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Database: UniProt
Entry: A0A498SMV6_ACAVI
LinkDB: A0A498SMV6_ACAVI
Original site: A0A498SMV6_ACAVI 
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
//
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