ID I2H1S5_TETBL Unreviewed; 676 AA.
AC I2H1S5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN Name=TBLA0C05310 {ECO:0000313|EMBL:CCH60327.1};
GN ORFNames=TBLA_0C05310 {ECO:0000313|EMBL:CCH60327.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH60327.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH60327.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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}.
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DR EMBL; HE806318; CCH60327.1; -; Genomic_DNA.
DR RefSeq; XP_004179846.1; XM_004179798.1.
DR AlphaFoldDB; I2H1S5; -.
DR STRING; 1071380.I2H1S5; -.
DR GeneID; 14495307; -.
DR KEGG; tbl:TBLA_0C05310; -.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_001485_12_4_1; -.
DR InParanoid; I2H1S5; -.
DR OrthoDB; 5476186at2759; -.
DR Proteomes; UP000002866; Chromosome 3.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR PANTHER; PTHR47972:SF28; PROTEIN CLARET SEGREGATIONAL; 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 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:UP000002866}.
FT DOMAIN 334..669
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT COILED 50..87
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 241..299
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 421..428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 676 AA; 77659 MW; FF1664D9EE7BD683 CRC64;
MENRINIKIN EIISSGKISH KRNEFLSNES QVKKQKYDSS INRSGDISLT KRQIDERKQL
NDTYEEMQSK KKLLEEERAE LEAILNEKRV FWDERSIGND SLITDYRNMT KELSKLPQIQ
ATRISVLQND FKSEKHVLCK QYKDKTEALR LKYEHILNKM DYEGKIKLEN QLNMSHNNIK
NVEKEIKAIA LKYKDDLETI NLQFNAWKND FNNNFHELLD DNIKKKDTIE NLQKDISEIC
RAKINTRAVH LQESLQNLEQ VTCNLKEATL KYPNIQDHID NLQNSIKNES ILIDSYKDKI
IRQQNLIPLH KADAIEQDTV RLVLHNQLQD LRGNFRVYCR VRPPLKGIEP LDTSHILINA
FNAELGSQSI EVEKNCNLTP IKYSFDKVFS QTDTNQEIFK EVSELIQSSL DGFNVCIFAY
GQTGSGKTFT MLNPKDGIIP STAKHIFDWI DNSAKNGWKY NVTCEFLEIY NDEIYDLLRS
DDNKSNSSNG PRHKIHHDDA SKTTVVENLE TITLTSKESV DAVLKNAMKL RATASTSSNE
RSSRSHSIFI IKIHGINEGL GEERNGLLNL IDLAGSERLS VSKVQSERIK ETQHINKSLS
FLGNVMNSLG SPDATTRHIS FRDSKLTYLL QYSLTGNSKT LMVVNISSSS DHINETIKSL
NFAKKVNSTK IIKRKS
//
