ID A0A091LW20_CARIC Unreviewed; 1976 AA.
AC A0A091LW20;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Myosin-11 {ECO:0000256|ARBA:ARBA00040393};
DE AltName: Full=Myosin heavy chain 11 {ECO:0000256|ARBA:ARBA00042406};
GN ORFNames=N322_08337 {ECO:0000313|EMBL:KFP63783.1};
OS Cariama cristata (Red-legged seriema).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cariamiformes; Cariamidae; Cariama.
OX NCBI_TaxID=54380 {ECO:0000313|EMBL:KFP63783.1, ECO:0000313|Proteomes:UP000054116};
RN [1] {ECO:0000313|EMBL:KFP63783.1, ECO:0000313|Proteomes:UP000054116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N322 {ECO:0000313|EMBL:KFP63783.1};
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}.
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; KK513045; KFP63783.1; -; Genomic_DNA.
DR Proteomes; UP000054116; 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; 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:UP000054116}.
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 1126..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1704..1733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1746..1808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1886..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 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 1886..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; 228376 MW; 6D55321FAC570137 CRC64;
MAQKPLSDDE 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
EQADFAVEAL AKAQFERLFR WILARVNKAL DKTKRQGASF LGILDIAGFE IFEVNSFEQL
CINYTNEKLQ QLFNHTMFIL EQEEYQREGI EWNFIDFGLD LQPCIELIER PTNPPGVLAL
LDEECWFPKA TDTSFVEKLC QEQGNHIKFQ KPKQLKDKTE FCIIHYAGKV TYNATAWLTK
NMDPLNDNVT SLLNKFTADL 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 TDQLEQFKRA KANLDKTKQT LEKDNADLAN EVRSLNQAKQ DVEHKKKKLE
VQLQELQSKY TDGERVRTEL NEKVHKLQVE VENVTSLLNE AESKTIKLTK DVATLGSQLQ
DTQELLQEET RQKLNVSTKL RQLEDEKNSL QEQLDEEVEA KQNLERHIST LTIQLSDSKK
KLQEYSSTIE TMEEGKKKLQ REIESLTQQF EEKAASYDKL EKTKNRLQQE LDDLVVDLDN
QRQLVSNLEK KQKKFDQMLA EEKNISSKYA DERDRAEAEA REKETKALSL ARALEEALEA
KEELERTNKM LKAEMEDLVS SKDDVGKNVH ELEKSKRTLE QQVEEMKTQL EELEDELQAA
EDAKLRLEVN MQALKGQFER DLQARDEQNE EKRRQLLKQL HEYETELEDE RKQRGLAAAA
KKKLEIDVKD LESQVDSANK AREEAIKQLR KLQAQMKDYQ RELDDARAAR EEIFATAREN
EKKAKGLEAE LIQLQEDLAA AERARKQADL EKEEMAEELA SATSGRTSLQ DEKRRLEARI
AQLEEELEEE QSNIEAMGDR MRKAVQQAEQ LNNELATERS TAQKNENARQ QLERQNKELK
SKLQEMEGAV KSKFKATIAA LEAKIASLEE QLEQEAREKQ AAAKTLRQKD KKLKDALLQV
EDERKQAEQY KDQAEKGNTR LKQLKRQLEE AEEESQRINA NRRKLQRELD EATESNEALG
REVAALKSKL RRGNEPASFV PPRRSGGRRV IENATEAADE EMDARDGDFN GTKASE
//
