ID H2YYW6_CIOSA Unreviewed; 1897 AA.
AC H2YYW6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Ciona savignyi (Pacific transparent sea squirt).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000010527.1, ECO:0000313|Proteomes:UP000007875};
RN [1] {ECO:0000313|Proteomes:UP000007875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M.,
RA Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.,
RA Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T.,
RA Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., Borowsky M.,
RA Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J.,
RA Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T.,
RA Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S.,
RA Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A.,
RA Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P.,
RA Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G.,
RA Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K.,
RA Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A.,
RA Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E.,
RA Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M.,
RA Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E.,
RA Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T.,
RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A.,
RA Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J.,
RA Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S.,
RA Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T.,
RA Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G.,
RA Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C.,
RA Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S.,
RA Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P.,
RA Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V.,
RA Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J.,
RA Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T.,
RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C.,
RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K.,
RA Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P.,
RA Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T.,
RA Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A.,
RA Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J.,
RA Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G.,
RA Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000010527.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC 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 Ensembl; ENSCSAVT00000010654.1; ENSCSAVP00000010527.1; ENSCSAVG00000006193.1.
DR GeneTree; ENSGT00940000163461; -.
DR Proteomes; UP000007875; Unassembled WGS sequence.
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-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 6.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 2.
DR Gene3D; 6.10.250.2420; -; 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 Gene3D; 4.10.270.10; Myosin, subunit A; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
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; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF67; MYOSIN-6; 1.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 3.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 6.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 2.
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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
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}; Reference proteome {ECO:0000313|Proteomes:UP000007875}.
FT DOMAIN 31..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 85..770
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1341..1383
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 647..669
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1173..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1794..1826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1852..1897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 831..1147
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1222..1275
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1173..1192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1868..1897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1897 AA; 220812 MW; 51DE7B84B9FFC59E CRC64;
MSFDYEACQD AAQYLRLSRE QIIANQTQKP DGKKYVWFPD KENAYVKGEL IKTDKGKCTI
KACEGGKEMT VKEDDLQEMN PPRYEKCEDM AGMTFLNEAS VLNNLRSRYE SFMIYTYSGL
FCVTVNPYKM LPVYAPYVIS AYKGKRRTEM PPHLYSIADN AYTEMLMNRE NQSMLITGES
GAGKTVNTKK VIQYFALVAA FGGSQDDGKG TLEDQIVQCN PAMEAFGNAK TVRNDNSSRF
GKFIRIHFGS TGLLASGDIE HYLLEKSRVI YQQEGERNYH IFYQIISGSK PELIDQLLVT
KDPYDYRSIS QGVVSVPSMD DGAELLLTDD AFRVLGFNQE EISGIYRLMA GIMHQQNMKF
KNKQREEQAE PDGTEDADKV AYLFGLNSAD FIKYLCHPRV KVGNEYVTKG HYGIGALSKG
LFGRHFDWLV KLINQTLSTK LPRSFFIGVL DIAGFEIFDS NSFEQLCINF TNEKLQQFFN
HHMFVLEQEE YKKEGIDWVF IDFGMDLAAC IELIEKPLGI MSILEEECMF PKASDDTFKE
KLYQNHLGKS KAFGKPVKKT KYEAHFELYH YAGTVQYNIC GWLEKNKDPL NNSVVDLYKK
ASMKLMQTIW EGYVSPEEAA SGGGGKGGKR KKGGSFMTVS SLHRQSLNAL MTNLRSTAPH
FVRCLIPNER KCPGEMDSHL VLHQLRCNGV LEGIRICRKG FPNRVPYGDF KQRYRILNPN
AAPEGQFMDS KKSSEKLLGS IDINHEAYKL GHTKVFFRAG MIGKLEEMRD NKLSSIFKLI
QARMRGMLMR REYQKMIERR QACRIIQSNL RAFFGMANCE WMKLMFKIKP LLKTAESAKE
LEMEKEFAET KVNLEKETKR RKELEEMQVS FIQEKNDLVM QLQAQQDQID DGEDRCDQLI
KTKVELDGKI KELTERLEDE EELNNELVSK KRKLEDECSE LKKDIDDLEI TLAKVEKEKH
ATENKLKNLQ EELATQDEQI AKLQKEKKAL QEAHQQTLDD LQSEEDKVNS LTKQKAKLEQ
QVDDLEASLE QEKKLRMELE RTKRKLEGDL RLTQETVMDL ENDKQRLEEK LKKQEFEYSQ
LATKLEDEQA LVSQLQKKIK ELQARIEELE EEIEAERAAR AKVEKQRADL SRELEELSER
LEEAGGATAA QIELNKRREA EFAKLRRELE ESNLGHEATV STLRKKHADT SSEMSEQVNS
QRKIERRLKE VSYQGEEDKK NLTRIQDLVD KLQIKVKTYK RQAEEAQANT NLSKYRKLQH
ELDDAEERAE MADFNGRGTK EVIQRYFLYR IYRLMAGIMH QQNMKFKNKQ REEQAEPDGT
EGMELSTCEL LFTNYTEPDQ QSNSFEQLCI NFTNEKLQQF FNHHMFVLEQ EEYKKEGIDW
KKVSRPSVTV YQLVNTVILK CSCKRRWRKR RQTQEGRFLY DSCRIIQSNL RAFFGMANCE
WMKLMFKIKP LLKTAESAKE LEEMEKEFAE TKVNLEKETK RRKELEEMQV SFIQEKNDLV
MQLQAQQDQI DDGEDRCDQL IKTKVELDGK IKELTERLED EEELNNELVS KKRKLEDECS
ELKKDIDDLE ITLAKVEKEK HATENKVSQQ YSNLKNLQEE LATQDEQIAK LQKEKKALQE
AHQQTLDDLQ SEEDKVNSLT KQKAKLEQQV DDVSKISQFN NILEASLEQE KKLRMELERT
KRKLEGDLRL TQETVMDLEN DKQRLEEKLK KQEFEYSQLA TKLEDEQALV SQLQKKIKEL
QARIEELEEE LEAERAARAK VEKQRADLSR ELEELSERLE EAGGATAAQI RELENELDSE
QRRNGESVKS QRKIERRLKE VSYQGEEDKK NLTRIQDLVD KLQIKVKTYK RQAEEAEEQA
NTNLSKYRKL QHELDDAEER AEMAESQLNK MRSKARD
//
