y
Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10013377 |
Family | CE10 |
Protein Properties | Length: 1680 Molecular Weight: 188977 Isoelectric Point: 4.8781 |
Chromosome | Chromosome/Scaffold: 812 Start: 429104 End: 438982 |
Description | P-loop containing nucleoside triphosphate hydrolases superfamily protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE10 | 1403 | 1674 | 0 |
VTTKDAIFDHQNNLKLRLYKPTSTQSTKLPIIFLIHGGGFCLGSIDEPYFRNCCFRLASQLEAIVISPAYRLAPESRLPAAIDDCYAALKWLQSQAEPWL SEVADFEKVFVSGESAGGNIVHNLAVRVGSGSDDMGPVKVKGYLLLDPFFGGVVRTKSEAEFGKDMLLNIDLIDWLFRYSVPVGETSDYPTVNPFGPRSK DLATVELDPMLVVAGGKDVLVDRIRDYAEKLKRMGKRIQYAEFEGQQHGFFTVNPDSEAANSVMDLIKKFIT |
Full Sequence |
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Protein Sequence Length: 1680 Download |
MPFNYEAAAS AIKSRFGFRD RSTSETVPNT PFLLNSVSRD EFASGKPLVA SSAARRIVDW 60 EDDSGNDNNG SDMQSSELID DFSFWKENNV QVIIRMRPLS GSEISQQGQK KCVRRDNPQM 120 ITWTGPPESR FTFDLVADEN VGQEQMFKAA GMPMVDNCMG GYNSCMFAYG QTGSGKTYTM 180 LGDIEGGTRR HSVHCGMTPR VFEYLFSRIQ KEKDVRDEEK LKFICKCSFL EIYNEQILDL 240 LDPSSNNLQI RADVKKGGYV ENLKEVEVSS ARDVIQQLIE GSTNRKVAAT NMNHASSRSH 300 SVFTCIIESK WESQGVTHHR FARLNLVDLA GSERQKSSGA EGERLKEATN INKSLSTLGL 360 VIMNLVSISN GKALHVPYRD SKLTFLLQDS LGGNSKTIIV ANISPALCNS LETLGTLKFA 420 QRAKFIKNNA IVNEDTSGDV IGMRMQIQQL KKEVSHLRSI VNNGAGSLSS MDTSAVSISG 480 SPTAFKWEGL QGSFSPFVSE KRASQKKDYD AALVGAFKRE QDKDLSLKAL TAENQAIMKL 540 AKQREDEIQG LKMRLRFREA GIKRLESVAA GKISAETHLL QEKEEYLKEI QVLRTQVDRN 600 QEVTRFAMEN LKLKEEIRRH VLLKSISEEG DRETLSEQIT VLQNKLLEAL DWKLMHESDT 660 LFVQKENSNK GKDEDSDLFK LCEESGSPRH SLLQEENEFL RMQAIQNKSE IDTLHEQLNF 720 CLEERERLQR DVNDLAEKLE EARRDVMEAK NNTEGSVGGT NDQIELKTMV DAIAAATQRE 780 AELSMENSEV RAMLETQIQE NEQLQLKLKA LIEEKNSLIE MYERAASESK YKGLDTSETA 840 RESDMDVDNS DFVRSNETES KTALENLEHQ LMEMHEENDR LLGLYETAMH ERDEFKRILS 900 CSEQQADEIE ADIGECLESD NSLTHSNAEH LKNSEPEVPK PENQTSHCFS LDGEDLMQLE 960 TESDAENKMD EVVGFKIPDL NSVKNKLESA QEKLSGSAKT LTVFTSLEKA FSEFDKVSKE 1020 VETKEKQLQA KQTEMKSFER LSAELHDKKS ITDKKFSALR CSLLSFTSSL AYFDQREAHA 1080 SAKMKASSSQ LSRKEEEFTR INTQKTELEA GIVKAKQSEA ELRSSISVLR TKLEEENRQQ 1140 ENEKVLFAID SNIEKCKFGK ATELLKSEEE KTKLQTELKS LERVITTTRK EIENLSRKLR 1200 KIETEMQSLE MEIVTSRKTT EEMKHAYEPI AKEKESLLAI IESGKLELES MIVEYQQQIF 1260 AADLVDAERE IVEDDALVEL GKAEELRGKK LAVAEEVAKL LGGMSSCSVS KKIEEELRGI 1320 EAEVMEAKSL LNVYDHNLPQ INRIHIFLSI STATMSKETP QPPPAAVDYE ECIGVLRVYI 1380 DGSTWRSSEQ ISNDIPISVP PSVTTKDAIF DHQNNLKLRL YKPTSTQSTK LPIIFLIHGG 1440 GFCLGSIDEP YFRNCCFRLA SQLEAIVISP AYRLAPESRL PAAIDDCYAA LKWLQSQAEP 1500 WLSEVADFEK VFVSGESAGG NIVHNLAVRV GSGSDDMGPV KVKGYLLLDP FFGGVVRTKS 1560 EAEFGKDMLL NIDLIDWLFR YSVPVGETSD YPTVNPFGPR SKDLATVELD PMLVVAGGKD 1620 VLVDRIRDYA EKLKRMGKRI QYAEFEGQQH GFFTVNPDSE AANSVMDLIK KFITEYSIQ* 1680 1740 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN03188 | PLN03188 | 7.0e-112 | 87 | 474 | 393 | + kinesin-12 family protein; Provisional | ||
