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Database: UniProt
Entry: A0A218UW39_9PASE
LinkDB: A0A218UW39_9PASE
Original site: A0A218UW39_9PASE 
ID   A0A218UW39_9PASE        Unreviewed;      1941 AA.
AC   A0A218UW39;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Kinesin-like protein KIF13A {ECO:0000313|EMBL:OWK57741.1};
GN   Name=KIF13A {ECO:0000313|EMBL:OWK57741.1};
GN   ORFNames=RLOC_00001052 {ECO:0000313|EMBL:OWK57741.1};
OS   Lonchura striata domestica (Bengalese finch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC   Estrildinae; Lonchura.
OX   NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK57741.1, ECO:0000313|Proteomes:UP000197619};
RN   [1] {ECO:0000313|EMBL:OWK57741.1, ECO:0000313|Proteomes:UP000197619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=White83orange57 {ECO:0000313|EMBL:OWK57741.1};
RA   Colquitt B.M., Brainard M.S.;
RT   "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL   Submitted (MAY-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   -!- 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:OWK57741.1}.
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DR   EMBL; MUZQ01000118; OWK57741.1; -; Genomic_DNA.
DR   STRING; 299123.ENSLSDP00000014818; -.
DR   Proteomes; UP000197619; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; 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; cd22729; FHA_KIF13A; 1.
DR   CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 6.10.250.2520; -; 1.
DR   Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR   InterPro; IPR032405; Kinesin_assoc.
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; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117:SF5; -; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF12473; DUF3694; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF12423; KIF1B; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16183; Kinesin_assoc; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM01052; CAP_GLY; 1.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF74924; Cap-Gly domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 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};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197619}.
FT   DOMAIN          1..323
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1828..1870
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1583..1624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1717..1745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1870..1919
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          335..380
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          578..643
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1588..1602
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1603..1623
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1881..1914
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         73..80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1941 AA;  216007 MW;  7BD95CFB96B58150 CRC64;
     MEGNQTVLHP PPSNAKQGER KPPKVFAFDH CFWSMDESNT TKYAGQEVVF KCLGEGILEK
     AFQGYNACIF AYGQTGSGKS FSMMGNAEQL GLIPRLCCAL FQRISVEENE SHSFKVEVSY
     MEIYNEKVRD LLDPKGSRQS LKVREHKVLG PYVDGLSQLA VTNFEDIESL MSEGNKSRTV
     AATNMNEESS RSHAVFNITV TQTLYDLHSG NSGEKVSKIS LVDLAGSERV SKTGAAGERL
     KEGSNINKSL STLGLVISSL ADQAAGKGKN KFVPYRDSVL TWLLKDNLGG NSQTAMIATI
     SPAADNYEET LSTLRYADRA KRIVNHAVVN EDPNARVIRE LREEVEKLKE QLSQAEAMKA
     PELKEKLEES EKLIKELTVT WEEKLRKTEE IAQERQRQLE SMGISLESSG IKVGDDKCYL
     VNLNADPALN ELLVYYLKDH TRVGADTSQD IQLFGIGIQP EHCEIDIALD GEVTLTPKDN
     ARSCVNGALV CSATQLWHGD RILWGNNHFF RINLPKRKRR DWLKDLEKET SLGEHDLDAA
     SEASSEPDYN YEFAQMEVIM KTLNSNDPVQ NVVQILEKQY LEEKRSALEE QRVMYERELE
     LLRQQLSPER QHPHGSDRLA YTAQAAQQKV NLWTEERDEL FRQSLAKLRE QIVKANTLVR
     EANFLAEEMS KLTDYQVTLQ IPAENLSANK KRGAIVSEPA IQVRRKGKGT QVWTIEKLEN
     KLIDMRDLYQ EWKEKIPEIR KLIGKRGDPF YEAQENHNLI GVANVFLECL FYDVKLQYAV
     PIISQQGEVA GRLHVEVMRV TGSVPERVVE GDDSSENSSE SGSLEVMDNN GEIIHRAKKL
     SCRVKIKEAT GLPPNLSNFV FCQYTFWDQC ESTVAAPVVD PDVPSPQSKD AHFTVTFSHC
     KDYVVNVTEE FLEFISEGAL AIEVWGHRCT GNGSSVWEVD SLHAKTRTLR DRWNEVTRRI
     EMWISIQELN EMGEYTAVEL HQAKDVNTGG IFQLRQGHSR RLQVTVKPVQ HSGTLPLMVE
     AILSVSVGGV TARSTKLQRG LDSYQEEDLN CVRERWSDAL IKRREYLDEQ IQKISNKQEK
     SEDDIEREAR LVEQWVGLTE ERNAVFVPAP GSGIPGAPAN WIPPAGMETH IPVLFLDLNA
     DDLSANEQLI GPHASGVNSI LPKEHGSPFF YLPIIKHSDD EVSATAAWDS SVHDSVHLNR
     VTPQNERIYL IVKTTVQLSH PAAMELVLRK RIAANIYNKQ SFTQSLKRRI SLKNIYYACG
     VTYEIVSNIP KATEEIEDRE TLALMAARSE NEGTSDGETY IEKYTRGVLQ VENILSLERL
     RQAVTVKEAL STKARNIRRS ISTPNVHNVS CSRLDLSACD DDDKGWSESH LDISDCCSSY
     QDVSCYGTLP RESPRKSKDG SGVVAENSHA LMASPFKAFS PQPPKFFKPL MPVKEEHKRK
     TPLESRPLLS QESMPPLQVH CAGYAVPAGS MASTMPEEKI DSEEEDNELE AINKKLISPQ
     NFQNFRPYVP EEFADFSIYN ASLENREWFS SKSDFMSSRV LEKEVSRSPT TSSITSGYFS
     HSASNATLSD MLVHCSDSTD QLASHSKELD SSDPSGSSLE HDLKSSLNKE CRESEKELSR
     EKLPVVPLKG NSALTEQVPL SFSAADRDSQ QLPRAGSLSA LSSLDGKNTI EFSACEVTVE
     HTMDVLEDHS FTEFMGVEDG KDFDHSAAPQ LCSLLSSNGA SASESPRGPG KGQSPCTGQQ
     SSAATPADGW LADAVESPFC SGLVKDPSDP ETYPDASMDD FIMKDHLDGS DCEEGASADQ
     AHILPSWVAV GEQVCVGSNK MGTVRYVGTV DFSAGIWVGV ELNVQLGKHD GIVKGREYFH
     CKPRHGVFVR PGRLSKAPAP ARKWSSTSRS QAPSSSEKRK SSVLQGSSAT PKTGGDVLCH
     SGDAAASAFS RKQENRKSWI N
//
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