ID A0A182UKQ1_9DIPT Unreviewed; 2093 AA.
AC A0A182UKQ1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:AMEC022177-PA};
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:AMEC022177-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:AMEC022177-PA}
RP IDENTIFICATION.
RC STRAIN=CM1001059 {ECO:0000313|EnsemblMetazoa:AMEC022177-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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 34690.A0A182UKQ1; -.
DR EnsemblMetazoa; AMEC022177-RA; AMEC022177-PA; AMEC022177.
DR VEuPathDB; VectorBase:AMEC022177; -.
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-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR CDD; cd20818; C1_Myosin-IX; 1.
DR Gene3D; 1.20.5.190; -; 2.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR046987; Myo9.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR46184:SF5; HEAVY CHAIN, UNCONVENTIONAL MYOSIN; 1.
DR PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..329
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1149..1202
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1390..1439
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1484..1682
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 32..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..233
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 450..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1364..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1766..1818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1873..2093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..534
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..560
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1909..1963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1979..2071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2093 AA; 221901 MW; 3632C0A30E72597F CRC64;
MSDITSGHSN NQACSPNSNL AYHRQSLGNA GYGAAGAASP GATGGTPRRS WSSFAFNNKN
FPDGKLNYEC NQQQDQTPQY HSKHLQSTTS SSSSIYGSGG GGKSSANANS SASGAPNSGA
VTGTGSGKGY GLGSAAARNR FERSGQDVMA RASQIVMKNK SFRPRERPKK GLKNLQSVKT
LSAGQNLSNQ TSAIKTRKQP LTVTAQFQNS LIALMETLNQ ANPFFIRCIK SNPNKIPNQF
DDATVTRQLR YTGMLETVRI RRAGYNVRLT YEEFIQLYRI LLPKGLVSSQ KDVRDFMSTM
DLNKQHYQLG LTKIYMRESQ KMRLDISLHT KIIDSIICIQ RWFRAILQRK KYCQYRNAAC
TIQSYWRDYL REKQEKFTRK IRNHAATVIQ ATWRGYTVRK WYSKLKTGVL IIQARIRGNQ
ARSRFKELLS KKLQRERAKL RSTQSLPVER PIGTTAAGGS YGGGGGGAGG GGSTYPEIVH
AIEHRKKPIP AVGRSFETAI DIVNKNRALF ADDSMSADFI DDDEDEEEEE EEETTGSRQA
TITATCGEEE EDEEDDEEGY EDLGLVDDPQ YMANNRSALM HPVKTAAPVT MSPTVNSALL
DRNEKYIKSL VISGGGGGGA TASSSPSAGG GGGANASSVG SSVSGAYQKA PLQRQEDVLD
RPLRMYDIER ASKSTFDDTE LAKYRYERGG GVSSTVKLPV RRVDSGPSSV AGSGTGSGGS
TMGRPGIQRF RYGDTASYGG SGMIRNQNHS NNSYSNSNVE IVFVNTGLDS VGAPAGSGGT
GSLSSSPAAR NLNRNSISSG TLTQTQVPPS LASSMRRDSL PLSHHLGTST RTPGDEINSN
YHMHQQQQQQ QLQQQHQQQQ QQQQQQQHQH HQQPLSSSSS SVASHHQQSQ TGSPMSHSPQ
SLPLVGSAGH IGNYQNLQFP PTSNYHQHHH HHQQSVYNNN AQPVSTGAKM VTSTPYGAAG
SNSSYATGAS ASVSSQRVSA AYPDDFAQNY YTTTTTTPKG KAAALLGTAK SEDSAVTNAG
LGQSKYPLDR ATLAKADSSD MVLSAGNKTA INQGAGNASG RRIKSTNLSE EQLVGSSGSS
VSYHPGTGLT RRGPVGASAS GGSGNTSSTG VASDTLKRRN SDPTNKIPLL EVNRGNDMYQ
SSTRINIAGH QFRKVQRINK AERCACCQEI DSFVNEGYRC LDCKVLVHTK CIQNGGIKSL
QCAVAKRSKR IRTGGAGGGS GGLGGSSSKH DKHHPIGGGS ASGQKISSTR EYTDSTDKII
SDAKELQLMQ DFITQKICKM ESDCEKPSEV DRVFKQALRE FKDNLVAQYS VAHRQNSDVL
NIKYRDLIAN FEQVIETTSG RKNDFPLTMG VNAFRGFMNE FMNSRETEKP KTKRKKDKKR
KHDDHTTFNG HTFQLTILNI ATACEICQQF LLWPIERGLV CQNCKLTCHK KCYQKSASCN
KIANADPNSL LGAGGSGSAV VAGGCGPDGQ PLYGGGIPTK LFGVPLTALC GNSSDGVKIP
AQINKLIMMI EMHGLYSEGI YRKSGVSSKI KDLKAKMDRA VTSADGGGGE MDFESYNVHV
LTNVLKSFLR EMPEPLLTFD RYDDFLRAAD LSDGSDRVQT LLSLVKKIPP AHHCLFERLI
FHLALVAKLE QYNRMSASSL AIVFAPCVLR TNRYVPAQDS LNDIGRQTKC METLITQKML
NVKSTLADID TLDTAAHTAT ARLSTLRSSK VFTQEEMANA RGGSGIAVGG LLETETEEML
LEGHIQEIRK EKALLTSTLP SLARASSDDD LLSTDLDGEG GSLDDLSNSK EKDLDVSSGG
GGGGGGGGGG GSSNMISDSG ISIRYQAPSD HGGSSNVSLN NDVPMAVSYS LRDQSGAGGV
GGGGGGTTAA GMEYFHKMGP SSGASPAPGV KTKSLSHQTL LEREAFLRGS GSTSVSSPQS
PTAATSVTAS STPSSSVSAP SMMKSQQQNG NGANGSTGGA SAGGASAAGS GTGGGGPGSG
GSIASTATNT LPITPGATIA ASPSGSGATS TSASSSSINS ANLHAKDNNG MGKDGLSSSG
GSSSTTTTTK LVSRRMSTGT NKRSGGGAGP SGGSNSAAGG PGPPAGDDEP IMV
//
