ID F6QF55_XENTR Unreviewed; 1960 AA.
AC F6QF55;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Myosin, heavy chain 10, non-muscle {ECO:0000313|Ensembl:ENSXETP00000035704};
GN Name=myh10 {ECO:0000313|Ensembl:ENSXETP00000035704};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000035704};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000035704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000035704};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000035704}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) 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; ENSXETT00000035704; ENSXETP00000035704; ENSXETG00000016345.
DR AGR; Xenbase:XB-GENE-5957388; -.
DR Xenbase; XB-GENE-5957388; myh10.
DR HOGENOM; CLU_000192_8_0_1; -.
DR Bgee; ENSXETG00000016345; Expressed in brain and 14 other cell types or tissues.
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 Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 4.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
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:SF24; MYOSIN-10; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 7.
DR SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 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|ARBA:ARBA00023054};
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}.
FT DOMAIN 31..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 85..779
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 657..679
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1109..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1678..1712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1753..1777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1841..1894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1907..1960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1753..1770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1915..1931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1960 AA; 227456 MW; 228EB93B97B4E0B4 CRC64;
MSQRSGQEDP ERYLFVDRDV VYNPTTQADW TAKKLVWVPS ERHGFEAASI KEERGEEVVV
ELAENGKKAM VNKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLKDRYY SGLIYTYSGL
FCVVINPYKN LPIYSENIIE MYRGKKRHEM PPHIYAISES AYRCMLQGEK NTGGESGAGK
TENTKKVIQY LAHVASSHKG KKDHTIPGEL ERQLLQANPI LESFGNAKTV KNDNSSRFGK
FIRINFDVTG YIVGANIETY LLEKSRAIRQ AKDERTFHIF YQLLAGSGEH LKSDLLLDGF
NNYRFVSNGY IPIPGQQDKD NFQETMEAMH IMGFSHEEIL SMLKVVSAVL QFGNITFKKE
RNTDQASMPE NTAAQKLCHL LGLNIMEFTR AILTPRIKVG RDYVQKAQTK EQADFAVEAL
AKATYERLFR WLVHRINKAL DRTKRQGASF IGILDIAGFE IFELNSFEQL CINYTNEKLQ
QLFNHTMFIL EQEEYQREGI EWNFIDFGLD LQPCIDLIER PANPPGVLAL LDEECWFPKA
TDKSFVDKLV QEQGTHSKFQ KPRQLKDKAD FCIIHYAGRV DYKADEWLMK NMDPLNDNVA
TLLHQSSDKF VGELWKDVDR IVGLDQVAGM AETAFGAAYK TKKGMFRTVG QLYKESLTKL
MATLRNTNPN FVRCIIPNHE KRAGKLDPHL VLDQLRCNGV LEGIRICRQG FPNRIVFQEF
RQRYEILTPN AIPKGFMDGK QACERMIRAL ELDPNLYRIG QSKIFFRAGV LAHLEEERDL
KITDIIILFQ AVCRGYLARK AFAKKQQQLI ALKVLQRNCA AYLKLRHWQW WRLFTKVKPL
LQVTRQEEEL LAKDEELLKV KEKQSKVEGE LVEMERKQQQ LVEEKNILAE QLQAETELFA
EAEEMRARLA IKKQELEEIL RDLEIRMEEE EERNQVLQNE KKKMQAHVQD LEEQLDEEEA
ARQKLQLEKV TAEAKIKKME EDILVLEDQN SKFLKEKKLL EERIAESTSQ LAEEEEKAKN
LAKLKNKQEM MITDLEERLK KEEKTRQELE KAKRKLDGET TDLQDQIAEL MREVELQEFL
WGDEEVLQKN NTLKVVRELQ AQIAELQEDL ESEKASRNKA EKQKRDLSEE LEALKTELED
TLDTTAAQQE LRTKREQEVA ELKKSIEEET RNHEAQIQEM RQRQATALEE LSEQLEQAKR
FKGNLEKNKQ SLESDNKELA TEVKSLQQMK AESEYKRKKL EGQVQELHTK VLEGDRLRAD
MVEKSSKLQN ELENVSSLLE EAEKKGIKLA KDAASLESQL QDTQELLQEE TRQKLNLSSR
IRQLEEEKNN LQEQQEEEEE ARKALEKQIL SLQSQLVEAK KKVDDDVGTI EGLEEVKKKL
LKDMESLGQR LEEKGIAHEK LEKTKNRLQQ ELDDLMVDLD HQRQIVSNLE KKQKKFDQLL
AEEKNISARN AEERDRAEAD AREKETKALS LARALDEALE GRDEFERLNK QLRAEMEDLM
SSKDDVGKNV HELEKSKRAL EQQVEEMRTQ LEELEDELQG TEDAKLRLEV NMQAMKAQFE
RDLQTRDEQN EEKKRALVKQ VRELEAELED ERKQRAMAVA IKKKLEMDMK DLESQIEAAN
KGREDAIKQL RKLQAQMKDY QRELEEARAS RDDIFAQSKE NEKKLKSLEA EILQLQEELA
SSERSRRHAE QERDELADEI SNSTSGKSAL LDEKRRLEAR IAQLEEELEE EQSNMELLND
RFRKTTLQVD TLNSELAGER SSAQKSENAR QQLERQNKEL KAKLQELEGS VKSKFKATIA
TLESKIAQLE EQLEQEAKER AASNKLVRRT EKKLKEVFMQ VEDERRHADQ YKEQMEKANT
RMKQLKRQLE EAEEEATRAN ASRRKLQREL DDATEANEVL SREVSTLKNR LRRGGPVSFS
SSSSRSGRRQ LQIEGASLDI SDDEIETKNA EVNEVPTPTE
//
