ID A0A1V4KTT5_PATFA Unreviewed; 2014 AA.
AC A0A1V4KTT5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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|EMBL:OPJ87795.1};
GN ORFNames=AV530_001188 {ECO:0000313|EMBL:OPJ87795.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ87795.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ87795.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ87795.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ87795.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ87795.1}.
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DR EMBL; LSYS01001700; OPJ87795.1; -; Genomic_DNA.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0060473; C:cortical granule; 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:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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; -; 1.
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 InterPro; IPR014751; XRCC4-like_C.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF23; MYOSIN-11; 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; 5.
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:UP000190648}.
FT DOMAIN 71..121
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 125..823
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..723
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 893..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1750..1769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1925..2014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1925..1955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1987..2014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 218..225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2014 AA; 232217 MW; CD9D6FA1C64A850C CRC64;
MAGRLGGRRT RAVPAGAAQV PDSPTHPLLP KPDTSGVYRV KMSQKPLSDD EKFLFVDKNF
VNNPLAQADW SAKKLVWIPS EKHGFEAASI KEEKGDEVTV ELAENGKKVT LSKDDIQKMN
PPKFSKVEDM AELTCLNEAS VLHNLRERYF SGLIYTYSGL FCVVVNPYKQ LPIYSEKIIE
MYKGKKRHEM PPHIYAIADT AYRSMLQDRE DQSILCTGES GAGKTENTKK VIQYLAVVAS
SHKGKKDTTI TGELEKQLLQ ANPILEAFGN AKTVKNDNSS RFGKFIRINF DVTGYIVGAN
IETYLLEKSR CIRQAKDERT FHIFYYLIAG ASEQMRNDLL LEAFNNYTFL SNGHVPIPSQ
QDDEMFLETL EAMKIMGFTD EEQTAILRVV SSVLQLGNIV FKKERNTDQA SMPDNTAAQK
VCHLMGINVT DFTRAILTPR IKVGRDVVQK AQTKEQADFA IEALAKAKFE RLFRWILARV
NKALDKTKRQ GASFLGILDI AGFEIFEVNS FEQLCINYTN EKLQQLFNHT MFILEQEEYQ
REGIEWNFID FGLDLQPCIE LIERPTNPPG VLALLDEECW FPKATDTSFV EKLIQEQGNH
PKFQKSKQLK DKTEFCIMHY AGKVTYNASA WLTKNMDPLN DNVTSLLNQS SDKFVADLWK
DVDRIVGLDQ MAKMTESSLP SASKTKKGMF RTVGQLYKEQ LTKLMTTLRN TNPNFVRCII
PNHEKRAGKL DAHLVLEQLR CNGVLEGIRI CRQGFPNRIV FQEFRQRYEI LAANAIPKGF
MDGKQACILM IKALELDPNL YRIGQSKIFF RTGVLAHLEE ERDLKITDII IAFQAQCRGY
LARKAFAKRQ QQLTAMKVIQ RNCAAYLKLR NWQWWRLFTK VKPLLQVTRQ EEEMQAKDEE
LQKTKERQQK AESELKELEQ KHAQLCEEKN QLQEQLQAET ELYAEAEEMR VRLAAKKQEL
EEILHEMEAR IEEEEERSQQ LQAEKKKMQQ QMLDLEEQLE EEEAARQKLQ LEKVTADGKI
KKMEDDILIM EDQNNKLTKE RKLLEERISD LTTNLAEEEE KAKNLTKLKN KHESMISELE
VRLKKEEKSR QELEKVKRKL EGESSDLHEQ IAELQAQIAE LKAQLAKKEE ELQAALARLE
DETSQKNNAL KKIRELEAHI SDLQEDLESE RAARNKAEKQ KRDLGEELEA LKTELEDTLD
TTATQQELRA KREQEVTVLK RALEEETRTH EAQVQEMRQK HTQAVEELTE QLEQFKRAKA
NLDKTKQTLE KENSDLANEV RSLSQAKQDV EHKKKKLEVQ LQELQSKYTD GERIRTELNE
KVHKLQVEVE NVTGLLNEAE SKTIKLTKDV ATLGSQLQDT QELLQEETRQ KLNVSTKLRQ
LEDEKNSLQE QLDEEVEAKQ NLERHISTLT IQLSDSKKKL QEFTSTIEVM EEGKKKLQKE
IESLTQQFEE KAASYDKLEK TKNRLQQELD DLVVDLDNQR QLVSNLEKKQ KKFDQMLAEE
KNISSKYADE RDRAEAEARE KETKALSLAR ALEEALEAKE ELERMNKMLK AEMEDLVSSK
DDVGKNVHEL EKSKRTLEQQ VEEMKTQLEE LEDELQAAED AKLRLEVNMQ AMKVQFERDL
QARDEQNEEK KRQLLKQLHE HETELEDERK QRALAAAAKK KLEMDVKDLE SQVDSANKGR
EEAIKQLRKL QAQMKDYQRE LDDARAAREE IFATARENEK KAKGLEAELI QLQEDLAAAE
RARKQADLEK EEMAEALASA TSGRTSLQDE KRRLEARIAQ LEEELEEEQS NIDAMGDRMR
KAVQQAEQLN NELATERAAA QKNENARQQL ERQNKELKSK LQEMEGAVKN KFKATIAALE
AKIASLEEQL EQEAREKQAA AKTLRQKDKK LKDALLQVED ERKQAEQYKD QAEKGNLRLK
QLKRQLEEAE EESQRINANR RKLQRELDEA TESNEALGRE VTALKSKLRR GNEPASFTAP
RRSGGRRVIE NATEGGDEEM DARDGDFNGT KASE
//
