Basic Information | |
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Species | Citrus sinensis |
Cazyme ID | orange1.1g001679m |
Family | CBM57 |
Protein Properties | Length: 1033 Molecular Weight: 117148 Isoelectric Point: 7.5896 |
Chromosome | Chromosome/Scaffold: 00059 Start: 23600 End: 29391 |
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 | 39 | 182 | 3.3e-29 |
LFVNAGGEASDEVDCSMKFLGDTYFEGGNVLRTNEHICDAGDYPFIYQSARFGNFCYRFNDIPPGHYYVDLHFAEIINTNGPKGMRVFNVFVQEEKVVSD FDIFSIVGANKPLQLVDIGVSVKEEGTVVVRFEGISGSPAVSGI |
Full Sequence |
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Protein Sequence Length: 1033 Download |
MEEEDGNEES FVDSMLCDSN SRLIPCGFIR SYCTGEFVLF VNAGGEASDE VDCSMKFLGD 60 TYFEGGNVLR TNEHICDAGD YPFIYQSARF GNFCYRFNDI PPGHYYVDLH FAEIINTNGP 120 KGMRVFNVFV QEEKVVSDFD IFSIVGANKP LQLVDIGVSV KEEGTVVVRF EGISGSPAVS 180 GICIRRASKV LSVPQTSHEF LKCNNCAAEI EVPSAQKKLM RIKATEKYEK KIEELNKQFQ 240 LKTNECHEAW MSLTAANEQL EKVRMELDNK AFQTLTLDQT VEKQAENLIN ITSRYECDKK 300 YWAAAVSDLQ EKVKMMKKEH SQLSREAHEC ADSIPELNKM VIGVQALVAQ CEDFKMKYSE 360 EQAKRKELYN QIQQTRGNIR VFCRCRPLNK VEISAGCATV VDFDAAKDGE LGVLTGSSTR 420 KTFKFDRVFT PNDGQVDVFA DASPLVISVL DGYNVCIFAY GQTGTGKTFT MEGTEQSRGV 480 NYRTLEQLFE IAKERSETFT YNISVSVLEV YNEQIRDLLA TSPTSKKLEI KQSSEGSHHV 540 PGIVEANVNS IREAWNVLQT GSSARAVGSN NVNEHSSRSH CMLCIMVRAK NLISGECTKS 600 KLWLVDLAGS ERLTRTDVQG DRLKEAQNIN RSLSALGDVI YSLATKSNHI PYRNSKLTHL 660 LQDSLGGDSK TLMFVQISPS EQDLSETLSS LNFATQVRGV ELGPARKQID TSELQKMKVM 720 LEKARQDSRS KDESLRKLEE NLQNLENRAK YKDQTYKNQQ EKVKELEGQV SLKSNLHDQS 780 DKQASQLLER LKGREELCST LQIKVKELEN RLRDRQQSES AIFQQKVKDI ENKLKEQERE 840 SESHSISLQH KVKELESKLK EQERQHVESL MLRQKIKELE DKLKEQEQQF QCRLSRDFAD 900 LIKYTPNEVK TSKGDDEVMS DIDLRILRSS NSVNRPMSHG SILPRGNGHQ HETRKKRDSR 960 SGETENNNIL KSSSYENKKR KSDPPRVAAT RVMRTAKPVT ATIQGPSVHK RINRDQVQGI 1020 KERDTKKKIW SR* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01369 | KISc_KHC_KIF5 | 3.0e-104 | 378 | 695 | 323 | + 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-121 | 378 | 698 | 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 | 4.0e-138 | 378 | 706 | 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 | 7.0e-139 | 384 | 700 | 326 | + Kinesin motor domain. | ||
cd01366 | KISc_C_terminal | 0 | 376 | 703 | 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 | CAN63715.1 | 0 | 3 | 1016 | 44 | 1063 | hypothetical protein [Vitis vinifera] |
EMBL | CBI40845.1 | 0 | 55 | 1032 | 1 | 979 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002266404.1 | 0 | 3 | 819 | 44 | 871 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002266404.1 | 4e-34 | 770 | 1032 | 719 | 982 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002532381.1 | 0 | 9 | 1030 | 48 | 1073 | 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 | 375 | 702 | 2 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 365 | 754 | 1 | 383 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 376 | 740 | 4 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 376 | 740 | 4 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 376 | 740 | 4 | 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 |
EY750292 | 252 | 512 | 762 | 0 |
EL442930 | 266 | 464 | 727 | 0 |
EH194227 | 317 | 511 | 825 | 0 |
DV990845 | 301 | 433 | 729 | 0 |
FL921658 | 258 | 468 | 725 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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