ID E3LVK3_CAERE Unreviewed; 629 AA.
AC E3LVK3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN Name=Cre-klp-15 {ECO:0000313|EMBL:EFP12488.1};
GN ORFNames=CRE_29540 {ECO:0000313|EMBL:EFP12488.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU000394}.
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DR EMBL; DS268416; EFP12488.1; -; Genomic_DNA.
DR RefSeq; XP_003112054.1; XM_003112006.1.
DR AlphaFoldDB; E3LVK3; -.
DR STRING; 31234.E3LVK3; -.
DR EnsemblMetazoa; CRE29540.1; CRE29540.1; WBGene00060018.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_001485_12_4_1; -.
DR InParanoid; E3LVK3; -.
DR OMA; MQLENDA; -.
DR OrthoDB; 2882208at2759; -.
DR Proteomes; UP000008281; 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 CDD; cd00106; KISc; 1.
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; 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; SSF57997; Tropomyosin; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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}; Reference proteome {ECO:0000313|Proteomes:UP000008281}.
FT DOMAIN 298..617
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 99..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 194..225
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 250..291
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 104..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 378..385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 629 AA; 69744 MW; FF0F141BA41689B2 CRC64;
MASRLKAHVI TREVAPGPDL LFSAKTCHSL ICRKFSRKVI ELVDNFLKEI FVFRHVRKAT
KRSASDSDCI AEKYSSHCLS RSAIPILTAR RTTMRASAIP RPTEPLPNTL TTGRHSTLGH
TGCPTLKKPI GSLPRVATAA KPLATTSRAG STSSARSTTL RSSTVANKTI AAPTARTSNM
ARAVPVSSRP PSEVASLKSE ITKLKEELKT REEQLKLTSE VLEMQKTNLT HSNAQLENAK
IKLDLVESFK ITLEEQLKVL KENMQQKTAH NEEMCQQLNE KEAILRKLHN DVVDMRGQIR
VAVRVRPMLK TEEESSNDGI EYPAVNAIAI NQGTRKGTTL MFEKVFTPLF SQKDVFVNIE
DFILSALHGY NVGLIAFGQT GSGKTHTMRG GDAEEEEGII PRAATFLFRE SKKLEATGWK
FEFSLSFLEI YNNEAYDLLN NHAAVKLRLV NQTVTLDGLS DHPLAKQSEI GSLLRTADKN
RKTAATKCNE YSSRSHAIYM WKIKAHQQAT GISTSSMLKL VDLAGSERAK ESGVIGQQFK
EMTNINQSLS VLQKCISLQK SKSQHVPYRD SKLTQVLMDC LGAGNSKTMV VVNINPCNDQ
ATESKRSIEF ASKMRDTHIG SAVQQRDLY
//