ID A0A1Y1S5P4_9MICR Unreviewed; 681 AA.
AC A0A1Y1S5P4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN Name=KLP6 {ECO:0000313|EMBL:ORD93737.1};
GN ORFNames=ECANGB1_1594 {ECO:0000313|EMBL:ORD93737.1};
OS Enterospora canceri.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC Enterospora.
OX NCBI_TaxID=1081671 {ECO:0000313|EMBL:ORD93737.1, ECO:0000313|Proteomes:UP000192639};
RN [1] {ECO:0000313|EMBL:ORD93737.1, ECO:0000313|Proteomes:UP000192639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB1 {ECO:0000313|EMBL:ORD93737.1,
RC ECO:0000313|Proteomes:UP000192639};
RX PubMed=28345194; DOI=10.1111/1462-2920.13734;
RA Wiredu Boakye D., Jaroenlak P., Prachumwat A., Williams T.A., Bateman K.S.,
RA Itsathitphaisarn O., Sritunyalucksana K., Paszkiewicz K.H., Moore K.A.,
RA Stentiford G.D., Williams B.A.;
RT "Decay of the glycolytic pathway and adaptation to intranuclear parasitism
RT within Enterocytozoonidae microsporidia.";
RL Environ. Microbiol. 19:2077-2089(2017).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC ECO:0000256|RuleBase:RU000394}.
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:ORD93737.1}.
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DR EMBL; LWDP01000051; ORD93737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1S5P4; -.
DR VEuPathDB; MicrosporidiaDB:ECANGB1_1594; -.
DR Proteomes; UP000192639; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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; PTHR24115; KINESIN-RELATED; 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|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Microtubule {ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Reference proteome {ECO:0000313|Proteomes:UP000192639}.
FT DOMAIN 41..332
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT BINDING 110..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 681 AA; 77474 MW; 6954E8EE637411A3 CRC64;
MKQRSQLMKE HRMMNSGLIG RQSGRSRGSF VDERVVSNKT SIDVLVRIRP SQNANPEIAH
QGNSISVRNK LFYFNTIYTG ETNQEIFSSK IADLVDVFSQ GGNATVIAYG QTGSGKTHTM
FSNKEDVGLV YQTLASLGSR IHDIEMYEIY NENIYDLLNE YNKCEIGEGG IKGIRRRVVE
EKEEMREIVE EGMKYRTTKS TCLNSSSSRS HLILRISNTP NSNKSGVFTF VDLAGSERTS
VTNEVGESER RKESIEINKG LLALGNVINT LHSNQSALNQ SIYVPYRSSK LTRILKESLV
GNVRFITCVR KDVSNTFESS NSLTYAARMS SIKETFTRNR VDMCETEMLK REIEKYKKEV
CELREFIRKN MGDRRNIVEN NKVEEKTTEI STSENISNNH LRKPIKVEFV TEPTTAEFIQ
NKHIDPIATK PTPIRITIRD IDQYNGGLVA YTDRCELVRI TNGSTITPIC KTSLTALLVT
DELIYIGNRN MLRSIGTGGM RLIRVFSHKI SNIFPNQNNL IIKLSNRVIE YDINHNTESL
LYSGSNINQI VVSNETVYFI FDRLIEYRNK RDESIPIYTS TTRIIRVLLL NSTLISISST
IALIQNDRIV RVIESGGIVD GCIDSGRIFT LSKEYVDEYD SDMIKIRRYS ILPNKYSRIR
VCGTKMYLVG DQTDVVDLID L
//
