ID H2YUM5_CIOSA Unreviewed; 1849 AA.
AC H2YUM5;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
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:ENSCSAVP00000009035.1, 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:ENSCSAVP00000009035.1}
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; ENSCSAVT00000009149.1; ENSCSAVP00000009035.1; ENSCSAVG00000005344.1.
DR GeneTree; ENSGT00940000154905; -.
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:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.58.530; -; 2.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR046987; Myo9.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46184:SF5; HEAVY CHAIN, UNCONVENTIONAL MYOSIN; 1.
DR PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00109; C1; 1.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..93
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 132..917
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1564..1613
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1632..1822
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 760..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..820
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1000..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 225..232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1849 AA; 210077 MW; 00576329CA16EB5C CRC64;
ATYMIHVHPV DCSTSSVVES ISCTKRTTAA EVVAKVTRKL GIENGLSYVL VEMHKDRGEE
MILAQSDLPV QRMLLWPTQF QHSYKFVLRE TDESGSVMYH GANSWHEKAE RVSTERDMAS
KGFLPPSKLS DSDCPDLCAI SSLSQNKILE ILRKRFLKDK IYTYSADTLI SINPYKFMPI
YNPKYMTLYQ NRRKEDLEPH IYAIADTAFN TMVQTKQNQC IVITGKSGSG KTQATHFLVH
HSLALCQKSY MTGVENMLTG AGPVLEAFGN AQTEHNNNSS RFGKFLKIHF YGSGLLSGAD
VQTYLLEKSR LVHQEPNEKN FHIFYYLLYG TSPEELKEIY LDQNTNYNYL KQCSKHANTD
APAELERLRQ AMEVMGFYIG AQRSIFRLIA AIILLGNITF KMKSGRDETL EIQDESYLTS
VSLLLGLDKN VVRKCLLTRK AKAGAGERFV LSLKLEEARA TRDAMSKALY QSLFDWAVSS
VNMALAQKTR DTKLKSQSQW IGLLDIFGFE DFVKNSFEQF CINYASEHLQ HYCIKHTFQL
EQEEYRAEGL TWKEVDYADN SGCLLLYEKK ITGLFHLIDE NFPGANNHTL LSQFNRVHGN
TRYYDTTVVK EDAFMIVHYA GKVKYQIKDF REKNHDQVRE DLITLVRTSQ SSFIQGIVSK
SPAAVVRWGV LRAIVRAMFA FKNAGKKTLR KFFSYFFLPV TIFTSARIWQ TFICRAGHNH
LKKIFVFEAT TNFKYKDIIC VKPSRMARLS LHQTGVAQSL SGSESPRETS FYGRRKVNAT
SRGRKKTNSI TQQYQASLSL LMSTLEQAHP FFVRCIQPNS KKVPLKVDEK LVLHQLRCSG
LLQTIQLHQT RYPERMTGAA FATQFKLLLP QSNATLPEIK NFLLKIRLQP GTDFQIGKTQ
IFLRDHASRV LKESLHRVVL KHVILLQSRI RGYLARRSYC QQRAAAVQIQ SYWRMSYRIK
KKQRSNAALL IQRNYRGHRS RLLYRTLKLE KMDEQRQSWP IYSSASKKEQ TIDDKSDETS
PCMSPPNRTP QFNDTNNNHD ISDKLKGTID SPEPQATPPV DKTPFRARTK AGELFLKAAY
PPNKIVVVKP VVYVPSSKRK QYDDETDYAK SYSLKPSVKT QDTGNFMYTT SPSKIDTEME
AAAPVQDKQA EKNTSDLKPT DHPLNGEIAE TNYLTRAHSE SGSPSSGWSN RGSSSISTGP
VIPNKPNSVP TKVEKLVPDK KSETSKNEDL ATTSQPTVPS FARSVSMERY YLNRGRQFYL
KLNITTVTHS VALSKPRRQR SNSAIETYMA SKVQPPSTDP VARKSASLSA EAFAKKCMQE
QFLMFSSLQE KASIPQYAPL HDSDQETHHH QHTVNHLVLK CHIKYYACNI TEDLTDGGKR
GSAFIEAVRK TFWGSSRGQS RTHPTLAERK SNDSAISAND AVNIRSLEEE KFSPKLLVSS
ADVLLLLDDF IKSKTSSFNG EHLVDQVFKI SLNEFCANLT ALYSFATLSG DTNGLRYKDI
VSNFRQVLEK TANHYSLDQY AAMMGVNGFR GYMNEFMNDV LPKYTAREAK SKRKKGKDDS
EKLGHHFTGV QWGITQVCEF CNNVMWLMEA GLMCKICKFA CHKKCFKQLT TRCPGSTEVD
KLKSKPKKLF GESLASLASK ESSVPTFIDK CISYMEMNGI YQEGIYRKSA AVAQNKLLEE
SLNKDIECQK VNFDDYNIHC VASCFKKFLR SLPSPLVPYD KYFEFLQAAR ITKEREKVNA
LYHVLEGIPR QNHATLERIV FHLARVAQQE PTNRMSPSNL AIVFTPCFFA APPHVSPIEA
AEQVGDMTKA VECVISEQVK KIRSTLESIS EIQSAESSTN ERLKQIRQS
//
