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Database: UniProt
Entry: A0A2G5FAS6_AQUCA
LinkDB: A0A2G5FAS6_AQUCA
Original site: A0A2G5FAS6_AQUCA 
ID   A0A2G5FAS6_AQUCA        Unreviewed;       734 AA.
AC   A0A2G5FAS6;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=AQUCO_00100491v1 {ECO:0000313|EMBL:PIA65047.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA65047.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA65047.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KZ305018; PIA65047.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5FAS6; -.
DR   STRING; 218851.A0A2G5FAS6; -.
DR   InParanoid; A0A2G5FAS6; -.
DR   OrthoDB; 239968at2759; -.
DR   Proteomes; UP000230069; Unassembled WGS sequence.
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   CDD; cd01367; KISc_KIF2_like; 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; PTHR47971:SF9; KINESIN-LIKE PROTEIN KIN-13B; 1.
DR   PANTHER; PTHR47971; KINESIN-RELATED PROTEIN 6; 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|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Microtubule {ECO:0000256|RuleBase:RU000394};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230069}.
FT   DOMAIN          193..518
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          568..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          603..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         284..291
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   734 AA;  82199 MW;  C0DC9D8C5F77D350 CRC64;
     MNAVGRQRSS TSSTVHHQRQ YSDHFLDTSS SNSNGKWLQS AGLQHFQSSN ATVPALQDYS
     GYFGGGGGGN GGGGVQGSRM FRNIQRSING GNELFSEPLT PPNQRRNGEE LINSSELSPG
     ILDLHSLDTE LLPEMPVPGL YDGSSHYHSG RGRSFDDSEP YISTNKQTNR TRGLPDNNLL
     KSFSADKPSS VAKIKVVVRK RPLNKKEVSR QEEDIISIEP GSNYLTVHET KLKVDLTEYE
     EKHEFVFDAV LSEGVSNDEV YRETVEPIVP TIFQRTKATC FAYGQTGSGK TYTMQPLPLK
     ASQDILRLMQ HTYRNQGFYL FVSFFEIYGG KLYDLLNERR KLCMREDGKQ QVCIVGLQEY
     KVSNVDTIRE LIEKGNATRS TGTTGANEES SRSHAILQLA VKRSADGSES KPPRVVGKLS
     FIDLAGSERG ADTTDNDKQT RMEGAEINKS LLALKECIRA LDSDQGHIPF RGSKLTEVLR
     DSFVGDSRTV MISCVSPNSG SCEHTLNTLR YADRVKSLSK GTTSKKDPLL STLNIRESTT
     LPLSSIAPTV SSIENNIYDV PNEHNRFGWS KQTERETLSH SMDRVSSGRE DDFDFSEEFY
     KPEKPSWKNS KQDSFRIPPL EDKTRKTDAQ PKWKEHQDFD NDLSADDDLS ALLKEEDDLV
     NAHRKEVEET IDIVREEMKL LVEADQPGNQ LDDYISRLNT ILSQKAAGIL HLQNRLAHFQ
     RRLNEHNVLV SSGQ
//
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