ID   A0A091IIE5_CALAN        Unreviewed;       915 AA.
AC   A0A091IIE5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
DE   Flags: Fragment;
GN   ORFNames=N300_02898 {ECO:0000313|EMBL:KFP08042.1};
OS   Calypte anna (Anna's hummingbird) (Archilochus anna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC   Trochilidae; Calypte.
OX   NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP08042.1, ECO:0000313|Proteomes:UP000054308};
RN   [1] {ECO:0000313|EMBL:KFP08042.1, ECO:0000313|Proteomes:UP000054308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP08042.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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; KL218769; KFP08042.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091IIE5; -.
DR   STRING; 9244.A0A091IIE5; -.
DR   Proteomes; UP000054308; 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; 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:SF57; KINESIN FAMILY MEMBER 5C; 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:UP000054308}.
FT   DOMAIN          1..285
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          884..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          290..331
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          372..490
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          549..872
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         44..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP08042.1"
FT   NON_TER         915
FT                   /evidence="ECO:0000313|EMBL:KFP08042.1"
SQ   SEQUENCE   915 AA;  104769 MW;  4CF67E3798C187CF CRC64;
     QGKPYVFDRV LPPNTTQEQV YNACAKQIVK DVLEGYNGTI FAYGQTSSGK THTMEGKLHD
     PQLMGIIPRI AHDIFDHIYS MDENLEFHIK VSYFEIYLDK IRDLLDVSKT NLAVHEDKNR
     VPYVKGCTER FVSSPEEVLD VIDEGKANRH VAVTNMNEHS SRSHSIFLIN IKQENVETEK
     KLSGKLYLVD LAGSEKVSKT GAEGAVLDEA KNINKSLSAL GNVISALAEG TKTHVPYRDS
     KMTRILQDSL GGNCRTTIVI CCSPSVFNEA ETKSTLMFGQ RAKTIKNTVS VNLELTAEEW
     KKKYEKEKDK NKSLKNVIQH LELELNRWRN GEAVPEDEQI SAKDQKNLEP CDNTPIIDNI
     TPVVASISTE EKQKYDEEIA SLYRQLDDKD DEINQQSQLA EKLKQQMLDQ EELLASTRRD
     YEKIQEELTR LQIENEAAKD EVKEVLQALE ELAVNYDQKS QEVEDKTKAN EQLTDELAQK
     SSALTATQRE LGQLQELSNH QKKRATEILN LLLKDLGEIG GIIGTNDVKT VTDVNGVIEE
     EFTMARLYIS KMKSEVKSLV NRSKQLESAQ MDSNRKMNAS ERELAACQLL ISQHEAKIKS
     LTDYMQNMEQ KRRQLEESQD SLNEELAKLR AQEKMHEVSF KDKEKEHLTR LQDAEEMKKA
     LEQQMETHRE AHQKQLSRLR DEIEEKQKII DEIRDLNQKL QLEQEKLSAD YDKLKIEDQE
     REMKLEKLIL LNDKREQARE DLKGLEETVA RELQTLHNLR KLFVQDLTTR VKKSVELDSD
     DGGGSAAQKQ KISFLENNLE QLTKVHKQLV RDNADLRCEL PKLEKRLRAT AERVKALESA
     LKEAKENAMR DRKRYQQEVD RIKEAVRAKN MARRAHSAQI AKPIRPGHYP ASSPTAVHAI
     RGGGMSNSSY YHNTK
//