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Database: UniProt
Entry: A0A3Q4BK05_MOLML
LinkDB: A0A3Q4BK05_MOLML
Original site: A0A3Q4BK05_MOLML 
ID   A0A3Q4BK05_MOLML        Unreviewed;       959 AA.
AC   A0A3Q4BK05;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
OS   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000020397.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000020397.1}
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       ECO:0000256|RuleBase:RU000394}.
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DR   AlphaFoldDB; A0A3Q4BK05; -.
DR   STRING; 94237.ENSMMOP00000020397; -.
DR   Ensembl; ENSMMOT00000020733.1; ENSMMOP00000020397.1; ENSMMOG00000015494.1.
DR   OMA; AYMEIYM; -.
DR   Proteomes; UP000261620; Unplaced.
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:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd01369; KISc_KHC_KIF5; 1.
DR   Gene3D; 6.10.250.1590; -; 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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR   PANTHER; PTHR47968:SF73; KINESIN HEAVY CHAIN ISOFORM X1; 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:UP000261620}.
FT   DOMAIN          9..327
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   COILED          332..373
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          408..435
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          482..547
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          592..675
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          703..789
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          819..899
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         86..93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   959 AA;  109679 MW;  23A0EE990F42E1AB CRC64;
     MADVPAECNI KVLCRFRPLN QSEILRGDLF LPKFQGDDSV IVGGKSFSFD HVFPTNTTQE
     QVYNTCAKQI VKDVLGGYNG TIFAYGQTSS GKTHTMEGKL HDPHQMGIIP RIAEDIFNHI
     FAMDENLEFH IKVSYFEIYM DKIRDLLDVT KTNLSVHEDK NRVPFVKGCT ERFVSSPDEV
     MDVIDEGKSN RHVAVTNMNE HSSRSHSIFL INIKQEHVET EQKLCGKLYL VDLAGSEKVS
     KTGAAGAVLD EAKNINKSLS ALGNVISALA EGTKTHVPYR DSKMTRILQD SLGGNCRTTM
     FICCSPSSFN DAETKSTLMF GQRAKTIRNT ASINLELTAE QWKRKYEKEK EKNKTLKESI
     QKLESELNRW RNGEDVPETE RTAPDVVTRF ESVEERPVLD NDNSSIVVRI SEEERQKYEE
     EIRKLYKQLD DKDDEINLQC QLVEKLKQQM LDQDELLASS KGDGDKVQAE LGRLQVESDC
     AKAEVKEVLQ ALEELAINYD QKSQEVEEKG LQNQLLADQL SQKMASLMEL EAELSRMQEV
     SGQQRKRIAD VLNGLMRDLS EFSTIVGNGE IKLPVEISGA IEEEFTVARL YISKIKSEVK
     SMVKRCRQLE NMQLECHRKM EETGRELSSC QLLISQHEAK IRSLTEYMQS VEHKKRLLEE
     SHDSLSEELA KLQDQGDMFH GFYSYKAVRQ QGESHRGLHH KQLARLRDEI NEKQRIIDEL
     TDRNSKLELE LAQVRADFER LKSQDSTKSE RLEELSLLHE RHEQTKQDLK GLEETVAREL
     QTLHNLRKLF VQDLTSRVKK SSEMEPDDSG GSCTQKQKIS FLENNLDQLT KVHKQLVRDN
     ADLRCELPKL EKRLRSTAER VKALETALRD AKEGAMMDRR RYQQEVDRIK DAMRAKNAMR
     RPHAAQIGTA LLLGYGHFHC INSCALPYTP FHTNSQASET EAATRLLSNQ PVLHLHPRR
//
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