ID E1F983_GIAIA Unreviewed; 1168 AA.
AC E1F983;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Kinesin-14 {ECO:0000313|EMBL:EFO61004.1};
GN ORFNames=GLP15_3203 {ECO:0000313|EMBL:EFO61004.1};
OS Giardia intestinalis (strain P15) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=658858 {ECO:0000313|EMBL:EFO61004.1, ECO:0000313|Proteomes:UP000008974};
RN [1] {ECO:0000313|EMBL:EFO61004.1, ECO:0000313|Proteomes:UP000008974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P15 {ECO:0000313|EMBL:EFO61004.1,
RC ECO:0000313|Proteomes:UP000008974};
RX PubMed=20929575; DOI=10.1186/1471-2164-11-543;
RA Jerlstrom-Hultqvist J., Franzen O., Ankarklev J., Xu F., Nohynkova E.,
RA Andersson J.O., Svard S.G., Andersson B.;
RT "Genome analysis and comparative genomics of a Giardia intestinalis
RT assemblage E isolate.";
RL BMC Genomics 11:543-543(2010).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFO61004.1}.
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DR EMBL; ACVC01000454; EFO61004.1; -; Genomic_DNA.
DR AlphaFoldDB; E1F983; -.
DR STRING; 658858.E1F983; -.
DR EnsemblProtists; EFO61004; EFO61004; GLP15_3203.
DR VEuPathDB; GiardiaDB:GLP15_3203; -.
DR OMA; EAQHINT; -.
DR OrthoDB; 5479900at2759; -.
DR Proteomes; UP000008974; Unassembled WGS sequence.
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; cd17039; Ubl_ubiquitin_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; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR PANTHER; PTHR47972:SF28; PROTEIN CLARET SEGREGATIONAL; 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 SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}.
FT DOMAIN 5..78
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 783..1153
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 81..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 877..884
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1168 AA; 130429 MW; 059F9BB161722FDE CRC64;
MDDRLQFTII HVAERRKFKI TVRVEDVPNV RVRMLKKSIF QATGIPVDCQ ALYLNKQLLS
DRMTGSELKL SPETTFVLHT SIPTQEEQLN VETQGNPTGE SAYEDEKIKS RGRSRSRSRS
RGKRQTSHST RRDTFGAPLF EGGNGAVGTY HSGSTNSLIN ELNTTTENLS SPNVISAHMA
SRDAILQSTA TRHFTISTKD CTKSSPRIQR SDVDKRSTAQ SVGLRNSSTS SLRDDSVKSI
VVKAAGRSSS QQKTYRTPSA RSVIKSSYFE PPVSYPRIQS ARSSKKKSQP KKPQTPQKSP
NQSGTVTASP RKHLSNGNYE PSPKEGSYSS ADSPPLIPTS NLCTKTKELT TSRISLTDLH
GSDRMYASIQ PEFPAKTTKI TVSQPSVANM LYKSTLGASK VGLPEAPELT SHAHLNDGEM
EEATTENKVT NDADYPSFTE DDIELLRQMN DNPHTSIEHV ENASVHDPTI DHALQKQSHR
TKELALVSEL QEQVTLIKQE MDTIKRTIAS TPTGNAVVDE PILSTQILQG SKKLYDQFQE
APMSDWGLFK HKYDEELAAL KLEVEQLRNA RDSTKSSNNP VTHQPPLTSE SHLGSAKTTK
DTFSTLTTDE SIELDTTEVA RRSSNTTPTT IRTRQSDGIP RPPSAKVLGI TKSQQNSSLL
AIQTIKQQIE AERAELTNIL QNLEIYSLMD TFFDIEIEIA NIEHSNMTQA LEESKASLVD
IQNNLSYALS KTPTFTPDVR KSAEMSLDYG MFQREYTRLQ GLMLVENKQR KTLHNTLEEM
KGSIRVIVRM RPMLQHEKEE LKTSKFKSFN YRNAFIFKDE HTLQLKLPYG VASQENYSFD
FYKILDETKT QEDVFHDMSH LLKSVIDGYN VCVLAYGCTG SGKTFTLIGD DSETAVAESV
VMSMQKDSEE KNPYERLGLL PRSIVELFNL IEADTSQSQR YELKCAMIEH YLDNILDLLH
TEDDTRTQLP SFNSDKLVVR QTAKGETYIQ NLSYKSVASA EELVGYLGYG LERRHIAATK
LNSLSSRSHT VFLIEITSYR ETAKGTRTAR SVLTFADLAG SENVTKSHSN GLRLKEAQHI
NTSLCALGDV IAALSRKKVA SYVPYRNNKL TMILQQSLGN NSKTLLFANI SPLPNLLYET
LSTLSFAARV KNVKNVAVKN LTNIESDQ
//
