ID A0A3Q0IWW6_DIACI Unreviewed; 1474 AA.
AC A0A3Q0IWW6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Kinesin-like protein KIF21A {ECO:0000313|RefSeq:XP_026680742.1};
GN Name=LOC113468188 {ECO:0000313|RefSeq:XP_026680742.1};
OS Diaphorina citri (Asian citrus psyllid).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Psylloidea; Psyllidae;
OC Diaphorininae; Diaphorina.
OX NCBI_TaxID=121845 {ECO:0000313|Proteomes:UP000079169, ECO:0000313|RefSeq:XP_026680742.1};
RN [1] {ECO:0000313|RefSeq:XP_026680742.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR RefSeq; XP_026680742.1; XM_026824941.1.
DR STRING; 121845.A0A3Q0IWW6; -.
DR PaxDb; 121845-A0A3Q0IWW6; -.
DR KEGG; dci:113468188; -.
DR OrthoDB; 1131899at2759; -.
DR Proteomes; UP000079169; Unplaced.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd22248; Rcc_KIF21; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF34; KINESIN-LIKE PROTEIN KIF21B; 1.
DR Pfam; PF00225; Kinesin; 2.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000079169};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT DOMAIN 1..218
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REPEAT 1342..1381
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1383..1417
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1425..1463
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 418..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 226..253
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 609..741
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1085..1133
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 418..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1474 AA; 164266 MW; 286E7B935A593BB8 CRC64;
MLQTGSGKTY TMGTGFETDV SEEMLGIIPR AITHLFEGIQ NIAEQARQNG DTPPEVVVQA
QFLELYNEEI IDLFDDTRDY GLSKMKSNIK IHEDSGHSIY VTGATSKSIR SAQEAMNALR
QGALSRTTAS TQMNSQSSRS HAIFTLHIQQ KRLVKVEDPE GEIVSKGSLY RDSKLTRLLQ
DSLGGNSRTV MIACVSPSDR DFMESLNTLK YANRARNIQN KIRLNQDKSS KTIMALRNEI
QQLQLELLEY KQGKRVVGED GEEHVNDMYH ENIMLQTEVN NLRTRTKAMQ ETIDDLTKKN
CQLLALKASG AWVNGGPGGG GGGGEEGGGD DCCVKEIITG YCGEIEDLRS KLLISEHTNT
QLRKSLSRIA PPCNIPGGPA GLMHSPSRAD DLYSVDTDLI AKAKEEVAKN LNTLAKKRRQ
LSENEEAERN SDSDSEDSSS DSDSNSEDRQ SVDSAYSAEL ANLTTEIDSL IRVNMLRKQS
RARNPSSTII GGKAKTGDIG VSPKAAKIKW QNLEKNIASN TLNKHSSTII GGKAKPGDIG
VSPKAAKIKW QNLEKNIASN TLNKQSVIGL ERDLEKLVVE RQEKSHELQT KLKKLNEYTM
KFPREKDFHK DLEDEIETLR ANLDYINDSI TEVQRNIIQF RFPATTKNQP TEKVRKVRDE
YENKLNMMQK EMRNLTDAKK EYQKLLRSQS SYENQVKTLR SEVNEMRQTR ILIAAQRESV
IRELEAKLSH TEKEFQLQRE LLNSLYGSRD QDNNMANSMS HSMTHSMTSS SNSSSPTPAD
SMNGNAMTGS NIMNTTFVLP SSPKAKRKTG LPRTFDEASG SVNGASGGRV SEAGDYLERL
TMPPPLGASQ QSNLMTKSTN SSVPVSLRSL KTDTGSPTMP RRTATSIDFS SSSPSPRLQR
RGTFVLPPNT NLYKPGSMLC FWEDGAEKPP ARRMFSTPLG AGSKAPLICT HVCQGHLRPV
LSVDATDDLL FSASKVTLCI YNLKFSLSVE DTKETLESGD LVSGLKTMPE VSYIIEKLYN
MSINQSLIAA QRESVIRELE AKLSHTEKEF QLQVSLSHIR IVSSHIRIVS GHIKIRIDTN
QSLIAAQRES VIRELEAKLS HTEKEFQLQI LIAAQRESVI RELEAKLSHT EKEFQLQLPW
SLLISFRTHN ANDSELNVNA FRPLHFSSSC RSFDSCTKKP TIRGAQGRSS GSRSGEASEV
FTFSDQGLDA SPPNSPPTYR RSVNLKLYDF TVSTKFWDQG LDASPPNSPP TYRRSVSREE
QSQNVFSRLT LGYIPPTDPV NSKGSIVPYQ GKVTLRDNVL FSGSRDYVIK KWDLNRQELI
TVFDVNTDVE DCSSTSPQMN LEPPHYDGIQ ALALRDNVLF SGSRDYVIKK WDLNRQELIT
SQSNAHKNWV CGLSYVPNQP LLLSACRSGT IKLWSTEPFS QLGEMKAHND SVNCITTNND
LVFTGSNGEI KLWRLPQVAN IMTMSTGHLL HLSV
//
