Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.001G436200.1 |
Family | CBM57 |
Protein Properties | Length: 1158 Molecular Weight: 129018 Isoelectric Point: 7.0789 |
Chromosome | Chromosome/Scaffold: 01 Start: 46763015 End: 46769087 |
Description | Di-glucose binding protein with Kinesin motor domain |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 146 | 288 | 3.1e-26 |
INAGCTGGAVFLGGVEFVEDDCFAGGDTVRTDATIGDGQDGGLSLYQTARYGNFSYCFRGLEPGTYDVSLHLAEIVFTEGPPGLRVFDVFIHEKKVVSCL DIYAQVGANKPLVVSDLKAFVEGDEGLLIRFEGVMGKPIVCGI |
Full Sequence |
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Protein Sequence Length: 1158 Download |
MVDSISFPNS NEVDMYWQET QSLESISTQK IIHPVENDTI EGRSVIGFSL TSPDLVICAA 60 SPDISRTGYG DSPDFMDKNK CSIEVSLENG IDGSGIKDSS KTPCVKFSPV FQTFNKELSP 120 ESSFELLPQT EKEEKLVKVF VPGVSINAGC TGGAVFLGGV EFVEDDCFAG GDTVRTDATI 180 GDGQDGGLSL YQTARYGNFS YCFRGLEPGT YDVSLHLAEI VFTEGPPGLR VFDVFIHEKK 240 VVSCLDIYAQ VGANKPLVVS DLKAFVEGDE GLLIRFEGVM GKPIVCGISV TKDSSAHTGE 300 AQLLKPVEMS QVAECESPKE DNGHLQVEGD YEKLLRDYEC QRRELTEMRR TMDELKRENR 360 LKSRECQDAL KSLQELQNEL MRKSMHVGSL AFAIEGQVKE KSRWFTSLRD LTRKLKLMKM 420 EHIKLSEEAL AYKNCVADME DMRFTIVSTM KQQVELHEDI KIKFVEGAKE RKELYNKVLE 480 LKGNIRVFCR CRPLKPEEVA AGALVTIDFE SAKDGELTVM SNGLPRKTFK FDAVFGPQAN 540 QADVFEDTAS FASSILDGYN VCVFAYGQTG TGKTFTMEGT EEDRGVNFRT LEQVFCMIKE 600 REELFRYDVS VSVLEVYNEQ IRDLLVSDSQ PGVAAKRLEI RQAGEGLHHV PGLVEARVHN 660 MSEVWEVLQT GSNARAIGST NANEHSSRSH CIHCVMVKGE NLLNGECTKN KLWLVDLAGS 720 ERISKTEVQG ERLRETQNIN KSLSALGDVI SALATKSPHI PFRNSKLTHL LQDSLGGDSK 780 TFMFVQISPN ENDLGETLCS LNFASRVRGI ELGPAKRQLD NAELLRYKQM SEKSKQDLKS 840 KDVQIKKMED TINGLDLKTK EKDLKYMMLQ DKVKELEAQL LVERKLARQH VDTKIAEQQQ 900 QQQMKQQQAE HIIAPPRPPL PNRILGSNWI YNEPANGALN KQQINPTQPL AGNTSNKSTI 960 PLPSTDGIVK LIDSTEKENN PDMANQPRLP KRTGRASICT TAGQVLAAPA PRRNSMIPLP 1020 SIPSLVQLPS IPSSFLLCQV DMKQDLEGTE TNCLHKQTHC DSPKGIRNGS KRLNTMLKRS 1080 LQKKANMKSP MQQHTRRGGI NVGMEKVRVS IGSRGRMAHR VLLGNGRRAG MRETHQKQML 1140 GEKERRWNSG TVARTPI* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01369 | KISc_KHC_KIF5 | 1.0e-98 | 484 | 810 | 332 | + 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 | 1.0e-120 | 484 | 808 | 333 | + 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 | 7.0e-136 | 490 | 810 | 330 | + Kinesin motor domain. | ||
smart00129 | KISc | 3.0e-137 | 484 | 816 | 340 | + Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. | ||
cd01366 | KISc_C_terminal | 5.0e-174 | 482 | 813 | 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 | |
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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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_002270779.1 | 2e-21 | 1 | 199 | 37 | 226 | PREDICTED: similar to kinesin motor protein-related [Vitis vinifera] |
RefSeq | XP_002270779.1 | 0 | 290 | 1157 | 201 | 1061 | PREDICTED: similar to kinesin motor protein-related [Vitis vinifera] |
RefSeq | XP_002300478.1 | 0 | 42 | 1138 | 5 | 1083 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317602.1 | 0 | 15 | 1157 | 1 | 1129 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002532828.1 | 0 | 14 | 1157 | 19 | 1147 | ATP binding protein, 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 | 2h58_A | 0 | 482 | 812 | 3 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 471 | 830 | 1 | 354 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 480 | 850 | 2 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 480 | 850 | 2 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 480 | 850 | 2 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DV990845 | 300 | 540 | 839 | 0 |
DW067034 | 268 | 457 | 724 | 0 |
ES865056 | 284 | 554 | 837 | 0 |
GW337702 | 300 | 671 | 970 | 0 |
FQ433065 | 257 | 675 | 927 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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