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Database: UniProt
Entry: A0A099YZI1_TINGU
LinkDB: A0A099YZI1_TINGU
Original site: A0A099YZI1_TINGU 
ID   A0A099YZI1_TINGU        Unreviewed;      1701 AA.
AC   A0A099YZI1;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Kinesin-like KIF13A {ECO:0000313|EMBL:KGL74303.1};
DE   Flags: Fragment;
GN   ORFNames=N309_11544 {ECO:0000313|EMBL:KGL74303.1};
OS   Tinamus guttatus (White-throated tinamou).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX   NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL74303.1, ECO:0000313|Proteomes:UP000053641};
RN   [1] {ECO:0000313|EMBL:KGL74303.1, ECO:0000313|Proteomes:UP000053641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL74303.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-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}.
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DR   EMBL; KL886935; KGL74303.1; -; Genomic_DNA.
DR   STRING; 94827.A0A099YZI1; -.
DR   Proteomes; UP000053641; 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   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; 2.
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; PS00845; CAP_GLY_1; 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:UP000053641}.
FT   DOMAIN          1..285
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1588..1630
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          770..789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1432..1451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1462..1490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1509..1559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1632..1701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          297..342
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          540..567
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1476..1490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1516..1534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         35..42
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:KGL74303.1"
FT   NON_TER         1701
FT                   /evidence="ECO:0000313|EMBL:KGL74303.1"
SQ   SEQUENCE   1701 AA;  189447 MW;  FC22371EFCCA0B0D CRC64;
     LKYYFVGQEV VFKCLGEGIL EKAFQGYNAC IFAYGQTGSG KSFSMMGNAE QLGLIPRLCC
     ALFQRISVEE NESHTFKVEV SYMEIYNEKV RDLLDPKGSR QSLKVREHKV LGPYVDGLSQ
     LAVTNFEDIE SLMSEGNKSR TVAATNMNEE SSRSHAVFNI IVTQTLYDLQ SGNSGEKVSK
     VSLVDLAGSE RVSKTGAAGE RLKEGSNINK SLSTLGLVIS SLADQAAGKG KSKFVPYRDS
     VLTWLLKDNL GGNSQTAMIA TISPAADNYE ETLSTLRYAD RAKRIVNHAV VNEDPNARVI
     RELREEVEKL KEQLSQAEAM KAPELKEKLE ESEKLIKELT VTWEEKLRKT EEIAQERQRQ
     LESMGISLES SGIKVGDDKC YLVNLNADPA LNELLVYYLK DHTRVGADTS QDIQLFGIGI
     QPEHCEIDIA VDGEVTLTPK ENARSCVNGA LVCSVTQLWH GDRILWGNNH FFRINLPKRK
     RRDWLKEFEK DAPLGEHDLD AASEASSEPD YNYEFAQMEV IMKTLNSNDP VQNVVQILEK
     QYLEEKRSAL EEQRLMYERE LERLRQQLSP ERQHPHGSDR LSYAAHAAQQ KVNLWTEERD
     ELFRQSLAKL REQIVKANTL VREANFLAEE MGKLTDYQVT LQIPAENLSA NKKRGAIVSE
     PAIQVRRKEK ATQVWTIEKL ENKLIDMRDL YQEWKEKVPE LRKINGKRGD PFYEAQENHN
     LIGVANVFLE CLFSDVKLQY AVPIISQQGE VAGRLRVEVM RITGSVPERV VEGDDSSENS
     SESGSLEVMD SNGEIIQRPK KLSCRVKIKE ATGLPPNLSN FVFCQYMFWD QCEPTVVAPV
     VGPDVPSAAS KEAHFTVTFS HCKDYVVNVT EEFLEFISEG ALAIEVWGHR CTGNGSSVWE
     VDSLRAKTRT LRDRWNEVTR RIEMWISIQE LNEMGEYTAV ELHQAKDVNT GGIFQLRQGH
     SRRVQVTVKP VQHSGTLPLM VEAILSVSIG GVTARSTKLQ RGLDSYQEED LNCVRERWSD
     ALIKRREYLD EQIQKISNKQ EKTEDDIERE ARLVEQWVGL TEERNAVFVP APGSGIPGAP
     ANWVPPAGME THIPVLFLDL NADDLSANEQ LTGPHASGVN SILPKEHGSP FFYLPIIKHS
     DDEVSATAAW DSSVHDSVHL NRVTPQNERI YLIVKTTVQL SHPAAMELVL RKRIAANVYN
     KQSFTQSLKR RISLKNIHYA CGVTYEIVSN IPKATEEIED RETLALMAAR SENEGTSDGE
     TYMEKYTRGV LQVENILSLE RLRQAITVKE ALSTKARNIR RSISSPNVHN VRVVAVLSQV
     SAKKLSPCVC VRVCTLACSE LEAINKKLSP QGFQSFRPYV PEEFADFSVY NASLEHREWG
     SSKTDFVNSR ALEKEVSRSP TTSSITSGYF SHSASNATLS DLLVPCSDST DQLAAHAREP
     DSGDSPAPSL AHDLRTSLNK EFRESEKELV TEKLPVSPLK QNSALTEQPS LPLNATKKDS
     QQLPAAAPFS ALDSSNDKPP CCTIEFSTQP RSSPEAPARG GPGKDPLDAS DGEEGASADQ
     AHVLPSWVAV GEQVCVGSNK MGTVRYVGTV DFSAGIWIGV ELNVQLGKHD GTVKGREYFQ
     CKPRHGVFVR PGRLSRAPAA ARKPSGTARP PAPPTLEKRR SSLLQGSAPT SRPGGDALCH
     AGDAAASAFS RKQENRKSWI N
//
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