
MHRFPKDFPG RMTSGGKQVK DPQRVCRTCH AVFKMRSAQK ESKSGFMARV LGYEWDEVTA
TN
//