Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.002G032500.2 |
Family | CBM57 |
Protein Properties | Length: 1136 Molecular Weight: 126598 Isoelectric Point: 7.8543 |
Chromosome | Chromosome/Scaffold: 02 Start: 2427826 End: 2433886 |
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 | 151 | 292 | 4e-24 |
SINAGCLNGAVELDGVIYSNDDCFVGGDVIIADRIVGDGGGNSLYNTARLGDFSYNFLTLECGFYAIDLHFAEIVFTTGPPGIRVFDVFVQEEKVVTSLD IYGQVGANKPLVISNIRTFVDSGGGLLIRFEGLMGSPIVCGI |
Full Sequence |
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Protein Sequence Length: 1136 Download |
MASHSENPSL SDLVSSPKQD SADVVDPRQS QSPNVISTPI REFDGRSMLG FSLTSPDLVI 60 CAGSPDIPSK AYGDSPEFLE KHRCSIEVSL ENGIEGSDNS KAKQKSPTVK FSTVCETFHK 120 ELSPESSFEL LPLRETADYS QHKHEDYPAI SINAGCLNGA VELDGVIYSN DDCFVGGDVI 180 IADRIVGDGG GNSLYNTARL GDFSYNFLTL ECGFYAIDLH FAEIVFTTGP PGIRVFDVFV 240 QEEKVVTSLD IYGQVGANKP LVISNIRTFV DSGGGLLIRF EGLMGSPIVC GITVRKDSLE 300 SFKEAGSEEI MGMDKVGGHE SPRDISDCEI EVKYQILQMD YERQKKELAE MRSALEGLKR 360 ENKLKTKECQ EACKSLQELQ NELMRKSMHV GSLAFAIEGQ VKEKSRWFSS LRDMTRKLKI 420 MKMERIKLSE EVSHYKNCIM DINDFGTKIQ SRINQQADLH EDLKTKYLKG AKERKELYNK 480 VLELKGNIRV FCRCRPLNSE EIAAGASLAI DFESAKDGEL TVISNGAPKK TFRFDAVFGP 540 HAEQADVFQD TAPFATSVLD GYNVCIFAYG QTGTGKTFTM EGTKEARGVN FRTLEELFRV 600 INERQKLYRY EISVSALEVY NEQIRDLLVS GSQQSTMAKR LEIRQVGEGM HHVPGLVEAH 660 VNNMNEVWEV LQTGSNARAV GSTNANEHSS RSHCIHCVMV KGENLLNGEC TKSKLWLVDL 720 AGSERVAKTD VLGERLKETQ NINRSLSALG DVISALATKS SHIPFRNSKL THLLQDSLGG 780 DSKALMFVQI SPNENDLGET LCSLNFASRV RGIELGPAKK QMDTSELLRW KQMQDMKIKD 840 LQIRKMEETI HGLDLKMKDK DLKNKNLQEK VKELESQLLI ERKLARQHVD TRIAEQQQKQ 900 QNEDVRPPLA TRLLGTNKSS NEVKNGTLMK EQVNLTRPLT ENSFRPSMPL SVTDGSFKHI 960 DPVEKENNPE VAEQLRLPTR TGRASMCPTI RRMPASSAPR RNSLIPLPST PSSAQLAPPF 1020 HPLPSQPDII EEVDEFIPEQ TVCNSPKGTK SGGKKLSSIL RRSLQKKVQL KSPMQQHLRR 1080 GLNVGMERVR VSIGSRGRMA SRVLVGNGRK GGKEIQQKQN QKEKERAWNI GRTAI* 1140 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01371 | KISc_KIF3 | 7.0e-98 | 487 | 813 | 339 | + Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. 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 group 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-121 | 487 | 811 | 333 | + 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-139 | 493 | 813 | 330 | + Kinesin motor domain. | ||
smart00129 | KISc | 5.0e-141 | 487 | 819 | 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 | 4.0e-178 | 485 | 816 | 333 | + 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 | 1 | 1119 | 36 | 1191 | kinesin motor protein-related [Arabidopsis thaliana] |
RefSeq | XP_002300478.1 | 0 | 43 | 1119 | 3 | 1083 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317602.1 | 0 | 43 | 1134 | 26 | 1125 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002532828.1 | 0 | 43 | 298 | 45 | 300 | ATP binding protein, putative [Ricinus communis] |
RefSeq | XP_002532828.1 | 0 | 369 | 1135 | 362 | 1147 | 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 | 485 | 815 | 3 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 474 | 833 | 1 | 354 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 483 | 833 | 2 | 346 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 483 | 833 | 2 | 346 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 483 | 833 | 2 | 346 | 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 | 289 | 544 | 832 | 0 |
ES865056 | 281 | 553 | 833 | 0 |
DW067034 | 268 | 460 | 727 | 0 |
DT575110 | 288 | 544 | 831 | 0 |
GW337702 | 295 | 674 | 958 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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