ID A0A091HRZ7_CALAN Unreviewed; 1870 AA.
AC A0A091HRZ7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Myosin-7 {ECO:0000256|ARBA:ARBA00039815};
DE AltName: Full=Myosin heavy chain 7 {ECO:0000256|ARBA:ARBA00041438};
DE AltName: Full=Myosin heavy chain slow isoform {ECO:0000256|ARBA:ARBA00043207};
DE AltName: Full=Myosin heavy chain, cardiac muscle beta isoform {ECO:0000256|ARBA:ARBA00041905};
DE Flags: Fragment;
GN ORFNames=N300_09318 {ECO:0000313|EMBL:KFO99078.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFO99078.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFO99078.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFO99078.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity
CC essential for muscle contraction. Forms regular bipolar thick filaments
CC that, together with actin thin filaments, constitute the fundamental
CC contractile unit of skeletal and cardiac muscle.
CC {ECO:0000256|ARBA:ARBA00037090}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC {ECO:0000256|ARBA:ARBA00004204}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL217813; KFO99078.1; -; Genomic_DNA.
DR STRING; 9244.A0A091HRZ7; -.
DR Proteomes; UP000054308; 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; 1.20.5.370; -; 5.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.10.250.2420; -; 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 Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 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 InterPro; IPR014751; XRCC4-like_C.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF1; MYOSIN-7; 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; 5.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000054308}.
FT DOMAIN 19..714
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 591..613
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1834..1870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1834..1864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112..119
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:KFO99078.1"
FT NON_TER 1870
FT /evidence="ECO:0000313|EMBL:KFO99078.1"
SQ SEQUENCE 1870 AA; 215307 MW; F32DCB41D7DB214A CRC64;
QTVTVKEADV HQQNPPKFDK IEDMAMLTFL HEPAVLYNLK ERYAAWMIYT YSGLFCVTVN
PYKWLPVYNA EVVAAYRGKK RSEAPPHIFS ISDNAYQNML TDRENQSVLI TGESGAGKTV
NTKRVIQYFA TIAAIGDRKK EAANSSKGTL EDQIIQANPA LEAFGNAKTV RNDNSSRFGK
FIRIHFGATG KLASADIETY LLEKSRVIFQ LKSERNYHIF YQILSNKKPE LLEMLLITNN
PYDYSYVSQG EVTVASIDDS EELLATDSAF DVLGFTAEEK AGVYKLTGAI MHFGNMKFKQ
KQREEQAEAD GTEDADKSAY LMGLNSADLL KGLCHPRVKV GNEYVTKGQN VQQVYYSIGA
LAKSVYEKMF NWMVVRINNS LETKQPRQYF IGVLDIAGFE IFDFNSFEQL CINFTNEKLQ
QFFNHHMFVL EQEEYKKEGI EWEFIDFGMD LQACIDLIEK PMGIMSILEE ECMFPKASDM
TFKAKLYDNH LGKSSNFGKP RNIKGKTEAH FSLTHYAGTV DYNILGWLEK NKDPLNETVV
GLYQKSALKL LANLFSNYAG TEAGGDGGKG KGAKKKGSSF QTVSALHREN LNKLMTNLKT
THPHFVRCLI PNERKESGVM DNALVMHQLR CNGVLEGIRI CRKGFPNRIL YGDFRQRYRI
LNPTAIPEGQ FIDSRKGAEK LLGSIDIDHN QYKFGHTKVF FKAGLLGLLE EMRDERLSRI
ITRIQAQARG QLMRIEFKKI LERRDALLVI QWNIRAFMGV KNWPWMKLYF KIKPLLKSAE
TEKEMQNMKE EFGRLKEALE KSEARRKELE EKMVSMLQEK NDLQLQVQAE QDNLNDAEER
CDQLIKNKIQ LEAKVKELTE RLEDEEEMNA ELTAKKRKLE DECSELKKDI DDLELTLAKV
EKEKHATENK VKNLTEEMAG LDETIAKLTK EKKALQEAHQ QALDDLQAEE DKVNTLTKAK
VKLEQQADDL EGSLEQEKKI RMDLERAKRK LEGDLKLTQE NIMDLENDKQ QLEEKLKKKD
FEIHQQNSKI EDEQALALQL QKKLKELQAR IEELEEELEA ERTGRAKVEK LRSDLSRELE
EISERLEEAG GATSVQLELN KKREAEFQKM RRDLEEATLQ HEATAAALRK KHADSVAELS
EQLDNLQRVK QKLEKEKSEL KLELDDLSSN MEQLIKAKVG MEKVSRTLED QAAEHRAKLE
ETQRVLNDTN TQRAKLQTEN GGMSRQLEEK EALISQLTRG KQSYTQQMED LKRQLEEEMK
AKNALAHALQ SARHDCDLLR EQYEEETEAK AELQRSLSKA NSEVAQWRTK YETDAIQRTE
ELEEAKKKLA QRLQEAEEAV EAVNAKCSSL EKTKHRLQNE IEDLMADVER SNAAAASLDK
KQRNFDKILS EWKLKFEESQ TELEASQKEA RSLSTELFKL KNAYEESLEH LETFKRENKN
LQEEISDLTE QLGASHKTIH ELEKVRKQLD AEKLELQAAL EEAEASLEHE EGKILRAQLE
FNQVKADYER KLAEKDEEME QAKRNHLRVV DSLQTSLDAE TRSRNEALRL KKKMEGDLNE
MEIQLSHANR SAAEAQSHLK GAQTHLKDTQ LQLDDVVRAN EDLKENIAIV ERRNNLLQAE
LEELRAVVEQ TERARKLAEQ ELIEASERVQ LLHSQNTSLI NQKKKMEGDI SQLQTEVEEA
IQECRNAEEK AKKAITDAAM MAEELKKEQD TSAHLERMKK NMEQTIKDLQ LRLDEAEQLA
LKGGKKQLQK LEARVRELEN ELEAEQKRNT ESIKGLRKSE RRVKELSYQT EEDKKNLLRL
QDLVDKLQMK VKAYKRQAEE AEEQANTNLA KFRKAQHELE EAEERADIAE SQVNKLRAKS
RDMGTKVGPD
//
