ID A0A0N0BJ62_9HYME Unreviewed; 1912 AA.
AC A0A0N0BJ62;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Kinesin-related protein 4 {ECO:0000313|EMBL:KOX78668.1};
GN ORFNames=WN51_07529 {ECO:0000313|EMBL:KOX78668.1};
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:KOX78668.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX78668.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX78668.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX78668.1};
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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; KQ435720; KOX78668.1; -; Genomic_DNA.
DR STRING; 166423.A0A0N0BJ62; -.
DR OrthoDB; 3035232at2759; -.
DR Proteomes; UP000053105; 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 Gene3D; 3.40.850.10; Kinesin motor domain; 2.
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:SF36; CENTROMERE-ASSOCIATED PROTEIN E; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF58100; Bacterial hemolysins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 2.
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:UP000053105}.
FT DOMAIN 4..187
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 207..265
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT COILED 708..742
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 901..1063
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1121..1155
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1202..1299
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1337..1612
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1653..1819
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1881..1908
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 88..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1912 AA; 224280 MW; C1B828B33386CCF2 CRC64;
MSSDVKVGIK LRPPTQQELD ENLSMQWIVK ENSIVSLEQK TSKWHDNGFH FDYNFDVNTK
NSIIFDSIVK SIVDATVNGF NGTVFCYGQF NSGKTYTMIG TSEDPGIIPL TVEYIFDAIS
NVIQREFLLR VSYLEICDEK INDLLDKNQI DLKLYKDNKG QIIVNCTEKI TNSSNDMLSI
MKKGIKNERI EENKNKHIGS HNIFQIMSKS QNIQDHIDYH NSKLTELLQS SLGGNALIAV
ICTVTPVILE ETYYTLSFAT EVKKVKTKPQ KDEIISNASL LCYAKRIKLE PIKNGNSSID
VEEVESNKVQ QKCHLLEEHI KLLKTQIISG RVKNGKKPVN NKSKRREIYY NPGMIKPYSP
IFYTQTCLPT IKEISPEKPH KKNIMQSIDI NQKTSDHEII DHEADYEIKE NDDIRNNHVK
CMGSNYFFLR SGTQDSLMQI SSSKVSPSTP KKVLRKCIVD LKTELDELRE FTTLEKQLIC
EEEHCYTHNM EEQTNKLFTC SDLKYDEIDK YSPNFAIQLK DEIKPDVQSI KLDIEKLEKT
ICLLTNENME MSNKLCVEKE LAKKTELNFQ KTINELYAQI SKITEEKIDL ENYTTVLNNQ
LESFRSKTSE NCDDEQLLIK YQNKIEALKT ENIDLSAIIA NQNKELENIK ESKALLYDHD
CIYKDKVTLL TEKNEYLIKE NNELSTDLID RIEENDILKE QCDILDNKMT LMRNMDSNES
DIEKLRSENN ILKARIAELG MRITILTDEN AKFSNNLLEH MENFDNSHNE KVHNSSIAPN
SPEKSNETIK KIVSNENYEE MSNKIIMLQK EITHLSRVNK KLSDLKLSSC SQCVHLKNVS
ESRRAFKLEA KILNHKLEDL QKKFDRKCAY TETLKLKANE ELNLSFTDPS LNASFVDKMN
VSFIEEKVHH LNNELQALKD DHDKLSISYK KKCDKLEKLH SADNVKKIER LQNNIDQVQN
DIDEIKKSST HFVSLYKMKK EKLLDKISNL TSNNEILQQT VADKETSISK ATEKVQILEN
ELSCMNKEIE QLSAMEKIMQ SEKMTLEIEL EELKLESEKK DNLITGLNKT IDDLNKCISL
LKHELDLITT QKNELTILIE KNECKYKDEL KLLRKQCDEL KEGKQKSIEI ERLRINELES
NIEKLKIDLE KQRNLHYEDT VKESMIKELK SLECISHSVD FSNKTANEIF NIFLQTIMLK
EEEIVKKMNE SFERDKQRLE DEKQQCADAE KRMMLWAKEL ETENEKLHID FKKTESLCMK
KQDEINQLKH SIKENNYEKE ILKEEIKTLE SDFNNLQNEF DKQCRVDIQQ KEETIIVAQK
REKEVREAFK CTEIELQSKM KCEKERYEKK IEELICTIEI YKTKNIELKN NIEGLEANEK
QLKNIIEANS LELRVKNQNI HKITLDFEEL REAYNELNCE MKEKTSRIEN ITLLLKNKCD
MLSEYKLKLE TIMPDYEILQ NQIKERKESI ERYKEEIEKL KMEKNKQIEE INDKLNLEEI
KNVGLNKQLN ELNSKNIVLK EELDNLKEKC EQLQQTNVKL ERKIRNSTSK VKVEAEMEEL
KDVNKRLQNN LEGASNRIIE LQESKNKTFK ELVNLKSQYE LLSQENVELK KMLSLCKSKQ
NTSYLLKEES KYDVLLQEKN KIALQLEGKK LLLTQKDKEI VEYVNQIKNL VTEKRELDNQ
LRECTNILHE RNEELSNLKD KMYMQQAENK LINELTRKLT SLEKENEEFK NQLQTQLENV
AIDTDYDQNT QTYQILRKKI QELELELVIK NGQISALETQ IQSENFPYLQ KCKELEEDML
TFRKKNADLN SEVRKLQRTL NDLNTWECDI CRRWRINRRN QACQTTLNNT SQLFTMNNEI
IKDDLKIAKL EKENALIKDV CRARCRKIKH LEDRVRELEE AQAMLYSDCN EL
//
