Species | Phytopythium vexans | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Oomycota; NA; ; Pythiaceae; Phytopythium; Phytopythium vexans | |||||||||||
CAZyme ID | EPrPVT00000013989-p1 | |||||||||||
CAZy Family | AA17 | |||||||||||
CAZyme Description | Kinesin | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 29716; End:36491 Strand: + |
MDAMTAADDA AARASLLRPA YDDDSASSSD DEHEDTSDVV MLVSVPEMEA GGQPHARASA | 60 |
EQASAPPDRP PRRRTRLLMP VMALCAVSMA LTVGGYAMAR YSVRRAASSL EGEFDLHKLT | 120 |
SAMHPNASTI DSPFYQRSSA FDRSVDRGRG VVICLYDDIL AMGLSLIREL RCHGNQELIQ | 180 |
VYHCLPDEIS NANRALLLRA DDRLEIVDVC SDLIERKLMS RDMADKFRNW WIKPLAAFHT | 240 |
DIREVMLLDV DDVLMKDPAV LRESEGYKKT GTTFFYDRVI GHCDKFFNKR DGYLQYLTKV | 300 |
LKKFDYEAFN LTGVISAWPN NDMKDHPDSL CGSILQYMPV ESDTPEMLYV NGKALIDPFP | 360 |
QGVDYVRKAR TNNMFNLVPT HMTPRQTRHE VERRQNTDKV TYHMECLTGL GSTPLPSSFA | 420 |
GHLLRRRLFF LGITTGVEGA LRHCETYELR RLAIDDASED RLLMRGSHMA LTGSAMLSFP | 480 |
PFGGQDVAFD PAWLVRAMQV RPSVFASPAY RRSKTFDKDV GRDKGIVVCM HNGNMAMGLS | 540 |
LIRELRCHGN QELIQVYHCL NEISNNNRAQ LLRTDDRLEI VDVCSDFIER KIMSKDLAVN | 600 |
FRNWWIKPLA VIHTDIREVM LLDADDVLMK DPAVLRESEG YKRTGTTFFY DRVASSCSKF | 660 |
FNRRDIFTPY LTKLFHKFDY EAFNLTEYAP SDHLLNSFAY AGKTCHEQDS SMVLIDKSRM | 720 |
GAAREIMWWF ITKERFRFTY SWGDKETFWL SYELAHVDYF FSPWGVSVIS SWPNSDMQSH | 780 |
PDSLCGSIVQ YMPVNDEMAE MLYVNGKALL HPFPQGVSRV ANAKPNNMFN LVPTHMTPRQ | 840 |
PRREVEQRHN TDRVTYEVEC LTGLGSVPLP KSFAGHLLRR RLFFLAISTG VNGALQHCET | 900 |
YEQPVAGRRL DFAGTLRGGA MHRGGHPARV SVSVSSVSPS SSASSSRRGS LGASPASSFF | 960 |
SPARMQRLSL SSSSLGGHGG SGLASSSSSS SGLPPRGSNF KVVIRVRPPL PRELHGDHPF | 1020 |
QNVIGVDASG HVLTVSENLS ALAVGSGGGG AGDDGVAGDE SGSSAAGIAA YGHHVFSFDH | 1080 |
VYDQLCTQRA VYENTAKAVV ESSLEGYNAT IFAYGQTGTG KTYTMEGFNS GAPALGVDVE | 1140 |
ARGIIPRAIE QIFGHIQQHV SPRLRFLVRA SYLQIYNESI SDLLKPERAN LTIREDKRRG | 1200 |
VFVEGLSEWV VRSPEEIYGL MERGGAMRAT GSTKMNELSS RSHAVFIIIA EQSRTSYVDA | 1260 |
RGNDMSPEDF TALAQAFQAR HGQAQAQGGS GKLPPKLESM VRQSFKVGKL NLVDLAGSER | 1320 |
VRLSGATGQR LEESKKINQS LSALGNVISA LTDARGRQHI PYRDSKLTRI LEDSLGGNCK | 1380 |
TTMMAMISPA LEAMTESLST LKFANRAKNI KNEAKVNEDL DQKSLLRKYE RELRRLRAEL | 1440 |
EEKSRNVVDK RRLLELDEQR RRAEEDKMAA IRALEERSRE FMREKEEKKK LEQRISMLTS | 1500 |
QMLMSNQRRL PLEHQDRIRK EYECRLADLE KERETIEEEK AQVDRYKQLL LKQRDIMIAL | 1560 |
TQRLNERDEQ ITALQDELDA YDRHQKELEE KLDEKTAHLI HLQRVTMEHN ASSPGKIDAE | 1620 |
LVKALGDWGA ASSGSAGLNS MAASPPVAPE LLITHKQFRP HAAEQVIMNS NNTLTSGSGG | 1680 |
GALLSADEKI QELKALVDTQ GAEQLRLAKE LEDVKSEKVS VEFVLRERVE KLVQIELAAR | 1740 |
LKSVETGGGG GNNSDEQERA RQLQRQLEVV AMENRRLRDQ LASPRGGDRA GELEARCETL | 1800 |
VKERRAVQTI MEHKIKALVN AVSEASDATL RSAGGVERLG ESAAWLTREV HALQRLVNAS | 1860 |
ILALRNADAG SNAVVGSSNS RPADGAARTT AVEQKLSRTS VAVPTGAPQL PTSYGKEGML | 1920 |
PQKTSSSAGL SVDELIQQRR EQLQRERQDN MG | 1952 |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT71 | 524 | 786 | 3.2e-45 | 0.9659090909090909 |
GT71 | 148 | 293 | 2e-25 | 0.5303030303030303 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
214526 | KISc | 3.53e-138 | 999 | 1417 | 1 | 335 | Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. |
