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Basic Information | |
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Species | Carica papaya |
Cazyme ID | evm.model.supercontig_229.5 |
Family | CBM57 |
Protein Properties | Length: 1169 Molecular Weight: 130637 Isoelectric Point: 7.1178 |
Chromosome | Chromosome/Scaffold: 229 Start: 47674 End: 54242 |
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 | 176 | 318 | 2.5e-29 |
ISVNCGCTNDGVMLGSVSFSKDYCFAGGDTVRTDAIIADEEGVSLYQTARFGNSYYKFQLFEPGSYMVDLHFAEIVFTNGPPGIRVFNVYIQERKVVSSL DIYAQVGEHNPLVISDLSAFVDCEGGLSIRFEGVMGSPIICGI |
Full Sequence |
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Protein Sequence Length: 1169 Download |
MEDADNQWHD PLLLTDVSWQ LSSSQSIELT APPSLKDSTM ADQDSKSEIN DDVSWYNKSS 60 EYVRTQEPGN PIDGRSVLGF SLTSPDLVIC AGSPDIVRNV YGDSPELLKN KNCSVELSLE 120 NGIHGSDSKH TQKTPHVKFS SICQTFSKEL SPESSFSLPP PTATKGSSEN DSLPVISVNC 180 GCTNDGVMLG SVSFSKDYCF AGGDTVRTDA IIADEEGVSL YQTARFGNSY YKFQLFEPGS 240 YMVDLHFAEI VFTNGPPGIR VFNVYIQERK VVSSLDIYAQ VGEHNPLVIS DLSAFVDCEG 300 GLSIRFEGVM GSPIICGISV RKDTEVAETL EVAEMTQGAE SKLEEDTTDC MVEGDYQMLK 360 REYECQRKEL TETRRVLEEL KRENQHKNKE CQKTWNSLRE LQDELMRKSM HVGSLAFAIE 420 GQVKEKSKWF SSLRDLTRKL KIMRMEQIKL SEEAEASKKF LADFNKIGSI IQSRINQQAD 480 LHEDLKKKFV QGAKERKELY NKILELKGNI RVFCRCRPLN PEEVAGGASM AIDFESAKDS 540 ELTVLSNGAP RKTFKFDAVF GPQAGQADIF EDTAPFATSV LDGYNVCIFA YGQTGTGKTF 600 TMEGTEEARG VNYRTLDELF YIIKEREKQH RYNISVSVLE VYNEQIRDLL VPGSQSGAAA 660 KRLEIRQLGE GIHHVPGLVE AQVSNMSEVW EVLQTGSKAR AVGSTNANEH SSRSHCIHCV 720 MVKGENLLNG ECTKSKLWLV DLAGSERVAK TEVQGERLKE TQSINRSLSA LGDVISALAS 780 KCPHVPFRNS KLTHLLQDSL GGDSKTLMFV QISPNENDLG ETLCSLNFAS RVRGVELGPA 840 RKQLDNTEFL RYKQMVEKSK QDMKIKDVQI KKMEDTVHGL ELKIKERDLK NKNLQDKVKE 900 LESQLLIERK LARQHIDTKI AEQQQQMKQH EDQNIAPSRP PLANRLLGSN KNLNEPAYGA 960 VMKEQVNSTR QLAENNYRTP QLASPADSLV KHIDPAEKEN NPEMSEHPQL PKRTGRASIC 1020 TAARRVPAAP VMRRNSLIPL PSLASLPPQF LPFSQCQVDV REGEEEGLEA NCLTEQTNCD 1080 SPKGIKFSRK KLSTILRRSL QKKIQLKSPL QQHLRRGGIN VGTEKVRVSI GSRGRFAHRV 1140 LLGSGRRAGT KEIQQKQNHK EKERGWNV* 1200 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01372 | KISc_KIF4 | 1.0e-97 | 510 | 833 | 344 | + Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during 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 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 | 8.0e-123 | 509 | 833 | 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. | ||
smart00129 | KISc | 7.0e-137 | 509 | 841 | 340 | + Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. | ||
pfam00225 | Kinesin | 5.0e-139 | 515 | 835 | 330 | + Kinesin motor domain. | ||
cd01366 | KISc_C_terminal | 1.0e-180 | 507 | 838 | 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 | 10 | 1157 | 6 | 1191 | kinesin motor protein-related [Arabidopsis thaliana] |
RefSeq | XP_002270779.1 | 0 | 328 | 1168 | 213 | 1053 | PREDICTED: similar to kinesin motor protein-related [Vitis vinifera] |
RefSeq | XP_002300478.1 | 0 | 74 | 1157 | 5 | 1083 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317602.1 | 0 | 70 | 1167 | 24 | 1120 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002532828.1 | 0 | 40 | 1168 | 1 | 1139 | 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 | 507 | 837 | 3 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 496 | 856 | 1 | 355 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 505 | 861 | 2 | 352 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 505 | 861 | 2 | 352 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 505 | 861 | 2 | 352 | 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 | 299 | 566 | 864 | 0 |
DW067034 | 268 | 482 | 749 | 0 |
ES865056 | 288 | 575 | 862 | 0 |
FQ433065 | 263 | 700 | 955 | 0 |
GW337702 | 297 | 696 | 991 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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