ID A0A182WI36_9DIPT Unreviewed; 1126 AA.
AC A0A182WI36;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
OS Anopheles minimus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN010040-PA, ECO:0000313|Proteomes:UP000075920};
RN [1] {ECO:0000313|Proteomes:UP000075920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA 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 minimus MINIMUS1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMIN010040-PA}
RP IDENTIFICATION.
RC STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN010040-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 AlphaFoldDB; A0A182WI36; -.
DR STRING; 112268.A0A182WI36; -.
DR EnsemblMetazoa; AMIN010040-RA; AMIN010040-PA; AMIN010040.
DR VEuPathDB; VectorBase:AMIN010040; -.
DR OrthoDB; 239968at2759; -.
DR Proteomes; UP000075920; Unassembled WGS sequence.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR CDD; cd01370; KISc_KIP3_like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR019349; Ribosomal_mS35_mit.
DR PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF13; KINESIN-LIKE PROTEIN; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF10213; MRP-S28; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}.
FT DOMAIN 7..345
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 623..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 360..394
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 463..490
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 623..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1126 AA; 127042 MW; 5FDFB17BD2913027 CRC64;
MTADSRKIRV AVRVRPFNEQ ELEKNPRNII KVLDKSTLMF DPDEDEDEFF FHGVKQTHRD
ITKRVKKKLT MEYDDVFDNT ATNNDIYEVC MKPLVQSVMN GYNCSVFVYG ATGAGKTHTM
LGSMDCPGIT FLTMKELFRQ IESCSELRKF DIGISYLEVY NELVMNLLNK SGPLKLREDT
NGVVVSGLVL RQIHNATELL DLLALGNRNR TQHPTDANAE SSRSHAIFQV HIRMVEKKTG
QKRTVKLSMI DLAGSERAAS TKGIGIRFKE GANINKSLLA LGNCINKLAD GLKHIPYRDS
NLTRILKDSL GGNCQTLMIA NISPSSLTYD DTYNTLKYAS RAKKIRTTVR QNIVPSNVPK
EFLVKKVNEQ AEEIERLKAK VADLEDQLQK KAQTVVETPV LNEPLMNTWI SRIDSCYASM
REALERLIAL KSKEKLINMR DIAKLEASID RCGKQVANQQ GDKSRWRERL RHARRNRNAL
REEVMQSELA TVLKGYLSGK DAEIEAITST LWKDHVLQMS FTYDQENKLW QNIMMLSGDI
IQQNYLLLRS MDRLDNVTME KLKRLVKLNQ RQRGVTFFDD ECHPDRNDID LSSNSIDDIA
NLSDCSEDAV DFPAENVTTL TNVGSGTTNK RAKLNDGSES ESEPYSSSVQ DSEMENSVDR
NVFKKPKTVS RTISFKTSAA GSLARPPISR RTPTKQPKLT ASAGMVASQR LKVPRLVVSN
TLGSSASTRQ PKLPGFGENK SDTSDESNGI GSIANSTFDI ATVKDSETES LFSNVLVESN
VDPHVLDKVL RRASMKGGKM TLSEDGARTG IEEEEFRVLN LKQTKSQRVA RRKAARPDVP
PPRSQQMATD QDWGAVWPGP RSFNPSTVPL PIRQGYVTKR NQMAPGKFAN AELMKIPNFL
HLTPPVIKRQ CEALKQFCTP WPKGLETEEK MRAHFPMTCV TSDYCHALPT IRNPLSRIVT
VQLQLGSLQL DRHAKDKLLR LVGERYNPET DLLTIVTDRC PLKKQNYDYA IYLLTALYHE
SNTVEPWEAT KSEADMEYFD FETSRSKRNA EATLNWNRKE GESGWLQVPE AYANAVSRLF
NEGENEYNLT KYKEQTLALL GLGTEAKYIS SMDCLDCNCS YSCIPS
//
