ID A0A2K5CQP2_AOTNA Unreviewed; 1938 AA.
AC A0A2K5CQP2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Myosin-11 {ECO:0000256|ARBA:ARBA00040393};
DE AltName: Full=Myosin heavy chain 11 {ECO:0000256|ARBA:ARBA00042406};
GN Name=MYH11 {ECO:0000313|Ensembl:ENSANAP00000011019.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000011019.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000011019.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 Ensembl; ENSANAT00000028825.1; ENSANAP00000011019.1; ENSANAG00000023118.1.
DR GeneTree; ENSGT00940000155421; -.
DR OMA; RCYFASK; -.
DR Proteomes; UP000233020; Unplaced.
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 CDD; cd14921; MYSc_Myh11; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 5.
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 PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF23; MYOSIN-11; 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};
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:UP000233020}.
FT DOMAIN 31..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 85..783
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 661..683
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 857..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1744..1802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1866..1938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1761..1787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1788..1802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1866..1915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1938 AA; 223528 MW; 77C08977D7700B3A CRC64;
MAQKGQLSDD EKFLFVDKNF INSPVAQADW AAKKLVWVPS EKQGFEAASI KEEKGDEVIV
ELVENGKKVT VGKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLRERYF SGLIYTYSGL
FCVVVNPYKH LPIYSEKIVD MYKGKKRHEM PPHIYAIADT AYRSMLQDRE DQSILCTGES
GAGKTENTKK VIQYLAVVAS SHKGKKDTSI TGELEKQLLQ ANPILEAFGN AKTVKNDNSS
RFGKFIRINF DVTGYIVGAN IETYLLEKSR AIRQARDERT FHIFYYMIAG AKEKMKSDLL
LEGFNNYTFL SNGFVPIPAA QDDEMFQETL EAMGIMGFNE EEQLSVLKVV SSVLQLGNIV
FKKERNTDQA SMPDNTAAQK VCHLMGINVT DFTRAILTPR IKVGRDVVQK AQTKEQADFA
VEALAKATYE RLFRWILTRV NKALDKTHRQ GASFLGILDI AGFEIFEVNS FEQLCINYTN
EKLQQLFNHT MFILEQEEYQ REGIEWNFID FGLDLQPCIE LIERPNNPPG VLALLDEECW
FPKATDKSFV EKLCTEQGNH PKFQKPKQLK DKTEFSIIHY AGKVDYNASA WLTKNMDPLN
DNVTSLLNAS SDKFVADLWK DVDRIVGLDQ MAKMTESSLP SASKTKKGMF RTVGQLYKEQ
LGKLMTTLRN TTPNFVRCII PNHEKRSGKL DAFLVLEQLR CNGVLEGIRI CRQGFPNRIV
FQEFRQRYEI LAANAIPKGF MDGKQACILM IKALELDPNL YRIGQSKIFF RTGVLAHLEE
ERDLKITDVI MAFQAMCRGY LARKAFAKRQ QQLTAMKVIQ RNCAAYLKLR NWQWWRLFTK
VKPLLQVTRQ EEEMQAKEDE LQKTKERQQK AENELKELEQ KHSQLAEEKN LLQEQLQAET
ELYAEAEEMR VRLAAKKQEL EEILHEMEAR LEEEEDRGQQ LQAERKKMAQ QMLDLEEQLE
EEEAARQKLQ LEKVTAEAKI KKLEDEILVM DDQNNKLSKE RKLLEERISD LTTNLAEEEE
KAKNLTKLKN KHESMISELE VRLKKEEKSR QELEKLKRKL EGDASDYHEQ IADLQAQIAE
LKMQLAKKEE ELQAALARLD DEIAQKNNAL KKIRELEGHI SDLQEDLDSE RAARNKAEKQ
KRDLGEELEA LKTELEDTLD STATQQELRA KREQEVTVLK KALDEETRSH EAQVQEMRQK
HAQAVEELTE QLEQFKRAKA NLDKNKQTLE KENADLAGEL RVLGQAKQEV EHKKKKLEAQ
VQELQSKCSD GERARAELND KVHKLQIEVE SVTGMLNEAE GKAIKLAKDV ASLGSQLQDT
QELLQEETRQ KLNVSTKLRQ LEEKKNRLQD QLDEEIEAKE NLERHISTLN IQLSDSKKKL
QDFASTVEAL EEGKKRFQKE IENLTQQYEE KAAAYDKLEK TKNRLQQELD DLVVDLDNQR
QLVSNLEKKQ KKFDQLLAEE KNISSKYADE RDRAEAEARE KETKALSLAR ALEEALEAKE
ELERTNKMLK AEMEDLVSSK DDVGKNVHEL EKSKRALETQ MEEMKTQLEE LEDELQATED
AKLRLEVNMQ ALKGQFERDL QARDEQNEEK RRQLQRQLHE YETELEDERK QRALAAAAKK
KLEGDLKDLE LQADSAIKGR EEAIKQLRKL QAQMKEFQRE LEDARASRDE IFATAKENEK
KAKSLEADLM QLQEDLAAAE RARKQADLEK EELAEELASS LSGRNALQDE KRRLEARIAQ
LEEELEEEQG NMEAMSDRVR KATQQAEQLN NELATERSAA QKNESARQQL ERQNKELRSK
LQEMEGAVKS KFKSTIAALE AKIAQLEEQV EQEAREKQAA TKSLKQKDKK LKEVLLQVED
ERKMAEQYKE QAEKGNARVK QLKRQLEEAE EESQRINANR RKLQRELDEA TESNEAMGRE
VNALKSKLRG PPQQETSQ
//
