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
//