ID A0A251RYL6_HELAN Unreviewed; 2040 AA.
AC A0A251RYL6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Plus-end-directed kinesin ATPase {ECO:0000313|EMBL:KAF5758637.1};
DE EC=5.6.1.3 {ECO:0000313|EMBL:KAF5758637.1};
DE SubName: Full=Putative kinesin motor domain-containing protein {ECO:0000313|EMBL:OTF90946.1};
GN ORFNames=HannXRQ_Chr16g0505211 {ECO:0000313|EMBL:OTF90946.1},
GN HanXRQr2_Chr16g0731491 {ECO:0000313|EMBL:KAF5758637.1};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232 {ECO:0000313|EMBL:OTF90946.1, ECO:0000313|Proteomes:UP000215914};
RN [1] {ECO:0000313|EMBL:KAF5758637.1, ECO:0000313|Proteomes:UP000215914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5758637.1};
RX PubMed=28538728; DOI=10.1038/nature22380;
RA Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA Vincourt P., Rieseberg L.H., Langlade N.B.;
RT "The sunflower genome provides insights into oil metabolism, flowering and
RT Asterid evolution.";
RL Nature 546:148-152(2017).
RN [2] {ECO:0000313|EMBL:OTF90946.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaves {ECO:0000313|EMBL:OTF90946.1};
RA Langlade N., Munos S.;
RT "Sunflower complete genome.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF5758637.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5758637.1};
RA Gouzy J., Langlade N., Munos S.;
RT "Helianthus annuus Genome sequencing and assembly Release 2.";
RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-12 subfamily.
CC {ECO:0000256|ARBA:ARBA00034488}.
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DR EMBL; MNCJ02000331; KAF5758637.1; -; Genomic_DNA.
DR EMBL; CM007905; OTF90946.1; -; Genomic_DNA.
DR STRING; 4232.A0A251RYL6; -.
DR EnsemblPlants; mRNA:HanXRQr2_Chr16g0731491; mRNA:HanXRQr2_Chr16g0731491; HanXRQr2_Chr16g0731491.
DR Gramene; mRNA:HanXRQr2_Chr16g0731491; mRNA:HanXRQr2_Chr16g0731491; HanXRQr2_Chr16g0731491.
DR InParanoid; A0A251RYL6; -.
DR OMA; YERHENI; -.
DR OrthoDB; 380786at2759; -.
DR Proteomes; UP000215914; Chromosome 16.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; IPR044986; KIF15/KIN-12.
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; PTHR37739; KINESIN-LIKE PROTEIN KIN-12D; 1.
DR PANTHER; PTHR37739:SF8; KINESIN-LIKE PROTEIN KIN-12D; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Isomerase {ECO:0000313|EMBL:KAF5758637.1};
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:UP000215914}.
FT DOMAIN 213..550
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 80..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 557..584
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 626..660
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 742..808
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 914..941
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1229..1270
