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Basic Information | |
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Species | Capsella rubella |
Cazyme ID | Carubv10022541m |
Family | CBM57 |
Protein Properties | Length: 1088 Molecular Weight: 123353 Isoelectric Point: 6.6366 |
Chromosome | Chromosome/Scaffold: 4 Start: 674169 End: 679962 |
Description | Di-glucose binding protein with Kinesin motor domain |
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 |
CBM57 | 81 | 225 | 7.2e-26 |
MFINAGGDDDAKVLDSELNILKDAYFEGGDVMRTEESIVEAGDFPFLYQSARVGNFCYRLNNLVPGEYLIDFHFAEIINTNGPKGIRVFNVYVQDEKVLA EFDIFSVVGANRPLLLVDLRVMVMDDGLIRVKFEGINGSPVVCGI |
Full Sequence |
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Protein Sequence Length: 1088 Download |
MEDVQIDATV PVDPGAITKI CSPEIPYSQF VNDATENLEI GDTSVDDCED SLGDSMVCDP 60 NSRLVPTGFT RPNSTADETI MFINAGGDDD AKVLDSELNI LKDAYFEGGD VMRTEESIVE 120 AGDFPFLYQS ARVGNFCYRL NNLVPGEYLI DFHFAEIINT NGPKGIRVFN VYVQDEKVLA 180 EFDIFSVVGA NRPLLLVDLR VMVMDDGLIR VKFEGINGSP VVCGICLRKA PKVSVPRTSQ 240 DYIKCENCAT EIEISPKRKR LMRAKAHEKY EKKIAELSER YEHKTNECHE AWMSLTSANE 300 QLEKVLMELD NKMYEARSLD QTVVTQADCL KSITSKYEID KRHWATALDA LQEKIEIMKR 360 EQSQLSHEAH ECVEGIPELY KMVDGVQALV SQCEDLKQKY SEEQAKRKEL YNHIQETKGN 420 IRVFCRCRPL NKDETSTKSA TIVDFDGAKD GELGIITGNN SKKSFKFDRV YTPKDGQVDV 480 FADASPMVVS VLDGYNVCIF AYGQTGTGKT FTMEGTPQNR GVNYRTVEQL FEVARERRET 540 ITYNISVSVL EVYNEQIRDL LATSPASKKL EIKQSSDGSH QVPGLIEANV ENINEVWNVL 600 QAGSNARAVG SNNVNEHSSR SHCMLSIMVK AKNLMNGDCT KSKLWLVDLA GSERLAKTDV 660 QGERLKEAQN INRSLSALGD VIYALATKSS HIPYRNSKLT HLLQDSLGGD SKTLMFVQIS 720 PSEHDVSETL SSLNFATRVR GVELGPARRQ LDTGELQKMK AMVEKARQES RSKDESIKKL 780 EENIQSLEGK NKGRDHSYRS LQEKNKELET QLDLLNSQSE KQNAQLQERL KSRDDICSNL 840 QQKVKELEYK LRERHQSDSA AYHQKAKDLE NKLKESEGNS LVWQQKVKYF ENKLKESEGN 900 SLVWQQKIKE LEIKHKAEQS QEAVLLRQKI KELEMRLKEQ EQHIQQMATT REFPDVANAT 960 PNEVRTCFKD DNFEKENMES NNNILRTSNR LKNKRPDSLN LNEMTRKKRA SRSGETENNG 1020 DDPHMKEKRI RKSDPPKVLL SRVVRPTRPV SGSSNPVPVA HKRVIKREQQ DVPVGKERDP 1080 KKKIWSR* 1140 |
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-107 | 420 | 738 | 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 | 2.0e-123 | 420 | 740 | 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-137 | 420 | 748 | 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 | 2.0e-139 | 426 | 742 | 326 | + Kinesin motor domain. | ||
cd01366 | KISc_C_terminal | 0 | 418 | 745 | 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 |
GenBank | AAD15569.1 | 0 | 1 | 1087 | 1 | 1068 | putative kinesin heavy chain [Arabidopsis thaliana] |
EMBL | CBI40845.1 | 0 | 98 | 1087 | 1 | 979 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_179846.2 | 0 | 1 | 1087 | 1 | 1093 | kinesin motor protein-related [Arabidopsis thaliana] |
RefSeq | XP_002266404.1 | 0 | 1 | 835 | 1 | 840 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002266404.1 | 0.00000001 | 842 | 1087 | 759 | 982 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 417 | 744 | 2 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 407 | 775 | 1 | 367 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 415 | 782 | 1 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 415 | 782 | 1 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 415 | 782 | 1 | 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 | 302 | 474 | 771 | 0 |
EL442930 | 266 | 506 | 769 | 0 |
ES865056 | 289 | 486 | 769 | 0 |
FL921658 | 258 | 510 | 767 | 0 |
EH194227 | 312 | 553 | 861 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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