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Database: UniProt
Entry: A0A2G5TJA3_9PELO
LinkDB: A0A2G5TJA3_9PELO
Original site: A0A2G5TJA3_9PELO 
ID   A0A2G5TJA3_9PELO        Unreviewed;       517 AA.
AC   A0A2G5TJA3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
GN   Name=Cnig_chr_V.g19621 {ECO:0000313|EMBL:PIC27328.1};
GN   ORFNames=B9Z55_019621 {ECO:0000313|EMBL:PIC27328.1};
OS   Caenorhabditis nigoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC27328.1, ECO:0000313|Proteomes:UP000230233};
RN   [1] {ECO:0000313|Proteomes:UP000230233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA   Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA   Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT   "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT   competition proteins.";
RL   Submitted (OCT-2017) 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}.
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:PIC27328.1}.
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DR   EMBL; PDUG01000005; PIC27328.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5TJA3; -.
DR   STRING; 1611254.A0A2G5TJA3; -.
DR   Proteomes; UP000230233; Chromosome v.
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; 1.
DR   InterPro; IPR002151; Kinesin_light.
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; 2.
DR   PRINTS; PR00381; KINESINLIGHT.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF48452; TPR-like; 2.
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:UP000230233};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}.
FT   REPEAT          239..272
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          365..398
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          24..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          100..134
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   517 AA;  58400 MW;  C77F84453027ACAF CRC64;
     MTNFVEERLA TDLKTIQQRI TSLRDEHNNS NTIEANSEGA DSNEPSLSKE IQVQINENME
     KLLDNENDVS MLLMVAQLLQ AADVQKAKSR DTEKLLLERN DWLVEELAET QSRLQESERL
     NGQLEEEVKH LRFLDTTKSI RCDIQSSTLA DETSRPLAID TLQELGFGPE DDENDINHNL
     RDGQPNCVNT NPSPSRLVTL NTLVIQYMKD GRYDIAGPLG KQALEDLINV HGRNHPDVAT
     MMNLLAMVYR DQQKYKEAAQ YLEDALAIRE SCFGENHQTT AANLNNLAIV LGKRGKFKEA
     EPLCRRALKI RETVLGEDHV EVARQLTNLG LLCLNMGKYE EVEACHKKAL NIYESKLGTD
     DPNTIKTKNN LASIYLKLGK YDEAETLYKQ ILTRAHEKQF GTSKYDSKPI WKIAEEREEK
     KQKGVLDTSL ESPVSVPYLE SEHYMSALTK LSALYRKQGE FEAADFLENV AVRTKTPDEG
     SRVDSHSLTT SSNEDSRVRV ANTGIRSKLL SALGFNI
//
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