ID A0A0E0JBV3_ORYNI Unreviewed; 2790 AA.
AC A0A0E0JBV3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
OS Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA12G16160.1};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA12G16160.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA12G16160.1};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA12G16160.1}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA12G16160.1};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 STRING; 4536.A0A0E0JBV3; -.
DR EnsemblPlants; ONIVA12G16160.1; ONIVA12G16160.1; ONIVA12G16160.
DR Gramene; ONIVA12G16160.1; ONIVA12G16160.1; ONIVA12G16160.
DR eggNOG; ENOG502QR1R; Eukaryota.
DR HOGENOM; CLU_000399_0_0_1; -.
DR OMA; MQSVEMD; -.
DR Proteomes; UP000006591; Unassembled WGS sequence.
DR GO; GO:0032153; C:cell division site; IEA:EnsemblPlants.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0009524; C:phragmoplast; IEA:EnsemblPlants.
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:0000911; P:cytokinesis by cell plate formation; IEA:EnsemblPlants.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:EnsemblPlants.
DR GO; GO:0080175; P:phragmoplast microtubule organization; IEA:EnsemblPlants.
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 Microtubule {ECO:0000256|ARBA:ARBA00022701};
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:UP000006591}.
FT DOMAIN 210..554
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2339..2360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2764..2790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 561..588
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 655..682
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 836..863
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 919..999
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1043..1137
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1310..1351
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1437..1503
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1724..1751
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1906..1933
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2104..2334
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2362..2428
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2547..2609
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2641..2750
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2339..2353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 291..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 2790 AA; 316689 MW; 94F0B0DC41FF4BE3 CRC64;
MVRDLAAVRR TPARASTSSS ASEVGNDENA PVDASDAAVV EPEAAAARPP LLAIQPPQSG
LKRKPESPAP TPSKLPFRTP EKAAARSRFG WVPPRGEEQP PPRVGGTPYS AVSTPGRHRG
KSSAAAASEG GGGSTQSTPT KSVTKPAYNI GMSASRPPMS GGQRGAGLGL GFSMAARGTP
MSFAPVTVVN TAEVPHFELR EDPSFWMENN VQVVIRVRPL NNTERNLHNY NRCLKQESAQ
