Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s403_54V6.1 |
Family | CBM57 |
Protein Properties | Length: 1458 Molecular Weight: 160391 Isoelectric Point: 6.3548 |
Chromosome | Chromosome/Scaffold: 403 Start: 301954 End: 308094 |
Description | Di-glucose binding protein with Kinesin motor domain |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 288 | 429 | 2.3e-39 |
ILAINCGGLPLDSEPHGISYSKDDYYTGGEALKTEKEISGVPDARLYQSSRYGNFSYSFRDLPNGNYLVDLHFAEITFRDGPPGMRVFNVAVQEEKVISE LDVYEEVGSNNALILSVCTSTTDGTLSITFEGLTGSPTISAI |
Full Sequence |
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Protein Sequence Length: 1458 Download |
MNGVQPDPPI RELRNRWPFF SEGELKWLLS PKKSGSNFHE DMESHMASSI GNTMQKDGSK 60 SDIAAENRQA PTTRESPFAF ALEDSFDAAA TSAQAVPVMD PRSSFSFEND RCDSLELQAI 120 NDIGSLRPQS LVSEVVATAS GADDTRMPLG VNNRANNFGE CKDDNTSLPT SSSQVQNGHP 180 NAFYKNPFAA GLEAIASDDV QEVASILYNG AETSKGRVML VNSKSEEYDI ADQYFTPTKE 240 CSDQQELSQS SVDVEAEDVV VLASAMKRES FSFEEGTDMR TFSADDVILA INCGGLPLDS 300 EPHGISYSKD DYYTGGEALK TEKEISGVPD ARLYQSSRYG NFSYSFRDLP NGNYLVDLHF 360 AEITFRDGPP GMRVFNVAVQ EEKVISELDV YEEVGSNNAL ILSVCTSTTD GTLSITFEGL 420 TGSPTISAIC IHSALPPSCT RLSRNSAVVK KLIVGTGKTP PNTKPLGCEH EFLLKEKELC 480 HITKHTAPHH ECNNETRKSD YEARVKELTN ECQEAWISLQ HSNRVNDTLR EDLCAKSLCV 540 DSLATAVENQ LSEMNAIKER TCQERQRWFT QVAAAYEEIV ALKKEQQLLL NNANEWVASF 600 PDPSIVTRSV QSLLTEHQDL RRKYANESYE RKQLYNKVLE LKGNIRVFCR CRPLSQAELL 660 ANSVSVTEYE SASSGDIVVR HGAAGKKLFK FDRVFSPQDD QCKPVALRAR SCTLAVKCLH 720 LILISDTLPF TADVFADTAP VVVSVLDGYN VCIFAYGQTG TGKTWTMEGS TGNRGVNYRT 780 LEELFTIAAQ RKGEINYDIS VSVMEVYNEQ IRDLLVPVAA QDQPTKKLEI KQAAEGGHHV 840 PGIVEARVTS MAEVWSVLQA GSNSRTVGST RANDHSSRSH CMLCVMVRGE NTITGEVTKS 900 KLWLVDLAGS ERVAKSDAQG DRLKEAQNIN KSLSALGDVI QALAMKSSHV PFRNSKLTHL 960 LQDSLGGDSK TLMFVQISPN EADLSETLCS LNFASRVRGV ELGPARKHLD SNELFKYKQL 1020 AEKSKQESRL KDELIRKLEE KLQTTDTKLK AKDQMCQALS EKLKEMGDLD AQLLNERRAR 1080 LVADASCRDQ KATMEKLVVE SKLSLDKLAE KLASESRHAK DASAAEARQA REALELVQSK 1140 EALEMELKEV KEALHSASAT HAKEVSRLMQ QLKANAICTT PMQESTRVNG LQTQVEALLR 1200 RPALVEAGSG SHAIDRTPTV EYVVKPPNIS EVMRNSCTGE VFANENAYPT QNTDVSDVQV 1260 RVKGILKTSN TKYVSPNNPP KRVPGRSRRS GFAVKPAVQV NSLVRRSHDS VSSSCNSLSA 1320 SFTEEELQRL CGGLDLIATS NTSTFDASLQ TLAQVLESTP INKGPSSRFP QPKSVHFRSP 1380 LLLPPRKDLE MRDGNSPVQE SENNRPPTTS NVLATKTARR TTLPAKPSSR SSAAGSNRVV 1440 APVKAQALPV LREKRWN* |
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-93 | 644 | 996 | 358 | + 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 | 9.0e-114 | 644 | 998 | 365 | + 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-129 | 650 | 1000 | 360 | + Kinesin motor domain. | ||
smart00129 | KISc | 3.0e-130 | 644 | 1006 | 370 | + 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 | 1.0e-166 | 642 | 1003 | 363 | + 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 | 305 | 1066 | 1 | 712 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001753390.1 | 0 | 620 | 1064 | 1 | 415 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001784407.1 | 0 | 620 | 1062 | 1 | 413 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002266404.1 | 0 | 280 | 1066 | 69 | 810 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002317602.1 | 0 | 304 | 1078 | 145 | 870 | predicted protein [Populus trichocarpa] |
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 | 642 | 1002 | 3 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 631 | 1033 | 1 | 367 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 640 | 1041 | 2 | 369 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 640 | 1041 | 2 | 369 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 640 | 1041 | 2 | 369 | 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 | 297 | 733 | 1029 | 0 |
ES865056 | 288 | 740 | 1027 | 0 |
DT575110 | 285 | 734 | 1018 | 0 |
EL442930 | 268 | 760 | 1027 | 0 |
FL921658 | 262 | 764 | 1025 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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