ID A0A3Q2E0S4_CYPVA Unreviewed; 1243 AA.
AC A0A3Q2E0S4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Kinesin family member 4A {ECO:0000313|Ensembl:ENSCVAP00000024864.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000024864.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000024864.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_015226828.1; XM_015371342.1.
DR RefSeq; XP_015226829.1; XM_015371343.1.
DR AlphaFoldDB; A0A3Q2E0S4; -.
DR STRING; 28743.ENSCVAP00000024864; -.
DR Ensembl; ENSCVAT00000003108.1; ENSCVAP00000024864.1; ENSCVAG00000009212.1.
DR GeneID; 107082580; -.
DR KEGG; cvg:107082580; -.
DR CTD; 16571; -.
DR GeneTree; ENSGT00940000158195; -.
DR OMA; PAFNKQH; -.
DR OrthoDB; 602895at2759; -.
DR Proteomes; UP000265020; Unplaced.
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:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd01372; KISc_KIF4; 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 InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF15; ZGC:66125; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM01114; CXC; 1.
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 Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000265020}.
FT DOMAIN 10..338
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 491..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 394..481
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 564..663
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 883..910
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 966..1013
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1023..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 89..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1243 AA; 140287 MW; E72E01BD8B874983 CRC64;
MTNEDAKVIP VRVALRCRPL VPKEINEGCQ TCLVFVPGEP QVIVGTEKAF TYDYVFDPTA
EQEEVFSTAV EPLLRGLFKG YHATVFAYGQ TGSGKTYSMG GTYTSAQEND PSVGVIPRVI
KRIFEEREKK TDSEFCLNVS YLEIYNEDIL DLLSASKDKP AISIREDPKE GIKIVGLTEK
QVFSAPEMVA CLEIGNSART VGSTAMNAAS SRSHAIFTIT LEQRRGSDKV DSIVSKLHLV
DLAGSERQKK TKAEGDRLKE GISINRGLLC LGNVISALGD ESKKNTFVPY RDSKLTRLLQ
DSLGGNSHTL MIACVSPADS NMEETINTLR YADRARKIKN KPIVNVDPRA AEMNRLKQQV
QELQVMLLHA RGGVAPVLSG PSSGEDVGKL LEKNRALQEE NGKLCRELSE AAGQTALMFE
KIIMTEQANE RLQSKLKQLE QHAACTVDLQ KVLQTLEDQE LKENVEVMKN LQELILELKN
ESAGISASIE GMSPREEVPE AAAVGSKDPT EQSSSDSPEA FTANHALRQA QLSKELIELN
KVLSLKEAFV RKMCENDSQL EPMQSEHKKN VQTLQSAVDS LQKEKEELVL ALQSAKKDSN
QAKLSEQRRK RLQELESQLV DMKKKLLDQS KLLKLKESSV QKVSKLMQEI QAMKTQRIQL
MKQMREDAEK YRQWKSKKDK EVLQLKEKDR KRQYELLKLE RDFQKQANVL RRKTEEAAAA
NKRLKDALQK RSEAAEKRKD HQSRGMEGAA ARVKTWLLNE VEVMVSLEEA RRHLSDLLDD
RKVLAQEINN LKQQIDAGER PAPKIRRRTL IISELETRGA LETPLSKQVE NLETEMGLRN
AQIADLQQKV LVADGEGRLK QRVDTLTSIV EAKSAVRVLM AELVSAKTAC SKLESELKQE
KGNSQDLRKM LAEERNVMST MDMEHQQQLV ELEQRHQEKV LYLLNQLQNK PICEESEETR
QEEETSSKER ELLQRLKVQE EELEKLRTLS EQNQKLMEQN EEYRQKLSLL HLASERKLLL
PVNKSDRSPD DSFEYVPPKP KPKKQTTAKA AVNTTINIAE LLSPSEDEKE EEEMDEWLPL
KGRRASRKTR MTGCACKGRC GNKQCRCRKG KMTCGENCLC DHEKCRNLDN QGKAEDASLA
DGISRDSASL QEPSCDSPDN ATFFKPPSCT PTTKVLKEIG DMGHSTADLK LVRKPSFTDE
DEGEEDDNEE DRTTVSFLKK KKRLLTSFQN SFFSGCTPIR EES
//
