ID Q7PML3_ANOGA Unreviewed; 1432 AA.
AC Q7PML3;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 4.
DT 27-MAR-2024, entry version 142.
DE SubName: Full=AGAP003925-PA {ECO:0000313|EMBL:EAA13643.5};
GN Name=1278752 {ECO:0000313|EnsemblMetazoa:AGAP003925-PA};
GN ORFNames=AgaP_AGAP003925 {ECO:0000313|EMBL:EAA13643.5};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA13643.5};
RN [1] {ECO:0000313|EMBL:EAA13643.5, ECO:0000313|Proteomes:UP000007062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000313|EMBL:EAA13643.5,
RC ECO:0000313|Proteomes:UP000007062};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [2] {ECO:0000313|EMBL:EAA13643.5}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA13643.5};
RG The Anopheles Genome Sequencing Consortium;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EAA13643.5}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA13643.5};
RX PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT "The Anopheles gambiae genome: an update.";
RL Trends Parasitol. 20:49-52(2004).
RN [4] {ECO:0000313|EMBL:EAA13643.5}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA13643.5};
RX PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT "Update of the Anopheles gambiae PEST genome assembly.";
RL Genome Biol. 8:R5.1-R5.13(2007).
RN [5] {ECO:0000313|EMBL:EAA13643.5}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA13643.5};
RG VectorBase;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EnsemblMetazoa:AGAP003925-PA}
RP IDENTIFICATION.
RC STRAIN=PEST {ECO:0000313|EnsemblMetazoa:AGAP003925-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; AAAB01008978; EAA13643.5; -; Genomic_DNA.
DR RefSeq; XP_318377.4; XM_318377.4.
DR STRING; 7165.Q7PML3; -.
DR PaxDb; 7165-AGAP003925-PA; -.
DR EnsemblMetazoa; AGAP003925-RA; AGAP003925-PA; AGAP003925.
DR GeneID; 1278752; -.
DR KEGG; aga:AgaP_AGAP003925; -.
DR VEuPathDB; VectorBase:AGAP003925; -.
DR eggNOG; KOG0245; Eukaryota.
DR HOGENOM; CLU_001485_35_2_1; -.
DR InParanoid; Q7PML3; -.
DR OMA; QVLNCRE; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR CDD; cd06874; PX_KIF16B_SNX23; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF6; KINESIN-LIKE PROTEIN KIF1C ISOFORM X1; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00787; PX; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000007062}.
FT DOMAIN 3..358
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1296..1432
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 915..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 637..682
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 793..848
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1206..1233
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 915..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1432 AA; 159960 MW; F54962EC1E6BA8C0 CRC64;
MASLKVAVRV RPFNQREHEL GAKLIVQMDG KKTRLLKPKL GTGNGVRGDL ASRAALDPFN
DFTFDHSYWS VDERDPHFTH QETVFDDLGT EIVDCAFQGY NACVFAYGQT GSGKTFTMMG
TPEAQGLIPR ICRSLFARMK LGQEEGTGYK TQCSYLEIYN ERVKDLLGPS SAGHGLRVRE
HRTLGPYVES LSQHPVSDYS EIQNCMIQGN IQRTTASTNM NDTSSRSHAI FTITFVQARY
LNDLPSETVS KIHLVDLAGS ERANATGATG QRLKEGAHIN KSLVTLGSVI SALAEQTNPT
NNKRVLYIPY RDSILTWLLK DSLGGNSKTI MIAAISPADV NYSETLSTLR YANRAKNIIN
KPTINEDPNV KLIRELRDEI YKLKLMLSSD SGAELEPQLK VLEDLHKKEA QEKVLTEEWT
EKWREAQSIL REQRSLGLRK SGVGVVLDSE VPHLIGIHDD ISTGVTLYSL KEGETTIGTD
EAPYPQDISL NGIGIAPEHC RIVLSNGNAT IYPNPNATCL LNASIIEVPT AISQGDILLL
GRTNMFRYNN PAEAAKMRQE SSHQQRASRL DLSRLSLIAA SRENLCASFM SDDDGGVSGS
SLSLFGGGGG GAGGMASPQG AFRFRQYTPS REDAELQDEH RKILQTIENA LRQLNLERTR
MHEQFKHKIR LCTEELERLE STKRDRLTVL DCRIGELMAR KEMVLWEKSN EKTQVDILVR
QLSALQTQLD TKKRDFYEYV AKELQELQDC GRLDEASSEL IRNAPQTEDY SEILLQISRS
LDNYSQQYIK EFVRRNRDEI NKYEAELSEK EQQLAESTQK IADLDQKIME LEQQNRELLQ
QRTQQELELI QQKKLGMTLN LTHTNGADDG EGTGEQAGLL LGTNRAGTLE TCDTFHTANS
DCSFVSALNT PALNSLNQLI PTPSSTEDGT ESDTGDRDYE EAISNGGLLH GGMSDSGVSF
ETNRATDTAA ALHTEADENE SEGSVDRQSS GAASGTAKLL FQSDDHCLLL ATSSTPNPKY
GGKKLPTTTT TVIVTDGGGL LKSNQQQPQQ SPRMRHKSSD SEEERTTITT MSSIGTPGSN
RLKLSVPNRN RSNSNNSKSS SMRTEIFDIR HGIHPLRVSS VSSGTDGSHE EEEYEEEDAH
GRRRHRQEVD DEEERRSRGS SIDNSSITSS TANLILCEMN HLRESIASKK AEIMKILETN
GDKKLLDGKI GELQDLQKRI VQLEIKIQDV EKSCLSDGEL QLDSMRDIPE SFTDSDDSRV
GNSCIYPGYM RARDQGSIYA PSVTRSLPSI EGTYRSDHLI NIPTYIIRGA GKQTHYEYEV
KINLPDERWT LLRRYSRFRE LHLTMKKLYG DKIATIPFPR RELFASNTES VAKTRRRQLE
TYLRRLLVVC AKIPHCPIYE GEGRPGLTKQ TLIEFHPFFK KGLFETGKHG TG
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