ID T0MKL9_9MICR Unreviewed; 631 AA.
AC T0MKL9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Myosin-like protein {ECO:0000313|EMBL:EQB61515.1};
GN ORFNames=NAPIS_ORF00919 {ECO:0000313|EMBL:EQB61515.1};
OS Vairimorpha apis BRL 01.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae;
OC Vairimorpha.
OX NCBI_TaxID=1037528 {ECO:0000313|EMBL:EQB61515.1, ECO:0000313|Proteomes:UP000053780};
RN [1] {ECO:0000313|EMBL:EQB61515.1, ECO:0000313|Proteomes:UP000053780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRL 01 {ECO:0000313|EMBL:EQB61515.1,
RC ECO:0000313|Proteomes:UP000053780};
RX PubMed=23829473; DOI=10.1186/1471-2164-14-451;
RA Chen Yp., Pettis J.S., Zhao Y., Liu X., Tallon L.J., Sadzewicz L.D., Li R.,
RA Zheng H., Huang S., Zhang X., Hamilton M.C., Pernal S.F.,
RA Melathopoulos A.P., Yan X., Evans J.D.;
RT "Genome sequencing and comparative genomics of honey bee microsporidia,
RT Nosema apis reveal novel insights into host-parasite interactions.";
RL BMC Genomics 14:451-451(2013).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; KE647132; EQB61515.1; -; Genomic_DNA.
DR AlphaFoldDB; T0MKL9; -.
DR VEuPathDB; MicrosporidiaDB:NAPIS_ORF00919; -.
DR HOGENOM; CLU_433518_0_0_1; -.
DR Proteomes; UP000053780; 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 Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
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 Pfam; PF00063; Myosin_head; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:UP000053780}.
FT DOMAIN 4..631
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT BINDING 196..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 631 AA; 73908 MW; 9D66ACE363706F40 CRC64;
MKHKDTDDLC TIEDVQEDTF VDILYDRFIN KCTYTHAGAI LISVNPYTYE CNGKLKFGNG
CEKDLDYEGN ILDKYEEIKY EYNNEKEKDF KCNINKEKDF KCDINEENDN EYNNYCNNEY
TSNNNFNNNN NNNEYNNNNN TTNQFINTYN NNNTTSKFNN EYKTTQINYQ TNISLLNTLA
DDSLSSKTPT TIIISGESGS GKTENTKHLL NYLITKTNTT YQISEYLYSL NVVLECMGNA
RTVLNDNSSR VGKMIRLCID DEIVSIKVET YLLEQFRVSQ QDKCEYNFHV FYIFVEWSIS
EGKVFNNEDV INDKEIINEE NINNEKFLYE ENINNESFND KYNMCEEKIN EDNVKKNIIV
NSENNTNKNI VNNENNTNKN IIFTNENNTK KNIINNENYT NKNIYNENIY EEFINDKVTR
NYQINKEHQK NTSLLQNNDF FTNTKNPKFN FTWHQFEKAL KFLKINSTNY IKDILLSIIL
LGKIKDNQSI YIKQVEHKLK INLYDILFKK ELKVKDEVIV IDNSVNEFIS VRDGLARQLY
CQLFEFIVRR INKCGSSKGI GKEGISKCTL NEENEEIDIC NKVNINKSSK NKDNDICSNK
ENFNKSSKVN ISNEDNDICS DKEIIKTPPQ T
//