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Database: UniProt
Entry: C3YN97_BRAFL
LinkDB: C3YN97_BRAFL
Original site: C3YN97_BRAFL 
ID   C3YN97_BRAFL            Unreviewed;       685 AA.
AC   C3YN97;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
GN   ORFNames=BRAFLDRAFT_76878 {ECO:0000313|EMBL:EEN58203.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN58203.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN58203.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN58203.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
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|RuleBase:RU367020}.
CC   -!- SIMILARITY: Belongs to the kinesin light chain family.
CC       {ECO:0000256|RuleBase:RU367020}.
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DR   EMBL; GG666533; EEN58203.1; -; Genomic_DNA.
DR   RefSeq; XP_002602191.1; XM_002602145.1.
DR   AlphaFoldDB; C3YN97; -.
DR   STRING; 7739.C3YN97; -.
DR   eggNOG; KOG4626; Eukaryota.
DR   InParanoid; C3YN97; -.
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; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR002151; Kinesin_light.
DR   InterPro; IPR006597; Sel1-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR19959; KINESIN LIGHT CHAIN; 1.
DR   PANTHER; PTHR19959:SF118; LIPASE_3 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   Pfam; PF13424; TPR_12; 6.
DR   PRINTS; PR00381; KINESINLIGHT.
DR   SMART; SM00671; SEL1; 10.
DR   SMART; SM00028; TPR; 12.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 10.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU367020};
KW   Cytoskeleton {ECO:0000256|RuleBase:RU367020};
KW   Microtubule {ECO:0000256|RuleBase:RU367020};
KW   Motor protein {ECO:0000256|RuleBase:RU367020};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}.
FT   REPEAT          15..48
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          59..92
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          191..224
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          235..268
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          279..312
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          323..356
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          367..400
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          411..444
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          455..488
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          499..532
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          553..664
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
SQ   SEQUENCE   685 AA;  76691 MW;  32B464FB0766495F CRC64;
     MRSTYCKGTA HPDIASSLNN LGNAWSNLGD HRKAISYYEQ SLQMKRSIYG EDTAHPDIAN
     SLNNLGSTWS NLGDNRKAIS YYEQSLQMKR SIYGEDTAHP DIAISLNNIG SACSDLGDYG
     KAISYYEQSL LTRRSIYGKN TAHPEIAASL NNMGTPGETS GDHRKAISYY EQSLQMKLSI
     YREDNAHPDI AASLNNMGNA WRDLGDHRKA ISYYAQSLQM RRSIYGKNTA HPEIAASLNN
     MGTAWRNLGD HRKAISYYEQ ALQMRRSICR EDNAHPNIAA SLNNLGATWR NLGDHRKAIS
     YYEQSLQMRR SIYGEDTAHP DIAASLNNMG TAWRNLGDHR KAISYYEQAL QMKRSICRED
     NAHPNIAASL NNLGATCSNL GDHRKAISYY EQSLQMMRSI YGEDNAHPDI AGSLNNMGNA
     WSNLGDHRKA VSYYEQALQM KRSICREDNA HPDIADSLNN LGNACSNLGD NRKAVSYYEQ
     ALEMRRSTYG KRTAHPNIAS SLNNLGGAWT NLGDHRKAIS YFDQALEMRR SIYVGQVLTM
     TSPDLQQRLQ DLDTFIQNLM TCESRPVVGL TVSVVKDGQT IFAKGYGQRD LQTGQAVDNR
     TLFGVGSISK SFTSALLAVI LGEREDVSWD TVLTDILGPS FRFRDRFRTE EATIRGLLAH
     KIALENPWYV AVIMGQDIDR SEFAQ
//
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