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Database: UniProt
Entry: A0A183DWE7_9BILA
LinkDB: A0A183DWE7_9BILA
Original site: A0A183DWE7_9BILA 
ID   A0A183DWE7_9BILA        Unreviewed;       467 AA.
AC   A0A183DWE7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
GN   ORFNames=GPUH_LOCUS13038 {ECO:0000313|EMBL:VDN21526.1};
OS   Gongylonema pulchrum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Spiruroidea; Gongylonematidae; Gongylonema.
OX   NCBI_TaxID=637853 {ECO:0000313|Proteomes:UP000050760, ECO:0000313|WBParaSite:GPUH_0001305201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:GPUH_0001305201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN21526.1, ECO:0000313|Proteomes:UP000271098}
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; UYRT01079857; VDN21526.1; -; Genomic_DNA.
DR   WBParaSite; GPUH_0001305201-mRNA-1; GPUH_0001305201-mRNA-1; GPUH_0001305201.
DR   Proteomes; UP000050760; Unplaced.
DR   Proteomes; UP000271098; 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:SF3; 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; 1.
DR   PROSITE; PS01160; KINESIN_LIGHT; 1.
DR   PROSITE; PS50005; TPR; 3.
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:UP000271098};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}.
FT   REPEAT          219..252
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          261..294
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          303..336
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          116..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          49..111
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        116..135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   467 AA;  53241 MW;  A5131622F3E63763 CRC64;
     MTALSQEEIL QSTRTGLNAD ESALIEEKAH IVDRNLEMLR LGIEEAQVMV ALAGHLQTVE
     AEKQKLKAQV RRLCQENAWL RDELNSTQQK LQASGQQVAQ LEEEKKHLEY MNSIKKYDDQ
     EENDKSVDHS DTRNDNTLQD LGFGPEEDEE MSGKEPTFPY KIDLQDIWPD SLLIQHRRIR
     WLQVIQYASQ GRYEVAVPLC KQALEDLEKT SGHDHPDVAT MLNILALVYR DQNKYKEAAN
     LLNEALHIRE KCLGESHPAV AATLNNLAVL YGKRGKYKDA EPLCKRALEI RENVLGADHP
     DVAKQLNNLA LLCQNQGKYD EVERYYKRAL EIYEAKLGPD DPNVAKTKNN LSSAYLKQGK
     YKDAEILYKQ ILTRAHEREF GKIADDNKPI WQIAEDREEH KHKGDDTSTY QEYGGWHKAA
     KVDSPTVTTT LKNLGALYRR QGKYEAAETL EDAALRAKKQ TSALSFG
//
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