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Database: UniProt
Entry: A0A3Q1B965_AMPOC
LinkDB: A0A3Q1B965_AMPOC
Original site: A0A3Q1B965_AMPOC 
ID   A0A3Q1B965_AMPOC        Unreviewed;       762 AA.
AC   A0A3Q1B965;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
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:ENSAOCP00000006536.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000006536.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC       {ECO:0000256|ARBA:ARBA00004138}.
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   AlphaFoldDB; A0A3Q1B965; -.
DR   STRING; 80972.ENSAOCP00000006536; -.
DR   Ensembl; ENSAOCT00000004438.1; ENSAOCP00000006536.1; ENSAOCG00000010184.1.
DR   GeneTree; ENSGT00940000153739; -.
DR   OMA; LESKMLC; -.
DR   OrthoDB; 5481713at2759; -.
DR   Proteomes; UP000257160; Unplaced.
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:0048839; P:inner ear development; IEA:Ensembl.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0048884; P:neuromast development; IEA:Ensembl.
DR   GO; GO:0043584; P:nose development; IEA:Ensembl.
DR   GO; GO:0035845; P:photoreceptor cell outer segment organization; IEA:Ensembl.
DR   GO; GO:0048793; P:pronephros development; IEA:Ensembl.
DR   GO; GO:0060042; P:retina morphogenesis in camera-type eye; 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:SF29; 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}; 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:UP000257160}.
FT   DOMAIN          9..341
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          370..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          703..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..410
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..743
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         97..104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   762 AA;  87165 MW;  00AEE2FCB9817636 CRC64;
     MSKSKSSESV KVVVRCRPMN EKERAAKFER VVSVDVKLGQ IIVRNPRDAS ASEVPKVFTF
     DSVYDWNSKQ IDLYDETFRP LVDSVLLGFN GTIFAYGQTG TGKTYTMEGV RNDPERRGVI
     PNSFEHIFTH ISRSQNQQYL VRASYLEIYQ EEIRDLLSKD QARRLELRER PDTGVYVKDL
     SSFVTKSVRE IEHVMNVGNQ NRSVGATNMN EHSSRSHAIF VITVECSELG VDGENHIRVG
     KLNLVDLAGS ERQTKTGAQG ERLKEATKIN LSLSALGNVI SALVDGRSSH IPYRDSKLTR
     LLQDSLGGNA RTVMVANIGP ASYNVEETLT TLRYSNRAKN IKNKPRVNED PKDALLREFQ
     EEIARLKEQL QKRSGKKKRR RQKRRAGEGS DGEDLEDGET EDDEEEGDDK GDYWREQQEK
     LERERKAIME DHSLVAEEKT RLLKEKEKKM EDLRKEREAG EMLAAKVKAM ESKLLVGGKN
     IVDHTNEQQR MLEQKRQEIT EQKRREREMQ QQMESRDEET LELKETYSSL QQEVDIKSKK
     LKKLFAKLQA VKEEIHDLQE AHINDRQDLE QTQNELTRDL KLKHLIIENF IPLEEKNKIV
     NRAFIDEEDE YWKMKPITRI EDDHQMMTRP LSAVGYRRPL SHHARMAMIL RPDVRYKAEN
     ILMLDMDLPA RTTKEYQEPV IAPKVAAALE DALRDEDEIQ VDASGFHSGS GSSPYASASS
     SLKKPKSGRP RTGKKSSTPT SPFSPSSPGS PLYPQSRGLV PK
//
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