| Basic Information | |
|---|---|
| Species | Linum usitatissimum |
| Cazyme ID | Lus10005582 |
| Family | CBM57 |
| Protein Properties | Length: 1104 Molecular Weight: 122054 Isoelectric Point: 7.8191 |
| Chromosome | Chromosome/Scaffold: 2324 Start: 180940 End: 185732 |
| 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 | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 127 | 272 | 3e-29 |
| INVGCTDDQTVTKDGLSYMKDSCFLGGDTVRTNAIIGDGLDEDESLCLYQTARMGDFSYCFRSLEPGDYDVALHFAEIVFTNGPPGLRVFDVFLQEKKVV SNLDIFARVGANNPLVLSDLKASVGLGEKLSIRLEGVTGTPILCAI | |||
| Full Sequence |
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| Protein Sequence Length: 1104 Download |
| MADPVSSTSP SCPSFSNGRS LLGFSLSSPD LVICAGSPEM ESNICGCSPE IVGSRKKQCM 60 DLSLDNGIAG YESGARETSR SVKFSPFCQT FYNKELSPES SIELLARPVK GEQIVGDVLP 120 ASAGITINVG CTDDQTVTKD GLSYMKDSCF LGGDTVRTNA IIGDGLDEDE SLCLYQTARM 180 GDFSYCFRSL EPGDYDVALH FAEIVFTNGP PGLRVFDVFL QEKKVVSNLD IFARVGANNP 240 LVLSDLKASV GLGEKLSIRL EGVTGTPILC AISVAKDDSA STGEASFPEH IKRSQAAEIE 300 SQKNADCEME DDYQKLLTAY ECQQRELTEM RKIVEELNRE NQVKTKECQN ALKTLQDLQS 360 ELMRKSMHVG SLAFAVEGQV KEKSRWFSAL KDLTEKIEMM KGDQIKLSEE ARSYKACFGE 420 MSEIASTIQS TMKQQSGLHG DLMKKFMEGV RERKELYNKV LELKGNIRVF CRCRPLNSEE 480 IAAGAAMAID FESAKDGELT VFSNGVPRKT FKFDSIFSPQ ANQADVFEDT AAFATSVLDG 540 YNVCIFAYGQ TGTGKTFTME GTKEARGVNY KTLNELFHMI KEREKIFKYE VSVSVLEVYN 600 EQIRDLLVSN SQPATVKRLE IRPAGDGLHC VQGLVEARVN NVNEAWEVLQ TGSNARAVGS 660 TSANDHSSRS HCIHCVMVKG ENLLNKECTR SKLWLVDLAG SERVAKTEVQ GERLKETQNI 720 NRSLSALGDV IFSLATKSPH IPFRNSKLTH LLQDSLGGDS KALMFVQISP NESDLSETLC 780 SLNFASRVRG IELGPAKRQF DMPELVRYKQ LAEKTRQELK LKDVQIRKMD DTVQGLELKV 840 KEKDIKNKHL QEKIKELESQ LLVERKLARQ HVDTKIAEQH SKQSDDQTCP PPRPPLGTRL 900 LGNSSNKASS NGSANVALNK ETMDAENFLP STDVIFKIPD PMEKENNPDM AENLGMQKRT 960 TGRFSICPAP RRNSLIPFSS PSPLPLLPVS LNQDAEKGVC ESQKEGKTGT RKRNSVLRRS 1020 VHKKLQSRSP MQQQIARKGG INVGMEKVRL SIGSRGRMAQ RVVLHGSAAA KRVVSKEITT 1080 QQKQVSHKEK ERGWNNATTT ARL* 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 | 2.0e-96 | 466 | 791 | 332 | + 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-118 | 466 | 789 | 332 | + 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 | 1.0e-134 | 472 | 791 | 329 | + Kinesin motor domain. | ||
| smart00129 | KISc | 2.0e-137 | 466 | 797 | 339 | + 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 | 3.0e-172 | 464 | 794 | 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. | ||
| 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 |
| RefSeq | NP_177370.1 | 0 | 11 | 982 | 65 | 1012 | kinesin motor protein-related [Arabidopsis thaliana] |
| RefSeq | NP_177370.1 | 2e-20 | 921 | 1084 | 1025 | 1191 | kinesin motor protein-related [Arabidopsis thaliana] |
| RefSeq | XP_002300478.1 | 0 | 17 | 1084 | 4 | 1083 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002317602.1 | 0 | 17 | 1099 | 27 | 1124 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002532828.1 | 0 | 1 | 1098 | 36 | 1141 | 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 | 464 | 793 | 3 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
| PDB | 3h4s_A | 0 | 453 | 812 | 1 | 355 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cob_C | 0 | 462 | 818 | 2 | 353 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cob_A | 0 | 462 | 818 | 2 | 353 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cnz_B | 0 | 462 | 818 | 2 | 353 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| DW067034 | 268 | 439 | 705 | 0 |
| DV990845 | 300 | 522 | 820 | 0 |
| ES865056 | 284 | 536 | 818 | 0 |
| GW337702 | 237 | 652 | 887 | 0 |
| FQ433065 | 222 | 656 | 877 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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