Basic Information | |
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Species | Citrus clementina |
Cazyme ID | Ciclev10000147m |
Family | CBM57 |
Protein Properties | Length: 999 Molecular Weight: 112347 Isoelectric Point: 7.9295 |
Chromosome | Chromosome/Scaffold: 5 Start: 35395149 End: 35401096 |
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 | 21 | 165 | 7.9e-28 |
MFVNAGGKAIMKEGNMGMNVESDRYFEGGDVLRTDESIIDGGDMAVLYQSARFRNFSYRIGNLSPGDYLVDLHFAEIVNANGPKGMRAFDVFMQEEKVLL EIDIYSIVGANKPLQVVDVRVSVGMDEVLLIRFDGVCGSPIVNGI |
Full Sequence |
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Protein Sequence Length: 999 Download |
MESYDTDSID SVLCTSDNIL MFVNAGGKAI MKEGNMGMNV ESDRYFEGGD VLRTDESIID 60 GGDMAVLYQS ARFRNFSYRI GNLSPGDYLV DLHFAEIVNA NGPKGMRAFD VFMQEEKVLL 120 EIDIYSIVGA NKPLQVVDVR VSVGMDEVLL IRFDGVCGSP IVNGICIKNA TNVPESLGDH 180 GHLICNGCGT EIEIAPAQDK LMRMKSMAKY EKRIKELKIQ RQLKTDECYE AWMSLTAAND 240 QLEKVRMDLD NKCFQNLCLD QALEKKAAKL KDVASLYERD KRLWIIAMNE IERKILIWKE 300 EHSQLAREAH ECASSVPQLN KMVSTIQVLV ARYDDLKLKF SEEQAKRKKL YNQVQEAKGN 360 IRVFCRCRPL SKEEASAGHA MVVDFSAAKD GELGILTGGS TKKFFKFDRV YSPRDEQVDV 420 FADASPLVTS VLDGYNVCIF AYGQTGTGKT FTMEGTQQNR GVNYRTLELL FKIAEERKET 480 FTYSISVSAL EVYNEQIRDL LDTSPTSKKL EIRQASEGFH HVPGLTEAKI ENIKEVWDVL 540 HIGSNARAVG SNNVNEHSSR SHCMLCILVK AKNLINGECT KSKLWLVDLA GSERLAKTEV 600 QGERLKEAQN INRSLSALGD VISSLATKSG HIPYRNSKLT HLLQDSLGGD SKTLMFLQIS 660 PSEQDLGETL SSLNFASRVR GVELSPARKQ IDISKLQKVK MMLEKTKQEV GSKDDVIQKL 720 EENFQNLEVK AKGNVQLCKN QQEKINELES QLESKTQLCR QLEKQLLQVS EGMKGKEEIC 780 SNVQRKVKEL ENKLKEHDQS ENVTALHHKV RELENRLKAR TQEFEVHSGM LQQKIAELEE 840 KLRKKEECAT AYCFGERPVT TPYNATVSRV ETTIDDMDPP SLRILNHNGS NRAMNAESES 900 DLLKGTNSLR ELRRKRQTRW RGSENNILLS ASLLEKNSLT AESNKPRLVD SSRAIARITR 960 STKTASIAQR ASFFNSKTNR DQVAGGKESG SKLKIWLR* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01369 | KISc_KHC_KIF5 | 8.0e-102 | 360 | 678 | 324 | + 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 | 6.0e-124 | 360 | 680 | 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 | 9.0e-138 | 360 | 688 | 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 | 2.0e-139 | 366 | 682 | 326 | + Kinesin motor domain. | ||
cd01366 | KISc_C_terminal | 0 | 358 | 684 | 329 | + 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 | CBI40845.1 | 0 | 38 | 796 | 1 | 785 | unnamed protein product [Vitis vinifera] |
EMBL | CBI40845.1 | 0.0000000006 | 865 | 998 | 847 | 979 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002266404.1 | 0 | 9 | 998 | 51 | 982 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002527363.1 | 0 | 1 | 772 | 1 | 788 | ATP binding protein, putative [Ricinus communis] |
RefSeq | XP_002527363.1 | 3e-25 | 830 | 998 | 868 | 1031 | 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 | 357 | 684 | 2 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 347 | 713 | 1 | 365 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 355 | 715 | 1 | 359 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 355 | 715 | 1 | 359 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 355 | 715 | 1 | 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 |
EH194227 | 309 | 493 | 801 | 0 |
FL921658 | 258 | 450 | 707 | 0 |
EL442930 | 266 | 446 | 709 | 0 |
DV990845 | 299 | 415 | 709 | 0 |
ES865056 | 289 | 426 | 709 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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