| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01016220001 |
| Family | GT77 |
| Protein Properties | Length: 1332 Molecular Weight: 149309 Isoelectric Point: 6.6737 |
| Chromosome | Chromosome/Scaffold: 13 Start: 6383670 End: 6407474 |
| Description | Armadillo/beta-catenin repeat family protein / kinesin motor family protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT77 | 1094 | 1311 | 0 |
| QDKVLVIAEDYATLYAVNDRWPGHAVLVPPAPDAQVAHKFGSQGFFNFTSRRPRHLLYILELGYNVMYNDVDMVWLADPFPYLQGDHDVYFTDDMTAVKP LNHSHDLPPPGKKGRTYICSCMIFMRPTDGAKLVMKDWIEELQAQPWSNAKKSNDQPAFNWALNRTAAQVDLYLLPQVAFPTGGLYFKNQTWVQETKGLH VIIHNNYITGFEKKIKRF | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1332 Download |
| MGFKCLVFLL LSSMGGTYVE GELKADSGRV RVAVRLRPRN ADDLLSDADF ADCVELQPEM 60 RRLKLRKNNW SSESYRFDEV FTESASQRRV YEVVAKPVVE SVLNGYNGTV MAYGQTGTGK 120 TYTLGRLGND DASERGIMVR ALEDIIANTS PTSDSVEISY VQLYMESIQD LLAPEKINIP 180 ITEDPRTGEV SLPGAAVVKI RDIDHFLQQL QIGEANRHAA NTKLNTESSR SHAILMVYVR 240 RSVHKKVEDE ISSQEKVNRS DVPGGSRIPI VRKSKLLIVD LAGSERVDKS GSEGQLLEEA 300 KFINLSLTSL GKCINALAEN SPHIPIRDSK LTRLLRDSFG GSARTSLIIT IGPSARHHAE 360 TTSTIMFGQR AMKIVNMVKL KEEFDYESLC RKLEKQVDQL TEEIERQQKL RKNDTDELEK 420 RLIECQNTFA EAEKNLVTRS EFLEKENTRL ELEMKDFLNE LNHQKDLNVL MRDEVASLEM 480 SLKHSKQYQL ENSTCQQVLA DTTQMYEKKI AELIKQLGDE RARYETAGEQ LDVIKKLLSE 540 SQQKIQQQKT ENSTYQKALA DTTQMYEKKI AELTKQLEDE HARFEGAEKQ LDEAKNLLSC 600 HQKPMQQDEI DELKMRLHEM GRHQELSVNE LQSLQSEYND LLSEKATLTE ELHAVNQTLS 660 VEEKQRKTIE NELVKLKKLV LENDHDFEDK KSYVKESIGK ESSAFGAPVG LHKSNPSRET 720 ISGQRATIAK ICEEGKIFLI LALLTSEDLD VQIHAVKVVA NLAAEDINQE KIVEEGGLDA 780 LLLLLRSSKS TTILRVASGA IANLAMNELN QGLIISKGGG QLLANMASKT DDPQTLRMVA 840 GAIANLCGNE KLHMMLKEEG GIKALLGMVR SGNSDVIAQV ARGVANFAKC ESRGIIQGHR 900 KGRSLLVEDG ALTWLISNCN TASASTRRHM ELALCHLAQN ENNAQDFKSS GGVRELKRIA 960 AESTREDIQN LAKKTLKSTP FQAEIHQHLL SDSYPISARS SPNWGRSISV FGRTGLLVLL 1020 TLVVVLGVVL PGMRAPDGLF GGSKVSVSKW REYTLEEAVP FAAKNGTLIV CAVSQPYLPF 1080 LNNWLISISR QKHQDKVLVI AEDYATLYAV NDRWPGHAVL VPPAPDAQVA HKFGSQGFFN 1140 FTSRRPRHLL YILELGYNVM YNDVDMVWLA DPFPYLQGDH DVYFTDDMTA VKPLNHSHDL 1200 PPPGKKGRTY ICSCMIFMRP TDGAKLVMKD WIEELQAQPW SNAKKSNDQP AFNWALNRTA 1260 AQVDLYLLPQ VAFPTGGLYF KNQTWVQETK GLHVIIHNNY ITGFEKKIKR FRDFGLWLVD 1320 DYALESPLGR I* 1380 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd01374 | KISc_CENP_E | 1.0e-81 | 30 | 374 | 350 | + Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation 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. | ||
| cd01369 | KISc_KHC_KIF5 | 1.0e-98 | 30 | 374 | 350 | + 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. | ||
| smart00129 | KISc | 9.0e-107 | 29 | 376 | 358 | + Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. | ||
| cd00106 | KISc | 2.0e-108 | 29 | 372 | 357 | + 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 | 6.0e-111 | 35 | 374 | 350 | + Kinesin motor domain. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003777 | microtubule motor activity |
| GO:0005515 | protein binding |
| GO:0005524 | ATP binding |
| GO:0007018 | microtubule-based movement |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI31422.1 | 0 | 1 | 1331 | 1 | 1331 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002273191.1 | 0 | 25 | 606 | 54 | 635 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002273191.1 | 0.00000000005 | 546 | 611 | 515 | 580 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002273191.1 | 0 | 608 | 989 | 715 | 1096 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002315323.1 | 0 | 23 | 986 | 98 | 1063 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1goj_A | 0 | 23 | 399 | 1 | 355 | A Chain A, Structure Of A Fast Kinesin: Implications For Atpase Mechanism And Interactions With Microtubu |
| PDB | 2y65_D | 0 | 30 | 396 | 13 | 355 | W Chain W, Crystal Structure Of Drosophila Melanogaster Kinesin-1 Motor Domain Dimer-Tail Complex |
| PDB | 2y65_C | 0 | 30 | 396 | 13 | 355 | W Chain W, Crystal Structure Of Drosophila Melanogaster Kinesin-1 Motor Domain Dimer-Tail Complex |
| PDB | 2y65_B | 0 | 30 | 396 | 13 | 355 | W Chain W, Crystal Structure Of Drosophila Melanogaster Kinesin-1 Motor Domain Dimer-Tail Complex |
| PDB | 2y65_A | 0 | 30 | 396 | 13 | 355 | W Chain W, Crystal Structure Of Drosophila Melanogaster Kinesin-1 Motor Domain Dimer-Tail Complex |
