ID A0A093K5G6_STRCA Unreviewed; 1985 AA.
AC A0A093K5G6;
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=N308_08910 {ECO:0000313|EMBL:KFV85704.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV85704.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV85704.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV85704.1};
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; KL206788; KFV85704.1; -; Genomic_DNA.
DR STRING; 441894.ENSSCUP00000021806; -.
DR Ensembl; ENSSCUT00000028834; ENSSCUP00000021806; ENSSCUG00000015883.
DR Proteomes; UP000053584; 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 GO; GO:0008307; F:structural constituent of muscle; IEA:Ensembl.
DR GO; GO:0055013; P:cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0048251; P:elastic fiber assembly; IEA:Ensembl.
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; 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:UP000053584}.
FT DOMAIN 30..80
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 84..795
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 673..695
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 865..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1712..1814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1896..1985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1712..1729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1738..1756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1776..1799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1800..1814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1896..1927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1959..1985
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 1985 AA; 229484 MW; 271ED791022A1365 CRC64;
MAQKPLSDDE KFLFVDKNFI NNPLAQADWS AKKLVWVPSE KHGFEAASIK EEKGDEVTVE
LSENGKKVTL SKDDIQKMNP PKFSKVEDMA ELTCLNEASV LHNLRERYFS GLIYTYSGLF
CVVINPYKQL PIYSEKIIDM YKGKKRHEMP PHIYAIADTA YRSMLQDRED QSILCTGESG
AGKTENTKKV IQYLAYVASS HKGKKDTSIT QGPSFAYGEL EKQLLQANPI LEAFGNAKTV
KNDNSSRFGK FIRINFDVTG YIVGANIETY LLEKSRAIRQ AKDERTFHMF YYLIAGASEQ
MKNDLLIENF NNYTFLSNGH VPIPAQQDDE MFQETLEAMR IMGFSDEEQT AILRVVSSVL
QLGNIVFKKE RNTDQASMPD NTAAQKVCHL MGINVTDFTR AILTPRIKVG RDVVQKAQTK
EQADFAVEAL AKAKYERLFR WILTRVNKAL DKTKRQGASF LGILDIAGFE IFEINSFEQL
CINYTNEKLQ QLFNHTMFIL EQEEYQREGI EWNFIDFGLD LQPCIELIER PTNPPGVLAL
LDEECWFPKA TDTSFVDKLG QEQGNHPKFQ KTKQLKDKTE FSIIHYAGKV NYNATAWLTK
NMDPLNDNVT SLLNKSSDKT TLNHSIHTFF YISVDRIVGL DQMAKMTESS LPSSSKTKKG
MFRTVGQLYK EQLTKLMTTL RNTNPNFVRC IIPNHEKRAG KLDAHLVLEQ LRCNGVLEGI
RICRQGFPNR IVFQEFRQRY EILAANAIPK GFMDGKQACI LMIKALELDP NLYRIGQSKI
FFRTGVLAHL EEERDLKITD IIIAFQAQCR GYLARKAFAK RQQQLTAMKV IQRNCAAYLK
LRNWQWWRLF TKVKPLLQVT RQEEEMQAKD EELQRTKERQ QKAESELKEL EQKHTQLCEE
KNLLQEQLQA ETELYAEAEE MRVRLAAKKQ ELEEILHEME ARIEEEEERS QQLQAEKKKM
QQQMLDLEEQ LEEEEAARQK LQLEKVTADG KIKKMEDDIL IMEDQNNKLT KERKLLEERI
SDLTTNLAEE EEKAKNLTKL KNKHESMISE LEVRLKKEEK SRQELEKMKR KLEGESSDLH
EQIADLQAQI AELKMQLAKK EEELQAALAR LEDETGQKNN ALKKIRELEA HISDLQEDLE
SERAARNKAE KQKRDLGEEL EALKTELEDT LDTTATQQEL RAKREQEVTV LKRALEEETR
THEAQVQEMR QKHTQAVEEL TEQLEQIKRA KANLDKTKQT LEKDKAELAN EVRSLSQAKQ
DVEHKKKKLE VQLQDLQSKY TEGERVRTEL NEKVHKLHVE VENVTGLLNE AESKTIKLTK
DVATLGSQLQ DTQELLQEET RQKLNVSTKL RQLEDEKNSL QEQLDEEVEA KQNLERHIST
LTIQLSDSKK KLQEYVSTVE TLEEGKKKFQ KEIEGLTQQF EEKAASYDKL EKTKNRLQQE
LDDLVVDLDN QRQLVSNLEK KQKKFDQMLA EEKNISSKYA DERDRAEAEA REKETKALSL
ARALEEALEA KEELERTNKM LKAEMEDLVS SKDDVGKNVH ELEKSKRAFE QQVEEMKTQL
EELEDELQAT EDAKLRLEVN MQAMKVQFER DLQARDEQNE EKRRQLLKQL HEHETELEDE
RKQRALAAAA KKKLEIDVKD LEGQADSANK AREEAIKQLR KLQAQMKDYQ RELDDARAAR
EEIFATAREN EKKAKSLEAE LIQLQEDLAA AERARKQADL EKEEMAEELA SATSGRTSLQ
DEKRRLEARI AQLEEELEEE QSNMEAMGDR MRKAVQQAEQ LNNELATERS TAQKNESARQ
QLERQNKELK SKLQEMEGAV KSKFKATIAA LEAKIASLEE QLEQEAREKQ VAAKTLRQKD
KKLKDALLQV EDERKQAEQY KEQAEKGNTR LKQLKRQLEE AEEESQRINA NRRKLQRELD
EATESNEALG REVAALKSKL RRGNEPTSFA PPRRSGGRRV IENATEGSEE VDARDGDFNG
TKASE
//
