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Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s9_137V6.1 |
Family | CBM57 |
Protein Properties | Length: 1415 Molecular Weight: 154713 Isoelectric Point: 6.1288 |
Chromosome | Chromosome/Scaffold: 9 Start: 1011922 End: 1018287 |
Description | Di-glucose binding protein with Kinesin motor domain |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 269 | 410 | 5.6e-38 |
VLAINCGGTLIENESHGISFERDEYYTGGDVLRTEEEVTGVHGAGLYQTSRYGNVSYVFKELPIGNYVVDLHFAEIIFTNGPPGMRVFDVTIQEEKVITE LDVYEEVGSNNALILSVSTSTADGNLTITFEGVIGSPSISAI |
Full Sequence |
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Protein Sequence Length: 1415 Download |
MSANKSDPPI RQLSNRWPFF SEGELKWLLS PKKSAYSEDI EAHMVASMDS TIEEGKRKVE 60 GEIESCPGPM PSESPVAFSL DDKLSWREAG VGGKSPTENT FASLGDRFTK LGIQCSTDIG 120 PLGPRSLLFQ DIAVTSVADK MKDSHAVTTI STADCSPGDA TRSSGDTSGV YQNSGQESFA 180 GKDTQGETSS IAGNDLTPTT EGVQEEIPTS SDHHTIQNHP LSKEGDQQES SDVDDEDEEE 240 EIMNSSVKRM SFAIQDGKQM PKFSADDVVL AINCGGTLIE NESHGISFER DEYYTGGDVL 300 RTEEEVTGVH GAGLYQTSRY GNVSYVFKEL PIGNYVVDLH FAEIIFTNGP PGMRVFDVTI 360 QEEKVITELD VYEEVGSNNA LILSVSTSTA DGNLTITFEG VIGSPSISAI CIRTGPPSSC 420 PAGARKSVAS KSMIEDAGAT APDSEPLGYE QELNRKDAKV RQLPEQKARR HKAKKKTRKS 480 EYEARLKELM DECHEAWISL QDTNRMNEML RDDLCAKSLC VDSLATAVET QLSEMNAIKE 540 RARNEKQKWL TTISKAYKEI MVLKEEQRLL STRTKQWVAS FPDPTVMTTS VRSLLNEHQD 600 LRKKYANECY ERKQLYNKVL ELKGNIRVFC RCRPLSPVEV AANASSVAEF ESAGNGDIVV 660 RNGTAGKKLF KFDRVFSPQD DQADVFADTA PVVVSVLDGY NVCIFAYGQT GTGKTFTMEG 720 NVANRGVNYR TLEELFNIAA QRKGETNYDI SVSVMEVYNE QIRDLLAPPA AQDQSTKKLE 780 IKQAAEGGHH VPGLVEAKVT SMEEVWDVLQ AGSSSRTVGS TRANDHSSRS HCMLCVMVKG 840 ENLVTGEHTK SKLWLVDLAG SERVAKSDAQ GDRLKEAQNI NKSLSALGDV IQALSIKSSH 900 IPFRNSKLTH LLQDSLGGDS KTLMFVQISP NDADLSETLC SLNFASRVRG VELGPARKHL 960 DSNELFKYKQ LAEKTKQESR SKDESVRKLE EKLQAAEAKL KAKDQLCQSL SDKVKENADA 1020 DTQLVNERRA RQTAEAMYRE LKANMEKITA DSKSSMDKLA EKSAAELRQT REALAALEAK 1080 QARESTELAQ ARDALAAELK QTKEALHSAS AAHANEVSRL LQQLQQANET RTTPMQQSTP 1140 STVLTGIQTN IETTLRRPAL VEAGTTPLDR TPTVEYVVKP PDATEVMRNS CTGEVFGNEN 1200 ACPQPINTEA AEAQNKAKGI LKQSSATKYV SPNNAAKRVL GKPRRPGFAV KPPVQVGSLV 1260 RRSHDSLAGS SVTASLSEDE LQRLCGGLDM IATSNTSTFD ASLRTLAHVL ESSTPTSVKS 1320 CSSVARPPAQ PKSVHFRSPL LLPPRDDLEV KEVNSTLRET EPNTRPSSMN STKTARRTLP 1380 TRPLSKAPVS GPHRVVAGPA KAQAVSALRE KRWN* 1440 |
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-97 | 625 | 947 | 328 | + 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 | 4.0e-120 | 625 | 949 | 335 | + 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 | 7.0e-134 | 625 | 957 | 340 | + Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. | ||
pfam00225 | Kinesin | 3.0e-134 | 631 | 951 | 330 | + Kinesin motor domain. | ||
cd01366 | KISc_C_terminal | 3.0e-174 | 623 | 954 | 333 | + 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 | CBI40845.1 | 0 | 286 | 1016 | 1 | 711 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001753390.1 | 0 | 601 | 1015 | 1 | 415 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001784407.1 | 0 | 601 | 1013 | 1 | 413 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002266404.1 | 0 | 265 | 1016 | 73 | 809 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002527363.1 | 0 | 254 | 1016 | 21 | 763 | 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 | 623 | 953 | 3 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 612 | 1005 | 1 | 383 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 621 | 991 | 2 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 621 | 991 | 2 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 621 | 991 | 2 | 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 |
DV990845 | 302 | 679 | 980 | 0 |
ES865056 | 288 | 691 | 978 | 0 |
DT575110 | 288 | 682 | 969 | 0 |
EL442930 | 268 | 711 | 978 | 0 |
FL921658 | 262 | 715 | 976 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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