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Database: UniProt
Entry: A0A0R3SDI9_HYMDI
LinkDB: A0A0R3SDI9_HYMDI
Original site: A0A0R3SDI9_HYMDI 
ID   A0A0R3SDI9_HYMDI        Unreviewed;       511 AA.
AC   A0A0R3SDI9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
GN   ORFNames=HDID_LOCUS2755 {ECO:0000313|EMBL:VDL21849.1};
OS   Hymenolepis diminuta (Rat tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX   NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000275701-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HDID_0000275701-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL21849.1, ECO:0000313|Proteomes:UP000274504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Kinesin is a microtubule-associated force-producing protein
CC       that play a role in organelle transport.
CC       {ECO:0000256|RuleBase:RU367020}.
CC   -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two light
CC       chains. {ECO:0000256|RuleBase:RU367020}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU367020}.
CC   -!- SIMILARITY: Belongs to the kinesin light chain family.
CC       {ECO:0000256|ARBA:ARBA00009622, ECO:0000256|RuleBase:RU367020}.
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DR   EMBL; UYSG01000724; VDL21849.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R3SDI9; -.
DR   STRING; 6216.A0A0R3SDI9; -.
DR   WBParaSite; HDID_0000275701-mRNA-1; HDID_0000275701-mRNA-1; HDID_0000275701.
DR   Proteomes; UP000046397; Unplaced.
DR   Proteomes; UP000274504; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005871; C:kinesin complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR002151; Kinesin_light.
DR   InterPro; IPR015792; Kinesin_light_repeat.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45783; KINESIN LIGHT CHAIN; 1.
DR   PANTHER; PTHR45783:SF3; KINESIN LIGHT CHAIN; 1.
DR   Pfam; PF13374; TPR_10; 1.
DR   Pfam; PF13424; TPR_12; 3.
DR   PRINTS; PR00381; KINESINLIGHT.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS01160; KINESIN_LIGHT; 1.
DR   PROSITE; PS50005; TPR; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|RuleBase:RU367020};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW   ECO:0000256|RuleBase:RU367020};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU367020};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175,
KW   ECO:0000256|RuleBase:RU367020};
KW   Reference proteome {ECO:0000313|Proteomes:UP000274504};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}.
FT   REPEAT          231..264
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          273..306
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          137..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          76..124
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   511 AA;  57830 MW;  A608AA344565FA01 CRC64;
     MEDVSQSEIL VQLRSSMKVL DSLRNEHKAA LEELNKNGDA KGQTKSAKVE SLESFVEKIE
     EAIYDGDELF VFSDYLQSAE AEKQRLKAQT KRLVHENRWL REELASLQSQ FRQSQVRIVA
     LEEEINKLKF ANEMSKYDAP DQSGLPASDS TKDLKTGQDK FENEQDVMNS SQTTALSQIM
     TNYEIPARLR TLHNLVIQYA SEGRYEVAVP LCKQALEDLE RTSGRDHPDV ATMLNILALV
     YRDQGKYKDA ANLLNEALVI RERHLGPDHP AVAATLNNLA VLYGKRGKYQ EAEPLCKRAL
     EIREKVLGAD HPDVAKQLNN LALLCQNQGK YAEVYEYLRR AQSIYEKNDV PQRVFKTLTT
     LVERYYERAL AIYISCLGAN DPNVTKTKTN LASAYLKQAK YVEAEALYKD ILTRAHELEY
     GKMTVSNKPI WMLAEDRQNG RWDTSLANQA QNQRSTLMEN PTIATTLRNL GALYRRSGKF
     EAAEVIEECA GRPVKSSEGV KGKPAFPSAK K
//
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