ID A0A421FEY9_9STRA Unreviewed; 1513 AA.
AC A0A421FEY9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BBI17_001460 {ECO:0000313|EMBL:RLN43786.1}, BBO99_00000643
GN {ECO:0000313|EMBL:RLN85367.1}, JM16_001475
GN {ECO:0000313|EMBL:KAG2530734.1};
OS Phytophthora kernoviae.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=325452 {ECO:0000313|EMBL:RLN43786.1, ECO:0000313|Proteomes:UP000285883};
RN [1] {ECO:0000313|EMBL:KAG2530734.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NZFS 2646 {ECO:0000313|EMBL:KAG2530734.1};
RX PubMed=26981359;
RA Studholme D.J., McDougal R.L., Sambles C., Hansen E., Hardy G., Grant M.,
RA Ganley R.J., Williams N.M.;
RT "Genome sequences of six Phytophthora species associated with forests in
RT New Zealand.";
RL Genom Data 7:54-56(2015).
RN [2] {ECO:0000313|Proteomes:UP000285624, ECO:0000313|Proteomes:UP000285883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chile2 {ECO:0000313|EMBL:RLN43786.1}, and Chile4
RC {ECO:0000313|EMBL:RLN85367.1};
RA Studholme D.J., Sanfuentes E., Panda P., Hill R., Sambles C., Grant M.,
RA Williams N.M., Mcdougal R.L.;
RT "Genome sequencing of oomycete isolates from Chile give support for New
RT Zealand origin for Phytophthora kernoviae and make available the first
RT Nothophytophthora sp. genome.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG2530734.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NZFS 2646 {ECO:0000313|EMBL:KAG2530734.1};
RA Studholme D.J.;
RL Submitted (JUN-2020) 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:RLN43786.1}.
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DR EMBL; JPWV03000017; KAG2530734.1; -; Genomic_DNA.
DR EMBL; MAYM02000342; RLN43786.1; -; Genomic_DNA.
DR EMBL; MBDN02000009; RLN85367.1; -; Genomic_DNA.
DR STRING; 325452.A0A421FEY9; -.
DR Proteomes; UP000285624; Unassembled WGS sequence.
DR Proteomes; UP000285883; Unassembled WGS sequence.
DR Proteomes; UP000785171; 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; cd00014; CH_SF; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
DR Gene3D; 1.10.418.10; Calponin-like 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 InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_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 PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00033; CH; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50021; CH; 1.
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 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:UP000285624}.
FT DOMAIN 3..110
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 617..1298
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 120..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1199
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1394..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..286
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 711..718
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1513 AA; 167653 MW; 94C9279D2CBDB95B CRC64;
MTVRRTEELQ EWVCSVTATS NDHGEHLSVM LRDGQLLCLL ANGVDPAANL KVNKLNTVFH
SKANIRLFLE WCKKQGLNDG EIFQTDDLLD TGADFVAVLN TLSILFDRFG TIGYNGEYEE
DPVSDAESQM STGSSQGASP VKKANSGNKL TSFMKGGFLS RKKKASSKKM VKSPEGTPPS
TPPPSSPQVG AGMLSPQGSP NAFQTPTAPP PNKQKDNRSG SGGTSRLNAF LNQVPASHQS
PLTHVDRPTG PPKKANSVRK PPAPKPKTPP PTVKKPVTPK QPPKPAPSGG DTRNKFAAFM
KTNPPSVDST HGSNSSSTSG GSNPSAVKSS ASPSATNKPA VSAPSQSKPA SNDKFAQRKA
AFTGNGSNNK ENQPKTAAST SSKPPANTGN KLNNFMKQQP TASPASTKPR SQSKLAQFLA
TTNSVPSIAS NPSAASAKPS LSSFNPVKKA GGMATPKPAY NAPESSTPTA FKPRHMIERS
SGRGNYIRKR QTYWVPPKRR RSNFSLEKKR KGFMKEQLEL KEEQLRQQAA GAGNRQNLIV
PGVQCFIPDK EEVWLHSEVV DYNERRKEVT ITAFMDSGDS EQRVVDLKNP EVIRAIAGPT
ATEVESLPIA ILHDSPEGVE DMRLLRFLNE PSILFNLKQR FGASKPYTYT NDIVIALNPY
KWIDNLYGDH LHEQYLRKDR DTLPPHVYST STAAYKHMKT NEMNQSILVS GESGAGKTET
TKIVMNHLAS VAGGRKDKTI AKVIDVNPLL ESFGNAKTTR NDNSSRFGKF TQLQFNDRGK
LIGAKCETYL LEKSRVVSIA EGERNYHIFY QLLAGLPSRE LKEFGLDPEC KYQYAGSLSE
MQIPGLDDSK WFAGTQKSLS LIGLETPGQK ILFKLLAGVL LLGEVSFDKS GESGSRISSG
SALSQVAKMF GLPATRIEEA LCNRTVITRN DSVTVPLDPV EATENRDALA KTIYSKMFDW
MVVKINAAIS TDESKISGQI GVLDIFGFED FVQNGFEQFC INYANEKLQQ KFTTDVFKTV
EDEYVREGLQ WDHIQYQDNQ GIVEVIEGKL GIIALMNDHL RQPRGTEEAL VNKFRTNHQK
KKNGDVNESI DFPKVKRTQF IINHYAGSVA YETVGFMEKH RDTLQKDLLD LIQLSSISFL
PELFEDAEIT LEGSERGSGG RGKKGPKSLG TQFKTSLSQL MDNIKCTNSH YVRCIKPNSN
KSPTEFNKRM IVEQLRSAGV IEAIRITRSG YPSRLTPKEL ATRYAIMFPP SMHSKDVRRT
CSVFMTSIGR KSPLEYQMGK TLVYFKNGVM EELEAMKSDF MYYEARTIQR IALGFLERRR
LRNKIAAAIV LQSYARMSLD YKEFHFQRRE IIKIQRGWRR YQAGPVTEPE YESGKEYGDG
GQWVDDLDDL DDSDADEGFG DDPASVRADR GKSISDRMES YKSAQGGRRG SVKRLNELSA
RAKSFMKTRS GSGSTSSSSG ISLEDENSIL KIENRNLKYD LELMREQCIE LQAIILEINK
SRKREYKLFQ QVK
//
