ID W2K6U0_PHYPR Unreviewed; 1599 AA.
AC W2K6U0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=L917_18642 {ECO:0000313|EMBL:ETL80906.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL80906.1};
RN [1] {ECO:0000313|EMBL:ETL80906.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL80906.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL Submitted (NOV-2013) 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; KI682598; ETL80906.1; -; Genomic_DNA.
DR EnsemblProtists; ETL80906; ETL80906; L917_18642.
DR VEuPathDB; FungiDB:PPTG_05570; -.
DR Proteomes; UP000054423; 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; cd15760; FYVE_scVPS27p_like; 1.
DR CDD; cd14902; MYSc_Myo41; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 3.
DR Gene3D; 1.20.58.530; -; 2.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 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; PF01363; FYVE; 1.
DR Pfam; PF00612; IQ; 5.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00015; IQ; 9.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 5.
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}; ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Coiled coil {ECO:0000256|SAM:Coils};
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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 64..855
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1510..1571
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 696..718
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1128..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1405..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1313..1340
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1128..1149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1203
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 167..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1599 AA; 180279 MW; 03BC2D621A50C2F0 CRC64;
MDVGTNVWVK TKDAAVWAAG EVVDYQDASG IVQVRRLDTG DIVMRRYPGF DDELCLRNMS
ANFPTMSSLT SLEHLHEAAL LQALSERFDH DQIYTSIGDI LVALNPLKPL PKLYSETQLN
AYKHSMTNTN PASVQKELPP HVFAIGGKAF GGLLKPERRN QSILVSGESG SGKTESTKFL
MQFLTSVGRD QSRSEQEGSD AVEIGKRILQ TNPILESFGN AQTIRNDNSS RFGKFIKIQF
GHNNEIVGAQ IVSYLLEKVR LLHQNPEERS FHIFYELLEG ADKELLDALG LQKGGKYELL
NSYGPSFARK RAVADKYAQL YVETVRAFED TGVGELERLA IFKILAALLH LGNVNFTAEN
GQEDATSVTA ASRFHLDKCA ELMGVDVDKL ETLLSSREIK AGVEVMVLKH NPEQAKEICG
SLAKAIYGRL FTWLVRRLSD EINYFDSAIS ISDEDDELAT IGILDIFGFE SLNRNGFEQL
CINYANERLQ AQFNEFVFVR EQQVYIAEGI DWTNISYPSN AACLALFDDK SNGLFSLLDQ
ECLMPKGSNQ ALSTKFYRYH GGEDSTGSLQ QQSTLTFMSS FSRYLHRAGS QEESVHQDTK
NHPFSASKME RVNHQFVVHH FAGRVCYNVE QFVEKNTDAL PADASDILSS SSNDVVVAIG
ADENVDSPTA DNGTAGRRRY SMLRAPSVSA QFKSQLDRLI VQIGHTEAHY VRCLKPNEVK
KPGIFDRERM VEQMRSVGVL EAVRIARHGY SVRLAHASFI ELFSGFKCFL STRDRAAKMN
NHDLAQALVT VLMDKVLLED GVEREEKNPG ALTAVTGDSS GTAFENDVRR KDVQVGRTLV
FCKSTTYNRF SRYRVELRSH CAAVLQKYYR GYRRRVLYQQ LRGFVIHVQA IVRGFLGRRR
VDKLRTLRRE QAATCIQACW RRFVVLRKFT EMLQQKRQVE AATAIQACFR RFKAQRILEE
MLMVKRQLAG VIRIQANVRR WLAQRQLAGL RKQKLRVVAA ICIQRNCRRW LAQLELARLR
EQKLQIIATV RIQAQCRRVL AQNQRQKLLR LQLEMSTAIR IQSHCRRWLA QRKREQLIQQ
KRERAAAISI QRHGRRWLQQ NSVVSAKLHH FHLNVAFSKF RRACQESQEA REMEAEPSPS
DDSAGSRAKR RMSKSIGLRA TQSSSEQEDS STSDDRMEPP LRISVPTHHR SNNRQRSRAN
SRRSRTSSSH VDDRNSLLEN EILRLQQMLV EQQSGSSRRD QQRRSSTFAR PPRSAPLDLS
QSARVTRSRS GRRRYSVDGA LSDDEDAEND DEVSLLPPRR ARSVMPAPQA DHVSMLSQKI
EELDAKCKFL EQLVARKNYE DAARESFMYG RGSFGGRERF PSADGSLYGD TPPSEAGSDV
DSIIFNIQSQ MNMLRQSIAV KEQALHTSRK SHAMSFSSST RPTRSSSAAS TTSFSNLPME
APPSLPSLPL SESQLSAGGS SHGNSRRSGS SSLGLPPTPT SSVASSFYQG PPRSSPAHFG
GRGMPRIVKW ARSTNCYECE EPFNLFVRRH HCRMCGNSFC HEHSSRRVSV FGIGFDDEPV
RVCDTCFAEY YATSHEPQYP PQYGFSSGPL STSSRLSGL
//
