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Database: UniProt
Entry: H2YYX2_CIOSA
LinkDB: H2YYX2_CIOSA
Original site: H2YYX2_CIOSA 
ID   H2YYX2_CIOSA            Unreviewed;      1842 AA.
AC   H2YYX2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Myosin motor domain-containing protein {ECO:0000259|PROSITE:PS51456};
OS   Ciona savignyi (Pacific transparent sea squirt).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000010533.1, 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:ENSCSAVP00000010533.1}
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}.
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DR   Ensembl; ENSCSAVT00000010660.1; ENSCSAVP00000010533.1; ENSCSAVG00000006193.1.
DR   GeneTree; ENSGT00940000163461; -.
DR   HOGENOM; CLU_000192_8_0_1; -.
DR   Proteomes; UP000007875; 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   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; -; 1.
DR   Gene3D; 6.10.250.2420; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 2.
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; 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; 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; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|PROSITE-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          17..702
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          579..601
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1105..1151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1713..1755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1792..1842
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          763..1079
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1808..1842
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         110..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1842 AA;  213773 MW;  375655D95346AB47 CRC64;
     MTVKEDDLQE MNPPRYEKCE DMAGMTFLNE ASVLNNLRSR YESFMIYTYS GLFCVTVNPY
     KMLPVYAPYV ISAYKGKRRT EMPPHLYSIA DNAYTEMLMN RENQSMLITG ESGAGKTVNT
     KKVIQYFALV AAFGGSQDDG KGTLEDQIVQ CNPAMEAFGN AKTVRNDNSS RFGKFIRIHF
     GSTGLLASGD IEHYLLEKSR VIYQQEGERN YHIFYQIISG SKPELIDQLL VTKDPYDYRS
     ISQGVVSVPS MDDGAELLLT DDAFRVLGFN QEEISGIYRL MAGIMHQQNM KFKNKQREEQ
     AEPDGTEDAD KVAYLFGLNS ADFIKYLCHP RVKVGNEYVT KGHYGIGALS KGLFGRHFDW
     LVKLINQTLS TKLPRSFFIG VLDIAGFEIF DSNSFEQLCI NFTNEKLQQF FNHHMFVLEQ
     EEYKKEGIDW VFIDFGMDLA ACIELIEKPL GIMSILEEEC MFPKASDDTF KEKLYQNHLG
     KSKAFGKPVK KTKYEAHFEL YHYAGTVQYN ICGWLEKNKD PLNNSVVDLY KKASMKLMQT
     IWEGYVSPEE AASGGGGKGG KRKKGGSFMT VSSLHRQSLN ALMTNLRSTA PHFVRCLIPN
     ERKCPGEMDS HLVLHQLRCN GVLEGIRICR KGFPNRVPYG DFKQRYRILN PNAAPEGQFM
     DSKKSSEKLL GSIDINHEAY KLGHTKVFFR AGMIGKLEEM RDNKLSSIFK LIQARMRGML
     MRREYQKMIE RRQACRIIQS NLRAFFGMAN CEWMKLMFKI KPLLKTAESA KELEMEKEFA
     ETKVNLEKET KRRKELEEMQ VSFIQEKNDL VMQLQAQQDQ IDDGEDRCDQ LIKTKVELDG
     KIKELTERLE DEEELNNELV SKKRKLEDEC SELKKDIDDL EITLAKVEKE KHATENKLKN
     LQEELATQDE QIAKLQKEKK ALQEAHQQTL DDLQSEEDKV NSLTKQKAKL EQQVDDLEAS
     LEQEKKLRME LERTKRKLEG DLRLTQETVM DLENDKQRLE EKLKKQEFEY SQLATKLEDE
     QALVSQLQKK IKELQARIEE LEEEIEAERA ARAKVEKQRA DLSRELEELS ERLEEAGGAT
     AAQIELNKRR EAEFAKLRRE LEESNLGHEA TVSTLRKKHA DTSSEMSEQI RELENELDSE
     QRRNGESVKS QRKIERRLKE VSYQGEEDKK NLTRIQDLVD KLQIKVKTYK RQAEEAEREI
     TTSSTRSSLV QSRSSLDAFR VLGFNQEEIS GIYRLMAGIM HQQNMKFKNK QREEQAEPDG
     TEGMELSTCE LLCVKCDTEL LITLNLTNRA TALNNFASTL QTRSSNTCIE LIEKVMSAQK
     KVSRPSVTVY QLVNTVILKC SCKRRWRKRR QTQEGRFLYD SCRIIQSNLR AFFGMANCEW
     MKLMFKIKPL LKTAESAKEL EEMEKEFAET KVNLEKETKR RKELEEMQVS FIQEKNDLVM
     QLQAQQDQID DGEDRCDQLI KTKVELDGKI KELTERLEDE EELNNELVSK KRKLEDECSE
     LKKDIDDLEI TLAKVEKEKH ATENKVSQQY SNLKNLQEEL ATQDEQIAKL QKEKKALQEA
     HQQTLDDLQS EEDKVNSLTK QKAKLEQQVD DLEASLEQEK KLRMELERTK RKLEGDLRLT
     QETVMDLEND KQRLEEKLKK QEFEYSQLAT KLEDEQALVS QLQKKIKELQ ARIEELEEEL
     EAERAARAKV EKQRADLSRE LEELSERLEE AVSTLRKKHA DTSSEMSEQI RELENELDSE
     QRRNGESVKS QRKIERRLKE VSYQGEEDKK NLTRIQDLVD KLQIKVKTYK RQAEEAEEQA
     NTNLSKYRKL QHELDDAEER AEMAESQLNK MRSKARDTKG EK
//
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