ID A0A091QKN3_LEPDC Unreviewed; 1306 AA.
AC A0A091QKN3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Kinesin-like KIF16B {ECO:0000313|EMBL:KFQ10044.1};
DE Flags: Fragment;
GN ORFNames=N330_06569 {ECO:0000313|EMBL:KFQ10044.1};
OS Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ10044.1, ECO:0000313|Proteomes:UP000053001};
RN [1] {ECO:0000313|EMBL:KFQ10044.1, ECO:0000313|Proteomes:UP000053001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ10044.1};
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}.
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DR EMBL; KK677478; KFQ10044.1; -; Genomic_DNA.
DR PhylomeDB; A0A091QKN3; -.
DR Proteomes; UP000053001; Unassembled WGS sequence.
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:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR CDD; cd22732; FHA_KIF16B; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR CDD; cd06874; PX_KIF16B_SNX23; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR000253; FHA_dom.
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; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF6; KINESIN-LIKE PROTEIN KIF1C ISOFORM X1; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00787; PX; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50195; PX; 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 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:UP000053001}.
FT DOMAIN 1..343
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1171..1296
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1061..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 358..406
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 584..621
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 647..792
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 818..852
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 919..1006
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1034..1061
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 87..94
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:KFQ10044.1"
FT NON_TER 1306
FT /evidence="ECO:0000313|EMBL:KFQ10044.1"
SQ SEQUENCE 1306 AA; 150826 MW; 3E727D706CCF61BD CRC64;
REKDLNAKFI ISMEKNKTTI TNLKVPEGIT GDTARERTKT FTYDFSYFSA DSKSPSFVCQ
EMVFKNLGTD VLKSAFEGYN ACIFAYGQTG SGKSYTMMGN AGDAGLIPRI CEGLFSKISE
KTKRNEASFR TEVSYLEIYN ERVRDLLRRK SSKTNNLRIR EHPKEGPYVE DLSKHLVQNY
TDVEELMDAG NINRTTAATG MNDVSSRSHA IFTINFTQAK FDSEMPCETV SKIHLVDLAG
SERADATGAT GVRLKEGGNI NKSLVTLGNV ISALADLSQD ASNSLSKKKQ VFVPYRDSVL
TWLLKDSLGG NSKTIMIATI SPADVNYGET LSTLRYANRA KNIINKPTIN EDPNVKLIRE
LRAEIARLKA LLAQGNQIAL LDSPTALSME EKLQQNEARV QELTKEWTNK WNETQDILKE
QTLALRKEGI GVVLDSELPH LIGIDDDLLS TGIILYHLKE GQTYVGREDA VTEQDIVLHG
LDLESEHCIF ENLNGTVNLI PLNGAQCSVN GIQITEATHL NQGAVILLGR TNMFRFNHPK
EAAKLREKRK SGLLSSFSLS MTDLSKSCEN LSAVMLYNPG LEFERQQREE LEKLESKRKQ
IEEMEEKQRS DKAELVRMQQ EVESQRKETE IVQLQIRKQE ESLKQRSVHI ESRLKDLLAE
KEKFEEERLR EQQEIEIQKK KQQEEIFARV KEELQRLQEL NHNEKAEKMQ IFRELEKLKK
EKDEQFIKLE SEKRRLEEQE REQMVLVAHL EEQLREKQVM IELLKRGDVQ RVEEEKSDLE
DIRESLLKVK EARSEGDENC EELERAQHDF VEFKRKQLEQ LTILEKDLVQ QMDHLEKEIA
DEKIALEHLK FAHEEHLNLK RDDENFLDAV LQAEEFDKLK PAEYRLQSKV RQLEYLKGNH
LPALLEEKQR ASEILDRGLL GLDNMLYQIE KEIEEKEEQL AQYRASTNQL QQLQETFEFA
ANVARQEEKV RKKEKEILES REKQQREALE QAVAKLERRH SALQRRSTID FEIEEQKQKL
ATLNNSCSEQ AGLQASLEAE QKALEQDRER LDQEIQQLKQ KIYEGDGGQK GNHGTLEERL
SHTTSPTSPT KPQPPTAPLV DDRINAFIEQ EVQRRLQNIH HKAEDNDVSL SWSTESLKDN
ERLNNGTIQR RLKYERMVCR SLGANPDDLK DPIKISIPRY VLCGQGKDEH YEFEIKITVL
DETWTVFRRY SRFREMHKTL KLKYPELATL EFPPKKLFGN KDERVIAERR SHLEKYLRSF
FSAMLKSPSS PLHIDKVRLT LSKHTICEFS PFFRKGVFDY SSHGTS
//
