ID A0A818S651_9BILA Unreviewed; 708 AA.
AC A0A818S651;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
GN ORFNames=JBS370_LOCUS6976 {ECO:0000313|EMBL:CAF3662100.1},
GN JXQ802_LOCUS32903 {ECO:0000313|EMBL:CAF1366343.1}, OTI717_LOCUS34232
GN {ECO:0000313|EMBL:CAF4103612.1}, RFH988_LOCUS31787
GN {ECO:0000313|EMBL:CAF1341117.1}, ZHD862_LOCUS18351
GN {ECO:0000313|EMBL:CAF1115561.1};
OS Rotaria sordida.
OC Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC Bdelloidea; Philodinida; Philodinidae; Rotaria.
OX NCBI_TaxID=392033 {ECO:0000313|EMBL:CAF3662100.1, ECO:0000313|Proteomes:UP000663836};
RN [1] {ECO:0000313|EMBL:CAF3662100.1}
RP NUCLEOTIDE SEQUENCE.
RA Nowell W R.;
RL Submitted (FEB-2021) 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|RuleBase:RU367020}.
CC -!- SIMILARITY: Belongs to the kinesin light chain family.
CC {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:CAF3662100.1}.
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DR EMBL; CAJNOT010000949; CAF1115561.1; -; Genomic_DNA.
DR EMBL; CAJNOO010003517; CAF1341117.1; -; Genomic_DNA.
DR EMBL; CAJNOL010001473; CAF1366343.1; -; Genomic_DNA.
DR EMBL; CAJOBD010000403; CAF3662100.1; -; Genomic_DNA.
DR EMBL; CAJOAX010011975; CAF4103612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A818S651; -.
DR OrthoDB; 19588at2759; -.
DR Proteomes; UP000663823; Unassembled WGS sequence.
DR Proteomes; UP000663836; Unassembled WGS sequence.
DR Proteomes; UP000663864; Unassembled WGS sequence.
DR Proteomes; UP000663870; Unassembled WGS sequence.
DR Proteomes; UP000663882; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
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; 3.
DR Gene3D; 3.90.176.10; Toxin ADP-ribosyltransferase, Chain A, domain 1; 1.
DR InterPro; IPR003540; ADP-ribosyltransferase.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_rpt.
DR PANTHER; PTHR45641:SF19; NEPHROCYSTIN-3; 1.
DR PANTHER; PTHR45641; TETRATRICOPEPTIDE REPEAT PROTEIN (AFU_ORTHOLOGUE AFUA_6G03870); 1.
DR Pfam; PF03496; ADPrib_exo_Tox; 1.
DR Pfam; PF13374; TPR_10; 1.
DR Pfam; PF13424; TPR_12; 2.
DR PRINTS; PR00381; KINESINLIGHT.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 1.
DR PROSITE; PS51996; TR_MART; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000663870};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT DOMAIN 211..383
FT /note="ADP ribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF03496"
FT REPEAT 485..518
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 527..560
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 569..602
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 611..644
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 653..686
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 708 AA; 83745 MW; 7FEA127ED8BF1471 CRC64;
MAETLTLNNN RSTNDENKES TTLIWFDPNI GSYEDTERTK QQLRLINDYV IFSTDLEQCI
SFIQSINIEK IFLITSGSKA SQILSRIFHR SQIDSIFIFC MNKKRYEYLL NEYSNIIGIY
INLDDLCKSI KEQIDFINKQ IQTFSYFDQH EKLTKDLSKE SAKFFWFQLF NYVITRLPRN
EQAKQQMIQI CKEYYRGNTK ELKLIYDFEQ NYQSKDAIRW YSKQSFIYKL INKALRIEDI
DLLYIFRFFI ADLSENLQRE HEKILLSKEK ILILYRGIKL DKEEFNKLKE NQRKLISMNG
YVSTSRQKSL ALNFALKPSK RIDVVPVLFI IQCNIKQIDK NIIFADIVQF SDHPEEQEVL
FDLNTCFEIE SIEESESLQI IKMNISNEGL KSTKDFLELT QKETEELSVA IVFGRLLCNL
GQYDKSQKYF QQLLNDSHDE DPAWIEFNIG RALEFKGEWK EARKYYNLAY NRMMNSEPVR
IKDSAHVLNN IGNILNRQGK YDEALEYHQR ALKIRETFYS FDHIDIAQSL NNIGIVLCLQ
RKYDEALDCY ERALKIQKKF YSSDHVFMAT SFIWIGNILR DKGKCDEALN YYQRALKIQE
KFYPSGHVDI AHTLNNIGAI RNTQGKYNEA LDYHQNALKI REKFYPSGHA DTACSLNNIG
VCYENQNKQK MALDYYQQAL TIYEKFLPVD HPNRQKTENN IRRLTGKN
//
