ID A0A182UE89_9DIPT Unreviewed; 1218 AA.
AC A0A182UE89;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0000259|PROSITE:PS51456};
OS Anopheles melas.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34690 {ECO:0000313|EnsemblMetazoa:AMEC018816-PA, ECO:0000313|Proteomes:UP000075902};
RN [1] {ECO:0000313|Proteomes:UP000075902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM1001059 {ECO:0000313|Proteomes:UP000075902};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles melas CM1001059_A (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMEC018816-PA}
RP IDENTIFICATION.
RC STRAIN=CM1001059 {ECO:0000313|EnsemblMetazoa:AMEC018816-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR AlphaFoldDB; A0A182UE89; -.
DR STRING; 34690.A0A182UE89; -.
DR EnsemblMetazoa; AMEC018816-RA; AMEC018816-PA; AMEC018816.
DR VEuPathDB; VectorBase:AMEC018816; -.
DR Proteomes; UP000075902; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR CDD; cd14881; MYSc_Myo20; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 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; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036029; MYSc_Myo20.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140:SF498; DACHS, ISOFORM E; 1.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 2.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 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|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 267..1008
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 34..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..899
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1055..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 7..34
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 60..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 355..362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1218 AA; 131501 MW; E482D597CD6B12FB CRC64;
MYAAQGNASS SNEAVHLQQR LKSLSSELVT LRNRLHTGGQ PPGAGPNGGG VPVGGGTVVS
PASGPNTNNA GSNHGTHGAT GLATHATNGL MTSSVGANGI NVLPHLANSC TNNNNNSTSN
NNNSTSNATN NATNNAKNHM LVTSAAQCIP SNQAGNNLNA SQPNVNVLPI VSPRNTSIPY
PLPHHNTSTG ALLHGDTVPC GGTLPRRTAM GFGGSNSIQY NVGGHAGSGG LGTIVSPSGC
GSGTLLTGTG PTTVHLRERQ ESSGRNEMDD LIHLPGPLTE DAVMRTLHNR FNDGKYFTNV
GPILLSVNPY HDVGNPLTLS STRSVPLAPQ LRKIVQEAVR QQAETGYPQA IILSGTSGSG
KTHCSMLLLR QLFAVAGGGP ETDAFKHLAA AFTVLRSLGS AKTTTNSESS RIGQFIEVQV
TDGALYRTKI HCYFLDQTRV IRPLPNEKNY HIFYQMLAGL NADECARLNL EGYSPANLRY
LQHGDIRQDE QEDAARFQAW KACLGILGIP FLDVVRVLAA VLLLGNVQFV DGQGLEVEVV
GETELNAVAN LLGVPPAQLF RGLTTRTHNA RGQLIKSVCD ANMSNMTRDC LAKALYCRTV
ATIVRRANSL KRLGSTLGTL SSDSNESVHN QAEVASQHAS TIGGNAGSKS MAALNNAVRH
ATDGFIGILD MFGFEEPRPA QLEHLCINLC AETMQHFYNT HIFKSSVESC REEGIICDTE
VDYVDNVPCI DLISSLRTGL LSMLDAECSV RGTAESYVAK IKVQHRNSAR LEQRALEPYD
PRLFAIRHFA GRVEYDTTDF LDTNRDVVPD DLVSVFYKHT CNFGFATHLF GTELKALYAQ
ESGPRGLSFR IAPTSHTDLL NGDEPVSTLT QDFHTRLDNL LRTLVHARPH FVRCIRSNTA
EKGGMFDRGA VVRQIRALQV LETVNLMASG FPHRMRFKQF TARYRMLAPF RLLRRCEEKA
LEDCKVILDF ALENPPELDG SVTLSWAPGK RHIFLSEGIR QHLERLRTEV RMKSATLIQA
TWRGWNLRKR LGTIRRTHDI HLMGGALLSI NKTSGARTGN VTHSNANNTG TATRPRPQPI
AGTPPPDPNE KCDSKIIAQT CTLFGLDLER PPPVPPSRSY TVTGNSKLGY PQTRIMKMNF
PEDPAAVGLG EQLRKGEAVT VTGASHRRGH LIVEHNGISL HVPFQYMELV KTIAPIPPGT
GPAGATVPSP PTASAVNI
//
