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Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.008G093800.1 |
Family | CBM57 |
Protein Properties | Length: 1071 Molecular Weight: 120718 Isoelectric Point: 7.0954 |
Chromosome | Chromosome/Scaffold: 08 Start: 23601301 End: 23607135 |
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 | 80 | 223 | 1.4e-30 |
MFINAGGEALNETDSSMKFLGDNYFEGGNVMQTNEPINEAGDCPFIYWSARIGSFSYRFNNLPPGDYFVDLHFAEIINTNGPKGMRVFNVYMQEEKVLSD FDIFSVVGANKPLQVVGLRVSVKEDGLIALRFEGVIGSPMVCGI |
Full Sequence |
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Protein Sequence Length: 1071 Download |
MDNAQLNAFL QNPETHFPDF SITRGFDSEK CDLALNLDNP TSAMDEGEEE SFADLMLCDS 60 NSRLIPSGFS KSNCTDEIVM FINAGGEALN ETDSSMKFLG DNYFEGGNVM QTNEPINEAG 120 DCPFIYWSAR IGSFSYRFNN LPPGDYFVDL HFAEIINTNG PKGMRVFNVY MQEEKVLSDF 180 DIFSVVGANK PLQVVGLRVS VKEDGLIALR FEGVIGSPMV CGICVRKTQN IPVTQGLQEY 240 LKCNNCAAEI EVSSAQMKLV RTKVTDKYEK KIQELTTQCQ LKTHECHEAW MSLTAANEQL 300 EKVRMELDNK IFLTRTLDDT VGKQAENLKN ITSSYEHYKK YWAAEVNNLR EKIKIMKNEH 360 AQLSHEAHAC AESIPELNKM VTGVQALVEQ CEDLKVKYSE EQAKRKELYN QIQETKGNIR 420 VFCRCRPLSK EEISAGSAQV VDFDAAKDGD IGILTGASTR KTFKFDRVYT PKDNQVDVFA 480 DALPLVTSVL DGYNVCIFAY GQTGTGKTFT MEGTDQNRGV NYRTLEQLFH IAKERSETFM 540 YNISVSVLEV YNEQIRDLLS TSPTSKRLEI KQSAEGFHHV PGIVEAQVEN IKEVWNVLQI 600 GSNSRAVGSN NVNEHSSRSH CMLCIMVKSK NLMTGECTNS KLWLVDLAGS ERLAKTDAQG 660 ERLKEAQNIN KSLSALGDVV YALATKSSHI PYRNSKLTHL LQDSLGGDSK TLMFVQISPS 720 ERDISETLSS LNFATRVRGV ELGPAKRQVD TSELQKMKTM LEKARQESRS KEESLKKLEE 780 SLQNLESKAK GRDQVYRTQQ EKIKELEGQL ELKNSMHNQS EKQLSQLSDR LKGKEEISTA 840 LQLKVKELEA KIKERHQSDS ASYQQKVKEL ENKLKEQVQE SESHSLSLQL KIKELERKLK 900 EQEQNPDSIF LRQKIKELED RLREQEQQLQ CALARSFADT IAASPSEGKW RKDDESMNEA 960 EPHILRSSNS TSSRPLSHGL KQPRISDLVH EPRKKRYSRS GETENNMVMA ASLADKRARK 1020 SDPPKIARGV KTTKPGSLAA QGPVAHKRVI NRGQVHGAME RDSKKKIWSR * 1080 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01369 | KISc_KHC_KIF5 | 2.0e-106 | 418 | 736 | 325 | + 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-122 | 418 | 738 | 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 | 1.0e-139 | 418 | 746 | 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 | 5.0e-143 | 424 | 740 | 326 | + Kinesin motor domain. | ||
cd01366 | KISc_C_terminal | 0 | 416 | 743 | 330 | + 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 | CAN63715.1 | 0 | 1 | 1061 | 1 | 1070 | hypothetical protein [Vitis vinifera] |
EMBL | CBI40845.1 | 0 | 96 | 1070 | 1 | 979 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_179846.2 | 0 | 77 | 1070 | 87 | 1093 | kinesin motor protein-related [Arabidopsis thaliana] |
RefSeq | XP_002266404.1 | 0 | 1 | 836 | 1 | 840 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002532381.1 | 0 | 1 | 1068 | 1 | 1073 | 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 | 415 | 742 | 2 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 405 | 780 | 1 | 376 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 413 | 780 | 1 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 413 | 780 | 1 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 413 | 780 | 1 | 368 | 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 |
FL921658 | 258 | 508 | 765 | 0 |
EL442930 | 265 | 504 | 766 | 0 |
DV990845 | 299 | 472 | 766 | 0 |
EH194227 | 309 | 551 | 859 | 0 |
ES827277 | 264 | 577 | 839 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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