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1331..1363
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1421..1462
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1573..1628
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1757..1823
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1895..2029
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 294..301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 2040 AA; 235201 MW; 4A269CE1A9F98208 CRC64;
MSRDCSKLSR RNSGKNLKFE ETENMPVNIS SIREPLVNRM SIDYQSRAPL NTIQDPVQNP
SKFDYELGLK SSKVYRTPTK PKVKYTESAM KTPEKQGGLG RNRYGWGQDS RDEGRIGNGN
TPKACKITRA ASCFTEGNST HTTPTKSVGK PPSVGLVYGG SSRPPVNGGV RTGNFTALSK
GIPVAFNACA PVNTVDVPHF DLREDPSFWM DHNVQVLIRI RPLNGMEISS QGYSRCLKQE
SAQSLTWVAQ PEARFTFDHV ACETIDQEAL FKTVGQPMVE NCLSGYNSCM FAYGQTGSGK
THTMLGEVND LEIKPSPNRG MTPRIFEFLF ARIIAEEESR KDERLEYNCK CSFLEIYNEQ
ITDLLDPSST NLQLREDVKK GVYVENLTEY EVHCVGDILK LLSQGSANRR VAATNMNRES
SRSHSVFTCV IESRWEKDST SNLRFARLNL VDLAGSERQK TSGAEGERLK EAANINKSLS
TLGHVIMVLV DGANSRTRHV PYRDSRLTFL LQDSLGGNSK TMIIANVSPS ISSATETLNT
LKFAQRAKLI QNNAVINEDA SGDVVALQHQ IRLLKEELAI LKRQNTSRSL TFSSKDENCS
NASSYGDDDK VLRVSCNQLK SLESSLNGAL RREKSTENCI KQLEAEIEQL NCLVHQREEE
NRCTKMMLKF REDKIQKMES VFSGMISADS YLIEENNTLT EEIKILRAKV DKNPEVTRFA
VENIRLLEQL KRFQDFYKEG EREMLLAEVS ELRDQLALLL DEHNHMNLST EKEAAEDKKR
IDSLQSELLK SQEELEKCRD NLNSCLEKNA KLCRDISDLN ALLERQKSSL NDQDGDIEVS
KESVSKCSSI EDQSSHTVQE KEEIFRKYPE EIVSLHLELE FLKSILEEER LIHRETGEKV
SSITKAYETS ILKQNETRQE LTLLREKCEE KDRNFDGLSE EFDFLTKKME EVLTVGHNAL
DDASNFIGHG KETRAFENLQ TIARKISEKE LRIDELNTCL EDAKVRGKEM ETMLRSLRGA
ILVMSEAHQK DCVRKDEEID RLLSELNEKN SIIILMEEQR KLYEVELMDA KTNAAQQDVE
SCCYLDKFAE IQHHIKEANL MINKLVSENE AMKMEISHQN EVINDKDEKL RCSEAAKKID
LENEKVHMSN VFEKIKEELI ISYVDMQVKD WILLEKDAEV GLLLEEKELY EVQLMDTMKN
ATQQALESCC YLNKFEETQH QIKEADYMIN KLVNENEATK IEINELKDSN SVIEKQLEEK
DEELRCLEEK LVTDLSAKDI ELFMMSSILE QVASKYNDFE KDKVRMSKVF ERFKEEAIIS
YVDLHFENFI LLEKYTENND AELRLHKEEN EKLVKVIKSQ KDEVEGFDAC FETLEYERHE
NIVKSVVLEA YLTEIFEDAL NAKRSAEEQL AKTDFDRNNL IESLKRDLES VTCERDDLHA
ELRLHKEENE KLVKIIKNHK DEVEGFDACF ETLEYERHEN IVKSVVLEAH LTENIKDALN
AKWSAEEQLA KTAFDRNNLI ESLKRDLESV TCERDDLHAE FLKAKQFYEV QLLDAMKNTT
EQAVESCCYL DKFEETQRKI KEADYMINKL VNENEAMKIE INELKYSYSV LEKQLNEKHE
DLRSLEERLV TDLSAKDMEL FMMSSKLEHV ASENYDLEKD KVNMSNVFDK FKEEAIISYV
EKYTETCILQ NEVDMRDEDL KLQLENKGAE IRLHKEENEK LVKIIENQKD EVEGFDAFFE
SLEYERHENI VKSVVIEAQL TENIEDANNL IESLKRDLEN VTRERDDLHA EFLNAKQLYE
TELKEADLTI NKLVTENEAM ETRIIHLNEV INAKEIELFI VLSRLEQVAS DNNDLEVEKV
NVYSGFEKFK EEITISYLDL QMAVETRKYY DDEKLKLYEK SVEELESTVN LLEKQVDLVK
GDAESQRLKK EELEQEVQEI HQQKELLITE NETFKTENAD YKIKVIELED EVNKLLIQQD
LQQHILPLAK ITEENNMLKA RNDENNDTLR KAEALVALVK EDLANYRASK SSLTAHTPAE
//
