Y4A0_ENCCU
ID Y4A0_ENCCU Reviewed; 1649 AA.
AC Q8SS35;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable myosin heavy chain ECU04_1000;
GN OrderedLocusNames=ECU04_1000;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GB-M1;
RX PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT "Identification of transcriptional signals in Encephalitozoon cuniculi
RT widespread among Microsporidia phylum: support for accurate structural
RT genome annotation.";
RL BMC Genomics 10:607-607(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], DEVELOPMENTAL
RP STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
CC -!- FUNCTION: Cellular myosin that appears to play a role in cytokinesis,
CC cell shape, and specialized functions such as secretion and capping.
CC {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; AL590444; CAD25287.2; -; Genomic_DNA.
DR RefSeq; NP_584783.1; NM_001041133.1.
DR AlphaFoldDB; Q8SS35; -.
DR SMR; Q8SS35; -.
DR STRING; 284813.Q8SS35; -.
DR PRIDE; Q8SS35; -.
DR GeneID; 858931; -.
DR KEGG; ecu:ECU04_1000; -.
DR VEuPathDB; MicrosporidiaDB:ECU04_1000; -.
DR HOGENOM; CLU_000192_7_14_1; -.
DR InParanoid; Q8SS35; -.
DR OrthoDB; 119761at2759; -.
DR Proteomes; UP000000819; Chromosome IV.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Coiled coil; Motor protein; Myosin;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..1649
FT /note="Probable myosin heavy chain ECU04_1000"
FT /id="PRO_0000383331"
FT DOMAIN 1..49
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 53..724
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 594..616
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT COILED 793..1614
FT /evidence="ECO:0000255"
FT BINDING 146..153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1649 AA; 193288 MW; FCFF7BA673B391DE CRC64;
MEKKWVWAPS SKEAYVCGFV VKEEGDVLEI DCRGVIVRHK SCEVFRMNPP KFDMVDDLAE
LSYLNEPGVL HNLRRRYQNG RIYTYSGLFL LAINPYKDLR IYGEKDARKY TLSKKYELEP
HIFAVANEAY RLMLSNRENQ SILITGESGA GKTENTKRVV EFLAMVGGCK GMEVSIDRQI
IDANPILEAF GNAQTVKNDN SSRFGKFIKI KFNGGNICGA HIEKYLLEKS RVTSQNRNER
NYHIFYQLLG CDDQMLKKQL FLDGEPKDYR FLKDSRFKIP DVDDAKEFRS LRESMRVLGI
GEEEQIGYFK IVSAILHLGN IEFREKDGAA EIANLDVAEK ACKLLSIPLA EFIKRLIHPV
IKAGNEYVAH SRSREQALKI VDGLSRILYD KMFEGVIDRI NMSLDSPHKG NFIGVLDIAG
FEIFEKNSFE QLCINYTNEK LQQFFNHHMF ILEQEVYRQE NIEWDFIDFG LDLQPTIDLI
EKSNPIGILS YLDEECVMPM ATEKTFLGKL MKNIRDEKFE VDKIRDAFVL NHYAGDVEYT
VDDWLSKNKD SHSEALTSLI RASGSELVSR LSLNEEAVKK GFFRTVSQKH KEQLASLMSE
LRRTNPHFVR CIIPNLEKSG EHLDNGIVLG QLKCNGVLEG IRISRQGFPS RMGHREFVQR
YRIMMKEKIL VDESWDEGVC MELYKEIGGK ILSEIGISTS QYRLGRTKVF FRQGVLADIE
DMRDVKVSEV VKEIQALIRR RLAFRKYNQA QRRMQGILVI QRNGRICCDL QRWNWWRLYL
KIKPLLDVRK RDGEMKEKEA MIQEYARMLD AEKSRREEVE DMLKAMSLKR ELLEKSVEDE
KRFSMEKDEL LMALRYKSDE TAQELEKARK EVFDGHEERK MWETRVNEVA IQLEEKDSEI
LRLRREVSEQ KGALSQQEKE ICSLREEVVS KLSEKDAMVE KMLRERDSEV QALKEKVKEK
DAEVERILEG MKRMEREGEE RNRMLKENES TIDELRTRCL NMKRWKDEYA ELREDYEALQ
KKLKDEVEDM QVENDRLHNE IRKISKEREE LGRMQKKLLD DLEFERNRGS KLEKAFQELR
GEYEAVEGQL QKERQFRDST QESLLEKTRG LERRVKSLNE KLRREEMANR QLMSEKDEMY
REIHVLQQSK LDEIFDREAG FNSIKKNLQM EIQRLEMENQ RLSVDLMEAK CMGEASEESI
SATERFCGML EEERKKRKEI EYQASEHENR NVILSSEVEM LREMVEMERR SKEEVIRGHE
KETGLCKAIA GVRKEVEDLG NEIDMAIEGF NGMYLNVLDG YKRDLKECKE QVMSKEQVIE
ELNGRIVRLG REVEERKEIE EEMSRKVHGL MKQYNGVMND FSLLSTKCSS LERTVSEKEE
EIKGYSERCS EYDKRFEGLV CRVDEEIENL RRSDEERRRC VEKLESGLNG SIAGIRKLDE
RYKARIEECA QSVLDGERRK LKAMEELCEQ LSKKLGELEE EHQGLLDEKM KGLLRIEQLE
GELCAFRESE VHRQDMISMY ESEISTLKRC TRFKDEVLGS LSGERNPVVV HVSDKEKCQV
LDRKRMTVEH ELARANDERQ SLMAINKKLR EEVEKLRGEI DAGRSKMLEM KKKLGCQSLA
VGHLSRELEE EREMVRFFRT LGGARKKKV