| Basic Information | |
|---|---|
| Species | Brassica rapa |
| Cazyme ID | Bra038507 |
| Family | CBM57 |
| Protein Properties | Length: 1048 Molecular Weight: 117806 Isoelectric Point: 6.7106 |
| Chromosome | Chromosome/Scaffold: 09 Start: 4990048 End: 4994936 |
| Description | Di-glucose binding protein with Kinesin motor domain |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 71 | 209 | 4.8e-21 |
| MFINAGGADSKVLDSEMSILGDTCFEGGGVLRTDESIVEAGDFPFIYQSARVGNFSYQLNNLLPGEYFVDFHFAEIVNTNGPKGIRVFNVYVLSEFDIFS VVGANRPLLLVDLRVVVVDDGLIKVRFEGINGSPVVCGI | |||
| Full Sequence |
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| Protein Sequence Length: 1048 Download |
| MEDVQINAAT SSSDSPPEIP DPQFVSDTTE KSKLGDTPMD ERDDSMVCDP NSRLVLTGFT 60 EANHSADDTI MFINAGGADS KVLDSEMSIL GDTCFEGGGV LRTDESIVEA GDFPFIYQSA 120 RVGNFSYQLN NLLPGEYFVD FHFAEIVNTN GPKGIRVFNV YVLSEFDIFS VVGANRPLLL 180 VDLRVVVVDD GLIKVRFEGI NGSPVVCGIC LRKAPQVSVV RTSQDCIKCQ NCATEIEISP 240 ARKRLMRAKA HEKYEKKIEE LSERYQHKSN ECHEAWMSLT SANEQLEKVM MELDNKMYEA 300 RSLDQTVETQ ADCLNSITSK YENDKRHWTA AIASLQEKIE IMKREQSQLS QEAHECVGSI 360 PELYKMVDGV QALGNIRVFC RCRPLNKEET STRCATAVDF DGAKDGELGV VTGNHSKKSF 420 KFDRVYTPKD GQVDVFADAS PMVVSVLDGY NVCIFAYGQT GTGKTFTMEG TPQNRGVNYR 480 TVEQLFEIAN ERRETISYNI SVSVLEVYNE QIRDLLATSP ASKKLEIKQS FDGSHHVPGL 540 VEAKVENINE VWNVLQAGSN ARAVGSNNVN EHSSRSHCML SIMVKAKNLM NGDCTKSTLW 600 LVDLAGSERL AKTDVQGERL KEAQNINRSL SALGDVIYAL ATKSSHIPYR NSKLTHLLQD 660 SLGGDSKTLM FVQISPSEHD VSETLSSLNF ATRVRGVELG PARKQVDTGE IQKMKAMVEK 720 ARHESRSKEE LIKKLEENIQ NLEGKNKGRD HSYRSLQEKN KELESQLESL HNQSEKQNAQ 780 LQEKLKSRDE TCTNLQQKVK ELECKLRERH QSDSAAYQQK VKDLETKLKD SEGNSLVLQQ 840 KAKDYENKLK DSESNALVWQ HKIKELERKQ KDEQTQEAVL LRQKIKELEV RLKEQELHVQ 900 QMAATREFPD VASATPNEVK TCFKEDNFGN ENAESNNNNN NILRTSNRLK ASAARRNDSL 960 NLNEATRKKR VSRSGETENN GGDEPQMKEK RIRKSDPPKV VARLTRPTRP VSSSNQVPVA 1020 QKRVVSREQQ QAVVGKERDP KKRMWTR* 1080 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd01369 | KISc_KHC_KIF5 | 4.0e-103 | 375 | 693 | 324 | + Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. 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. | ||
| cd00106 | KISc | 3.0e-124 | 375 | 695 | 329 | + 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. | ||
| smart00129 | KISc | 3.0e-136 | 375 | 703 | 336 | + Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. | ||
| pfam00225 | Kinesin | 9.0e-138 | 381 | 697 | 326 | + Kinesin motor domain. | ||
| cd01366 | KISc_C_terminal | 0 | 374 | 700 | 329 | + Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. 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 this subgroup the motor domain is found at the C-terminus (C-type). 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. | ||
| Gene Ontology | |
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| GO Term | Description |
| GO:0003777 | microtubule motor activity |
| GO:0005524 | ATP binding |
| GO:0007018 | microtubule-based movement |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAD15569.1 | 0 | 1 | 1047 | 1 | 1068 | putative kinesin heavy chain [Arabidopsis thaliana] |
| EMBL | CAN63715.1 | 0 | 36 | 1029 | 40 | 1063 | hypothetical protein [Vitis vinifera] |
| EMBL | CBI40845.1 | 0 | 87 | 1047 | 1 | 979 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_179846.2 | 0 | 1 | 1047 | 1 | 1093 | kinesin motor protein-related [Arabidopsis thaliana] |
| RefSeq | XP_002266404.1 | 0 | 36 | 809 | 40 | 865 | PREDICTED: hypothetical protein [Vitis vinifera] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2h58_A | 0 | 374 | 699 | 4 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
| PDB | 3h4s_A | 0 | 374 | 743 | 13 | 375 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cob_C | 0 | 374 | 718 | 5 | 347 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cob_A | 0 | 374 | 718 | 5 | 347 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cnz_B | 0 | 374 | 718 | 5 | 347 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| DV990845 | 298 | 429 | 722 | 0 |
| ES865056 | 287 | 441 | 722 | 0 |
| EL442930 | 264 | 461 | 722 | 0 |
| FL921658 | 258 | 465 | 722 | 0 |
| CN735539 | 243 | 775 | 1017 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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