ID F6WUL2_XENTR Unreviewed; 1987 AA.
AC F6WUL2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Myosin, heavy chain 10, non-muscle {ECO:0000313|Ensembl:ENSXETP00000041404};
GN Name=myh10 {ECO:0000313|Ensembl:ENSXETP00000041404};
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:ENSXETP00000041404};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000041404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000041404};
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:ENSXETP00000041404}
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; ENSXETT00000041404; ENSXETP00000041404; ENSXETG00000016345.
DR AGR; Xenbase:XB-GENE-5957388; -.
DR Xenbase; XB-GENE-5957388; myh10.
DR eggNOG; KOG0160; Eukaryota.
DR eggNOG; KOG0161; Eukaryota.
DR HOGENOM; CLU_000192_4_4_1; -.
DR TreeFam; TF333601; -.
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 CDD; cd14920; MYSc_Myh10; 1.
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..793
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 671..693
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1136..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1705..1739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1780..1804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1868..1921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1934..1987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1707..1727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1780..1797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1942..1958
FT /note="Polar 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 1987 AA; 230440 MW; 982B065A680DACFA CRC64;
MSQRSGQEDP ERYLFVDRDV VYNPTTQADW TAKKLVWVPS ERHGFEAASI KEERGEEVVV
ELAENGKKAM VNKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLKDRYY SGLIYTYSGL
FCVVINPYKN LPIYSENIIE MYRGKKRHEM PPHIYAISES AYRCMLQDRE DQSILCTGES
GAGKTENTKK VIQYLAHVAS SHKGKKDHTI PTESPKAMKH QGELERQLLQ ANPILESFGN
AKTVKNDNSS RFGKFIRINF DVTGYIVGAN IETYLLEKSR AIRQAKDERT FHIFYQLLAG
SGEHLKSDLL LDGFNNYRFV SNGYIPIPGQ QDKDNFQETM EAMHIMGFSH EEILSMLKVV
SAVLQFGNIT FKKERNTDQA SMPENTAAQK LCHLLGLNIM EFTRAILTPR IKVGRDYVQK
AQTKEQADFA VEALAKATYE RLFRWLVHRI NKALDRTKRQ GASFIGILDI AGFEIFELNS
FEQLCINYTN EKLQQLFNHT MFILEQEEYQ REGIEWNFID FGLDLQPCID LIERPANPPG
VLALLDEECW FPKATDKSFV DKLVQEQGTH SKFQKPRQLK DKADFCIIHY AGRVDYKADE
WLMKNMDPLN DNVATLLHQS SDKFVGELWK DVDRIVGLDQ VAGMAETAFG AAYKTKKGMF
RTVGQLYKES LTKLMATLRN TNPNFVRCII PNHEKRAGKL DPHLVLDQLR CNGVLEGIRI
CRQGFPNRIV FQEFRQRYEI LTPNAIPKGF MDGKQACERM IRALELDPNL YRIGQSKIFF
RAGVLAHLEE ERDLKITDII ILFQAVCRGY LARKAFAKKQ QQLIALKVLQ RNCAAYLKLR
HWQWWRLFTK VKPLLQVTRQ EEELLAKDEE LLKVKEKQSK VEGELVEMER KQQQLVEEKN
ILAEQLQAET ELFAEAEEMR ARLAIKKQEL EEILRDLEIR MEEEEERNQV LQNEKKKMQA
HVQDLEEQLD EEEAARQKLQ LEKVTAEAKI KKMEEDILVL EDQNSKFLKE KKLLEERIAE
STSQLAEEEE KAKNLAKLKN KQEMMITDLE ERLKKEEKTR QELEKAKRKL DGETTDLQDQ
IAELQAQIEE LKLQLAKKEE ELQAALARGD EEVLQKNNTL KVVRELQAQI AELQEDLESE
KASRNKAEKQ KRDLSEELEA LKTELEDTLD TTAAQQELRT KREQEVAELK KSIEEETRNH
EAQIQEMRQR QATALEELSE QLEQAKRFKG NLEKNKQSLE SDNKELATEV KSLQQMKAES
EYKRKKLEGQ VQELHTKVLE GDRLRADMVE KSSKLQNELE NVSSLLEEAE KKGIKLAKDA
ASLESQLQDT QELLQEETRQ KLNLSSRIRQ LEEEKNNLQE QQEEEEEARK ALEKQILSLQ
SQLVEAKKKV DDDVGTIEGL EEVKKKLLKD MESLGQRLEE KGIAHEKLEK TKNRLQQELD
DLMVDLDHQR QIVSNLEKKQ KKFDQLLAEE KNISARNAEE RDRAEADARE KETKALSLAR
ALDEALEGRD EFERLNKQLR AEMEDLMSSK DDVGKNVHEL EKSKRALEQQ VEEMRTQLEE
LEDELQGTED AKLRLEVNMQ AMKAQFERDL QTRDEQNEEK KRALVKQVRE LEAELEDERK
QRAMAVAIKK KLEMDMKDLE SQIEAANKGR EDAIKQLRKL QAQMKDYQRE LEEARASRDD
IFAQSKENEK KLKSLEAEIL QLQEELASSE RSRRHAEQER DELADEISNS TSGKSALLDE
KRRLEARIAQ LEEELEEEQS NMELLNDRFR KTTLQVDTLN SELAGERSSA QKSENARQQL
ERQNKELKAK LQELEGSVKS KFKATIATLE SKIAQLEEQL EQEAKERAAS NKLVRRTEKK
LKEVFMQVED ERRHADQYKE QMEKANTRMK QLKRQLEEAE EEATRANASR RKLQRELDDA
TEANEVLSRE VSTLKNRLRR GGPVSFSSSS SRSGRRQLQI EGASLDISDD EIETKNAEVN
EVPTPTE
//
