ID A0A091RJ25_9GRUI Unreviewed; 1938 AA.
AC A0A091RJ25;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Myosin-4 {ECO:0000313|EMBL:KFQ39576.1};
DE Flags: Fragment;
GN ORFNames=N332_02148 {ECO:0000313|EMBL:KFQ39576.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ39576.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ39576.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ39576.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK819673; KFQ39576.1; -; Genomic_DNA.
DR Proteomes; UP000053369; 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; -; 4.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 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 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:SF44; MYOSIN-13; 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; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 4.
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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
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:UP000053369}.
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 86..782
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 659..681
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1058..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1889..1914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1168..1550
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT NON_TER 1938
FT /evidence="ECO:0000313|EMBL:KFQ39576.1"
SQ SEQUENCE 1938 AA; 223574 MW; 59E7E00A5D96F7F6 CRC64;
MSSDAEMAIF GEAAPYLRKP EKERIEAQNR PFDAKAACFV VDGKQMYVKG TIQSREGSKV
TVKTYDDTIV TVKDDEVFPM NPPKFDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNPEVV TGYRGKKRQE APPHIFSISD NAYQFMLTDR NNQSILITGE
SGAGKTVNTK RVIQYFATIA VTGEKKKDQQ PGKMQGTLED QIIQANPLLE AFGNAKTVRN
DNSSRFGKFI RIHFGTTGKL ASADIETYLL EKSRVTFQLA SERSYHIFYQ IMSNKKPELI
DLLLISTNPY DFAYVSQGEI TVASIDDSEE LLATDSAVDI LGFNPDEKVG MYKLTGAVMH
YGNMKFKQKQ REEQAEPDGT EVADKAAYLM GLNSADLLKA LCYPRVKVGN EYVTKGQNVQ
QVYNSVGALA KSVYEKMFLW MVTRINQQLD TKQPRQHFIG VLDIAGFEIF DFNSLEQLCI
NFTNEKLQQF FNHHMFVLEQ EEYKKEGIEW EFIDFGMDLA ACIELIEKPM GIFSILEEEC
MFPKATDTSF KNKLYDQHLG KSNNFQKPKP VKGKAEAHFS LMHYAGTVDY NISGWLDKNK
DPLNETVVGL YQKSSLKLLS FLFSNYAGAE TSDSGGGKKG AKKKGGSFQT VSAVFRENLN
KLMTNLRSTH PHFVRCLIPN ETKTPGEMDH YLVMHQLRCN GVLEGIRICR KGFPSRIIYA
DFKQRYKILN ASAIPEGQFI DSKKASEKLL SSIDVDHNQY RFGHTKVFFK AGLLGLLEEM
RDEKLVSLIT HTQAMCRGYL MRIKFKKMNE RRESIYIIQY NVRAFMNVKH WPWMKLFFKI
KPLLKSAESE KEMANMKEEF EKTKEELAKS EAKRKELEEK MVTLLQEKND LQLQVQSESE
NLADAEERCE GLIKSKIQLE AKIKELSERL EDEEETNAEL IAKKRKLEDE CSELKKDIDD
LELTLAKVEK EKHATENKVK NLTEEMAALD ENISKLTKEK KALQESHQQT LCDLQVEEDK
VSTLTKTKTK LEQQVDDLEG SLEQEKKLRM DLERAKRKLE GDLKMSQDSI MDLENDKQQM
DDRLKKKDFE FSQLQSKLED EQAQSSQLQK KIKELQAQIE ELEEEIEAER AIRAKTEKQQ
VDLSRELEEI SGRLEEAGGA TAAQIEMNKK REAEFQKMRR DLEEATLQHE ATVATLRKKH
ADSTAELGEQ IDNLQRVKQK LEKEKSELKM EIDDLASNME TVSRAKSNLE KMCRVLEDKF
SEVRTKDEEH LRLINDLNMQ KTRLQTENGE LTRQLEEKES LISQLTRGKH AFTQQNEELK
RQLEEENKAK NALAHALQSA RHDCDLLREQ YEEEQEAKGE LQRALSKANS EVAQWRTKYE
TDAIQRTEEL EEAKKKLAQR LQESEEQIEA VNSKCASLEK TKQRLQGEVD DLMTVVERLN
TACAAFDKKQ KNFDKVLAEW KQKYQESQAE LEAGQKESRS LSTEIFQMKN AYEEMLDQAE
TVRRENKNLQ QEISDLTEQI AESGKANHGL EKAKKQIEQE KCDLQAALEE AEASGSLEHE
EGKILRVQLE LNQVKSDVDR RSAEKDEEIQ QLKRNHQRVL ESMQTMLDAE TRSRNDALRL
KKKMEGDLND MEIQLSHANR QVAETQKHLK AMQGQLKDSQ LHLDDALREN DNLKEQLAMV
ERRNNLMTTE MEEMRAAMEQ TERARKVSEQ ELTDANERVQ LLHSQNTSLL NTKKRLEVDI
THLQNEVEDS TQEARNAEEK AKKAITDAAM MAEELKKEQD TSAHLERMKK NLEQAVKDLQ
HRLDEAEQLA LKSGKKQLQK LEMRINELEN ELDAEQKQRT ESLKGVRKYE RRLKELTYQS
EEDKKNILRL QDLVNKLQLK VKAYKKQAEE AEEQANTNLS RCRKTQHKLE EAEERADIAE
CQVNKLRAKS HDIGGQVS
//
