ID A0A0P1AC49_PLAHL Unreviewed; 1469 AA.
AC A0A0P1AC49;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Myosin-like protein {ECO:0000313|EMBL:CEG38263.1};
OS Plasmopara halstedii (Downy mildew of sunflower).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Plasmopara.
OX NCBI_TaxID=4781 {ECO:0000313|EMBL:CEG38263.1, ECO:0000313|Proteomes:UP000054928};
RN [1] {ECO:0000313|Proteomes:UP000054928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma Rahul, Thines Marco;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CCYD01000321; CEG38263.1; -; Genomic_DNA.
DR STRING; 4781.A0A0P1AC49; -.
DR EnsemblProtists; CEG38263; CEG38263; CEG38263.
DR OMA; YSWLDIY; -.
DR OrthoDB; 91020at2759; -.
DR Proteomes; UP000054928; 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 CDD; cd00124; MYSc; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 2.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 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 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 PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000054928}.
FT DOMAIN 73..799
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 662..684
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1132..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 919..1088
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1255..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 166..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1469 AA; 164520 MW; FEC934E8C1E3C0C8 CRC64;
MEDQQTKIYV PDPEVSWVEA TITKGHVVSE TTIEVMIEGD LAEEDASKQP EAGVVRTIDK
SLMLLQNELT SEDGCADMVS LNYLHEPAIL FNLKHRFLRQ IPYTYTGAIC IAVNPYSWLD
IYTKELQEQY MERDRNELPP HVYATSAGAF QHMRVFGENQ SILVSGESGA GKTETTKILM
SHLASAGSQS TTEAQAKEAN IIERVLDANP LMESFGNAKT SRNDNSSRFG KFSELQFDPR
GQLIGARSRT YLLEKSRVSL QGLGERNYHI FYQLLAAPED VTTQVKVTGL EAKDFPFIRP
HEEDLSNGID VNAGMKDAKR FQQTVSCLET MGVSKEDQLS IFKVVAAILH LSRLQFESTP
GNDDASQLTA TPENQHVSEV VSQLLEFDDN QLHTALCTRE MTAVADTYEV PLNVSQAEGA
RTALGVALYS QMFSWLIHRV NMSTSATHAT VAHKICILDI FGFEIFEKNS FEQLCINYAN
EKLQQKFTQD VFKSIQQEYE DEGIPWTRIE FADNVNVLTL LEGRFGVLAL LNEECMRPKG
SDAAFANKLK AHYSDNDRFE CPRFARDAFV IKHYAGPVQY DTNGFLIKNT DALQNDLILL
IKKSKAPFLK KLFPEEHVGD AMTGIPGTNA ITAANELHGR SVMKRKNSIV ADTVGTQFKS
QLNGLMEDIR RTNVHYIRCI KPNGKKSPLV FNKLRVTEQL RCAGVVEAVR ISRMAFPNRV
MQTMFLERFR GVALTATTNA LAVLTATENE NISNDEKVAA AVRELLTNLM PDKESEYQIG
KTRIFFRQGA LEGLEELRTR KFNAAAVVLQ RYAKKWMAMA VFQKIKEAAL VAQKVYRGHR
AMVQYKKQRK AAISVQKYVR RHRARQLLVH MREEYRATQI QNVCKMFVAR RKYQVKVKAI
RTMQSVVRMH LAVKAFSGLQ KQAREDAKLE NQIQLLKKRL QQEREARIEL EQQAQYGSRA
SVHMRSEEAL EDADFVIDQL RRENAALKEA NTNLKTYGVQ LRKEKEVMER GAYVNGASFA
AANQRAMKLQ DENEALKSEL ARYKTGHRNL KAQHAGVMEK ITLMQSSLSE ALNERQTLRH
TVDHLKQHTE HLQGENMALA KANARLRLIL RQDPELSRKH REEVPRLTKL ALSSKQPQQK
VTVQKTSATP SKAIELSEPS MGMRVPLSTL QPPTPPTDNS VSVTQQLSLP IKRANSLSSK
KFTHETSKSS RVVNIREIPS AGPEEEPAVN VLSPTAENTG ERLSFAEVIK GRDRRSSSIS
STGSSSETST SQANASPVLT CTAIRQPTGE DGPLESPAKV IGIVLEGEPE DSSDRVSFSV
TLGIDMVEDA KQQQQQNQRL SLTGGNMVVR QSTSNGTGKS KSRVRRGSYD RSDNDNGNRR
SLSSRQSITG SVEGNRTRRG SYDRNDSYDG MRNTSLRQSL TGGNHHNGGN RGRARRGSYD
RNGYKSRQTS DTMSNASNSS GGGGKRIEL
//
