ID A0A3Q3MRX2_9TELE Unreviewed; 1278 AA.
AC A0A3Q3MRX2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Kinesin family member 16Ba {ECO:0000313|Ensembl:ENSMAMP00000027647.2};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000027647.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000027647.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; A0A3Q3MRX2; -.
DR STRING; 205130.ENSMAMP00000027647; -.
DR Ensembl; ENSMAMT00000028361.2; ENSMAMP00000027647.2; ENSMAMG00000018548.2.
DR GeneTree; ENSGT00940000162838; -.
DR Proteomes; UP000261640; 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:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd22732; FHA_KIF16B; 1.
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 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}; Reference proteome {ECO:0000313|Proteomes:UP000261640}.
FT DOMAIN 3..358
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1144..1259
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1007..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 373..421
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 599..806
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 834..861
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1034..1058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1088
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1107
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 1278 AA; 147274 MW; D77C9047627EEB55 CRC64;
MASVRVAVRV RPMNRREKDL TSKNIIKMDG TKTSITNLKI PDGVSGDSMR DRTKTFTYDF
SYDSSNCQSS TFISQEEIFK DLGSDVLKAA FEGYNACIFA YGQTGSGKSY TMMGTPGDAG
LIPRICEGLF SRVSEATRRD EASFRTEVSY LEIYNERVRD LLRRKSTQTY NLRVREHPKD
GPYVEDLSKH LVQNYNDVEE LMEAGNINRT TASTSMNDVS SRSHAIFTVN FTQAKFDAEM
PIETVSKIHL VDLAGSERAD ATGATGVRLK EGGNINKSLV TLGNVISALA DMTQDGVNTN
LKKKSVFVPY RDSVLTWLLK DSLGGNSKTI MIATVSPADV NYAETLSTLR YANRAKNIIN
KPTINEDANV RLIRELRAEI ARLKALLVQG NQIALLDSPT ALSMEEKLHQ NEARVLELTK
EWTNKWNETQ NILKEETLAL RKEGIGVVLD SELPHLIGID DDLLSTGIIL YHLKEGRTYV
GREDASTEQD IILHGLDLES EHCMFENQNG TVTLVPLGGA QCSVNGVQVT EPSQLNQGAV
ILLGRTNMFR FNHPKEAAKL REKRKSGLLP TFSLSMTDLS KSCENLSTVM LYNPGLEFER
QQREELEKLE LKRRLIKEME AKQQSEKAEL ERLQQEVESQ RKESEEVQQR ILHQEESLRR
RSQDIESRLR DFLVEKERFE EERRLEIQGM DLWRQRRRQQ QEGVAEEEDE EQRRQQEATE
HTEIYRELER LKREREEQKI RLETERRRLE EQEREQLSLV GRLEEQLREK QEAATTLLTP
EDICRLEEER RALAEIREAL LRAKEAGERP GGEDPSEEAR FAQARYIDFK VAQVKELGQL
EEGLREQRER LEKEAAADRN TLLLLAHSLK ERQQQLKETQ ERGAQDATAV CQEDQLVKQA
EHRLQFKERQ LASLADRLLP SLAEEKQRAV EMLERSGGGY NGNCDSPPAL DNMLYQVEKE
LEDKEEKINL HRHSAHQLQQ LQETYEFTAN VARQEEKVRQ KEKEILESKE KQQREAMEQA
VSRLERRHSA LRRSISLEPN TEEQRPNSSV QRNLRTGADL EQQRVEREIQ KLRQRISEGE
ENRTQSISSD EKTGHSSSPV SHVQSLNPLL PLSDDRINAY IEEEVQRRLR RMNLLNGSSS
MDLSLSCESL RDDEKLQIDN PRRQKYEITV MDETWTVFRR YSRFREMHKS LKLKYPELAA
LEFPPKKLFG NRDERMVSER RSHLERYLRS LFRVMLSSSS SPLRPDTDGS FHLSKHGICE
FSSFFKKGVF EHSSHGTC
//
