GenomeNet

Database: UniProt
Entry: A0A0C2JLL8_THEKT
LinkDB: A0A0C2JLL8_THEKT
Original site: A0A0C2JLL8_THEKT 
ID   A0A0C2JLL8_THEKT        Unreviewed;      1030 AA.
AC   A0A0C2JLL8;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Kinesin-like protein KIF11 {ECO:0000313|EMBL:KII70283.1};
GN   ORFNames=RF11_10713 {ECO:0000313|EMBL:KII70283.1};
OS   Thelohanellus kitauei (Myxosporean).
OC   Eukaryota; Metazoa; Cnidaria; Myxozoa; Myxosporea; Bivalvulida;
OC   Platysporina; Myxobolidae; Thelohanellus.
OX   NCBI_TaxID=669202 {ECO:0000313|EMBL:KII70283.1, ECO:0000313|Proteomes:UP000031668};
RN   [1] {ECO:0000313|EMBL:KII70283.1, ECO:0000313|Proteomes:UP000031668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wuqing {ECO:0000313|EMBL:KII70283.1};
RX   PubMed=25381665; DOI=10.1093/gbe/evu247;
RA   Yang Y., Xiong J., Zhou Z., Huo F., Miao W., Ran C., Liu Y., Zhang J.,
RA   Feng J., Wang M., Wang M., Wang L., Yao B.;
RT   "The genome of the myxosporean Thelohanellus kitauei shows adaptations to
RT   nutrient acquisition within its fish host.";
RL   Genome Biol. Evol. 6:3182-3198(2014).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIN-5/BimC subfamily.
CC       {ECO:0000256|ARBA:ARBA00034704}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KII70283.1}.
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DR   EMBL; JWZT01002103; KII70283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2JLL8; -.
DR   EnsemblMetazoa; KII70283; KII70283; RF11_10713.
DR   Proteomes; UP000031668; 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:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0007051; P:spindle organization; IEA:UniProt.
DR   CDD; cd01364; KISc_BimC_Eg5; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR047149; KIF11-like.
DR   InterPro; IPR047241; KIF11-like_kin_motor_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   PANTHER; PTHR47970; KINESIN-LIKE PROTEIN KIF11; 1.
DR   PANTHER; PTHR47970:SF12; KINESIN-LIKE PROTEIN KIF11; 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; 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}; Coiled coil {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:UP000031668}.
FT   DOMAIN          23..368
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          383..447
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          501..538
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         112..119
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1030 AA;  117404 MW;  B06B2DA9E45BB8D6 CRC64;
     MLPGGNFSAM DSKLKSQKKK GQNITVVVRC RPRNDLEKRM NSPNCVDINT EKRQVSLSGD
     QSVIGHWGHN RSFVFDRVFD YRSKQIEVYK SVVVPLLEEV IQGYSCTIFA YGQTGTGKTY
     TMEGARCSER IHYSWEQDPQ SGIIPRSIHQ LFEMLERKQD IQEFSVRVSF LEIYNEELFD
     LLGQPFESQK LRIFEDTSRK GSVFVQGLEE VIVHNKSEVY SILEKGGARR QTAATILNAH
     SSRSHTVFSI TVNMKDSNIQ GEDIIKTGRL YLVDLAGSEN IGRSGAIERR AREAGTINQS
     LLTLGRVIFA LVEKTKHVPY RESKLTRLLQ DSLGGRTKTV IIATISPSAY NIEETVSTLE
     YAQRAKHIKN RPEVNQLNKK GLIKEYSETI EKLNKDLMAA REKNGIFLSE DTFGNMQNTL
     ASQKETIIEL EDQIAGVREQ LERITHMFEE NQASLETNRK ELSRAKQWLA WVKGELSHAH
     ESIKHQGCVI KHKDVVGQEL VKQQNELYND ANELLQHVKE ELNQIQLLNS KISMIRQKDR
     DNQMSIDKYT KYLEDNLEIF VGSIEKIKKC NDLNGFQFKE HLNNFVSQAK QKLDGYLEMY
     NEESKKILNQ VGETQDRTNQ NYESFSNGLQ SAKTRLKESR AAFTCDIERL TNNLDKANTD
     TGSFCESFTT KIGGFSEHIY GNINKSTNDL GTFHSDITGR IEAIKQFISG YRVDNHLDDI
     KASFGHFQKS IEPWKHQLTK ELLTVIDTFF DKLSFQLVTQ MNIIDKSLNS ISSEHELVRK
     TTSELCSHLQ SHFDEMKSAI SGDCEGSKTM ITQFFGELEA FYSAYYQDII QSQNKVRQII
     ELIKANRDSQ SAQIDEDLSL LTNQMGKQLV EAQKCFSFVH KQALSLKSAT AECIGSNLEL
     SSETIGTLES LFFKFQSDVE ELRSNSLEIF NDIVEMYRKT ISDRSFESKP AGDTPKVSNV
     KIRNVPAPRS IDEIAQNVRL ESDIINTPTP SRKRTALNKL NTIDEDLPIP SFCIDPETSK
     SVIEKENQNE
//
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