SITWIGQPES RFTFDHVACE AVNQEVLFRV AGLPMVENCM AGYNSCIFAY GQTGSGKTYT
MLGEISELEV RPSQDRGMTP RIFEFLFARI RAEEESRRDE KLKYNCKCSF LEIYNEQITD
LLDPSSTNLP LREDIRNGVY VENLTELEVG CVSDIIKLLM QGSANRKVAA TNMNRESSRS
HSVFTCIIES RWEKDSASNL RFARLNLVDL AGSERHPPEH RQRTSGAEGE RLKEAANINK
SLSTLGLVIM SLVDQAHGKQ RHVPYRDSRL TFLLQDSLGG NSKTMIIANV SPSVWYSASE
TLSTLKFAQR ARLIQNNAVV NEDASGDVLA LQRQIRLLKE ELAVLKRQRA PRSLSFTSDI
FERSGVDVDD GTESMNMDEE NDNDAHDRRS LQDLRISNKQ LRLLEETLAG AFRRESVAEA
TVKQLEAEIE QLNRMVNFWW QETTFVIFLE GIINGLLVYE RENDTRSAKM TLKFREDKIH
QMEALVRDKL PAESYLLEEN NTLLKEIDLL RAKIDKNPEV TRFALENIRL SNKLKSYNQF
CNEGEREHLL NEVSILRNQV LQILERRAEA EQPNNFPTNF ELKRTSQELE TCRGELQACL
EANKKLAREI ADLQNELSNI HSSNREGHPN VVEKFSSALN QYDSHAPEKK DQCFQEGFMI
NTDDILNLQL ELDIIKTILA EERTTRAEVE KRITCLDDEL KAANIHILQT CRQSETMQRE
LSDARSVIEA LESQQIMLIN ELDELKESNQ QSLEHLKKRD LEISRLNNEL DVHCRQEFLA
MEEPKVQLLK CFENDDSPLQ TKLKRMQASL EKARKLNTRY QRDQSSHSSA QQEMDEVSRQ
VEVETAEVIM CLQEELISLQ QQLDASSKNE LLANQRIDEA RLEREQLNDR LLEVMKENEC
FSALIEEKDK KIGMLTNDWD KLASDIGNFL LDGNAALDEA SDQVAFISES ISQRKWIEDQ
VQKMCRGISQ RDELLKELQS RLKEADDIRC DLDLKLRSLR GAMQAINDTH QQEKNDQENA
MSVLRSQESN ERYVNQQQLQ ELQRIQLLLD ESIESFVQKE VIEQSYISLQ RAMEEVIHHL
ESQLDQSKRD LTQLLSETQD KEQALERLKN EENGVLLTVL SDVLKAKGVI HEFETGFNAI
QSSFSVDPEE VVCQNSDLNL EDRVGCDPTG AFEAGEKHNG DVLCKLSKEM ECVVYTMQML
QSQMVKLLQE KENAKEYHFQ SQRTIKDVSA KVLQLKSEII DKEKGYEARL KELEIKMQEK
EKDTAESFIS WNKEREALEL EVSEAKSLAI QKSFEASTLI SKFEEAQATI SDADTTVNAL
VEANEKAKLQ IQNFKENEAL FLSEKERLLT EISSLKMLLD VKDQTYENLL LEKLEFVSSD
VEWMKSKLQQ FAELARTWLE ENWLEIIGKD CAVSVLHLCH MGILLERITG LSAENGFLQR
GLCESNSLIS KLREHNDRAK NELEMCSVLK GKLLLDINHN FSRIAKKEQE ATELNSRLDA
FEKKILHLQA QEEAMLARSN SMYNELSILV EEIDATNKSA LATESKEKEE LRHQLDEALL
CNAMLKDIIQ EDVDLPQVNN YMKGCSEFEL CNRLADYHNE LVTTNIIAKD IESFVLSSEL
VQHKAQLQKQ ELMFIDALDG LTTEATLSRV DKDLGSAVIF SLLDDSNKIM IDFDNLKQNK
DELMENLHVL SEENLNLRSV VGSLESSIES LQTELDGKTK ALMELQYSHT TILEEFKLKS
KATELGVSRE NDLRSENNLL KHEYLDIVRK EQMMAELVAN LDSEKLFVTI QGRLEQVADQ
VQMYTSDQLN MVTKVSNEID FIQMSIEGLI THNGFLQSEL IRKDELAKGL SFDLSLLQES
ASVAKDQADE LIQLTEAIES LEQELDSKSN ELVDAVSGRQ LLEAQILKSN QKVSALEEQL
ASKINELKEV SVEKDELMSK LNHIEGISYT MEDELADKGK AIERLEEELI ELRSLLDART
CFLQNLQNDF SKLLDEKKYC ETQVLILNEK LEMAQALAEE SEAIATEAKQ MAEERKTHAE
EKDEEVKLLE RSIEELETTV CALENKVDII KEEAERQRMH REEIELELQK VRQQMLAVPS
SGQATSSLEG GMGDFTDSSR HSREIKNELL AAQENIRILQ KDVAEKETEI AQCKAHISEL
NIHAEAAARE YKQKFMELEA MAQQVKSDNT SANACSTRPE KISLKPRGSG SPFKCIGLGF
VQQMNSEKDE ELSAAKQRIM ELEGIAASRQ REIFMLNARL ATTESMTHDV IRDMLGVKMN
MATWAALVDN QQQMDTQESA VTQAHESKEQ SDELMKLRSQ LDELIEERQS WLDEINQRQS
ELGAARITIE KLRQKEHFMV AEIELLKAEN ANGKAIIFNL EDEVKKLTRQ QNLQLRINHH
NEELSAKLQK LGAVVARTKE ELARYRVSDG KDPYEQMEEE ELLRNRLEES EQDRSKLAEN
LSSLCATVLK IAGVRNHESD ASLLKALEAL NQIQLRIASM EAGVEDLKLK CKLLHEKARL
SELRSESSSL SSGRSRSPSV CRSPSISSFR
//
