ID A0A182QMI4_9DIPT Unreviewed; 637 AA.
AC A0A182QMI4;
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-like protein {ECO:0000256|RuleBase:RU000394};
OS Anopheles farauti.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF013179-PA, ECO:0000313|Proteomes:UP000075886};
RN [1] {ECO:0000313|Proteomes:UP000075886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
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 farauti FAR1 (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AFAF013179-PA}
RP IDENTIFICATION.
RC STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF013179-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,
CC ECO:0000256|RuleBase:RU000394}.
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DR EMBL; AXCN02000214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A182QMI4; -.
DR STRING; 69004.A0A182QMI4; -.
DR EnsemblMetazoa; AFAF013179-RA; AFAF013179-PA; AFAF013179.
DR VEuPathDB; VectorBase:AFAF013179; -.
DR OrthoDB; 5481713at2759; -.
DR Proteomes; UP000075886; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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 Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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 PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF50; KINESIN-LIKE PROTEIN; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 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}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..637
FT /note="Kinesin-like protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013380224"
FT DOMAIN 1..298
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 335..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..367
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 53..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 637 AA; 72725 MW; ED26A5C809C2A374 CRC64;
MIVLMMRSVL MSVHLARICK LWFLVPIDLY VDTARPIVEK VLEGYNGTIL AYGQTGTGKT
YTMSGNPESP QTKGIIPNTF AHIFGHIARG KENQKFLVRV SYMEIYNEEV RDLLGKELNK
SLEVKERADI GVFVKDLSGY VVHNADDLDN IMKLGNKNRV VGATKMNSES SRSHAIFSIT
IESSETDEAG RQYVRMGKLQ LVDLAGSERQ SKTQSSGLRL KEATKINLSL SVLGNVISAL
VDGKSTHIPY RNSKLTRLLQ DSLGGNSKTV MCASISPADS NYVETISTLR YACRAKSIQN
LAHINEEPKD ALLRHFQEEI EELKRQLEEG IFQQGIASGD EEEEEDGDGG DENDEDAVEE
ECDPDEDRER ERLERREKRR KEKARERKEK SDAEKELLEK KAMENQQELK KAKSEQDQLR
AKLSSLENKI LVGGENLLEK AKEQELLLEN SITELEQRTK TERELKENLQ KIEAERIDIE
ERYSSLQEEC VGKTKKLQRV MSMLMSIKSE LADQQQEQQR EKEGIYENIR SLSRELALCE
LVINSYIPKE YQNMIEKFTH WNEDIGEWQL KCVAYTGNNM RKNIPEPKVN TKETDLVDLS
HVYLSYNTDS VAEPIRAKTA RPRTSGIARP TTARKYY
//