Basic Information | |
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Species | Carica papaya |
Cazyme ID | evm.model.supercontig_21.41 |
Family | CBM57 |
Protein Properties | Length: 891 Molecular Weight: 100379 Isoelectric Point: 8.3831 |
Chromosome | Chromosome/Scaffold: 21 Start: 600322 End: 606511 |
Description | Di-glucose binding protein with Kinesin motor domain |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 77 | 221 | 1.6e-27 |
IFINAGGGSLCKEGGYRNCVQPDSSFEGGDVLRTDENIIDGGDITCIYQSARFGSCSYRVPFLSPGDYLVDFHFAEIVNTNGPRGMRVFDVFIQGEKVLS ELDIYSVVGSNKPLQVVDVRVSVGENEDMLIRFAGVCGSPIVSGI |
Full Sequence |
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Protein Sequence Length: 891 Download |
MEEESFNRNH HQDLKTPRTN SWSCTNNSKN IRSDCRKYAC VEEDGDEALV DSVLCIPGSR 60 IIKSGFTIAN CTDNLVIFIN AGGGSLCKEG GYRNCVQPDS SFEGGDVLRT DENIIDGGDI 120 TCIYQSARFG SCSYRVPFLS PGDYLVDFHF AEIVNTNGPR GMRVFDVFIQ GEKVLSELDI 180 YSVVGSNKPL QVVDVRVSVG ENEDMLIRFA GVCGSPIVSG ICIKRASELP ACQVKQEFLI 240 CSNCTAEINI SSSQNKYMLT KSAAKYERKI TELKRQCQQK ADECYEAWMS LTNVNQQLEK 300 VKTELDNNFF QNMRLEQVMD KQSAELKEIS TQYIRDKKLW ASSIYELQKK IKTMKEEHHQ 360 LSIEAHECAN SIPALNEMLF AVKALVTKYD DLKVKFCEEQ AKRKKLLEIR QPSERVHHVA 420 GMVEAKVENI NEAWEVLQAG SSTRAVGSNN INEHSSRSHC MLCILVRAKN LISGECTKSK 480 LWLVDLAGSE RLTKTEVQGE RLKEAQNINR SLSALGDVIS ALATKSNHIP YRNSKLTHML 540 QDCVGGDSKT LMFVQISPSE QDLGETLSSL NFATRVRGIE LGPAKRQIDK GELQKLKIVV 600 DKAKQELRSK DEALQKLEES FHNLEVKAKG RDQLSKDQQE KVNELESLLA SKTELCRQLQ 660 KQLSQFSDRM QGKEEICLNF QKKVEELESR LKERERVESI ILQNKVRELE SKLTMENENS 720 QCQLLQEKIK VLERKLKEQQ HQEHMLTQCQ YSAGKLGATP NESKILRAES MGDIGPIGMR 780 ILQSGNRTSN HGSGLLKGTD SLREIRRKQI QSKGSENNIL LSASLLERKK SSSDELEKSK 840 NATSSKALAR FTRSIKPVST VQPVISNGKV NRSFDPRLKE KGNKLNMRLR * 900 |
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-53 | 392 | 579 | 197 | + 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-61 | 403 | 577 | 179 | + 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-67 | 402 | 585 | 188 | + Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. | ||
pfam00225 | Kinesin | 3.0e-74 | 399 | 579 | 184 | + Kinesin motor domain. | ||
cd01366 | KISc_C_terminal | 4.0e-94 | 398 | 582 | 185 | + 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 | CAN72159.1 | 0 | 45 | 385 | 2 | 334 | hypothetical protein [Vitis vinifera] |
EMBL | CAN72159.1 | 0 | 405 | 872 | 478 | 939 | hypothetical protein [Vitis vinifera] |
EMBL | CBI40845.1 | 0 | 99 | 406 | 6 | 311 | unnamed protein product [Vitis vinifera] |
EMBL | CBI40845.1 | 0 | 405 | 713 | 472 | 783 | unnamed protein product [Vitis vinifera] |
EMBL | CBI40845.1 | 0.000005 | 758 | 884 | 852 | 973 | unnamed protein product [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 | 418 | 581 | 167 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 380 | 619 | 135 | 376 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 376 | 619 | 123 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 376 | 619 | 123 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 376 | 619 | 123 | 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 |
EX268153 | 257 | 625 | 881 | 0 |
ES827277 | 259 | 415 | 672 | 0 |
EH194227 | 273 | 409 | 681 | 0 |
DR938652 | 225 | 410 | 634 | 0 |
ES843162 | 224 | 426 | 649 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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