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Database: UniProt
Entry: A0A099Z5D1_TINGU
LinkDB: A0A099Z5D1_TINGU
Original site: A0A099Z5D1_TINGU 
ID   A0A099Z5D1_TINGU        Unreviewed;       534 AA.
AC   A0A099Z5D1;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
DE   Flags: Fragment;
GN   ORFNames=N309_08151 {ECO:0000313|EMBL:KGL77709.1};
OS   Tinamus guttatus (White-throated tinamou).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX   NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL77709.1, ECO:0000313|Proteomes:UP000053641};
RN   [1] {ECO:0000313|EMBL:KGL77709.1, ECO:0000313|Proteomes:UP000053641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL77709.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) 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; KL890369; KGL77709.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099Z5D1; -.
DR   STRING; 94827.A0A099Z5D1; -.
DR   Proteomes; UP000053641; 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; 1.
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:SF8; KINESIN LIGHT CHAIN; 1.
DR   Pfam; PF13374; TPR_10; 2.
DR   Pfam; PF13424; TPR_12; 2.
DR   PRINTS; PR00381; KINESINLIGHT.
DR   SMART; SM00028; TPR; 5.
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:UP000053641};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}.
FT   REPEAT          251..284
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          293..326
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          152..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          85..147
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        152..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         534
FT                   /evidence="ECO:0000313|EMBL:KGL77709.1"
SQ   SEQUENCE   534 AA;  60734 MW;  5E5014EDE240595E CRC64;
     MSTMVYPREE KLDKLSQEEI ISNTKLVMQG LEALKNEHNS ILHSLLETIK CLKKDEEANL
     VHEKSNLLRK SVEMIELGLG EAQVMMALSN HLNAVESEKQ KLRAQVRRLC QENQWLRDEL
     ANTQQKLQRS EQTVAQLEEE KKHLEFMNQL KKYDEDVSPS EEKEGDSTKD SLDDLFPNEE
     EEHGPGLPHQ HSSAVAAAQQ GGYEIPARLR TLHNLVIQYA SQGRYEVAVP LCKQALEDLE
     KTSGHDHPDV ATMLNILALV YRDQNKYKEA AHLLNDALSI REKTLGKDHP AVAATLNNLA
     VLYGKRGKYK EAEPLCKRAL EIREKVLGKD HPDVAKQLNN LALLCQNQGK YEEVEYYYCR
     ALEIYESRLG PDDPNVAKTK NNLASCYLKQ GKYKDAEVLY KEILTRAHVK EFGSVDDEHK
     PIWMHAEERE EMSKSKHRDS APYAEYGGWY KACKVSSPTV NTTLRNLGAL YRRQGKLEAA
     ETLEECAVRS RRQGIDPINQ TKVVEILKEG NGTERRRSLG GSVKYENATD GSEE
//
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