ID A0A453F8A0_AEGTS Unreviewed; 2161 AA.
AC A0A453F8A0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Myosin-J heavy chain {ECO:0008006|Google:ProtNLM};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET3Gv20606100.2, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET3Gv20606100.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. Plant myosin class XI subfamily.
CC {ECO:0000256|ARBA:ARBA00008049}.
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DR EnsemblPlants; AET3Gv20606100.2; AET3Gv20606100.2; AET3Gv20606100.
DR Gramene; AET3Gv20606100.2; AET3Gv20606100.2; AET3Gv20606100.
DR Proteomes; UP000015105; Chromosome 3D.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030048; P:actin filament-based movement; IEA:UniProt.
DR CDD; cd01384; MYSc_Myo11; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 3.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR002710; Dilute_dom.
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; IPR036018; MYSc_Myo11.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF737; MYOSIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 3.
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}; Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
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:UP000015105}.
FT DOMAIN 8..57
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 62..732
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1801..2104
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 613..635
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1669..1736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 877..1124
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1153..1432
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1482..1572
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1670..1685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 156..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2161 AA; 245363 MW; ACB3959BB25B5464 CRC64;
MAPVLNIVIG SHVWVADKDL TWIDGEVFKI DGQNAHVCTT KGKTVTANVS DIHPKDTEAP
PDGVDDMTRL SYLHEPGVLD NLAVRYAKNI IYTYTGNILI AINPFQRLPN LVDVQTMEKY
KGANLGDLDP HVFAIADVSY RQMMNEGKSN SILVSGESGA GKTETTKLLM RYLAFLGGRS
GTGGRTVEQQ VLESNPVLEA FGNAKTVRNN NSSRFGKFVE LQFDKSGKIS GAAIRTYLLE
RSRVCQTSSP ERNYHCFYFL CSAPSEDIKK YKLGDPSSFH YLNQSSCIRV DGINDAEEYL
ATRNAMDMVG ITEEEQEAIF RVVAAVLHLG NISFAKGTEA DSSVIKDAKS RFHLNTAGEL
LMCDCEKLEN ALIKREINTP EGVITTTVGP NSATVSRDGF AKQIYSRLFD WLVNRINASI
GQDPSSDKLI GVLDIYGFES FKTNSFEQLC INFTNEKLQQ HFNQNVFKME QEEYTREQIN
WSYIEFVDNQ DVLDLIEKKP GGIIALLDEA CMFPKSTHET LSQKLYEKFK NHKRFAKPKL
SRTAFTIQHY AGDVIYQSDH FLDKNKDYVV AEHQELLNAS RCSFVSVLFP PAPEENTKSS
KSSSIATRFK MQLHELMETL SSTEPHYIRC VKPNSVLKPA IFENTNVLQQ LRCSGVLEAI
RISCAGYPTR KLFHDFLHRF RILAPEILKE KNDEKTTCQK VLDKIGLEGY QIGRTKVFLR
AGQMAELDAR RTEVRNTAAR GVQSQLRTHV AREQFLILRN ASVCLQSFVR ARLACKLHGF
LRQQAAVLKI QKNIRRYFAR RTYSQLCLSA ITLQTGLRTM AARNEFNSRN QDKASIHIQS
RWRRHRDNLS YIKLKRAALT YQCAWRGRVA RRELRQLKMA ARDTQALKVA KEKLEERVEE
LMSRLSLEKK LRTDLEKSKA TEISKLQSAL HDMEQRVEEA AAMKENESAK KAVEEALAQE
REKISSLTSE IEGLKVLLVA EREENDVTKK AHANSQERNE ELNRKVQDAD EMIKQLNDIV
KRLEETVREG EALLLTEKQQ KEEASAALAE SHLRDQAFAI KIEEAEKQIT LLQENVERFE
YSMADLQSSL TIEKQQHEAS VVELAEAQGK IEELLREVGD ADEKSTLLET TVQRLEERLT
ENDALSTTER QENEATKKLL NEVQGKNEEL LKKLEDAGKN IVHYQDTTQR LEENVAAVEV
SLKDERQQND VIMKQLADAQ VEIVELQRNL EGADKRNSLL QDSLQRLEES TSVMDSQLAI
ERHENSKLRS ELSDARLRID ELLNEAQDNH ASLAERDDMI KRLEENVSTK ETLLLTEREQ
NASTSKLLAE EQLKIAELIK NIEEAHRKSD SLQTTIERLE EDGTAKDVLL LTEKQAHEAT
RKTLVEAQER NEELLKKIHD DDKNILQLQF TIQRLEENTA TKENLLLRER EQNDATTKSQ
IESQERSEEL LKKFVDVDRK IDLLQDSIER LGESSTTKDA LLLSERQEKD AMKKELAEAG
EKNGELLMKI EDTNEKIEHL QNTIIKLEED IAAKDVSLEA ARQENDSIRK SLTEAQERNE
ELLRKISDNE YRIHLLQDTV QKIQVDAISR LSSFVMEKQD SDVAKRALTE AQERNEDLLK
RNEDLLNRNN DLVKKIEESG KVITHLQESL QRIEGKAANL EADNHVLRQQ AAATPPSTAK
SPPSRSKITR IHRSPENGHV LNGELRQAEM RPSAGMPEAT PPIGNAPNSS NQKDFEHGEK
LQRVLNQKHQ PQQPQDDQQW LLTCIPQYLG FSGSKPVATL LIYQCLLHWR SFEAMKTGVF
DRILHAINSA IEAEHDVRTL AYWLSNLSAL TVLLQRSFKT TRTALSTPQR RRFSSERTFH
TSQTSNAGLA YLGGQSVVGA TGLPQVEAKY PALLFKQQLV DLIEKVYGMI SDSVKKELNP
LLELCIQDPR TSHSNLAKSN TNGLGQQNQL AHWLNIVKVL ANYLDVLKAN HVPSILVHKL
FVQIFSLIDV QLFNRLLLRR ECCSFSNGEY VKAGLAELKH WSDNATREFA GSAWEALKHI
RQAVDFLVIS LKPMRTLREI RADVCQALSI QQLERIVGMY LDDVNGSNTI SAEFASSLKA
AAREEANTVT TFSILLDDDS SIPFSLDDIT KTMPIIEMAD DDLLRFVREN PGFAFLLQRG
E
//
