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Database: UniProt
Entry: A0A3P9NAU6_POERE
LinkDB: A0A3P9NAU6_POERE
Original site: A0A3P9NAU6_POERE 
ID   A0A3P9NAU6_POERE        Unreviewed;       701 AA.
AC   A0A3P9NAU6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000006676.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000006676.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000006676.1};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC       ECO:0000256|RuleBase:RU000394}.
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DR   RefSeq; XP_008418284.1; XM_008420062.2.
DR   AlphaFoldDB; A0A3P9NAU6; -.
DR   STRING; 8081.ENSPREP00000006676; -.
DR   Ensembl; ENSPRET00000006763.1; ENSPREP00000006676.1; ENSPREG00000004605.1.
DR   GeneID; 103471214; -.
DR   KEGG; pret:103471214; -.
DR   CTD; 11127; -.
DR   GeneTree; ENSGT00940000156386; -.
DR   OMA; NMRKHIE; -.
DR   OrthoDB; 5481713at2759; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000004605; Expressed in head and 1 other cell type or tissue.
DR   GO; GO:0005871; C:kinesin complex; IEA:Ensembl.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR   GO; GO:0046907; P:intracellular transport; IEA:Ensembl.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR   GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR   GO; GO:0035845; P:photoreceptor cell outer segment organization; IEA:Ensembl.
DR   CDD; cd01371; KISc_KIF3; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR   PANTHER; PTHR47969:SF32; KINESIN-LIKE PROTEIN; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|RuleBase:RU000394};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000242638}.
FT   DOMAIN          14..345
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          372..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          419..538
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        382..397
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         100..107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   701 AA;  79922 MW;  599F2A66B71FA4AB CRC64;
     MPSSKAEKQE VSDNVKVVVR CRPLNQKEKM MAFKQAVSVD EIRGTITVNK LEIPHEPPKT
     FTFDTVFGPD SKQLDVYNLT ARPIIDSVLE GYNGTIFAYG QTGTGKTFTM EGVRAVPELR
     GIIPNSFAHI FGHIAKAEGD TRFLVRVSYL EIYNEEVRDL LGKDQLQRLE VKERPDVGVY
     IKDLSGYVVN NADDMDRIMT LGHKNRSVGA TNMNEHSSRS HAIFTITIEC SEKGVDGNQH
     VRMGKLHLVD LAGSERQGKT GATGQRLKEA TKINLSLSTL GNVISALVDG KSTHVPYRNS
     KLTRLLQDSL GGNSKTMMCA NIGPADYNYD ETISTLRYAN RAKNIKNKAR INEDPKDALL
     RQFQKEIEEL KKKLEEGEEI SGSEGSGSEE MDEGDDYAGE AGEGRRRRRG RKKVSPDKMV
     EMQAKIEEER KALEAKLDME EEERNKARAE LEKREKDLLK AQQEHHLLLE KLSALEKKVI
     VGGVDLLAKA EEQERLLEES NNELEERRKR AEQLRKELEE KEQERLDIEE KYTSLQEEAQ
     GKTKKLKKVW TMLMAAKSEM ADLQQEHNRE IEGLLENIRQ LSRELRLQML IIDNFIPQEY
     QAMIENYVHW NEDIGEWQLK CVAYTGNNMR KQTPVPDKKE KDPFEVDLSH VYLAYTEESM
     RQSLMKLERP KASKGSKSGR PKTSRRKRSA KPDTVIDSLL Q
//
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