| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G334142_T01 |
| Family | GT2 |
| Protein Properties | Length: 919 Molecular Weight: 101773 Isoelectric Point: 8.1732 |
| Chromosome | Chromosome/Scaffold: 5 Start: 206307947 End: 206316209 |
| Description | cellulose synthase-like A3 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT2 | 578 | 704 | 2.7e-23 |
| WRWASKGVNVKYEVRDSRRGYKAGALREGMKRAYARGCDLVAIFDADFQPEPDFLWRAVPFLLHNPDLALVQARWKFVNADECLMTRMQEMSLDYHFAVE QEVGSSTYAFFGFNGTAGVWRISALNE | |||
| Full Sequence |
|---|
| Protein Sequence Length: 919 Download |
| MASSLADFAQ VLEASRLHEH GVTSGGLRSG AGGIATSRAR HNLRRASCVG GQAKATRGRR 60 QSGSIRRFKS GEIMIRVPME TSEAAAAHPQ KDSVKVAVNI RPLITVELQD GCTDCVTVTP 120 GEPQVQIGPH VFTFDHVYGS SGPSSSLIFE QCVHPLIDAL FSGYNATVLA YGQTGSGKTY 180 TMGTDYSGEG NCGGIIPQVM DTIFRKVDTS KDGSEFLIRV SFIEIFKEDV FDLLDANQAA 240 VRLDAGSMAK ASAPGRVPIQ IRETATGGIT LAGVTEAEVK SKEEMASYLT RGSSSRATAS 300 TNMNRQSSRS HAIFTICVEQ KRTSGTSDKS ANGDYDILSS KFHLVDLAGS ERAKRTGADG 360 HRLKEGIHIN KGLLALGFFK CISMHSPADI KAEETINTLK NANRARNIQN KAVVIRDPAT 420 AEMQKLRSQL EQLQTELLFS RSGSAALEEL QLLQKKVSLL ELKNSELNNE LKEKELSYEQ 480 LAERARAAQL ERDQLMLKIE SVRNGKSLDD IENIDNDQDM DLLKGYISKI QQLESELMRQ 540 NFSNACRHGL HDQLAMDQDI FLNELGSGCE ELVRAECWRW ASKGVNVKYE VRDSRRGYKA 600 GALREGMKRA YARGCDLVAI FDADFQPEPD FLWRAVPFLL HNPDLALVQA RWKFVNADEC 660 LMTRMQEMSL DYHFAVEQEV GSSTYAFFGF NGTAGVWRIS ALNEAGGWKD RTTVEDMDLA 720 VRASLKGWKF VYIGDLMKVT LWKKIHVIYN FFLVRKIVAH AVTFVFYCIV IPTTVLVPEV 780 QVPKWGSVYI PTVITLLSAV ATPRSAHLVV FWTLFENVMS LHRTKATFIG LLEAGRVNEW 840 VVTEKLGDAL RTKVPGKKPR MRIGDRLHVL ELGVAAYLLF CGCYDIAFGN NRYYIFLFLQ 900 SIAFFIVGIG YVGTFVPH* 960 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00106 | KISc | 2.0e-85 | 93 | 406 | 359 | + 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. | ||
| cd06437 | CESA_CaSu_A2 | 1.0e-86 | 570 | 736 | 167 | + Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex. Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal. | ||
| pfam00225 | Kinesin | 8.0e-87 | 100 | 408 | 354 | + Kinesin motor domain. | ||
| smart00129 | KISc | 2.0e-94 | 93 | 414 | 366 | + Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. | ||
| cd01372 | KISc_KIF4 | 5.0e-130 | 93 | 409 | 358 | + 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. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003777 | microtubule motor activity |
| 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 |
| GenBank | EEC73989.1 | 0 | 79 | 570 | 1 | 533 | hypothetical protein OsI_08901 [Oryza sativa Indica Group] |
| GenBank | EEE57794.1 | 0 | 79 | 570 | 1 | 533 | hypothetical protein OsJ_08347 [Oryza sativa Japonica Group] |
| RefSeq | XP_002311972.1 | 0 | 509 | 918 | 75 | 520 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002315357.1 | 0 | 509 | 918 | 84 | 529 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002452565.1 | 0 | 79 | 570 | 1 | 529 | hypothetical protein SORBIDRAFT_04g028210 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3zfc_A | 0 | 94 | 414 | 10 | 343 | A Chain A, Crystal Structure Of The Kif4 Motor Domain Complexed With Mg-amppnp |
| PDB | 3zfd_A | 0 | 94 | 414 | 10 | 343 | A Chain A, Crystal Structure Of The Kif4 Motor Domain Complexed With Mg-amppnp |
| PDB | 4a14_A | 0 | 90 | 377 | 9 | 280 | A Chain A, Human Kif7, A Kinesin Involved In Hedgehog Signalling |
| PDB | 2xt3_A | 0 | 90 | 377 | 9 | 280 | A Chain A, Human Kif7, A Kinesin Involved In Hedgehog Signalling |
| PDB | 3b6u_B | 0 | 92 | 427 | 21 | 372 | A Chain A, Crystal Structure Of The Motor Domain Of Human Kinesin Family Member 3b In Complex With Adp |
