ID A0A084W8S2_ANOSI Unreviewed; 1167 AA.
AC A0A084W8S2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Myosin motor domain-containing protein {ECO:0000313|EnsemblMetazoa:ASIC014661-PA};
GN ORFNames=ZHAS_00014661 {ECO:0000313|EMBL:KFB46616.1};
OS Anopheles sinensis (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB46616.1};
RN [1] {ECO:0000313|EMBL:KFB46616.1, ECO:0000313|Proteomes:UP000030765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT of mosquito competence for malaria parasites.";
RL BMC Genomics 15:42-42(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASIC014661-PA}
RP IDENTIFICATION.
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 EMBL; ATLV01021509; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ATLV01021510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE525319; KFB46616.1; -; Genomic_DNA.
DR STRING; 74873.A0A084W8S2; -.
DR EnsemblMetazoa; ASIC014661-RA; ASIC014661-PA; ASIC014661.
DR VEuPathDB; VectorBase:ASIC014661; -.
DR VEuPathDB; VectorBase:ASIS019243; -.
DR VEuPathDB; VectorBase:ASIS020238; -.
DR OMA; KPCNINV; -.
DR Proteomes; UP000030765; 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; SM00015; IQ; 1.
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};
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:UP000030765}.
FT DOMAIN 241..952
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 36..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..843
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 995..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 329..336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1167 AA; 125432 MW; 40260D2B8248384E CRC64;
MPCAQVTSGP NASSSNEAVH LQQRLKSLSS ELVTLRNRLH TGGQPTGTGP NGGVPVGGVV
SPNAGPNSNL NNHNGSNHNG GGGVHSTSNH ATHTTSGLMA TTNHMLVTSA AQCIPSSVQA
GGNGNNLNAS QPNVNVLPIV SPRNTSIPYP LPHHNSSTNG TMLHGDTIPC GGTLPRRTGT
MGFGGSGAQY AMGHIGGSVG SITSPNGAGT GGGLPGMLGG SGQSTGHVRD RQDAGGTAAS
EMDDLIHLPG PLTEDAVMRT LHNRFNDGKY FTNVGPILLS VNPYHDVGNP LTLSSTRSVP
LAPQLRKIVQ EAVRQQAETG YPQAIILSGT SGSGKTHCSM LLLRQLFAVA GGGPETDAFK
HLAAAFTVLR SLGSAKTATN SESSRIGQFI EVQVTDGALY RTKIHCYFLD QTRVIRPLPN
EKNYHIFYQM LAGLNADECA RLNLEGYSPA NLRYLQHGDI RQDEQEDAAR FQAWKACLGI
LGIPFLDVVR VLAAVLLLGN VQFVDGQGLE VEVVGETELN AVANLLGVPP AQLFRGLTTR
THNARGQLIK SVCDANMSNM TRDCLAKALY CRTVATIVRR ANSLKRLGST LGTLSSDSNE
SVHNQAEVAS QHASTIGGNA GSKSMAALNN AVRHATDGFI GILDMFGFEE PRPAQLEHLC
INLCAETMQH FYNTHIFKSS VESCREEGII CDTEVDYVDN VPCIDLISSL RTGLLSMLDA
ECSVRGTAES YVAKIKVQHR NSARLEQRAL EPYDPRLFAI RHFAGRVEYD TTDFLDTNRD
VVPDDLVSVF YKHTCNFGFA THLFGTELKA LYAQESGPRG LSFRIAXXXX XXXHFVRCIR
SNTAEKGGAF DRGAVVRQIR ALQVLETVNL MASGFPHRMR FKQFTARYRM LAPFRLLRRC
EEKALEDCKV VLDFALENPP ELDGSVTLSW APGKRHIFLS EGIRQHLERL RAEVRTKSAT
LIQATWRGWN LRKRLGTIRR THDIQLMGGA LHSIKQNSGS GARTGNVTHG NGTGNNTGTA
TRPRPQPIAG TPPPDPNEKC DSKIIAQTCT LFGLDLERPP PVPPSRSYTV TGNSKLGYPQ
TRIMKMNFPE DPAAVGLGEQ LRKGEAVTVT GASHRRGHLI VEHNGISLHV PFQYMELVKT
IVPAGATNGP SPGAPAPPPP TATAVNI
//
