ID M4BXS7_HYAAE Unreviewed; 1851 AA.
AC M4BXS7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
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:HpaP811358, 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:HpaP811358}
RP IDENTIFICATION.
RC STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP811358};
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; JH598034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 559515.M4BXS7; -.
DR EnsemblProtists; HpaT811358; HpaP811358; HpaG811358.
DR VEuPathDB; FungiDB:HpaG811358; -.
DR eggNOG; KOG0160; Eukaryota.
DR eggNOG; KOG0817; Eukaryota.
DR HOGENOM; CLU_000192_7_12_1; -.
DR InParanoid; M4BXS7; -.
DR OMA; GKCQSIL; -.
DR Proteomes; UP000011713; 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-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR CDD; cd14892; MYSc_Myo31; 1.
DR CDD; cd00821; PH; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 4.
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; 2.60.40.150; C2 domain; 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; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR025939; Aida_C.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR035892; C2_domain_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; IPR004009; Myosin_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF845; MYOSIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF14186; Aida_C2; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00015; IQ; 15.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS51911; C2_AIDA; 1.
DR PROSITE; PS50096; IQ; 11.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51844; SH3_LIKE; 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|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:UP000011713}.
FT DOMAIN 3..53
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 57..768
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REPEAT 1291..1311
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1452..1551
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REPEAT 1582..1620
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1621..1653
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1709..1851
FT /note="C2 Aida-type"
FT /evidence="ECO:0000259|PROSITE:PS51911"
FT REGION 646..668
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1321..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1366..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 151..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1851 AA; 211434 MW; EDF7C242110D58A0 CRC64;
MRREGEKVWC PDPRNVWQLG TVVEDDGEKL HVLLPEADAA QQFTVDQVHP YDPSHALDLR
NVAGMDNLHE APLLDLLHRR YLQDQIYTYT GDILISINPY KNIPMLYNFP ELDSVIGRLS
ENPIPHVYST AHGAYHAMKQ HGKCQSILVS GESGAGKTEA SKYIMRYLAN ISEIGKKTPK
GPKVEADASS VEQCVLQSNP LLEAFGNAKT IRNDNSSRFG KFIKIYYHAN GTISGATTSH
FLLEKSRIVG SAEAERNYHI FYQICAGMLA EEKKALYLKP ASEFCFLNQG RCIQVPEIND
KKDFRELVEA MGTVGIPTEL KHTIFRLVAC VLHLGNLEFT ENAKNESQIA HPEDVTKLAE
LMMVTPSELE FALTKRTMSA GARGSVAEIA LTAVESIKSR NGLAKDMFSK IFDWLVSQIN
KSTAYVGGSL GVGTGSKFIG ILDIFGFESL QINSFEQLCI NYTNEMLQQQ FNQHVFVYEQ
EVYVEEGIDF SRLEFKDNRP CLDLIDKKPL GILPLLDEQG MLGRRASDEN FIQKLHQTHL
PKSKVPEGTT IYYSKPRFAT DEFVVHHYAG EVTYNVTGFL EKNDDSLHND LISLMDSSTC
EFLRKLYPVT QAGVAAGGVN SRKPIRKAGN KMTGTMTVGR KFRDQMADLM VELKATTPSF
VRCVKPNNLR FPQGWNAELI LNQLTYLGVM ETVRIRRSGF PVRRLFEEFH QKYQILTRNI
AKDKRANMTD KDYCEVILRF ICRENWQLGH KKVFLRDSQL RILDNETRKL LHDAATIIQK
YVRGRRQCRR YLDLRKKVIQ IQGMVRMFLA RRHYRVMRHR ITLLNAMAKQ FVQRRKYQRL
RKATIFVQNH VRGNVARRYA LYLRNAAPAA TKIQAQVRRY LARRSFLKQR HAAAKIANAR
KMRKQRAEFL EMRTAANTIA SRYKGYAARR KYRDMQKAAV VLHAAGRGYN ARLKYGKTAR
MRAAARNKAQ IRISRAVRGF LAQRFFQVSR RRIIMIQARV RANRVRTEYL KGREATISSQ
AMIRRSLVRR KFLREKKMAT RIEAFGRMIV CRRRYRDERN KVILLQSLWR MHYARKQYQK
RDRQVILLQS LWRCHAQAKK YHDTREKIVT VEAFARMTVE RTRYLKMRSA ARVVQKTVRA
FLGHRQKVRF RRGLVRTQAL CRGYVQRKKY RRTIQRIIMV QSVFRQKRAN KLADVRRRAM
ARVLAVVRIF MSRVRMRNRT QALFSAANTY DLTTVLHIAQ EMPGMLRVRD RDHDMMSLIH
VAAKNNDLNL ARFALEENPQ LEDLVYGKDI TGSTPLHYAC RLAHLDMVRL LARVANRNST
PGTHFDFGTA RTRSSSNTSS GSDDPPDTKL RSVSCVSTVP MSTPLFRSPS KSVSVGNRSP
VAGISPRSHG MSTGLPPSFS MQPGFKPGDH NAPKRHGRRS LVSSITKTGN SRRLSSSIGR
LPPVLPTTLQ IEVYKKGFLQ TISGSRRAKK RYVMVDEVCL SYYKTEKDKI PLQMAELCDV
TIKRVSNVNC SFEIRSPRLQ SSKNPDGMLS FLADTEREVH EWMLAIRKVR GVRVTTTSPP
NHNMICIDSG LRRDYVNMKN KLGFTPLHLV VQNDEDEGFE AAKVCVWLIE NGADPNAVDE
NGDTALHYAV ELDRYDLVET LMKRGADSSI KNLKGLSAVE IAEEDDLKEI LNPANHAWKA
EEASGADEEA QPDRAALVEN RARLTPSLFP PPDRLHDSTY VSVFLGAVAV ATCPIMETPH
FNLYIMDYKG AIVDTAQRTP KSLIQSGGNY WWFGNTWYLQ TPLEHLKDGS VAVMELRHRS
LVTQEVEVGC WTFFHLDVSK ITTAPASFEM YAPPVDPLSR NQRVAVSCVS L
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