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Database: UniProt
Entry: F6UD31_ORNAN
LinkDB: F6UD31_ORNAN
Original site: F6UD31_ORNAN 
ID   F6UD31_ORNAN            Unreviewed;      1914 AA.
AC   F6UD31;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 3.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Myosin-2 {ECO:0000256|ARBA:ARBA00039812};
DE   AltName: Full=Myosin heavy chain 2 {ECO:0000256|ARBA:ARBA00041436};
DE   AltName: Full=Myosin heavy chain 2a {ECO:0000256|ARBA:ARBA00042414};
DE   AltName: Full=Myosin heavy chain, skeletal muscle, adult 2 {ECO:0000256|ARBA:ARBA00041387};
OS   Ornithorhynchus anatinus (Duckbill platypus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX   NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000005357.3, ECO:0000313|Proteomes:UP000002279};
RN   [1] {ECO:0000313|Ensembl:ENSOANP00000005357.3}
RP   IDENTIFICATION.
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000005357.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Muscle contraction. Required for cytoskeleton organization.
CC       {ECO:0000256|ARBA:ARBA00037212}.
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). Interacts with GCSAM.
CC       {ECO:0000256|ARBA:ARBA00038665}.
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; 9258.ENSOANP00000005357; -.
DR   Ensembl; ENSOANT00000005358.3; ENSOANP00000005357.3; ENSOANG00000042276.1.
DR   eggNOG; KOG0161; Eukaryota.
DR   GeneTree; ENSGT00940000161336; -.
DR   HOGENOM; CLU_000192_8_1_1; -.
DR   InParanoid; F6UD31; -.
DR   OMA; IHIIEVM; -.
DR   TreeFam; TF314375; -.
DR   Proteomes; UP000002279; Unplaced.
DR   Bgee; ENSOANG00000042276; Expressed in testis and 2 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR   GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR   GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
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:SF39; MYOSIN-2; 1.
DR   Pfam; PF00063; Myosin_head; 2.
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}; 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:UP000002279}.
FT   DOMAIN          33..82
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          86..757
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          634..656
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1103..1149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1103..1130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         179..186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1914 AA;  220511 MW;  0442D1CE6CC0FD17 CRC64;
     MSSDQEMAVF GEAAPFLRKS EKERIEAQNK PFDAKTSVFA VEPKESFVKS TIQSREGGKV
     TVKTEGGATL TVRDDQVFPM NPPKFDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
     LFCVTVNPYK WLPVYNPEVV AAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
     SGAGKTVNTK RVIQYFATIA VTGEKKKEEP GKMQGTLEDQ IISANPLLEA FGNAKTVRND
     NSSRFGKFIR IHFGTTGKLA SADIETYLLE KSRVTFQLKA ERSYHIFYQI TSNKKPELIE
     MLLITTNPYD YPFVSQGEIS VASIDDQEEL MATDSAIDIL GFTSEEKGAI YKLTGAVMHY
     GNMKFKQKQR EEQAEPDGTE VADKAAYLQG LNSADLLKAL CYPRVKVGNE YVTKGQTVEQ
     VTNSVGALAK AIYDKMFLWM VTRINQQLDT KQPRQYFIGV LDIAGFEIFD YNSLEQLCIN
     FTNEKLQQFF NHHMFVLEQE EYKKEGIEWE FIDFGMDLAA CIELIEKPMG IFSILEEECM
     FPKATDTSFK NKLYDQHLGK SANFQKPKPT KGKAEAHFSL IHYAGTVDYN ITGWLEKNKD
     PLNETVVGLY QKSSLKTLAY LFSGAAAAAE AENLNKLMTN LRSTHPHFVR CIIPNETKTP
     GAMEHELVLH QLRCNGVLEG IRICRKGFPS RILYADFKQR YKVLNASAIP EGQFIDSKKA
     SEKLLGSIDV DHTQYKFGHT KVFFKAGLLG LLEEMRDEKL AQLMTRTQAR CRGFLMRVEY
     QKMVERRESV FCIQYNVRAF MNVKHWPWMK LFFKIKPLLK SAETEKEMAT MKEEFEKTKE
     ELAKSEAKRK ELEEKMVSLL KEKNDLQLQV QSEAEALADA EERCDQLIKT KIQLEAKIKE
     VTERAEDEEE INAELTAKKR KLEDECSELK KDIDDLELTL AKVEKEKHAT ENKVKNLTEE
     MAALDETIAK LTKEKKALQE AHQQTLDDLQ AEEDKVNTLT KAKTKLEQQV DDLEGSLEQE
     KKLRMDLERA KRKLEGDLKL AQESIMDVEN EKQQIDEKLK KKEFEISNLQ SKIEDEQALG
     IQLQKKIKEL QARIEELEEE IEAERASRAK AEKQRSELSR ELEEISERLE EAGGATSAQI
     EMNKKREAEF QKMRRDLEEA TLQHEATAAA LRKKHADSVA ELGEQIDNLQ RVKQKLEKEK
     SEMKMEIDDL ASNMETVSKA KGNLEKMCRT LEDQVSELKT KEEEQQRLIN DLSAQRGRLQ
     TEAGEYSRQL DEKEALVSQL SRGKQAFTQQ IEELKRQLEE ETKAKNALAH ALQSSRHDCD
     LLREQYEEEQ ESKAELQRAM SKANSEVAQW RTKYETDAIQ RTEELEEAKK KLAQRLQDAE
     EHVEAVNAKC ASLEKTKQRL QNEVEDLMID VERTNAACAA LDKKQRNFDK ILAEWKQKYE
     ETQAELEASQ KESRSLSTEL FKMKNAYEES LDHLETLKRE NKNLQQEISD LTEQIAEGGK
     HIHELEKVKK QIEQEKCELQ AALEEAEASL EHEEGKILRI QLELNQVKSE IDRKIAEKDE
     EIDQLKRNHL RVVETMQTAL DAEIRSRNDA IRIKKKMEGD LNEMEIQLNH ANRMAAEALR
     NYRNTQGILK DTQLHLDDAL RGQEDLKEQL AMVERRANLM QAEVEELRAA LEQTERSRKI
     AEQELLDASE RVQLLHTQNT SLINTKKKLE TDISQIQGEM EDMVQEARNA EEKAKKAITD
     AAMMAEELKK EQDTSAHLER MKKNMEQTVK DLQLRLDEAE QLALKGGKKQ IQKLEARVRE
     LEGEVDSEQK RNVETVKGLR KHERRVKELT YQTEEDRKNI LRLQDLVDKL QAKVKAYKRQ
     AEEAEEQSNT NLSKFRKIQH ELEEAEERAD IAESQVNKLR VKSREVHTKI VSEE
//
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