ID A0A091MNS9_9PASS Unreviewed; 1332 AA.
AC A0A091MNS9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Myosin-6 {ECO:0000313|EMBL:KFP77041.1};
DE Flags: Fragment;
GN ORFNames=N310_04526 {ECO:0000313|EMBL:KFP77041.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP77041.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP77041.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP77041.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Muscle contraction. {ECO:0000256|ARBA:ARBA00037488}.
CC -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy
CC chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
CC regulatory light chain subunits (MLC-2).
CC {ECO:0000256|ARBA:ARBA00038612}.
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 EMBL; KK831746; KFP77041.1; -; Genomic_DNA.
DR Proteomes; UP000053537; Unassembled WGS sequence.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
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; -; 4.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 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; 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:SF11; MYOSIN-6; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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:UP000053537}.
FT DOMAIN 18..713
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 590..612
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT COILED 777..1331
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 111..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP77041.1"
FT NON_TER 1332
FT /evidence="ECO:0000313|EMBL:KFP77041.1"
SQ SEQUENCE 1332 AA; 153199 MW; 96C6E4E2551E65E8 CRC64;
TVTVKETDIH QQNPPKFDKI EDMAMLTFLH EPAVLYNLKE RYAAWLIYTY SGLFCVTVNP
YKWLPVYNAE VVAAYRGKKR SEAPPHIFSI SDNAYQNMLT DRENQSILIT GESGAGKTVN
TKRVIQYFAS IAAIGDRKKE ATNSSKGTLE DQIIQANPAL EAFGNAKTLR NDNSSRFGKF
IRIHFGATGK LASADIETYL LEKSRVIFQL KAERNYHIFY QILSNKKPEL LEMLLITNNP
YDYSYVSQGE VTVASIDDSE ELLATDSAFD VLGFTAEEKA GVYKLTGAIM HFGNMKFKQK
QREEQAEPDG TEDADKSAYL MGLNSADLLK GLCHPRVKVG NEYVTKGQNV QQVYYSIGAL
AKAVYEKMFN WMVVRINNSL DTKQPRQYFI GVLDIAGFEI FDFNSFEQLC INFTNEKLQQ
FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL QACIDLIEKP MGIMSILEEE CMFPKASDMT
FKAKLFDNHL GKSANFGKPR NVKGKPEAHF SLIHYAGTVD YNIIGWLEKN KDPLNETVVG
LYQKSALKLL ANLFSNYAGA DAGGDGGKGK GAKKKGSSFQ TVSALHRENL NKLMANLKTT
HPHFVRCIIP NERKEPGVMD NPLVMHQLRC NGVLEGIRIC RKGFPNRILY GDFRQRYRIL
NPAAIPEGQF IDSRKGAEKL LGSIDIDHNQ YKFGHTKVFF KAGLLGLLEE MRDERLSRII
TRIQAQARGQ LMRIEFKKIL ERRDSLLVIQ WNIRAFMGVK NWPWMKLYVK IKPLLKSAET
EKEMQNMKEE FGRLKEALEK SETRRKELEE KMVSMLQEKN DLQLQVQAEQ DNLNDAEERC
DQLIKNKIQL EAKVKELTER LEDEEEMNAE LTAKKRKLED ECSELKKDID DLELTLAKVE
KEKHATENKV KNLTEEMAGL DETIAKLTKE KKALQESHQQ TLDDLQAEED KVNTLTKAKL
KMEQQVDDLE GSLEQEKKIR MDLERAKRKL EGDLKLTQEN IMDLENDKQQ LEEKLKKKEF
EINQQNSKVE DEQALALQLQ KKLKELQARI EELEEELEAE RTGRAKVEKL RSDLSRELEE
ISERLEEAGG VTSVQIELNK KREAEFQKMR RDLEEATLQH EATAAALRKK HADSVAELSE
QIDNLQRVKQ KLEKEKSDLK LELDDLSSNM EQLIKAKVEG SQVSRTMEDQ AAEHRAKLEE
TQRVLNDTST QRAKLQTENG ELSRQLEEKE ALVSQLTRGK QSYTQQMEDL KRQLEEEMKA
KNALAHALQS ARHDCDLLRE QYEEETEAKA ELQRSLSKAN SEVAQWRTKY ETDAIQRTEE
LEEAKKKLAQ RL
//
