Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_180169g0010 |
Family | CBM57 |
Protein Properties | Length: 1351 Molecular Weight: 149248 Isoelectric Point: 5.1655 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 302 | 440 | 6.5e-32 |
MCINAGDQQPLGSAFQQDLYYVGGDVLRTDETIVEKEGSSVYQTARFGNFSYIISDLPAGDYFVDLHFAEIVFTNGPAGMRVFDVFIQEDKILSELDIYA RVGSNTPLVLMDAPAHVLDGGTLTLRFEAVTGSPIVCAI |
Full Sequence |
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Protein Sequence Length: 1351 Download |
MDFTVKARDR GFCLGFSVLV EIDAFVCLCI CICLCLCVVL CKYLDNHRPH PRLFSMENSF 60 PSLLMESWSP GQGVSPDTVV CAGSPDMELD SEAFSFNANA ASMEQQSLTQ AMFPEVSPSS 120 AAEGWSEILL NTPLAKEDEK KPQIDSEAIE LPESGVESQT LGSIAIPCSE ACDLYDSPSD 180 ACNVGGNPSS DTCNVGSNPS SDTCNVGGNP SSDTCKVGSN PSSDTCNVGD GDQSDHNHMD 240 FENLDGDQSD HNGMDFENPD GSQSDDVDMD FENPDDTTLC YRHLKLVTGY ENIEMPKEDA 300 VMCINAGDQQ PLGSAFQQDL YYVGGDVLRT DETIVEKEGS SVYQTARFGN FSYIISDLPA 360 GDYFVDLHFA EIVFTNGPAG MRVFDVFIQE DKILSELDIY ARVGSNTPLV LMDAPAHVLD 420 GGTLTLRFEA VTGSPIVCAI CIRKAQSLGR KGHKKPIIIV EDDLKQTNQD QELAVVEEGY 480 NQKSKGRSCK SVVEYEKKIE ELRKDYELKK KECHEAWMSL EDSNRQLEKL RNELMRKSLH 540 VGSLAHAVEG QVNELRDLQD QHEREKKLWA LSVNQLNDKI KVLKSEYVKL LDEANCYASA 600 LPDISEMTSS VQALVNQHED LKVQYTELKT KFVEESKERK QLYNKLLELK GNIRVFCRCR 660 PLSAQEVAEG AVSVAEFDTA KDSEISIRTN GAPKKVFKFD SVFTPEDDQV DVFADTAPVV 720 VSVLDGYNVC IFAYGQTGTG KTFTMEGTEE NRGVNYRTLE ELFRVANERK GQFKYDISVS 780 VLEVYNEQIR DLLASPQPGQ TVKKLEIKQM AEGIHHVPGL VEAQVHSMNE VWEVLQTGSS 840 ARAVGSTNAN EHSSRSHCIL YVMVRGENSI NGECTRSKLW LVDLAGSERV AKTDVQGDRL 900 KEAQNINKSL SALGDVISSL ATKNSHIPFR NSKLTHLLQD SLGGDSKTLM FVQISPNEND 960 ISETLCSLNF ASRVRGIELG PARKQFDSTE LLKYKQMVEK AKQDGKSKEG SMKKMEETIQ 1020 NLEAKLKGRD QANKLLHDKV KELEGQLANE RKARLNLESK LKEQQQQAGK VSEKPPLIRQ 1080 FGGVRTVNET NVLSKDLVNL SDALTENKQM LNAMECNGKP QEGEFPLKNG LIDPYSKGQK 1140 ENKSELYDDQ NVKPIPRKTG RASMCTTARR TSIVPLAARR LTMVPLPVTR NEGILDVNTS 1200 SSQTNEDEQA NNKESFTANS KEPVTASSKE PSTANKAPVL LPTATPVSLR GLRNSNTLNK 1260 LRQSINKKVH FNSPLLKGPN DGTSTAAPSS TSGGQKLPPI DTTRIRRVSS TRAWGRISGT 1320 GTISAQRVLC ANRGGIKPTV QLREKERGWN R |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01369 | KISc_KHC_KIF5 | 6.0e-99 | 652 | 977 | 331 | + 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 | 7.0e-121 | 652 | 975 | 334 | + 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 | 9.0e-139 | 652 | 983 | 339 | + Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. | ||
pfam00225 | Kinesin | 4.0e-140 | 658 | 977 | 329 | + Kinesin motor domain. | ||
cd01366 | KISc_C_terminal | 0 | 650 | 980 | 332 | + 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. |
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 | CBI40845.1 | 0 | 316 | 1074 | 3 | 736 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002266404.1 | 0 | 238 | 1074 | 10 | 834 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002300478.1 | 0 | 313 | 1187 | 122 | 965 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317602.1 | 0 | 302 | 1350 | 130 | 1120 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002532828.1 | 0 | 313 | 1350 | 163 | 1138 | 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 | 650 | 979 | 3 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 639 | 1033 | 1 | 385 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 648 | 1017 | 2 | 365 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 648 | 1017 | 2 | 365 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 648 | 1017 | 2 | 365 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |