ID A0A3B3RMA4_9TELE Unreviewed; 1699 AA.
AC A0A3B3RMA4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Kinesin-like protein KIF16B {ECO:0000313|Ensembl:ENSPKIP00000018861.1};
GN Name=KIF16B {ECO:0000313|Ensembl:ENSPKIP00000018861.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000018861.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000018861.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR STRING; 1676925.ENSPKIP00000018861; -.
DR Ensembl; ENSPKIT00000035697.1; ENSPKIP00000018861.1; ENSPKIG00000004258.1.
DR GeneTree; ENSGT00940000162838; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000261540; Unplaced.
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 GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor 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; 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 PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA 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};
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}.
FT DOMAIN 3..358
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1021..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 373..421
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 590..627
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1058..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1699 AA; 190622 MW; B745CC21A0008BA2 CRC64;
MASVRVAVRV RPMDRRETDL LSKCIVYMEG NKTSITNLKV PKGTVGDSSR ERTKMFTYDF
SYDSSDSKSA NFVSQEKVFM DLGSDVLVAA FQGYNACVFA YGQTGSGKSF TMMGDPDDRG
LIPRICEGLF GRIAGMTLWD EASFCIEVSY LEIYNERVRD LLRKKSSKAY NLRVREHPKE
GPYVEELSKH LVQNYCDVEE LMKVGNMNRT TASTGMNDVS SRSHAIFTMK FTQAKFGAEM
PCETVSKIHL VDLAGSERAD TTGTSGVRLK EGCSINKSLV TLGNVVSALA DLSQDNVSAN
SKKKHIFVPY RDSVLTWLLK DSLGGNSKTI MIATISPADI NYSETLSTLR YANRAKNIIN
QPEINEDTNV KLIRELRAEI AHLRELLVQG KQIALLDSPT ALSMEERLHE NEARVMELTK
EWTNKWNETQ NILKDETLAL RKEGIGVVLD SELPHLIGID DDLLSTGIIL YHLKEGRTSV
GYEDSETEQD IVLRGTDLES EHCVFENIND TVTLIPLGGA QCAVNGAQVM EPTQLRQGAV
ILLGKTNMFR FNHPKEAANL REKRKSGLLS SFSVSNENLS MLYNSGLEFE RQQREELQKL
ELKRRTIEEM EEKQKNEKAE LEHIQQDIKA LHEISEQFHL RNQQKEEALK CCCQAIENQL
CFLQSEIDCF DELLEGELKT LVEEKQELSL VTQLKMEIFQ ELKQLKVVWD KEAVEMKMEE
KRLHEQGCKV ELEQVYREER LHEKQFLLCL LKKYNMHWKE GEEITLEEIR KMLLKTSEEH
LDGHEDHKDI QGMRMDFQVM PVEKPAILPN ELLRQERSSD SCLCSKQKAH ELLFSDDETP
KQEEHDALLE RNPLQNQESQ QVNVYRLPAL AVEKHGGREV MNPGGSKLKH GSTDQQRGSI
IELEILEQMR ILAALCHTRN LPGMQENHKA GWTVLEQDQD RITVHIEEEV QRRLQKLNKS
NVDNNTDLHL SSESQVKPVS PNKTDGITVN CKINAMTVLQ PSFLYIPILK AAAVLDGEKS
SREQEGTCCV NEPSSPVEPG YANRAHEGHL PQERATLTTV KTEKEQDVSP HKSSELEMLA
VSPVEGQGWR ESSDQGGEGP TDHSSHSEAV SRLDGSGTGQ SCGNEGPRRE ASDLLAHNTD
GDISHLELGK PLLETAPVCL SASLEADGRD VNKAGIQENA KFAIQCLPNF PLLDIAHDPS
GDTGTSEVSM ESLVGEGQEE VSEDNLECQD LGEDHCNSLG YKLAGKLSWL YKGASGHLQN
TERAIRRIIE HSYPQEDSWY KQICTLVKDL PVNHRINLKV TMKSDLGETA QVSESLGDLK
YIGESNAVPL PSTAWSPGNT VEISQDLQVF CQKLVDFPLC LQELQSLSPK DVLARFQHLI
PDIKCVSELL LGIYWLRVAN SQHPVPQPGC VLLFESMIHV LVVDCDHAGD EGALAVFHES
PFLQIKEIHV GFAGQHVRLQ GFTEDSILTI YTHSKQLTQN LCQTLLKVPS QTGAEGDHWS
HPLLQQDLAQ LSLDWSSYTP DCVLDGGLQL SSQFKRVLAD LVYFLHGNME EKPSLADMQL
LLYTSVKAEV NHPPRPDALS QFLLMESHLG LVQEDGVFHP APRSITMVSR RAHFEGLTLR
KLSDIRCVLV GDKDSSIRVD IVFKATSMSR AEIHNQGKNS TAALHSLSGY NLFPQSEIWK
LTFGCSTEAA FLINYLSTV
//
