ID A0A0N0U647_9HYME Unreviewed; 1303 AA.
AC A0A0N0U647;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Kinesin-like protein KIF16B {ECO:0000313|EMBL:KOX77052.1};
GN ORFNames=WN51_10446 {ECO:0000313|EMBL:KOX77052.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX77052.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX77052.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX77052.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX77052.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) 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; KQ435736; KOX77052.1; -; Genomic_DNA.
DR STRING; 166423.A0A0N0U647; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000053105; 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:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR CDD; cd22708; FHA_KIF16; 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; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000053105}.
FT DOMAIN 1..344
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1166..1279
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 912..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 585..683
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 741..789
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"
SQ SEQUENCE 1303 AA; 147275 MW; 83967EDEA3CCC469 CRC64;
MMCVAHGSEH YSPPPRMRLL LQGNDTPGSC REIDREKYKD FTFDHSYWSF DTNDDNYASQ
EEVFYDLGTD VIESAFEGYN ACVFAYGQTG SGKTFTMMGT PEAQGLIPRI CKTLFARMAA
GKESGASYRT EVSFLEIHNE RVRDLLRLDQ SQSHSLRVRE HPKRGPYVQD LSSHLVYDYS
DIQECMVRGN THRTTASTNM NDVSSRSHAI FTITFVQAGL SEGNMPSETV SKVHLVDLAG
RVLSILKMQY VKFTSVCPCL SSERANATGS VISALAELSS TGDASSSSKR NVFIPYRDSV
LTWLLKDSLG GNSKTIMIAA ISPADCNYGE TLSTLRYANR AKNIINKPTI NEDPNVKLIR
ELREEIQKLK SLIGKDISVE RPPQVLLAQI HEKQEQEKVL TEEWTEKWRE TQQILQEQKA
LGLRKSGVGV VLDSEMPHLV GIDDDLLSTG VTLYHLKEGR TLVGTEEAPT TQDIVLTGAD
VEPEHCVVEL DGGVATLHPL SSHCWINTAQ VDKPTRLSQG CIILLGRNNM FRYNDPAEAA
KLRKEGGMGN GNLQSTVVNL SRLSLLSWSV SDLHASSSSD NLLNSSEDLR ALEELEQQKA
ALIKEKEDFK REQEEREERW AARREALEGA QRELEREWGA QWKEWADAIA TLESRQRELR
TRRHILEQER RDEMTQVENL CREVASLRTT LQSRHRQFQE FMSNHERAQR FHQWWEKTDD
GAGSDGSLPE SWSSLNDDKC VDAVRELVNH HKKELAVLET ELQNKVKSLN EHQCKVDKME
EELMEIAKKQ KHMLNLEVGV LVEEEGNTEK KLLLAKRSQE QLQEILRRKQ NLSLNLKRAL
PAFPGDRSLS GDEVLHNGDT QSFQDGCNRK LQIASALSLL PQNVPSSIDT ADTFHTAAAD
SPEPRIPFED FETKESQTSP SKQKEPDKQQ KPSPEVHLEN DRAKLCEAAE NRSLLNLNGK
SSVIDTTAVK SGKCNGSASV QQNPAMKRLN QRIARQRMMV MRCLEASTPS KEDLNRQIAI
LQDLQKQQIE LEVSLLEDER KNLKQQSASQ CGLDDRLAAD DANDIAQTVE TSCIGRNVDS
TTNSATLLTV ATTRSPVLRN HRPNNTNGEE NLSESVAPRV SSGRGYSTVY LTSQNRGDRL
SSPYSLTITR SLPSLIANDA DYDSVINVIV SIPSYVIRGA GTSSHYEYEV RVVAQDDSWT
LLRRYRRFRE LYISMRQKYG SKVAAIRFPP RQVFPRYEVV ARQRRKRLEE YLRRLIQVCS
ELPHCEPLYK YNGNLSNIDK QSLLEFSSFF RRGTFESSKY GTS
//