395169 | Kinesin | 1.06e-135 | 1073 | 1410 | 39 | 326 | Kinesin motor domain. |
276812 | KISc | 1.89e-122 | 999 | 1408 | 1 | 326 | Kinesin motor domain. 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. |
276822 | KISc_KIF3 | 7.84e-118 | 999 | 1410 | 2 | 334 | Kinesin motor domain, kinesins II or KIF3_like proteins. 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. |
276823 | KISc_KIF4 | 1.50e-110 | 1001 | 1411 | 4 | 341 | Kinesin motor domain, KIF4-like subfamily. 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CCA15193.1|GT71 | 9.71e-107 | 519 | 899 | 127 | 516 |
CCA22801.1|GT71 | 2.60e-105 | 490 | 898 | 36 | 430 |
BAP68847.1|GT71 | 9.13e-89 | 466 | 808 | 13 | 358 |
AIG56397.1|GT71 | 5.95e-69 | 503 | 882 | 72 | 452 |
AIG56246.1|GT71 | 1.10e-55 | 524 | 869 | 65 | 435 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3B6U_A | 1.44e-82 | 1076 | 1430 | 70 | 372 | Crystal structure of the motor domain of human kinesin family member 3B in complex with ADP [Homo sapiens],3B6U_B Crystal structure of the motor domain of human kinesin family member 3B in complex with ADP [Homo sapiens] |
1GOJ_A | 2.17e-80 | 1076 | 1420 | 49 | 340 | Structure of a fast kinesin: Implications for ATPase mechanism and interactions with microtubules [Neurospora crassa] |
3B6V_A | 2.53e-79 | 1076 | 1429 | 70 | 395 | Crystal structure of the motor domain of human kinesin family member 3C in complex with ADP [Homo sapiens],3B6V_B Crystal structure of the motor domain of human kinesin family member 3C in complex with ADP [Homo sapiens] |
7A3Z_A | 1.28e-75 | 1076 | 1438 | 49 | 355 | Chain A, Osmotic avoidance abnormal protein 3 [Caenorhabditis elegans] |
2Y5W_A | 1.04e-73 | 1075 | 1432 | 52 | 355 | Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer [Drosophila melanogaster],2Y5W_B Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer [Drosophila melanogaster],2Y65_A Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer-tail complex [Drosophila melanogaster],2Y65_B Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer-tail complex [Drosophila melanogaster],2Y65_C Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer-tail complex [Drosophila melanogaster],2Y65_D Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer-tail complex [Drosophila melanogaster] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
sp|F1QN54|KIF3B_DANRE | 2.41e-82 | 1075 | 1444 | 57 | 374 | Kinesin-like protein KIF3B OS=Danio rerio OX=7955 GN=kif3b PE=2 SV=1 |
sp|O15066|KIF3B_HUMAN | 1.10e-81 | 1076 | 1444 | 57 | 373 | Kinesin-like protein KIF3B OS=Homo sapiens OX=9606 GN=KIF3B PE=1 SV=1 |
sp|Q61771|KIF3B_MOUSE | 1.48e-81 | 1076 | 1444 | 57 | 373 | Kinesin-like protein KIF3B OS=Mus musculus OX=10090 GN=Kif3b PE=1 SV=1 |
sp|P46871|KRP95_STRPU | 3.28e-81 | 1076 | 1443 | 56 | 371 | Kinesin-II 95 kDa subunit OS=Strongylocentrotus purpuratus OX=7668 GN=KRP95 PE=1 SV=1 |
sp|P46872|KRP85_STRPU | 1.42e-80 | 1076 | 1449 | 58 | 380 | Kinesin-II 85 kDa subunit OS=Strongylocentrotus purpuratus OX=7668 GN=KRP85 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000065 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.