ID A0A0A0AJA0_CHAVO Unreviewed; 1971 AA.
AC A0A0A0AJA0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Myosin-11 {ECO:0000256|ARBA:ARBA00040393};
DE AltName: Full=Myosin heavy chain 11 {ECO:0000256|ARBA:ARBA00042406};
GN ORFNames=N301_11078 {ECO:0000313|EMBL:KGL94569.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL94569.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL94569.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL94569.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-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; KL872115; KGL94569.1; -; Genomic_DNA.
DR RefSeq; XP_009884874.1; XM_009886572.1.
DR STRING; 50402.A0A0A0AJA0; -.
DR GeneID; 104287837; -.
DR CTD; 4629; -.
DR OrthoDB; 2877572at2759; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
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; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 5.
DR Gene3D; 1.20.5.370; -; 1.
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 InterPro; IPR014751; XRCC4-like_C.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF23; MYOSIN-11; 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; 6.
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}; Reference proteome {ECO:0000313|Proteomes:UP000053858}.
FT DOMAIN 30..80
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 84..789
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 667..689
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1039..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1698..1728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1741..1760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1770..1801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1881..1971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1698..1714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1770..1784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1785..1801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1881..1912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1944..1971
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1971 AA; 227647 MW; 870759C02952EC1B CRC64;
MAQKSLSDDE KFLFVDKNFI NNPLAQADWS AKKLVWIPSE KHGFEAASIK EEKGDEVTVE
LAENGKKVTL SKDDIQKMNP PKFSKVEDMA ELTCLNEASV LHNLRERYFS GLIYTYSGLF
CVVINPYKQL PIYSEKIIDM YKGKKRHEMP PHIYAIADTA YRSMLQDRED QSILCTGESG
AGKTENTKKV IQYLAVVASS HKGKKDTSIT QGPSFSYGEL EKQLLQANPI LEAFGNAKTV
KNDNSSRFGK FIRINFDVTG YIVGANIETY LLEKSRAIRQ AKDERTFHIF YYLIAGASEQ
MRNDLLLEGF NNYTFLSNGH VPIPAQQDDE MFQETLEAMK IMGFNEEEQI AVLKVVSSVL
QLGNIVFKKE RNTDQASMPD NTAAQKVCHL MGINVTDFTR SILTPRIKVG RDVVQKAQTK
EQADFAIEAL AKAQFERLFR WILARVNKAL DKTKRQGASF LGILDIAGFE IFEINSFEQL
CINYTNEKLQ QLFNHTMFIL EQEEYQREGI EWNFIDFGLD LQPCIELIER PTNPPGVLAL
LDEECWFPKA TDTSFVEKLC QEQGNHPKFQ KPKQLKDKTE FCIMHYAGKV TYNATAWLTK
NMDPLNDNVT SLLKQSSDKF VADLWKDVDR IVGLDQMAKM TESSLPSASK TKKGMFRTVG
QLYKEQLTKL MTTLRNTNPN FVRCIIPNHE KRAGKLDAHL VLEQLRCNGV LEGIRICRQG
FPNRIVFQEF RQRYEILAAN AIPKGFMDGK QACILMIKAL ELDPNLYRIG QSKIFFRTGV
LAHLEEERDL KITDVIITFQ AQCRGYLARK AFAKRQQQLT AMKVIQRNCA AYLKLRNWQW
WRLFTKVKPL LQVTRQEEEM QAKDEELQKT KERQQKAESE LKELELKHTQ LCEEKNLLQE
QLQAETELYA EAEEMRVRLA AKKQELEEIL HEMEARIEEE EERSQQLQAE KKKMQQQMLE
AARQKLQLEK VTADGKIKKM EDDILIMEDQ NNKLTKERKL LEERISDLTT NLAEEEEKAK
NLTKLKNKHE SMISELEVRL KKEEKSRQEL EKTKRKLEGE SSDLHEQIAE LQAQIAELKA
QLAKKEEELQ AALARLEDET SQKNNALKKI RELESHISDL QEDLESERAA RNKAEKQKRD
LGEELEALKT ELEDTLDTTA TQQELRAKRE QEVTVLKRAL EEETRTHEAQ VQEMRQKHTQ
AVEELTEQLE QFKRAKANLD KTKQTLEKDN ADLANEVRSL NQAKQDVEHK KKKLEVQLQE
LQSKYTDGER VRTELNEKVH KLQVEVENVT GLLNEAESKT IKLTKDVATL GSQLQDTQEL
LQEETRQKLN VSTKLRQLED EKNSLQEQLD EEVEAKQNLE RHISTLTIQL SDSKKKLQEY
SSTIETMEEG KKKLQKEIES LTQQFEEKAA SYDKLEKTKN RLQQELDDLV VDLDNQRQLV
SNLEKKQKKF DQMLAEEKNI SSKYADERDR AEAEAREKET KALSLARALE EALEAKEELE
RTNKMLKAEM EDLVSSKDDV GKNVHELEKS KRTLEQQVEE MKTQLEELED ELQAAEDAKL
RLEVNMQALK GQFERDLQAR DEQNEEKRRQ LLKQLHEYET ELEDERKQRA LAAAAKKKLE
MDVKDLESQA DSANKAREEA IKQLRKLQAQ MKDYQRELDD ARAAREEIFA TARENEKKAK
GLEAELIQLQ EELAAAERAR KQADLEKEEM AEELASATSG RTSLQDEKRR LEARIAQLEE
ELEEEQSNIE AMGDRMRKAV QQAEQLNNEL ATERSTAQKN ENARQQLERQ NKELKSKLQE
MEGAVKSKFK TTIAALEAKI ASLEEQLEQE AREKQAAAKT LRQKDKKLKD ALLQVEDERK
QAEQYKDQAE KGNTRLKQLK RQLEEAEEES QRINANRRKL QRELDEATES NEALGREVAA
LKSKLRRGNE PASFAPPRRS GGRRVIENAT DGADEEMDAR DGDFNGTKAS E
//
