ID A0A151X6N1_9HYME Unreviewed; 849 AA.
AC A0A151X6N1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Kinesin-like protein KIF18A {ECO:0000313|EMBL:KYQ56051.1};
GN ORFNames=ALC60_05034 {ECO:0000313|EMBL:KYQ56051.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ56051.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ56051.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ56051.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ56051.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ982476; KYQ56051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151X6N1; -.
DR STRING; 64791.A0A151X6N1; -.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:UniProt.
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; cd01370; KISc_KIP3_like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF13; KINESIN-LIKE PROTEIN; 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 PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
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:UP000075809}.
FT DOMAIN 50..389
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 716..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 410..502
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 720..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 849 AA; 95554 MW; 9D0EF76E37682A11 CRC64;
MVFNKKDLGK AFSPSKAKKV GLKRKLSASG SVKPSTSSST IKTEDISEIS IKVIVRVRPP
NERELQDNSR TIIEVVDDKM LIFDPKEQET PFFFHNVAQK GRDMLKKQNK QLQFIFDRVF
DSTSTNTNVF EGSTKRLINS LLDGYNCSVF AYGATGAGKT HTMLGNREDP GITYHTVAEL
FSEIENQSKH REFALGVSYL EIYNENVQDL LHKSGQLHLR EDGRCGVVVA GLEPIAIQNA
EELLSLLAEG NKNRTQHPTD ANKESSRSHA VFQVYIKIIN KLDSQVQRVK LSMIDLAGSE
RASATGCKGV RFKEGANINK SLLALGNCIN NLADGIKYIP YRDSKLTRLL KDSLGGNCHT
VMIANIAPGS ITYEDTHNTL RYANRAKKIK SNAKKNVSCE THVAGYIKIV EEQKKEIDIL
KSKLAAYENG TPQPVIENKP NVDMLDAYNK LIKLHEKKKD LIEKILSLES ADKILSCRIL
YKKDADERLH NLTAASDILS QEEQNASGKL RINKSLQHFQ RQREALKAQT EETWQELCSI
ETEIQETKAK PLDENLQSKL SLEIFKIEKC WISSMQQHMK KLSSVLQSER QSINTITKSM
SNILQNYYNM VKGFGTMTEK MQQEFKELIK LLEGFRNIKW SDTDEANKVD DFNMFKCLST
GGIDPLNNPM PAIAEMDDEG QNNTNILNCT FDAATGENNI DSNICNLSNG SNLSNGSHEN
KFLSKDESMQ ASPRERTVAK NIIRKRALSD KNSENSSTPS KQTKKLITNN KVQNTGRDKE
NKQQRPIQMS AKSVAILNKL KSDTTTLSSL SRHNNTEEKT DVAFKAIRNK ERRGLMTTHP
YQKPTIGKK
//
