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Database: UniProt
Entry: A0A2I0LLC2_COLLI
LinkDB: A0A2I0LLC2_COLLI
Original site: A0A2I0LLC2_COLLI 
ID   A0A2I0LLC2_COLLI        Unreviewed;      1429 AA.
AC   A0A2I0LLC2;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Kinesin family member 24 {ECO:0000313|EMBL:PKK18218.1};
GN   Name=KIF24 {ECO:0000313|EMBL:PKK18218.1};
GN   ORFNames=A306_00014415 {ECO:0000313|EMBL:PKK18218.1};
OS   Columba livia (Rock dove).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX   NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK18218.1, ECO:0000313|Proteomes:UP000053872};
RN   [1] {ECO:0000313|EMBL:PKK18218.1, ECO:0000313|Proteomes:UP000053872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Blood {ECO:0000313|EMBL:PKK18218.1};
RX   PubMed=23371554; DOI=10.1126/science.1230422;
RA   Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA   Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA   Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT   "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL   Science 339:1063-1067(2013).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PKK18218.1}.
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DR   EMBL; AKCR02000220; PKK18218.1; -; Genomic_DNA.
DR   RefSeq; XP_005507850.1; XM_005507793.1.
DR   STRING; 8932.A0A2I0LLC2; -.
DR   GeneID; 102090730; -.
DR   KEGG; clv:102090730; -.
DR   CTD; 347240; -.
DR   InParanoid; A0A2I0LLC2; -.
DR   OrthoDB; 239968at2759; -.
DR   Proteomes; UP000053872; Unassembled WGS sequence.
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   CDD; cd09541; SAM_KIF24-like; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 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   InterPro; IPR013761; SAM/pointed_sf.
DR   PANTHER; PTHR47971:SF8; KINESIN-LIKE PROTEIN KIF24; 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   SUPFAM; SSF47769; SAM/Pointed domain; 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   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:UP000053872}.
FT   DOMAIN          220..543
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          108..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          882..925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1050..1069
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1197..1219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1247..1280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        882..900
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        901..925
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1248..1269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         310..317
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1429 AA;  159359 MW;  A58AB5D3E88D4768 CRC64;
     MASCLYECLC EAELEKYYPH FAAFGLQKID ELAKVSMKDY TKLGVHDMND RKRLFQLIRI
     IKIMQEDDVA CLSKQDFQPS DLFIQPQVTR SGPRRQLRFE SFFEENDSTV KDSESQSCGS
     SDFSANEEKN SGGEMLGHIQ PHDSELIRLT RRDLNTPATC TRKDLSCPTV SDDIASLLGD
     SEAPIIQRIT HISGYNYGLP RSCARPSTSE KDTPWTESEK IRVCVRKRPL GLREERRGEV
     NIITVKDKET LLLHEKKEAV DLTQYILQHV FYFDEVFGES CTNQDVYMKT AHPLIQHIFN
     GGNATCFAYG QTGAGKTYTM IGTHRNPGLY ALAAKDIFGH LEASQSRKDL HVLISFYEIY
     CGQLYDLLNG RKRLFAREDG KHIVQIVGLR EVQVDSVDLL LEVILKGGKE RSTGATGVNS
     DSSRSHAIIQ IQIKDAANRT FGRISFIDLA GSERAADARD SDRQTKMEGA EINQSLLALK
     ECIRALDQEH AHTPFRQSKL TQVLKDSFIG NSKTCMIANV SPSHTATEHT LNTLRYADRV
     KELKKGIKCS TPVTKRRRTA GNVSPKCVQN SHSLPPGEKS SPKKVKPGLQ HPSSATKTKA
     CPAALQPPSV SFSSTHRGIN KGHSYKGNAS SPWFHHTSPV KGVLWVAHPL KKKADDLSTQ
     SEKNPTTKDL TIKNAATAET KESGQRDKHM QDRPPVQCLK VQTVQPVQKQ LVSRDDTSFG
     DGNLPSNGRQ EWGNVFAKQC VETWTNVPPF QKEREEHLRL YHQQFQQPPI LQQKLNYQPL
     ERFLTEYKPQ EIQVKPELSV TPTELQSKEG MQLEDLDDSD FSEDSFSPVC SQSVKSRNTN
     KCSQHSFFLH QREIETEEEQ KGQKRQDLFF KYAVPMQEHE LDDSWDYSEG SPKREESIKN
     SGCSKTPSEW SYDLTTEPSP SNTAEKPYCL QEDPACNWKN GKDFLADNKQ YKSKHRSLVY
     SSEATLTPEK DAPNTYVSPV LKSGMSDCKE VDLQHKEKEQ SPLDRQAALA GDKKLKVQKD
     GFNHCGSSSC SPEFTPELTA PLPVSVLDYE ETTDTEKVSS NPEKSPPVKQ MLDRNVHGCQ
     NRFEDEGWQC TRSRALTDSM LDLGEQTRRG GRHCARLHSP QSGDKWLSPT CCGVKPCCCL
     LGPGPSKQGA AHRLFVGRDL METSAAESTG SRGEREGGLF LSNPMCKEYS AGRQCDADVK
     NSTGNSGKSN SNQGPSLEPT AQEINADIPE KSYFPGVPCF VSVGNMDDAV PSPSQESSLL
     SQPKSGPRNE DFSYSDDPAK SSLSNEEIAL LKNKLMQSTF TQETFAVHSG SVTKDNKLLA
     NAKSLSGMSN GSSPSATSEV GKWQREALEK AQQAVIWAHQ QQLDEMASLC FKEECLINQM
     SAMDFQSFVT KLDEVLVLKS KCIQTARAHL QPYLASPGTD MSPQTSPPV
//
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