ID A0A1W4WQ32_AGRPL Unreviewed; 1950 AA.
AC A0A1W4WQ32;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Myosin heavy chain, muscle isoform X50 {ECO:0000313|RefSeq:XP_018322150.1};
GN Name=LOC108734887 {ECO:0000313|RefSeq:XP_018322150.1};
OS Agrilus planipennis (Emerald ash borer) (Agrilus marcopoli).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia;
OC Buprestoidea; Buprestidae; Agrilinae; Agrilus.
OX NCBI_TaxID=224129 {ECO:0000313|Proteomes:UP000192223, ECO:0000313|RefSeq:XP_018322150.1};
RN [1] {ECO:0000313|RefSeq:XP_018322150.1}
RP IDENTIFICATION.
RC TISSUE=Entire body {ECO:0000313|RefSeq:XP_018322150.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_018322150.1; XM_018466648.2.
DR EnsemblMetazoa; XM_018466648.2; XP_018322150.1; LOC108734887.
DR GeneID; 108734887; -.
DR OrthoDB; 2877572at2759; -.
DR Proteomes; UP000192223; Unplaced.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0030017; C:sarcomere; IEA:UniProt.
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; cd14909; MYSc_Myh1_insects_crustaceans; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 5.
DR Gene3D; 1.20.5.370; -; 4.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 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:SF40; MYOSIN HEAVY CHAIN, MUSCLE-RELATED; 1.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 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; 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}; Muscle protein {ECO:0000256|ARBA:ARBA00023179};
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:UP000192223};
KW Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT DOMAIN 34..83
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 87..779
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 624..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..681
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 900..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1655..1676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1697..1716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1825..1844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1922..1950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1656..1674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1697..1711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 180..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1950 AA; 222683 MW; 026DF728948B480F CRC64;
MPKKEAAAEE DPDPTPYLFV SLEQKRIDQT KPYDAKKSCW VPDEKEGFLL GEIRGTKGDL
VTVGIPGGEE RTLKKDSLFQ VNPPKFEKVE DMADLTFLNE AAVLHNLKQR YYCKLIYTYS
GLFCVAINPY KRFPVYTHRC AKLYRGKRRN EVPPHIFAIS DGAYVNMLTN HENQSMLITG
ESGAGKTENT KKVIAYFATV GASTKKTESD SKKGSLEDQV VQTNPVLEAF GNAKTVRNDN
SSRFGKFIRI HFGPTGKLAG ADIETYLLEK ARVISQQPLE RSYHIFYQIM SGAVPGVKEI
CNLGKNILEY PFVSQGKTTI PGLDDGEEFR ITDEAFDVLG FTQEEKNDIY KITAAVMHMG
GMKFKQRGRE EQAEADGTEE AERVAKLLGI DTQGFVTALL KPRIKVGNEF VTQGRNVAQV
NYSVGALAKA MFDRLFKFLV KKCNETLDTK QKRQHFIGVL DIAGFEIFDF NSFEQLCINF
TNEKLQQFFN HHMFVLEQEE YQREGIEWAF IDFGMDLVAC IDLIEKPMGI LSILEEESMF
PKATDKTFEE KLNNNHLGKS PNFMKPKPPK PGQQAAHFAI GHYAGNVPYN ITGWLEKNKD
PLNDTVVDLY KKGSNKLLQE IFADHPGQSG QADAGGGKGG RGKKGGGFAT VSSAYKEQLN
NLMTTLRSTQ PHFVRCIIPN ELKQPGVIDS HLVMHQLTCN GVLEGIRICR KGFPNRMVYP
DFKLRYKILA ASKIKDMSPT EATRVIVDLV GIDPEQYRFG HTKVFFRAGV LGQMEELRDE
RLGKIMTWLQ SWARGYLSRK EFKRLQEQRL ALQVVQRNLR KYLKLRTWPW YKLWQKVKPL
LNVTRVEDEI AKLEEKAKKA QEAFEREEKA KKELEGLYAK LLEEKTSLLS QLEGEKGSLS
EVQERANKLQ AQKSDLESQL SETQDRLTQE EDARNQLFQQ KKKLEQEISG YKKDVEDLEL
SLQKSEQDKA SKEHQIRNLN DEIAHQDELI NKLNKEKKLS GENNQKVAEE LQAAEDKVNH
LNKVKAKLEQ TLDELEDSLE REKKLRGDVE KAKRKVEGDL KLTQEAVADL ERNKKELEQT
IQRKDKEISS LTAKLEDEQS VVGKQQKQVK ELQARIEELE EEVEAERQAR AKAEKQRADL
ARELEELGER LEEAGGATSA QIELNKKREA ELAKLRRDLE EANIQHEGTL ANLRKKHNDA
VAEMGEQIDQ LNKLKAKAER DRASIYAELQ QTRAAVDQVG REKAAQEKIS KQLQQQLNDV
QGKLDETNRT LNDFDAAKKK LSIENSDLLR QLEEAESQVS QLSKIKISLT TQLEDTKRLA
DEEARERATL LGKFRNLEHD LDNIREQVEE EAEAKADIQR QLSKANADAQ LWRSKYESEG
IARSEELEEA KRKLQARLAE AEETIESLNQ KVVALEKTKQ RLATEVEDLQ LEVDRATAIA
NAAEKKQKAF DKIIGEWKLK VDDLAAELDA SQKECRNYST ELFRLKGAYE EGQEQLEAVR
RENKNLADEV KDLLDQIGEG GRNIHEIEKA RKRLEAEKDE LQAALEEAEA ALEQEENKVL
RSQLELSQVR QEIDRRIQEK EEEFENTRKN HQRALDSMQA SLEAEAKGKA EALRMKKKLE
ADINELEIAL DHANKANAEA QKTIKRYQQQ LKDTQQALEE EQRARDEARE QLGISERRAN
ALQNELEESR TLLEQADRAR RQAEQELGDA HEQLNDLSAQ NASISAAKRK LESELQTLHA
DLDELLNEAK NSEEKAKKAM VDAARLADEL RAEQDHAQTQ EKLRKALETQ IKDLQVRLDE
AEANALKGGK KAIQKLEQRV RELENELDGE QRRHADAQKN LRKSERRIKE LSFQAEEDRK
NHERMQDLVD KLQQKIKTYK RQIEEAEEIA ALNLAKFRKA QQELEEAEER ADMAEQAIAK
FRAKGRSGSA ARGVSPAPPR PRPIDAFDEF
//
