ID A0A091PVP3_LEPDC Unreviewed; 1976 AA.
AC A0A091PVP3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Myosin-11 {ECO:0000256|ARBA:ARBA00040393};
DE AltName: Full=Myosin heavy chain 11 {ECO:0000256|ARBA:ARBA00042406};
GN ORFNames=N330_06424 {ECO:0000313|EMBL:KFQ12012.1};
OS Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ12012.1, ECO:0000313|Proteomes:UP000053001};
RN [1] {ECO:0000313|EMBL:KFQ12012.1, ECO:0000313|Proteomes:UP000053001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ12012.1};
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; KK679828; KFQ12012.1; -; Genomic_DNA.
DR RefSeq; XP_009950071.1; XM_009951769.1.
DR GeneID; 104346872; -.
DR CTD; 4629; -.
DR OrthoDB; 2877572at2759; -.
DR PhylomeDB; A0A091PVP3; -.
DR Proteomes; UP000053001; 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 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; 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; 5.
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:UP000053001}.
FT DOMAIN 30..80
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 84..785
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 663..685
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1129..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1704..1808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1830..1851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1868..1976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1704..1719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1728..1746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1766..1789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1790..1808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1868..1917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1949..1976
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 1976 AA; 228316 MW; DBABF0496E46CCCD CRC64;
MAQKALSDDE KFLFVDKNFI NNPLAQADWS AKRLVWIPSE KHGFEAASIK EEKGDEVTVE
LAENGKKVTL SKDDIQKMNP PKFSKVEDMA ELTCLNEASV LHNLRERYFS GLIYTYSGLF
CVVINPYKQL PIYSEKIIDM YKGKKRHEMP PHIYAIADTA YRSMLQDRED QSILCTGESG
AGKTENTKKV IQYLAVVASS HKGKKDISIT QGPSFSYGEL EKQLLQANPI LEAFGNAKTV
KNDNSSRFGK FIRINFDVTG YIVGANIETY LLEKSRAIRQ AKDERTFHIF YYLIAGASEQ
MRNDLLLEGF NNYTFLSNGH VPIPAQQDDE MFQETLEAMT IMGFTEEEQT AILRVVSSVL
QLGNIVFKKE RNTDQASMPD NTAAQKVCHL MGINVTDFTR SILTPRIKVG RDVVQKAQTK
EQADFAIEAL AKAQFERLFR WILARVNKAL DKTKRQGASF LGILDIAGFE IFEINSFEQL
CINYTNEKLQ QLFNHTMFIL EQEEYQREGI EWNFIDFGLD LQPCIELIER PTNPPGVLAL
LDEECWFPKA TDTSFVEKLC QEQGNHPKFQ KTKQLKDKTE FCIIHYAGKV TYNATAWLTK
NMDXXXXXXN QSSDKFVADL WKDVDRIVGL DQMAKMTESS LPSASKTKKG MFRTVGQLYK
EQLTKLMTTL RNTNPNFVRC IIPNHEKRAG KLDAHLVLEQ LRCNGVLEGI RICRQGFPNR
IVFQEFRQRY EILAANAIPK GFMDGKQACI LMIKALELDP NLYRIGQSKI FFRTGVLAHL
EEERDLKITD VIIAFQAQCR GYLARKAFAK RQQQLTAMKV IQRNCAAYLK LRNWQWWRLF
TKVKPLLQVT RQEEEMQAKD EELQKTKERQ QKAESELKEL ELKHTQLCEE KNLLQEQLQA
ETELYAEAEE MRVRLAAKKQ ELEEILHEME ARIEEEEERS QQLQAEKKKM QQQMLDLEEQ
LEEEEAARQK LQLEKVTADG KIKKMEDDIL IMEDQNNKLT KERKLLEERI SDLTTNLAEE
EEKAKNLTKL KNKHESMISE LEVRLKKEEK SRQELEKIKR KLEGESSDLH EQIAELQAQI
AELKAQLAKK EEELQAALAR LEDETSQKNN ALKKIRELES HISDLQEDLE SERAARNKAE
KQKRDLGEEL EALKTELEDT LDTTATQQEL RAKREQEVTV LKRALEEETR THEAQVQEMR
QKHTQAVEEL TEQLEQFKRA KANLDKTKQT LEKDNADLAN EVRSLNQAKQ DVEHKKKKLE
VQLQELQSKY TDGERVRTEL NEKVHKLQVE VENVTGLLNE AESKTIKLTK DVATLGSQLQ
DTQELLQEET RQKLNVSTKL RQLEDEKNSL QEQLDEEIEA KQNLERHIST LTIQLSDSKK
KLQEYSSTVE TMEEGKKKLQ KEIESLTQQF EEKAASYDKL EKTKNRLQQE LDDLVVDLDN
QRQLVSNLEK KQKKFDQMLA EEKNISSKYA DERDRAEAEA REKETKALSL ARALEEALEA
KEELERTNKM LKAEMEDLVS SKDDVGKNVH ELEKSKRTLE QQVEEMKTQL EELEDELQAA
EDAKLRLEVN MQALKGQFER DLQARDEQNE EKRRQLLKQL HEYETELEDE RKQRALAAAA
KKKLEIDVKD LESQADSANK AREEAIKQLR KLQAQMKDYQ RELDDARAAR EEIFATAREN
EKKAKGLEAE LIQLQEDLAA AERARKQADL EKEEMAEELA SATSGRTSLQ DEKRRLEARI
AQLEEELEEE QSNIEAMGDR MRKAVQQAEQ LNNELATERS TAQKNENARQ QLERQNKELK
SKLQEMEGAV KSKFKTTIAA LEAKIASLEE QLEQEAREKQ AAAKTLRQKD KKLKDALLQV
EDERKQAEQY KDQAEKGSTR LKQLKRQLEE AEEESQRINA NRRKLQRELD EASESNEALS
REVAALKSKL RRGNEPVSFA PPRRSGGRRV IENATEGGDE EMDARDGDFN GTKASE
//
