ID A0A498SMV6_ACAVI Unreviewed; 520 AA.
AC A0A498SMV6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Kinesin light chain {ECO:0000256|RuleBase:RU367020};
DE Flags: Fragment;
GN ORFNames=NAV_LOCUS8026 {ECO:0000313|EMBL:VBB33235.1};
OS Acanthocheilonema viteae (Filarial nematode worm) (Dipetalonema viteae).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Acanthocheilonema.
OX NCBI_TaxID=6277 {ECO:0000313|EMBL:VBB33235.1, ECO:0000313|Proteomes:UP000276991};
RN [1] {ECO:0000313|EMBL:VBB33235.1, ECO:0000313|Proteomes:UP000276991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-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; UPTC01002241; VBB33235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498SMV6; -.
DR STRING; 6277.A0A498SMV6; -.
DR Proteomes; UP000276991; 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:UP000276991};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT REPEAT 248..281
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 290..323
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 332..365
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 139..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 73..135
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 139..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 520
FT /evidence="ECO:0000313|EMBL:VBB33235.1"
SQ SEQUENCE 520 AA; 58228 MW; C769E5F6C8CED911 CRC64;
MTALSQEEIL QSTRTVVQGL EALKDEHESI KGTLMSSIQE LNADESALIE EKTHIVDRNL
EVLRLGIEEA QVMMALAGHL QTVEAEKQKL KAQVRRLCQE NAWLRDELNS TQQKLQATGQ
QVAQLEEEKK HLEYMNSIKK YDDQQENDKT MDQSDSRSDN TLQDLGFGPE EDEEISGHMT
GQFAHPTPAH SMAASASAGY EIPARLRTLH NLVIQYASQG RYEVAVPLCK QALEDLEKTS
GHDHPDVATM LNILALVYRD QNKYKEAANL LNEALHIREK CLGESHPAVA ATLNNLAVLY
GKRGKYKDAE PLCKRALEIR ENVLGVDHPD VAKQLNNLAL LCQNQGKYDE VERYYKRALE
IYESKLGPDD PNVAKTKNNL SSAYLKQGKY KDAEILYKQI LTRAHEREFG KVADDNKPIW
QIAEDREENK HKGGSGDTNT YQEYGGWHKA AKVDSPTVTT TLKNLGALYR RQGKYEAAET
LEDAALRAKK QCLDAAHQAK IASLIAEHTT GLSPPHGGVE
//