ID   A0A3B4H4W0_9CICH        Unreviewed;      1233 AA.
AC   A0A3B4H4W0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Kinesin family member 4A {ECO:0000313|Ensembl:ENSPNYP00000030807.1};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000030807.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000030807.1}
RP   IDENTIFICATION.
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}.
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DR   AlphaFoldDB; A0A3B4H4W0; -.
DR   STRING; 303518.ENSPNYP00000030807; -.
DR   Ensembl; ENSPNYT00000031556.1; ENSPNYP00000030807.1; ENSPNYG00000023210.1.
DR   GeneTree; ENSGT00940000158195; -.
DR   Proteomes; UP000261460; 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}.
FT   DOMAIN          10..338
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          720..749
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1067..1099
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          381..443
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          567..673
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          879..920
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          984..1011
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        720..748
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   1233 AA;  140689 MW;  4CDDB9C913B47D8F CRC64;
     MTNEDEKVIP VRVALRCRPL VPKEINEGCQ SCLTFVPGEP QVIVGTEKAF TYDYVFEPTA
     EQEEVFSTAV SPLLSGLFKG YHATVLAYGQ TGSGKTFSMG GTYTTAQENE PSVGVIPRVI
     RCIFAEKEQR TDCEFCLAVS YLEIYNEEIL DLLCSSKDKP AISIREDPKE GIKIVGLTEK
     QVFSAPEMVS CLELGNSART VGSTAMNAAS SRSHAIFTIT LEQRRGTDKA DSVVSKLHLV
     DLAGSERQKK TKAEGDRLKE GISINRGLLS LGNVISALGD ESKKNTFVPY RDSKLTRLLQ
     DSLGGNSHTL MIACVSPADS NMEETINTLR YADRARKIKN KPVVNIDPRA AEMNRLKQQV
     QKWVINITHK AKGHNSCPCC RSESAENVTK LLERNRALRD ENNKLSRELS EAAGQTAHMF
     EKIIMTEQAN EKLQSKLEQL RHHAACTVDL EKVMKTLEDQ ELKENVEVMK NLQNIILELK
     VWMSSYITIQ SKKYKSSNNR VNCSGASHFF YLDATALKDS PEAFTAHHAL RQAQLSKELI
     ELNKVLSLKE AFVKKMCQND SQLEPMQSEH QKNVQTLQSA VDSLQKEKEE LVLALQSAKK
     DTNQAKLSEQ RRKRLQELES QLVDMKKKLL EQSKLLKLKE SSVQKVSKLM EEIQAMKTQR
     TQLMRQMRED SEKFRQWKNK KDREVLQLKE KDRKRQYELL KLERDFQKQA NVLRRKTEEA
     AAANKRLKDA LQKRSEVAEK RKDAQNKGME GAAARVKTWF LNEVEVMVST EEARRHLNDL
     LEDRKVLAQE INHLKQQLEA GERPAPKIRR RTLIISELES QGALETPLTK QVENLETEIG
     LRNAQIADLQ QKVLAADSEG RFKQRIDNIT SIVETKCALK VLMSELVSAK TAHAKLESEV
     TQEKANAQDL RKMLAEERNV MSTMDMEHQQ QLVELEQRHQ EKVLHRWARF RLKNIDLSQL
     HIFTFLPCFF RFFTSLTSFR TNLSEEELEK LRELSEQNQK LVEQNEEYRR KLSVVHLASE
     KKILVPKTNN ENNPDDSFEY IPPKPKSRRF TTAKAQLNAT INIEELMSPS EDENEEETEE
     WRPEKQERGR RVSKKPKQTG CACKGRCSNK QCRCRKGKMT CGENCQCDHE KCRNMDNQVP
     AEAGFSSFLL PDSSPGNNTF FKPPSCTPTK KVLKEIGDMG HTTADLKVAE EEQEDNDDEE
     DKTTVSFLKK KKRLLTSFQN SFFSGCTPIR EES
//