ID A0A1Q9E5Y0_SYMMI Unreviewed; 841 AA.
AC A0A1Q9E5Y0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Myosin-52 {ECO:0000313|EMBL:OLQ02822.1};
GN Name=myo52 {ECO:0000313|EMBL:OLQ02822.1};
GN ORFNames=AK812_SmicGene14279 {ECO:0000313|EMBL:OLQ02822.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ02822.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLQ02822.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ02822.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:OLQ02822.1}.
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DR EMBL; LSRX01000253; OLQ02822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9E5Y0; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:InterPro.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
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 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 PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR Pfam; PF00063; Myosin_head; 2.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Membrane {ECO:0000256|SAM:Phobius};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..841
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012570722"
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 750..773
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 779..802
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..737
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 140..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..633
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 820..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 92295 MW; 01A05D322C2847FC CRC64;
MTVTVIIIFA VPNSAIVGLT AIDAGIFGEV QDFSQKRWLP RFKGRGSGAQ LTQDTEHESE
KKNKLEELLL RGAQTTAVAL GVPQASLEAV MRRRSVKTGR DVIETPLRED QARAVRDGLS
RAIYGRLFDW LIEHMNERLH MPNGEEDSPT PQPNGAGPGA HPDGRDRLIG ILDISGFESF
ATNSLEQLLI NLRLRGVSAV FKSEIEDCAA EGVDLGATIS YVDNSDCVLL LEGRSGILDM
LDEEIAMPQS SDVTFANKVL KLHGGHSRLV VPKFSGSAAF GIRHYAATVS YSCEGFLEKN
AERPLSDGII ELLLSSSLPL LRVLAPRIRG QAASTSPKGI QAKLLQSCGE PNVIDAVAEY
PLGRELAIVG SPPGPRDLPA FRSLLLPCWQ DGSPGSLLLQ RARAPPPAPE APVAAAEHAA
AVEEAVVVAE ELPPPTQRPP QRPHRRGGGP REQLASGPSA PVEEEEAEQR LDAGPVLPRD
DQPKRKAKRA RKAKVPAEEE AEEVVGEEVE LPASAEDDGA GVGDVPLEDA IQQKKRREEK
AERKKMERRI ERLPITFEYR LHCERKMKEI GKQLDYVQRQ IQEAPAWIER AEDVERRGLA
KSATLRFRRS LRDLMAKIQV AETHYVRCIK PNAANVPEAF TAGMVHEQLR YSGVLEAVRI
RKQGFAARLR FEEFVHRFRC IRLLIGLPTI GEEKGDPKHT TKALLKLVGM DGPEAVLGNT
KVFLKEAVLT SLEDFRSGFR KSLTMTMMNM MMVVMMMMMM MMMGVVVVVA VMVVVAVVVV
AVVVAVAVAA AVAVVVMVVM TIRRKMVVLV LKKNMTITGR DEDDGSDDAD EVDARDNFCC
D
//
