ID   A0A3Q1C3K9_AMPOC        Unreviewed;      1312 AA.
AC   A0A3Q1C3K9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Kinesin family member 15 {ECO:0000313|Ensembl:ENSAOCP00000021897.1};
GN   Name=KIF15 {ECO:0000313|Ensembl:ENSAOCP00000021897.1};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000021897.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000021897.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIN-12 subfamily.
CC       {ECO:0000256|ARBA:ARBA00034488}.
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DR   Ensembl; ENSAOCT00000009373.1; ENSAOCP00000021897.1; ENSAOCG00000000384.1.
DR   GeneTree; ENSGT00940000156463; -.
DR   Proteomes; UP000257160; 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; cd01373; KISc_KLP2_like; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR044986; KIF15/KIN-12.
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; PTHR37739; KINESIN-LIKE PROTEIN KIN-12D; 1.
DR   PANTHER; PTHR37739:SF8; KINESIN-LIKE PROTEIN KIN-12D; 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   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:UP000257160}.
FT   DOMAIN          19..357
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   COILED          364..391
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          475..511
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          589..627
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          726..881
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1027..1096
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1139..1173
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1210..1275
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         103..110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1312 AA;  150576 MW;  F9BBC77A3E5F97A6 CRC64;
     MNSSGKGSAT NTSVGDNDSI KVFVRVRPLT QGTGLTTDGD QSLCLTVTSP NTIRLLSKPE
     PRTFTYDHVA DMDTSQDSVF SSVAKNIVES CMNGYNGTIF AYGQTGSGKT FTMLGPSELD
     NFTDELRGVI PRSFEYLFFL INREAERSGQ SKNFLCKCSF IEIYNEQIYD LLDTASASLF
     LRENIKKGVF VEGAVEKFVN SAAEAYQVLS MGWRNRRVAS TSMNRESSRS HAVFTMTLES
     KESINEVVNI RMSQLNLVDL AGSERQKDTH TEGSRLKEAS SINRSLMCLG QVIMALVDVS
     NGKNRHICYR DSKLTFLLRD SLGGNAKTYI IANVHPGSKC FGETLSTLQF AQRAKLIKNK
     AVINEDTQGN VRQLQAEVKK LKEQLQRALS LERYLFIYFF LTNIKWLFLP GPTTEMQHII
     SYKSKFMSAV RLWRKQDEEK KMLLKKVAQL EEAWTQKDKF IHSSRMIVRF REDHISRLEK
     KLKAGQSLLS DKESQALIDQ LKEEIKILRD QVEHHPKMTR YAAENYSLRE ENRLLRSLES
     VVKAEEVAAQ VAAELEDAFQ MAIESERLPE TAAVSSSTVA TDTVSAATIE KLNAKLLQKQ
     SDLTAALRAF EEYKEVTKKQ MSQLESEKRY LDKSNRHLEN ILEATNAYKK REVSELNRIH
     VETIKILTTP TKAYNLRSRF VPLSSPDHLK DEDNKAENIW AEQPPSDMGE MALTEELRQV
     RVQTQLNEEE LKNSKLLQQI AKLEEQITMM SQEADQKDEV ELPHLHVLKL NVFPLLSVLR
     SEIRDLRLVL QSSDKELASV KNELRDGQNE QEKEMSQLSN SLISTQLQLD KVQLEWEQLL
     EQHRTLQDSF DQLQAEAKFE ADQARQQLHD KQQETDELKT QVMVSELRNS GAIFDEKCRF
     LWLNFYGLCL NLELTETVEQ NTHLRKQVSD LTVQNQQQVS HKECVHICKV EQIKSLEQKI
     EQDKDVVLDL INQTRDLRSE LSHKDQTINH LSGDIKDITA KYSAACLERE DIKEQNCKMH
     AEICGLKETL DRRAASNKIE VEVLQEEIAY ATEEVERLTK VLDEQNSLLQ ASQEQTAQKE
     VTIQNLEQKQ EAVEKTIRNG IFKPLVEPTT PCTPGSFNRD LTQVLESQEQ ELESRRSSMM
     TMEILLAELN AERAAKNEEI QRLKTQLTEK EMVRMEIQEL LDKFYTKQSQ LTQNGNNSEE
     LNEVIKQSML KELQEERAEK AQESMLAQSQ TCVQELTTEL RNRCLELREL SQRIHDEEKL
     ENEVLRKQNV KLSEENGKLV GHKNHKQRIE YLVKLKKDNT KLQEVTNISS II
//