ID A0A1Q9DVI4_SYMMI Unreviewed; 1869 AA.
AC A0A1Q9DVI4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Myosin-2 {ECO:0000313|EMBL:OLP99203.1};
GN Name=MYO2 {ECO:0000313|EMBL:OLP99203.1};
GN ORFNames=AK812_SmicGene18286 {ECO:0000313|EMBL:OLP99203.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP99203.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP99203.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP99203.1,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OLP99203.1}.
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DR EMBL; LSRX01000371; OLP99203.1; -; Genomic_DNA.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR CDD; cd00124; MYSc; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_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; PF12796; Ank_2; 1.
DR Pfam; PF07690; MFS_1; 1.
DR Pfam; PF00063; Myosin_head; 2.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 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}; ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Membrane {ECO:0000256|SAM:Phobius};
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:UP000186817};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 201..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 388..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 530..551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 571..590
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 602..624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 780..812
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 813..845
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1130..1759
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1721..1743
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT BINDING 1236..1243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1869 AA; 206282 MW; CB86F715DA0B49CF CRC64;
MPLRCQTELE RWHRQLSKRA DHPNAGCARD TPNQIDVAMQ LARTVSALRS EPDGPELYRL
NDAANELMRM LPVTHSTRKA AAREGLVLPG RPNYRYFGRC AELRYVVEAV QSLHAEKTEG
PELAAETATA EAAAPSAMST KQNGGLTVQL LARAYWKQYL AQALANIAAR AASSQHTIAN
RAEGVEDPME MSQAPSQRNS FQILVALGSI VPWTLVASIG SGMLTPLSTY VSLNFFAQRH
TDIPPQELTC QIDMSPQHCQ LALVDGNRLV TVLAFIMPLC QFVTLPLVGV LSDAYGRKKT
ILAVYIASNV TLVFTDLFVF FNVSYWFAIA LNPFMNAQLV TTVLNSTCVD LLESHERSAG
IALISSMDTV AYVIGLLVGM HFTLHQTFLI ASCIVPVCIL WCIFVFPETL PPEKRSLSIN
YRSLLPWDPL PILWRTNTLA RLSLATAIAA FVDESSSRMM GTYYQRVMNW TAQDSYWFET
FWDFSMIVWL TFIFGLLVIY IGEIGTMAFG RLVGSIYVFI AVFIKRPSLA MINCLICAGP
MTFALPAVAG LKSRLVDESE QGRMQAAIST VYMVSGSLGS ILGGFIFEAF GNVNAEGTFD
RMYLVAVFLV VLNIAGMLVS FALFHDLFRR THHLMDERAR QLFPSMKRQL SEDAMLAAGL
ENSRPSDRFD GVALCDASDD DLMQFFSAWP SEQRKRVSGL LSSCSKKGTG DIEAAIAEAE
DQVAAEGKKA AAAAEATTSA DQKPVEATKT LDEKQVKQVH SAIRWGKPVE EIQKAVDAQN
GNLALHISAQ NGHMGLTSFL LDSRANVNAQ NFNGQTALHM SVEYDMYFQT KLLLDAKADP
NLENTGGHKA LTGLEGAKTG QDAWDNPMNI LKAAGDTEEE LKLAFEALAA ADAKDMDRVV
LAQTGMCFEK QCLMRVARSN CQPTGSGSGG PSSSACQAGR AKVYVQDARG SWQRGTVQAA
LGSGRYKAQK YANGSGGLDR ASRKVALQGW EEDELQTSQT TEVDASNMEG GMLPFQNADL
PNNGFPDMTT LDHLHEPALL HNLRRRFFSQ ACDPDHDQES LDMDTSTEEF AARPWNDETL
IKEGLKQDQS LLDMLQGQWY RKEDGQPVGQ ISGAYLVWNP RWKFAEMISP LFEDLSGALV
IELESQLHFG RPFFGPETLI SWGDGDLWAC PYTYTADIVI AMNPYRWFPE LYTDDKRKEY
LVFDRPKLDP HVYTTSSFAY SGLQETKSNQ TILVSGESGA GKTETVKNLG LRDVLILMAH
LAFMAAQLHL WAVIDTSHIK RIVESNPLLE SFGNAQTAVR NDNSSRFGKF IELQLNSGCR
LEGRVNKLSW KFSSIAEERN FHIFYQMLAA DAETRTAIGL GASKTDTIEG KSDAERFHGR
DLGGTVSALA LLSIDGEKLT RLLQTLASVL LLGDESSKLA DCAGQAAAAA QVLAVDAGHP
GDALAKEIYA RVQGARADYP LRRVWSNTRW APHANLNRLC INYANEKLQQ KFTHDVFKAV
QQEYTAESFM QQGRERLGDR PCEGGKSGFS LQCDLVSEAG GKKEGIPWDR IEFKDNAPIL
ALQLGEALRF YALGALRLAE NGKKEMHAEH ANPRIESKLG IVAMLNEECV RPKGSNEFLG
QMSDMVTSAL VVSRNFVSKL LSVHKEDAAF SVPKLGKMRE LQFCIRHYAG EVMYTAEGWL
DRNNDTVSED VINLMRGSGN ELLASLFTEE TQVVTKFKTS LSQLMETIGQ TNTQYVRCIK
PNQNKSPREV NNEMVVDQLL GMIRSALAGC EGNFCNSYVF QELCKCALGG DDAAICRRLL
GALVKDEEKY QVYFKSGVLE SLEERMQAAA VEFGTKLASS GVHLLCFDAG AQLPTLPRAE
VEFWASVIK
//
