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Database: UniProt
Entry: A7SJR5_NEMVE
LinkDB: A7SJR5_NEMVE
Original site: A7SJR5_NEMVE 
ID   A7SJR5_NEMVE            Unreviewed;      1227 AA.
AC   A7SJR5;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDO36037.1};
GN   ORFNames=NEMVEDRAFT_v1g171362 {ECO:0000313|EMBL:EDO36037.1};
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO36037.1, ECO:0000313|Proteomes:UP000001593};
RN   [1] {ECO:0000313|EMBL:EDO36037.1, ECO:0000313|Proteomes:UP000001593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC       ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; DS469680; EDO36037.1; -; Genomic_DNA.
DR   RefSeq; XP_001628100.1; XM_001628050.1.
DR   AlphaFoldDB; A7SJR5; -.
DR   STRING; 45351.A7SJR5; -.
DR   EnsemblMetazoa; EDO36037; EDO36037; NEMVEDRAFT_v1g171362.
DR   eggNOG; KOG0163; Eukaryota.
DR   HOGENOM; CLU_000192_7_2_1; -.
DR   InParanoid; A7SJR5; -.
DR   OMA; MIDHEFE; -.
DR   PhylomeDB; A7SJR5; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR   CDD; cd21759; CBD_MYO6-like; 1.
DR   CDD; cd01382; MYSc_Myo6; 1.
DR   CDD; cd21958; MyUb_Myo6; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 1.
DR   Gene3D; 6.10.220.10; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR049016; MYO6_lever.
DR   InterPro; IPR032412; Myosin-VI_CBD.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR008989; Myosin_S1_N.
DR   InterPro; IPR036114; MYSc_Myo6.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF745; UNCONVENTIONAL MYOSIN-VI; 1.
DR   Pfam; PF21521; MYO6_lever; 1.
DR   Pfam; PF16521; Myosin-VI_CBD; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001593}.
FT   DOMAIN          2..53
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          57..751
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          631..653
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          918..984
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1097..1119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          823..857
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1105..1119
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         151..158
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1227 AA;  141791 MW;  370978829A090D44 CRC64;
     MDGGRKLWVP DNEHGYLLGS IVDIGSDEIT VQLDGFKGKH VTAPYDRTFP AEKDSNKDVE
     DNCALMFLNE GTLLNNLRVR YKKDKIYTYV ANILLAVNPY HEVKELYTKE TIMKYHGKSL
     GTLPPHVFAI ADKAYRDMRA YKQSQSIVVS GESGAGKTES TKYILRYLTE SWGSGDQGRI
     EQRIVEANPL LESFGNAKTM RNINSSRFGK YVEVHFNEKV IVVGGFISHY LLEQSRICMQ
     SKGERNYHVF YRLCAGAPKQ IKDMLRLTRA QDFNYLNQGS LSDPNLDDTS DFKRMDASMD
     NVGFSKEEKS NIYRVVAAVL HLGNIIFEDI DDTHGGCQVS SKCSDEVNIT AKLLGVSPEE
     LQQALTTRLM SAGGADVRVP LKLEQAYAAR DALAKSIYTK LFDHIVAQVN QCFPFTSSFT
     YIGVLDIAGF EYYELNSFEQ FCINYCNEKL QQFFNDRILK QYRIIPAQPS INQDRVTPAI
     NQSGSHLIEA KKTGILDILD EESKLPKPTS AHFTSDIHLK HKNHFRLALP RKSPLMYHRN
     LRDDEGFLIR HFAGAVCYHT QEFIDKNNDA LHNDLAELIS ESKDSFVKSL FPSASGNGDR
     IIGGVTMAGS GRQGSKKLAF VSVGSKFRTQ LQQLMDKLDS TGASFIRCIK PNGKMSANLF
     EGGSILSQLE CAGMVSVLAL MQDGWPSRTQ FTELYQMYKN FLPSKLARLD PRMFCRALFH
     ALGMSDKDYK FGSSKIFFRP GKFAEFDAVM QTDPENLKKL VSKVTTWLIR TRWRRAIYGT
     LSVIKLANKI KFRTQAIIRI QKTVKMFIAV TRHKPRYQGI MKIRRLEVQV DNLAQLASSL
     KKDKDKVSKQ IQDLRNATQS AIKKIKSTMM KRKMIDEVYC DLVKRVNHHL ADLNERQKQQ
     KIAEEQERLR KIQEQMELER KRREEEERKR KQEEEERKRK EEEEQKKRDE EERKRREKEE
     KDRQFQLEKQ RLAEEEQKRQ AMIDQERRDR ELAMRLANDP DAIINDQPES QTLQRSVNTL
     GSNLPAKPEK KYDLTKWKYA ELRDTINTSC DIELLEACRE EFHRRLKVYH HWKKANKSRD
     PSQDAGDQRA PQDIMQAENA PPIPPRAHTQ EPEVPPALPP RRQQRFFRVP FVRPKDKYRE
     SEYRKQGWWF AHFDGQWVAR QMEFHPGKDP LLLVSGEDDL DMCELSLDET GLTRRQGAEI
     AQQEFEVLWH QFGGTPRVYR AKMYQDH
//
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