Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 98850 |
Family | CBM57 |
Protein Properties | Length: 755 Molecular Weight: 84124.5 Isoelectric Point: 6.2796 |
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 | 25 | 167 | 2.3e-35 |
VAAINAGGSSILDTSFGIDFVDDRFFSGGDVLRTAEDIVDAQEPSLYRTARYGEVTYALDGLESGDYYVDIHFAEIIFTNGPPGMRIFDVYIQDEKVVSD LDVYGRVGSNRPLILLNVRAAVDGGVLTLAFRGVVGNPTISAI |
Full Sequence |
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Protein Sequence Length: 755 Download |
MFLFLREASR NTLPPCLCLF PDKVVAAINA GGSSILDTSF GIDFVDDRFF SGGDVLRTAE 60 DIVDAQEPSL YRTARYGEVT YALDGLESGD YYVDIHFAEI IFTNGPPGMR IFDVYIQDEK 120 VVSDLDVYGR VGSNRPLILL NVRAAVDGGV LTLAFRGVVG NPTISAICVH RAPPLGAEPV 180 VSHDQFTSLR WKTARSRMLA DSRFMRDKSR GAVTESEQRL EELRNECHQA WISVQESNRQ 240 AEKLRDELSV KSLTVDTLAN AVETQVLELR DLKEKEMNEK TKLKLAVSDA QRKVEELRIL 300 YSLLSKDARD CICSFPDPHG MVSAVQALVN EQKELKKRLL DESQERKFLY NKLIEMKGNF 360 LPGNVRVFCR CRPLNASEAS ASSVSVVEFD SARENELVIR AGTNPKKLYK FDRVFTPEDD 420 QPEVFADTSP VVVSVLDGYN VCIFAYGQTG TGKTFTMEGI PGNRGVNYRT LEELFRLSTV 480 RKGEVNYEIK VSVLEVYNEQ IRDLLTTPSQ AGLAPKRLEI KQDADGGHRV PGLVEAEVHS 540 MTEVWEVLQS GSAARAVGST NANEHSSRSH CMLCVKVRGE NMTTGECTRS KLWLVDLAGS 600 ERVAKSDVQG DRLKEAQNIN KSLSALGDVI HALTTKSNHV PYRNSKLTHL LQDSLGGESK 660 TLMFVQISPT EADVGETLCS LNFASRVRGV EMGPAKKQLD SSEFFKYKQM AEKAKQDVKT 720 KDDSVRRLED SLRTTESKLK VKEQLCQSLA EKVKD |
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-105 | 364 | 686 | 328 | + 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 | 364 | 688 | 335 | + 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 | 3.0e-137 | 370 | 690 | 330 | + Kinesin motor domain. | ||
smart00129 | KISc | 2.0e-138 | 364 | 696 | 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 | 6.0e-180 | 363 | 693 | 332 | + 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. |
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 | 42 | 755 | 1 | 711 | unnamed protein product [Vitis vinifera] |
GenBank | EEC74382.1 | 0 | 22 | 710 | 60 | 749 | hypothetical protein OsI_09716 [Oryza sativa Indica Group] |
GenBank | EEE58202.1 | 0 | 22 | 710 | 60 | 749 | hypothetical protein OsJ_09155 [Oryza sativa Japonica Group] |
RefSeq | XP_002266404.1 | 0 | 22 | 755 | 74 | 809 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002527363.1 | 0 | 22 | 755 | 32 | 763 | 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 | 363 | 692 | 4 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 346 | 737 | 1 | 384 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 361 | 723 | 3 | 359 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 361 | 723 | 3 | 359 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 361 | 723 | 3 | 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 |
DV990845 | 302 | 418 | 719 | 0 |
ES865056 | 288 | 430 | 717 | 0 |
DT575110 | 288 | 421 | 708 | 0 |
EL442930 | 268 | 450 | 717 | 0 |
FL921658 | 263 | 454 | 715 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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