Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 29596.m000713 |
Family | CBM57 |
Protein Properties | Length: 1031 Molecular Weight: 116598 Isoelectric Point: 7.9011 |
Chromosome | Chromosome/Scaffold: 29596 Start: 208202 End: 213660 |
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 | 38 | 181 | 3e-28 |
TNAGGGSIKLKERNFEIDIEEDKNFNGGDVLRTEESIINGGDLPIIYQSARFGSFCYQFTSLPTGDYFVDLHFAEIVNTNGPKGMRVFDVFIQEEKVISE LDIYSIVGANKPLQVLNVLVSVGEDREILIRFEGILGSPIVSGI |
Full Sequence |
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Protein Sequence Length: 1031 Download |
MENTGQDFLD SILCISGSKL IQSGLITSHI TEKPLIFTNA GGGSIKLKER NFEIDIEEDK 60 NFNGGDVLRT EESIINGGDL PIIYQSARFG SFCYQFTSLP TGDYFVDLHF AEIVNTNGPK 120 GMRVFDVFIQ EEKVISELDI YSIVGANKPL QVLNVLVSVG EDREILIRFE GILGSPIVSG 180 ICIKQAPEFP SFEEKHEHII CDNCATEIKI SQSQKKVATA KCISKYEKKI EELNALCQVK 240 ADECYEAWMS LTAASQQLEK ARMEVDNRFF QNMCLDQALK KQSAELSDIS GRYKCDKLSW 300 FAAIEKLEKQ VQMMKIEQSQ LSHEAHECAT SISDLNKMIF SVQALVDQYD DLKLKFNKEQ 360 AERKKLFNQV QEAKGNIRVF CRCRPLSMEE TSAGYQTVVD FDAAKHGDLG VVMSSSTKKT 420 FKFDRVFTPR DDQVDVFVDV SPMVISVLDG YNVCIFAYGQ TGTGKTFTME GTEGNRGVNY 480 QTLQTLFRIA GERKETVKYD ISVSVLEVYN EQIRDLLATS PTAKRLEIKQ FSEGVHHVPG 540 LVEAKVENIK EVWDVLQAGS NARAVGSNNV NEHSSRSHCM LCTMVRAKSL INGECTKSKL 600 WLVDLAGSER LAKTEVQGER LKEAQNINRS LSALGDVISA LATKSSHIPY RNSKLTHLLQ 660 DSLGGDSKTM MFVQISPSER DLGETLSSLN FATRVRGVEL GPAKKQIDLV ELQKLKMMLD 720 KAKQELRSKD DVMYKLEENF QNLEGKAKSK DQLCKNQQEK TNELERQLAM KTELCGKLEN 780 QLLQLSQGMK GKEEICTNFQ QKVKELENKL KEREQAESVN LQYKVNELEN RMKERAQEFE 840 IHSKMLQQKI RELENKLTME RDYSDPRLLQ QKIKVLEEKL REHEQGECIS KLWSAEKLGA 900 TPIQTTSSRL GDVDSSNRRS LSASNRSMNQ GSLLLKGPDS LREVRRKRDI PSKGTENNFL 960 LATSLLEKKT SSPQISKLRH LDPSKVLSRI TRNAKPTING QTAYSRNNTR INRDQVTGVK 1020 DNNNKLKVWL R |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01372 | KISc_KIF4 | 8.0e-99 | 377 | 696 | 341 | + Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. 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 | 2.0e-113 | 376 | 696 | 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 | 1.0e-133 | 376 | 704 | 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 | 5.0e-134 | 382 | 698 | 326 | + Kinesin motor domain. | ||
cd01366 | KISc_C_terminal | 6.0e-179 | 374 | 701 | 330 | + 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 |
EMBL | CBI40845.1 | 0 | 59 | 812 | 6 | 785 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002266404.1 | 0 | 1 | 815 | 43 | 867 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002266404.1 | 4e-17 | 791 | 1031 | 749 | 982 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002302362.1 | 0 | 9 | 1031 | 1 | 1046 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527363.1 | 0 | 1 | 1031 | 1 | 1031 | 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 | 373 | 700 | 2 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 363 | 752 | 1 | 383 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 371 | 731 | 1 | 359 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 371 | 731 | 1 | 359 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 371 | 731 | 1 | 359 | 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 |
EH194227 | 309 | 509 | 817 | 0 |
FL921658 | 258 | 466 | 723 | 0 |
DV990845 | 299 | 431 | 725 | 0 |
EL442930 | 266 | 462 | 725 | 0 |
ES865056 | 289 | 442 | 725 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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