ID W5ZSG9_MAIZE Unreviewed; 2298 AA.
AC W5ZSG9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Myosin {ECO:0000313|EMBL:AHI45152.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AHI45152.1};
RN [1] {ECO:0000313|EMBL:AHI45152.1}
RP NUCLEOTIDE SEQUENCE.
RA Wang G., Zhong M.;
RT "New Insights into Plant Myosins: a Case Study of the Myosin Gene Family in
RT Maize (Zea mays).";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. Plant myosin class XI subfamily.
CC {ECO:0000256|ARBA:ARBA00008049}.
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DR EMBL; KF493895; AHI45152.1; -; mRNA.
DR ExpressionAtlas; W5ZSG9; baseline and differential.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030048; P:actin filament-based movement; IEA:UniProt.
DR CDD; cd01384; MYSc_Myo11; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 3.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR002710; Dilute_dom.
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; IPR036018; MYSc_Myo11.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF737; MYOSIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 2: Evidence at transcript level;
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}; Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
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}.
FT DOMAIN 8..57
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 62..731
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1746..2037
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 612..634
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1610..1675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2048..2071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2245..2265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 876..1067
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1093..1123
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1159..1312
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1424..1514
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1610..1626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1642..1665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 156..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2298 AA; 260436 MW; 85B2666788B35F12 CRC64;
MASTLNIVIG SHVWVEDKDL SWVDGEVSRI DGKKAHVRTT KGKTVIANIS DIHPKDTEAP
PDGVDDMTRL SYLHEPGVLD NLAVRYAKNI IYTYTGNILI AINPFQRLPN LVDARTMEKY
KGANLGDLDP HVFAIADVSY RQMINEGKSN SILVSGESGA GKTETTKLLM GYLAYLGGRS
GTGERTVEQQ VLESNPVLEA FGNAKTVRNN NSSRFGKFVE IQFDKSGKIS GAAIRTYLLE
RSRVCQINSP ERNYHCFYFL CAAPSEDLKK YKLGDPSLFH YLNQSACIKV DGINDAEEYL
ATRKAMDTVG ITDQEQEAIF RVVAAVLHLG NINFTKGREA DSSIIKDDKS RFHLNTAGEL
LMCDCEKLEN ALIKREINTP EGVITTTVGP NSATISRDGL AKQIYSRLFD WLVNRINASI
GQDPNSNKLI GVLDIYGFES FKTNSFEQLC INFTNEKLQQ HFNQNVFKME QEEYTREQIN
WSYIEFVDNQ DVLDLIERKP GGIIALLDEA CMFPKSTHET LSQKLYEKFK NHKRFTKPKL
SRTAFTIQHY AGDVTYQSDQ FLDKNKDYVV AEHQELLNAS KCSFVSGLFP QATEENTKSS
KSSIATRFKI QLHELMETLS STEPHYIRCI KPNSVLKPGI FENTNVLQQL RCSGVLEAIR
ISCAGYPTRK LFHDFLHRFR VLAPEILKEK NDEKVSCQKV LDKMGLQGYQ IGRTKVFLRA
GQMADLDARR TEMRNNAAKG VQSQFRTHVA REQFLVLRDT SIYLQSFVRA RLACKQHEFL
RQQAAALRIQ KNARWYFAWK TYYQLRLSAI TLQAGLRSMA ARNEFTFRKK NKASVHIQSQ
WRCHRDYSNY MNLKRAALTY QCAWRRRVAR KELRKLKLAA RDTQALKVAK EKLEERVEEL
TSRLDREKKL RADLEKSKAD EVSKLKEALH EMEQRVEEVK AMQEQESAKK AVEEALAQER
EKISLLTTEI EGLKVLLVAE REENDKMKKA HANALETNEE LNKEVSDADE KIKQFSDTVR
RLEGTVSEHE GLLLTERQQN EAANAALAES QARNEALVSK LEDAVKQNDL LHEADQRFQE
ATKNLESSLT FEKQRHEANL IELAEAREKI EELQREVGDT DEKFTLLQTS IQSVEERLRE
KDALLTTERL ESEATKKSLN ESEDRNQDLL LKIEIAQKDI AHFQETVRRH EENMAALETS
LRSERQQNDA IMKQLAESQG EIGELQRKLE DADARNGLLQ DSLQRLEEST ADKDSLLAIE
RHENSETKKE LVGSQKKIAE LLTEVQDTRA NVAELEDLIR RLEQDVTAKE ALLLTEKEAH
DATRKTLTEA QEESGELLKK IHDNDKHILQ LQFTIQRLEE TTVANENLLL REREQNDITT
KAHNESQEKY EELLSKFVDV DRKIDLLQGT IERLGENTTK DSLLLSERHE KDAIKKALTE
AQEKNEELLM KVEDANEKIE QLQTTIDMLE DNVAAKDVSL EAAMKENDAI RRSLTEAQER
NDELLKKISD SEYRIHLLQD TIQKLQVDAI SRLSSFVMEK QESDASKRAV TEAHERNEDL
LKRNEDLLKR NDDLIKKIED SSKIVTQLQE ALQRLEGKAC NLEAENQVLR QQATSTPPTS
AKSPASRAKI SRIHRSPENG HNLNGDIRQT EMKPSTGTSE AITSAANVPD LGDQKDFEHG
EKLQRIPKQK YQPSHHQQPQ DDQQWLLACI PQHLGFSGSK PVAALLIYQC LLHWKSFEAM
KTGVFDSILH AINSATEAQN DMRTLAYWLS NLSTLTVLLQ RSFKTTRTAI STPQRRRFSS
ERIFHGNQTS NAGLAYLSGQ SVVGSAGLPQ VEAKYPALLF KQQLVDLIEK VYGMISDSVK
KELNPLLELC IQDPRTSHSS IAKGNLNGMG QQNQLTYWLG IVKILTSYLD VLRVNHVPSI
LVHKLFTQIF SLIDVQLFNR LLLRRECCSF SNGEYVRAGL TELKHWSDNA TREFAGSAWE
ALRHIRQAVD FLVRLPVLAR LGPQADSHPI VAPFSKTRAP VRQPEDILSK VISAAQGSPL
LTMQALRGPQ DLSHPPNESG SIKPAPAISP EKPRRICSEE ITSGFSTVGA GPEEPRCDCS
CPLGTGNCKD WASQSGECFE EAGHPQASTV EQPLLAAPID VPTLSDQQGI GLSIEQIPEQ
HIEDQGIYLN DDQSTEQNPE QHIEDQGLIL YDDQSTEQNS EQNIEQQTSL IPSGLNLLNS
QPVTTQLNVQ DDRRLLQAYP LVYSRRRRHS RSPPPLTKTP QETPEVAAVR KLMKASKAIE
ALLPQPVIHK QKPKLQAP
//
