| Basic Information | |
|---|---|
| Species | Brassica rapa |
| Cazyme ID | Bra016076 |
| Family | CBM57 |
| Protein Properties | Length: 1125 Molecular Weight: 125182 Isoelectric Point: 7.2118 |
| Chromosome | Chromosome/Scaffold: 07 Start: 19552159 End: 19556843 |
| Description | Di-glucose binding protein with Kinesin motor domain |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 137 | 287 | 1.3e-22 |
| VMSVNSGSINEDVTVADVTFLKDEFFSGGGTVMTDDVVGSEEEALLYQTARVGDFAYTFKALDPGDYFIDLHFAEIEFTEGPAGVRVFDIFIQGAKARLE LFFVISGLDLFSQVGSNTPFVISDLRMLVGVEGELTVRLEGVIGAAILCGI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1125 Download |
| MADLDSYCEL SNGKVTRNSR SLCIPQVLTL ESGFRFVDVV DMEQSSDPVA LGFSLASPDL 60 VNCGVSPDIP RGSYVDSPEI AKKLRFSTEL SLENGIDGGR KTRSVKFSAI NQTFEFELSP 120 ESSFELPSPP GNATTPVMSV NSGSINEDVT VADVTFLKDE FFSGGGTVMT DDVVGSEEEA 180 LLYQTARVGD FAYTFKALDP GDYFIDLHFA EIEFTEGPAG VRVFDIFIQG AKARLELFFV 240 ISGLDLFSQV GSNTPFVISD LRMLVGVEGE LTVRLEGVIG AAILCGISVR KEATATYGED 300 TGVLAVKGKT DTVLSLPPQE NVDCGTEEET PEVSSDCEQQ KKEMADMKRM VDELKQENQR 360 KSRECEEALN SLRELQNELM RKSMHVGSLA FAVEGQVKEK SRWFSSLRDL TRKLKIMKME 420 QIMLLEEAST YKSLVQDINV FSSHIHSRVK HDAELHENLK AKFVEGEKER KELYNKILEL 480 KGNIRVFCRC RPLNFEEIEA GVSMGIDVES TKNGEVIVMS NGFPKKSFKF DSVFGPNASQ 540 ADVFEDTAPF ATSVIDGYNV CIFAYGQTGT GKTFTMEGTQ DNRGVNYRTL KNLFEIMKER 600 ENRYSYEISV SVLEVYNEQI RDLLVPASQN ASAAKRFEIR QVNEGSHHVP GLVEARVSTM 660 EEVWDVLKTG SNARAVGKTT ANEHSSRSHC IHCVMVKGEN LLNGECTKSK LWLVDLAGSE 720 RVAKTEVQGE RLKETQNINK SLSALGDVIY ALANKSSHIP FRNSKLTHLL QDSLGGDSKT 780 LMFVQISPNE KDNSETLCSL NFASRVRGIE LGPAKKQLDN TELLKYKQMV EKWKQDMKGK 840 DEQMRKMEET MLGLEAKVKE RDTKNKTLQE KVKELESQLL VERKLARQHV DTKIAEQHTK 900 QQSEDENNTS KRPPLANMLL GSNKTSNETA SSKETVSTSS YDLPPLPNSG LKCNDLTEKE 960 NNPDMAERLP IPKRTGRFSV GPKRILPAPA PRRSTLAPTP YLPITSTSPL RSSRQATITN 1020 SPDEKSGTNQ VPCISPKLHK SNGKTLTSIL RRSMQKRMQT KSSTPRQQQQ PLRRGGINVG 1080 MEKVRLSIGS RGKLAHRVQL TNARKAGLKE TPLKQAQKEK ERWI* 1140 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd01369 | KISc_KHC_KIF5 | 2.0e-99 | 483 | 809 | 333 | + 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 | 9.0e-119 | 483 | 807 | 336 | + 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 | 5.0e-134 | 483 | 815 | 340 | + Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. | ||
| pfam00225 | Kinesin | 5.0e-139 | 489 | 809 | 330 | + Kinesin motor domain. | ||
| cd01366 | KISc_C_terminal | 1.0e-173 | 481 | 812 | 333 | + 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 | |
|---|---|
| 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 |
| RefSeq | NP_177370.1 | 0 | 1 | 1008 | 36 | 1012 | kinesin motor protein-related [Arabidopsis thaliana] |
| RefSeq | NP_177370.1 | 0 | 929 | 1124 | 1009 | 1195 | kinesin motor protein-related [Arabidopsis thaliana] |
| RefSeq | XP_002300478.1 | 0 | 50 | 1115 | 8 | 1083 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002317602.1 | 0 | 35 | 1123 | 16 | 1119 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002532828.1 | 0 | 1 | 1123 | 1 | 1137 | ATP binding protein, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2h58_A | 0 | 481 | 811 | 3 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
| PDB | 3h4s_A | 0 | 470 | 849 | 1 | 376 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cob_C | 0 | 479 | 849 | 2 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cob_A | 0 | 479 | 849 | 2 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cnz_B | 0 | 479 | 849 | 2 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| Hydropathy |
|---|
 |
| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| CN737350 | 229 | 515 | 743 | 0 |
| DV990845 | 300 | 539 | 838 | 0 |
| ES865056 | 288 | 549 | 836 | 0 |
| DW067034 | 268 | 456 | 723 | 0 |
| DK481848 | 298 | 1 | 297 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
|---|
 |
| Phylogeny |
|---|
 |