ID A0A0W8CCL9_PHYNI Unreviewed; 1377 AA.
AC A0A0W8CCL9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Myosin-I heavy chain {ECO:0000313|EMBL:KUF81822.1};
GN ORFNames=AM587_10010249 {ECO:0000313|EMBL:KUF81822.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF81822.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF81822.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) 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:KUF81822.1}.
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DR EMBL; LNFO01003972; KUF81822.1; -; Genomic_DNA.
DR STRING; 4790.A0A0W8CCL9; -.
DR EnsemblProtists; KUF81822; KUF81822; AM587_10010249.
DR OMA; HEPGICH; -.
DR Proteomes; UP000052943; 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:UP000052943};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 77..812
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REPEAT 976..1008
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1009..1041
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1072..1104
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1142..1177
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1214..1246
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1276..1349
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 660..682
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 872..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 186..193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1377 AA; 155902 MW; 984077C27DCFCFED CRC64;
MEKGVGVWLR DAETDEWHRA TVVKLGEPRD DSDEREVTLR LTEGPHARTE KTLQIDVQAL
EEEQIDGVML ANSSDMDVVE DLIQLPHLHE PGICHTLNER FKINEIYTLT GEILLAINPF
QNLGIYTDKI TRKYIRNGDK RALGQEVPDM PPHVFSIADK AYRSLVNPIG HSSNGGPANQ
SILVSGESGA GKTETTKFVM NYLATISQHK NASADSNVMK QVLSSNPILE SFGNARTIRN
DNSSRFGKFI KMEFSSEGSL IGASIQTYLL EKVRLAYQAE SERNYHIFYE IIAGATAEEK
KRWNLKAPTK FHYLNQSTCV KRKDGVNDAE QFGVLKNAMQ TMGFDEDDME SIFVTISALL
HIGNLEFDET HHASGTEGSE ISNMCEDSMK VVLDFLEVDK DGLEQAICNR NIQTKDEHYS
IGLLPDAAEN ARDALARFLY GKLFDWLVSR INEIVENDDR DVPFIGLLDI FGFEDLEHNS
FEQLCINFAN ETLQQHFNRT VLRMEQETYE KEEIQWSFIN FPDNGPCIDL IQGKPFGILP
ALDEECIVPQ GNDQNFARKL YRQHELNPHF SASKTEMANH LFVVHHYAGA VTYDTFGFCE
KNKDILYPEI TAIIKRSSKP FVRGLLQVSP EKKTPSKKTK GRASSIATRV SLGLQFRTQL
KTLLETINVT DCHYVRCLKP NDKAKANLLV PKRVCLQLKA GGVLEAVRVN RAGYPVRIAH
QQFIKRYRPL ANGEYLQRIP AEAAEEVFDS TERKEAASLL VEFLLKAHAE RYPELAGVSS
DNQETAVAGI QVGLTRVFFR RSAIQFVEAQ LAKRYGEFVX LIQAAVRGLI ARRRYARMQV
SAVVLQKVIR GFNTRCRFYK LRERHRELKR QKELAEKKQR EQERRAAEEQ RILDEKRKAA
ELEEQNRLTA QSASSDPVSD DSSDGDRGSS MKLPRYSRNS EESRGSRAVS RFRFTKDYGD
EDYSMPNTSR QVAMDPGDTV LHVAANCCNE QDVLKLLQNG SDINARNRRG RTPLHTASLY
QNVEVVGILL DWEADVLVQD DDGNTPLHLT KDPRIARMLL EAGCTPNIVN ADGRTALINA
VDRGDAKTVK LLLHFKADVL FRELKHHQTA LHLAVRKGHY QIVMELCKSD DIQDLILLTD
RNENNALHFA VSRDRKNGYR LVDYLIKHGA EVDKVNARFQ SPLVVHIMTT RQTDPAITEL
FLSRGADPNI QLADGSTLLH VAVERELIDI GCALIKHGAS LNAPDAKGRM VIEVANKKFL
KKLFSAITQP PTWIDEKERR SCMLCSSNFK FGNRRHHCRH CGRVCCSDCS AFTVEMHRFP
KEFPGRMTNG GKQVKDPQRV CRTCHAVFKM RSAQKESKSG FMARVLGYEW DEVTATN
//
