ID A0A225WUQ1_9STRA Unreviewed; 1378 AA.
AC A0A225WUQ1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Myosin {ECO:0000313|EMBL:OWZ21376.1};
GN ORFNames=PHMEG_0004093 {ECO:0000313|EMBL:OWZ21376.1};
OS Phytophthora megakarya.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4795 {ECO:0000313|EMBL:OWZ21376.1, ECO:0000313|Proteomes:UP000198211};
RN [1] {ECO:0000313|Proteomes:UP000198211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=zdho120 {ECO:0000313|Proteomes:UP000198211};
RA Ali S., Shao J., Larry D.J., Kronmiller B., Shen D., Strem M.D.,
RA Melnick R.L., Guiltinan M.J., Tyler B.M., Meinhardt L.W., Bailey B.A.;
RT "Phytopthora megakarya and P. palmivora, two closely related causual agents
RT of cacao black pod achieved similar genome size and gene model numbers by
RT different mechanisms.";
RL Submitted (MAR-2017) 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}.
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:OWZ21376.1}.
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DR EMBL; NBNE01000232; OWZ21376.1; -; Genomic_DNA.
DR STRING; 4795.A0A225WUQ1; -.
DR EnsemblProtists; OWZ21376; OWZ21376; PHMEG_0004093.
DR OrthoDB; 36097at2759; -.
DR Proteomes; UP000198211; 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; 2.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR01415; ANKYRIN.
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; 5.
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:UP000198211};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 75..809
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REPEAT 977..1009
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1010..1042
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1073..1105
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1143..1178
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1215..1247
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1277..1350
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 657..679
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 868..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 183..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1378 AA; 155748 MW; 5C4B624F856D38B8 CRC64;
MEKGVGVWLR DADTDEWHRA TVVKMGELQD DERQVTLRLT EGPHARTEKT LQIDVTALEE
EQVDGVLLAN SSDMDVVEDL IQLPHLHEPG ICHTLNERFK INEIYTLTGE ILLAINPFQN
LGIYTDKITR KYIRNGDKRA LGHEVPDMPP HVFSIADKAY RSLISPIGQS AQTAANQSIL
VSGESGAGKT ETTKFVMNYL ATISQHKNAS ADSNVMKQVL SSNPILESFG NARTIRNDNS
SRFGKFIKME FSAEGSLIGA SIQTYLLEKV RLAYQAESER NYHIFYEIIA GANAEEKKRW
NLKAPTKFHY LNQSTCVKRK DGVNDAEQFG VLKSAMQTMG FDDDDMESIF VTIAALLHIG
NLEFDETHQA SGTEGSEISN MCEDSMKVVL GYLEVDKAGL EKAICNRNIQ TKDEEYSIGL
LPDAAENARD ALARFVYGKL FDWLVSRINE IVENEDRDVP FIGLLDIFGF EDLEHNSFEQ
LCINYANETL QQHFNLTVLR MEQETYEKEE IQWSFINFPD NGPCIDLIQG KPYGILPALD
EECIVPQGND QNFSRKLYRQ HELNPHFSAS KTEMANHLFV VHHYAGAVTY DTFGFCEKNK
DILYPEITAI IKRSSKPFVR GLLQVSSEKK TPSKKPKGRA SSIATRVSLG LQFRNQLKNL
IETINVTDCH YVRCLKPNDK AKANLLVPKR VCDQLKAGGV LEAVRVNRAG YPVRIAHQQF
VKRYRPLANG EYLQRIPADA AEDTFDGAER KEAANLLVEF LLKAHAERYP ELVGASSDNQ
EATVAGIQVG LTRVFFRRSA IQFVEAQLAK RYGEFVVLIQ AAVRGLLARR SYAHMKESAV
VLQKVIRGFN TRCRFYLLRE RHRQKQAELQ RQKDLVEKKQ REEERRAAEE QRIMDEKRKA
AELEEQNRLT AQSASSDPVS DDSSDGDRGS SIKLPRYSRN SEESRGSRAV SRFRFTKDYG
DDDYSMPNTS RQVAMDPGDT VLHVAANCCN EQDVLKLLQN GSDINARNRR GRTPLHTASL
YQNVEVVGIL LDWEADVLVQ DDDGNTPLHL TKDPRIARML LEAGCTPNIV NADGRTALIN
AVDRGDAKTV KLLLHFKADV LFRELKHHQT ALHLAVRKGH YQIVMELCKS EDIQDLILLT
DRNENNALHF AVSRDRKNGY RLVDYLIKHG AEVDKVNSRF QSPLVVHIMT TRQTDPAITE
LFLSRGADPN IQLADGSTLL HVAVERELID TGCALIKHGA SLNAPDAKGR MVIEVANKKF
LKKLFSAITQ PPTWIDEKER RSCMLCSSNF KFGNRRHHCR HCGRVCCSDC SAFTVEMHRF
PKEFPGRTTN AGKQVKDPQR VCRTCHAVFK MRTAQKESKS GFMARVLGYE WDEVTATN
//