cd00106 | KISc | 2.0e-121 | 89 | 424 | 344 | + Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward. | ||
pfam00225 | Kinesin | 2.0e-130 | 95 | 424 | 338 | + Kinesin motor domain. | ||
smart00129 | KISc | 6.0e-134 | 89 | 433 | 351 | + Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. | ||
cd01373 | KISc_KLP2_like | 1.0e-158 | 89 | 426 | 338 | + Kinesin motor domain, KLP2-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward. |
Gene Ontology | |
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GO Term | Description |
GO:0003777 | microtubule motor activity |
GO:0005524 | ATP binding |
GO:0007018 | microtubule-based movement |
GO:0008152 | metabolic process |
GO:0016787 | hydrolase activity |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI24411.1 | 0 | 10 | 1152 | 9 | 1093 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002273307.1 | 0 | 1 | 1331 | 1 | 1424 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002328088.1 | 0 | 1 | 922 | 1 | 877 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002328088.1 | 0 | 1008 | 1268 | 882 | 1149 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002528807.1 | 0 | 1 | 1301 | 1 | 1344 | kinesin, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3b6u_B | 0 | 90 | 435 | 23 | 362 | A Chain A, Crystal Structure Of The Motor Domain Of Human Kinesin Family Member 3b In Complex With Adp |
PDB | 3b6u_A | 0 | 90 | 435 | 23 | 362 | A Chain A, Crystal Structure Of The Motor Domain Of Human Kinesin Family Member 3b In Complex With Adp |
PDB | 1goj_A | 0 | 88 | 437 | 6 | 341 | A Chain A, Structure Of A Fast Kinesin: Implications For Atpase Mechanism And Interactions With Microtubu |
PDB | 3zfc_A | 0 | 90 | 433 | 10 | 344 | A Chain A, Crystal Structure Of The Kif4 Motor Domain Complexed With Mg-amppnp |
PDB | 3zfd_A | 0 | 90 | 433 | 10 | 344 | A Chain A, Crystal Structure Of The Kif4 Motor Domain Complexed With Mg-amppnp |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HS268666 | 231 | 260 | 490 | 0 |
HS023444 | 231 | 260 | 490 | 0 |
ES789966 | 322 | 1367 | 1677 | 0 |
CU528611 | 225 | 272 | 495 | 0 |
BQ238936 | 257 | 248 | 501 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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