ID A0A022RFU4_ERYGU Unreviewed; 1010 AA.
AC A0A022RFU4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=MIMGU_mgv1a000707mg {ECO:0000313|EMBL:EYU38653.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU38653.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU38653.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000256|ARBA:ARBA00004186}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-5/BimC subfamily.
CC {ECO:0000256|ARBA:ARBA00034704}.
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DR EMBL; KI630480; EYU38653.1; -; Genomic_DNA.
DR RefSeq; XP_012836131.1; XM_012980677.1.
DR AlphaFoldDB; A0A022RFU4; -.
DR STRING; 4155.A0A022RFU4; -.
DR GeneID; 105956779; -.
DR KEGG; egt:105956779; -.
DR eggNOG; KOG0243; Eukaryota.
DR OMA; HCRMEVL; -.
DR OrthoDB; 536293at2759; -.
DR PhylomeDB; A0A022RFU4; -.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0051231; P:spindle elongation; IBA:GO_Central.
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|PROSITE-ProRule:PRU00283};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000030748}.
FT DOMAIN 12..359
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT BINDING 98..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1010 AA; 113583 MW; CB13612E3F39AE03 CRC64;
MSSRHEREKG VNVQVLLRCR PFSDDELRNN APQVLTCNEY QREVAVSQNI AGKHIDRVFV
FDKVFGPNAQ QKDLYEQAVI PIVNEVLEGF NCTIFAYGQT GTGKTYTMEG ECKKSKSGPN
GELPSEAGVI PRSVKQIFDT LEGQNAEYSV KVTFLELYNE EITDLLAPED ISKVAMEDKQ
KKQLPLMEDG KGGVLVRGLE EEIVTSASEI FTLLERGSAK RRTAETLLNK QSSRSHSLFS
ITIHIKESTP EGEELIKCGK LNLVDLAGSE NISRSGAREG RAREAGEINK SLLTLGRVIN
ALVEHLGHIP YRDSKLTRLL RDSLGGRTKT CIIATVSPAV HCLEETLSTL DYAHRAKNIK
NKPEVNQKMM KSTLIKDLYG EIERLKGEVY AAREKNGVYI PKERYYQEES ERKAMADQIE
QMGMTTENHL KQIEELQGKY DSQVRECCDL SNKLDATQKD LNVTSKLLAN TEDNLKRCQY
SLKERDFIIS EQKKAENALA HQACILRADL EKSQKDNTSL FLKLAREDEL NADNRSTVNS
FQADLAQQLG TLCSSLAASV TQQGKHLACV ENLCNSFIQV HDKVSVELKQ KVSSSRALYV
SHFESVQNVV RLHKAGANAD LEELSALASA NSQSIEEFLA AEAVEAKAIF DDLQETLSSH
QGEMAHLARE LRQRFLVSIE HLTTTSDSVH GFLDELLKES KKLECHTTEV DEIQTKCIAE
LRNAYEEQSR SEAEKLIADM TSLVSDCMRR QKEMVDAKLD DMMDSATGNK MFLDGHLLTI
DGITTDLKRK WQDCFVKAET SFKDNADFSA AKHCRMELLL QKCVNTSDTA LKRWQRTQES
LNDMGNQHAS AITSHVRDMW YNNEQHDAEI GSALVIVEDD IQTNSEATIQ CLNGLSEQEK
LSVSKILENS RNHSETLENL LKDHSQQSAC IEQHAADTFR QKYMDYEPTG STPVRCEADI
PSKVTIESLR AMPTEALEEE FRENNSFDSF HVKEVKPTLI PRAPFSQINQ
//
