GenomeNet

Database: UniProt
Entry: T1KB01_TETUR
LinkDB: T1KB01_TETUR
Original site: T1KB01_TETUR 
ID   T1KB01_TETUR            Unreviewed;      1619 AA.
AC   T1KB01;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN   Name=107362415 {ECO:0000313|EnsemblMetazoa:tetur08g02360.1};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur08g02360.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur08g02360.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
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; CAEY01001943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015784966.1; XM_015929480.1.
DR   STRING; 32264.T1KB01; -.
DR   EnsemblMetazoa; tetur08g02360.1; tetur08g02360.1; tetur08g02360.
DR   GeneID; 107362415; -.
DR   KEGG; tut:107362415; -.
DR   eggNOG; KOG0244; Eukaryota.
DR   HOGENOM; CLU_001485_4_5_1; -.
DR   OMA; GECTPIG; -.
DR   OrthoDB; 1131899at2759; -.
DR   Proteomes; UP000015104; Unassembled WGS sequence.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IEA:UniProt.
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   CDD; cd01372; KISc_KIF4; 1.
DR   CDD; cd22248; Rcc_KIF21; 1.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR   PANTHER; PTHR47969:SF15; KINESIN-LIKE PROTEIN KIN-4A; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   DOMAIN          6..363
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REPEAT          1293..1332
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          1531..1572
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REGION          564..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          773..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          837..861
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1043..1125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1222..1243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          371..498
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          895..949
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        564..592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        845..859
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1043..1080
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1097..1115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         85..92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1619 AA;  180822 MW;  4555DDDB7C8CE71B CRC64;
     MEAETSVKVC VRIRPQVPKE IIEMCKVCTN VTPNEPQVWL GSTKAFTFDH VFNMDSKQEE
     IYTNCVYSLI EGCLDGYNAT VLAYGQTGSG KTFTMGTGFD VRVEKSENKG IIPRAVDHLF
     RGIREKQQKA KEMGIPPPEF KVNVQFLELY NEHIIDLLAD DSGTNINQIK IHEDASGGIY
     TVNTCARSVS SVESTLDCLK KGSLSRTTAS TNMNSQSSRS HAIFTLYIKQ QRIVSLDDHL
     KLGVSSDGTM PSHEFETLTA KFHFVDLAGS ERLKRTGATG DRAKEAVSIN AGLLALGNVI
     SALGDKRKQG CHVPYRDSKL TRLLQDSLGG NSQTLMIACI SPSDRDFMET LNTLRYANRA
     KNIKNKVVAN QDKASETINL LRKEIQQLQL ELMEYKQGKR IIGEDGNEQI NDMYHENTML
     QKEIGNLKLR VKALQDTNER LIARNTELTL EKATGGWITN DGEPSDLKDM VQNYLREIEE
     LRTKLIEMEE TCSQLRKQAQ RSTMSRMSMS PFSSTAVAVV GNYDVAEETE TCDTILKEAK
     KEIAKQKKIS RNLSKSYKDI DTICETNGNR NIDGDIERTT SGGTNPSPIN GESDSGWGGG
     GTDGATDGGT DGGEDDEGGN GASSSPASDE SDASDEESDT EFQLAELSNE ISVKEKLIIE
     LEKSQRKMMS MKHHYEEKLL QLQAKINEIE SERDRVLAKL TNVGSGGNDK AKKVRDDYQQ
     KLNALQTEMK KLKMAEKEHA TAMKSQSKYE LQLRSLKNEV SEMKKQKVGL LKKMKEEAQR
     HKEAESRQNK KLSQLAKQER LKDVKIRNLE TEANRVKSLL KRKEDQVMAM KKMIKPMSDK
     VAGRVKSSSR MRKGSEKSSV VRSPKVIKQK WQSIEQDINK VMIYKKNIAI HELQMERFLA
     QRRRLVRERE DTKAKLSESR RAGKSEDIIA ELLEELGNIE DNILYLNQNI DECQSTIMQL
     EETAGDTPTL EMNTLLADVG LEEMKYLFEK VLTMAINQSL LAVQKEEEAH EYEMKYNQLE
     DSSVAQENLL NLLLDTTFIE DTKRPPTANS NNNNNNNNIN NNAFEAPING NSNNETIDKL
     GTSNTHEKYH NGDTVGPLMG PSSSSSGNNV NENGSGRPEK ARRLTKTPQE LLFEQSRNSI
     NMADDPMTQS LVNPISTLAK NNSDLHRVPS APSLKDICKP SSRIESPILK RKTFEKNQLL
     ETRRLIKPSC VLSVFGNSPS QTHVTRQISS ETNETTPPSS PQIYRRNKEE NVFSRLTSGT
     ISNGQNNPDR GIMVPCTNRS YDKYSPLILS STAEGHSRPV LSVSLTDDVM FSGSKDCTVK
     IWDLHTGREI QSLEDHPDSV VKVVYNEYIR LAFSVSKSII KVWDTRENPA RCIKILNSLG
     LADGLVASAA RPNELGQNEN RILDIQLNKY GTVLFSTSGH TVRVWDLRKY YCIGKLNTSH
     QANVICMAVE ESGNDSNIVA TGSKDHYIKL FEVMEDIGGI HQPICTLDPP HYDGIEALTL
     SGDLLFSASR DACIKKWDLT LPHKKLVQSI NQAHKDWIQA LAIKKGGSTL ISGCRSGFVK
     LWSTDTCQPL GELRAHSSAI HAVDVNSKLV ATGSADNNIG LFRWRSSADP SPDLCDYEP
//
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