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Database: UniProt
Entry: F0WPF5_9STRA
LinkDB: F0WPF5_9STRA
Original site: F0WPF5_9STRA 
ID   F0WPF5_9STRA            Unreviewed;      1695 AA.
AC   F0WPF5;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Myosinlike protein putative {ECO:0000313|EMBL:CCA23203.1};
GN   Name=AlNc14C185G8300 {ECO:0000313|EMBL:CCA23203.1};
GN   ORFNames=ALNC14_093460 {ECO:0000313|EMBL:CCA23203.1};
OS   Albugo laibachii Nc14.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA23203.1};
RN   [1] {ECO:0000313|EMBL:CCA23203.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA   Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA   Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA   Jones J.D.;
RT   "Gene gain and loss during evolution of obligate parasitism in the white
RT   rust pathogen of Arabidopsis thaliana.";
RL   PLoS Biol. 9:e1001094-e1001094(2011).
RN   [2] {ECO:0000313|EMBL:CCA23203.1}
RP   NUCLEOTIDE SEQUENCE.
RA   MacLean D.;
RL   Submitted (FEB-2011) 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; FR824230; CCA23203.1; -; Genomic_DNA.
DR   EnsemblProtists; CCA23203; CCA23203; ALNC14_093460.
DR   HOGENOM; CLU_000192_7_11_1; -.
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; -; 2.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.20.240.20; -; 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   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; 3.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00015; IQ; 5.
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; 1.
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          361..1121
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1562..1623
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          972..994
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1343..1363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1455..1477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1299..1326
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1343..1362
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1462..1477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         459..466
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1695 AA;  194647 MW;  707C75E88A8488F9 CRC64;
     MAQERDFQVI QKLHSVLESP VDASVLCWTE DGHQVRLLYR RRPQLHRLLQ VSFRVFHRIL
     SKYLFTHLKD ITTRDDLYFH PAFGRSSRPE CVLQCFTKQT AKKMDALEPS KSELQWPLVS
     FDSKFGPLEI QFQIRTTGEM EGCQIIVAPT TSMPVSYIAD REEEWFFAPS TFPDSMFEGS
     LDVNAFGDNH SKPEIIGDTF ETGKALFSIP SGLLSESQSQ LLSDSEILSQ ISSFYGRVVK
     IIKQLIILSK STKFNWILRK YQKKEAGWTG FVRKRGSSSP MEAGTHIWIP CDSQVWTPAA
     VLSHPTKNST DSVQVQLLEN GEIKIVWLLK KARNAALSMS TLQRQARLHQ WFLCNNIHTV
     ESLHCLTELA HLHEPSILHV LHQRYQRDRI YTFLGEILVA LNPFKTIEDL YSSSQLALYD
     PSLHSDQLSS RQPHVFAVGG RTFDRMRRNR CNQSILVSGE SGAGKTETAK YLLHFFTATQ
     ETLASGNDNS SKIGKYILQT NPILESFGNA LTIRNDNSSR FGKFTTLQFD ATSHVLIGAR
     VASYLLEKVR LIHQAQDEQN FHIFYELYFG ASQETKNRLL GGQNSFRYLP HLTQFTTSQQ
     NAYTSRYKNT IQALSDIGTL QSERDDLLSL LGAVLHLGNV EFSTTDQRLV VSELCEEHLE
     RAAELLELPV ESLLKLMSTK KIQAGGETVH LDVSPHQAEE MCHSLGKFIY CGLFEWLVQR
     LNNTIDAGSA SQTRNSLLCI GILDIFGFEN VHQNGFEQLC INYANERIQA QFNECVFQKE
     QQIYKEQGIL WKEIEYSDNL NCLSFFDDRV QGFFSLLNQE CMLPKGSNEA LITKLYRAYV
     KRGCSRLDSV LANVCFSAGN IEQSRFQFVI KHFAGHVRYE LDRFLEKNMD TLPLNAQQLF
     IQSSNDILSF IGLRGRMDGE SSSNTLGDTE RLSSSRQVFT RNSLIKPTSD KRYRRNSTVC
     VASLSAQFRS QLDSLLYEIG KTEPHYIRCI KTNDFKEPNY LDRTRVVEQL RCAGVVEAAR
     IARAGFSVRI CYKEFIQQFK CVLSSQKRAD SMSRNAALAT NNTLQFCCLE ICRALLPQSN
     LQDDFDACAF NSSCSNAGVQ VGRTMIFCQQ KTYEQFAIVR SECRKSAALC IQRNVRRVRE
     ERLYRIKVRS IITLQSFFRV CLARRFVQRR RLSVWNAAAL RIQKYWRRYA VMRHAAIRRH
     SVIVIQASFR GFRTRKALKK RQRMLHRKAA LKIQRFYRDC RSRRLQAKRF FAARLIQLWW
     RESIKAHSIK RSKDTQMPMV SIVTRRMDID EEKKVNETRV DLESRNKALL HEIAQLRNRL
     EQGESKAPTQ ETPSKKLDSF YKISQSQEEH ESANDHKDIS SQPEETNGIQ LLNRKIDDLT
     FKCDFLEQFV FKLLSKNGSE AIATGSERMS FDAEQFAKQI DDMHAHPERT SELLEGIHYQ
     MEVIRQSLHN RPYRGRVPSI DSVASSRPTR TSSVSTGMSV GGQVPCIELD TDEETKPRRV
     ATRMRPNMRL QNCLDETHDQ STLLDSNAPM RLSEISNYSR AVDIVNNDST MNSSRLFRIT
     KWARSSECYE CHEAFNLFVW RHHCRLCGNS FCHEHSSRRV TLFAMGHDHE PVRVCDECYA
     EYQIILMQQM PTAMNQTRSF MRQTAPLQHA SPSWNSMVKA STATSPRMSS IHLELHSPRV
     SCPSIKNASF FSGAA
//
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