ID A0A3Q3X002_MOLML Unreviewed; 1929 AA.
AC A0A3Q3X002;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Myosin, heavy chain b {ECO:0008006|Google:ProtNLM};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000015134.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000015134.1}
RP IDENTIFICATION.
RG Ensembl;
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 STRING; 94237.ENSMMOP00000015134; -.
DR Ensembl; ENSMMOT00000015381.1; ENSMMOP00000015134.1; ENSMMOG00000011556.1.
DR OMA; IHIIEVM; -.
DR Proteomes; UP000261620; Unplaced.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
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:0048731; P:system development; IEA:UniProt.
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; -; 4.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 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 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; 5.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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:UP000261620}.
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 86..781
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 658..680
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1871..1898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 845..1643
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"
SQ SEQUENCE 1929 AA; 221003 MW; B37007D3A0FE1EBA CRC64;
MSTDSEMKQF GPAAIYLRKP EKERIEAQNT PFDAKTAFFV VDPGEMYVKG KLVKREGGKV
TVETLSGKTV TVKEDDIYPM NPPKFDKIED MAMMTHLNEP GVLYNLKERY ASWMIYTYSG
LFCVVVNPYK WLPVYENQVV VSYRGKKRVE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQFFATIA VSSGVKKSEP IPGKMQGSLE DQIIAANPLL EAYGNAKTVR
NDNSSRFGKF IRIHFGTSGK LASADIETYL LEKSRVTFQL SAERSYHIFY QLTTGHKSEL
LESLLITTNP YDYPMISQGE ITVKSIDDVE ELIATDSAID ILGFTSDEKL GIYKLTGAVM
HHGNMKFKQK PREEQAEPDG TEVADKIAYL LGLNSADMLK CLCYPRVKVG NEMVTKGQTV
SQVHNAVMAL CKSIYEKMFL WMVIRINEML DTKQSRSYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKASDTT FKNKLHDQHL GKTKGFDKPK PAKGKAEAHF SLAHYAGVVD YNISGWLDKN
KDPLNNSAVQ LYQKASNKLL SLLYMAHASG DEAGGGGKKG KKKGGSFQTV SALFRENLGK
LMTNLRSTHP HFVRCLIPNE TKTPGLMENH LVIHQLRCNG VLEGIRICRK GFPSRILYGD
FKQRYKVLNA SVIPEGQFID NKKASEKLLG SIDVDHTQYR FGHTKVFFKA GLLGLLEEMR
DEKLATLMTM TQARCKGFLM RKEFIKMMER RESIFTIQYN VRSFMNVKNW PWLKLYFKIK
PLLKSAETEK ELQQMKENYE KMKTDLAVAL AKKKELEEKM VSLLQEKNDL HLQVAAESEN
LSDAEERCEG LIKSKIQLEA KLKDTTERLE DEEEINAELT AKKRKLEDEC SELKKDIDDL
ELTLAKVEKE KHATENKVKN LTEEMASQDE SIAKLTKEKR ALQESHQQTL DDLQAEEDKV
NTLTKVKTKL EQQVDDLEGS LEQERKIRMD LERAKRKLEG DLKLAQESIM DLENDKQQSE
EKIKKKDFEI NQLLSKIEDE QTLGAQLQKK IKELQARIEE LEEEIEAERA ARAKVEKQRA
DLSRELEEIS ERLEEAGGAT AAQIEMNKKR EAEFQKMRRD LEESTLQHEA TAAALRKKQA
DSVAELGEQI DNLQRVKQKL EKEKSEYKME IDDLSSSVEA VAKSKGNLEK MCRTLEDQLN
ELKAKHDENV RQFNDINAQK ARLQTENGEF ARQLEEKEAL VSQLTRAKQA YTQQVEELKR
HIEEELKAKN ALAHAVQSSR HDCDLLREQF EEEQEAKAEL QRGMSKANSE VAQWRTRYET
DAIQRTEELE EAKKKLAQRL QDAEESIEAV NSKCASLEKT KQRLQGEVED LMTDVERANA
LAANLDKKQR NFDKVLAEWK QKYEEGQAEL EGAQKEARSF STEIFKMKNS YEEALDQLET
LKRENKNLQQ EISDLTEQIG ESGKSIHELE KAKKTVENEK AEIQSALEEA EGTLEHEEAK
ILHIQLELNV VKNEVDRKLA EKDEEIEQIK RNSQRVIESI IKKKMEGDLN EMEIQLSHAS
RQAAEALKQL RNVQGQLKDA QLHLDDALRG QEDMKEQVTM VERRNGLMLA EIEELRAALE
QTERGRKVAE QELVDASERV GLLHSQNTSL LNTKKKLEAD FVQVQGEVDD AVQEARNAEE
KAKKAITDAA MMAEELKKEQ DTSAHLERMK KNLEVTVKDL QHRLDEAESL AMKGGKKQLQ
KMESRVRELE AEVEAEQRRG ADAIKGVRKY ERRVKELTYQ TEEDKKNVIR LQDLVDKLQL
KVKAYKRQAE EAEEQASSHI SRLRKVQHEM EEAHERADIA ESQVNKLRVR SRDIGKVSLL
FSSSNGQWS
//
