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Database: UniProt
Entry: E3LVK3_CAERE
LinkDB: E3LVK3_CAERE
Original site: E3LVK3_CAERE 
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
//
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