Basic Information | |
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Species | Medicago truncatula |
Cazyme ID | Medtr5g088330.1 |
Family | GH5 |
Protein Properties | Length: 1552 Molecular Weight: 177684 Isoelectric Point: 8.1724 |
Chromosome | Chromosome/Scaffold: 5 Start: 37283827 End: 37298839 |
Description | Cellulase (glycosyl hydrolase family 5) protein |
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 |
GH5 | 111 | 416 | 4.7e-35 |
DDSTGERVKLVCGNWAGHLQPMIPEGLDRIPLKELVGELVKNRFNCVRLTYAVYMWTRHAHGIVNNTFNYLDAPEVVAGIAKYNPSILKMTHIEAFDAVV NELGARNVKVLLDNHVSEPKWCCNDDDDNGFFHDQHFDPQEWIHGLTLAAKHFYGHQPIVAMSLRNELRGPRQNLRDWYKYMSHAALVIHKTNPNVLVVI SGLNYDTELQFLRNNPLKIDLGEKMVYEAHLYSWSGIGTLKLKEFWSKQPLNRICAENIEGLDQSAGFLTSGKNAVPLIITEFGFDQTGSSVEDNRFLTC LQTYLV |
Full Sequence |
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Protein Sequence Length: 1552 Download |
MLNKKHQWSS GRIVPCHGTD PGSIPGWCIS ESCDENSCGV GYITFPETWM KKLLLRNDET 60 FSNRLKEPME VVEEIKLLKS FQSLILLLFV FTSSSHSNAY PLSTQSRWII DDSTGERVKL 120 VCGNWAGHLQ PMIPEGLDRI PLKELVGELV KNRFNCVRLT YAVYMWTRHA HGIVNNTFNY 180 LDAPEVVAGI AKYNPSILKM THIEAFDAVV NELGARNVKV LLDNHVSEPK WCCNDDDDNG 240 FFHDQHFDPQ EWIHGLTLAA KHFYGHQPIV AMSLRNELRG PRQNLRDWYK YMSHAALVIH 300 KTNPNVLVVI SGLNYDTELQ FLRNNPLKID LGEKMVYEAH LYSWSGIGTL KLKEFWSKQP 360 LNRICAENIE GLDQSAGFLT SGKNAVPLII TEFGFDQTGS SVEDNRFLTC LQTYLVGRDL 420 DFEDKLQLDE SFGVVDATWH KLRYPNFADK FQLLQRKNQD PTSKVSEAYI MYHPLTGQCG 480 QVNDKNELEI GSCENQTRWI YNGSQILLND SKKCLTAIGE GLPVAISDDY ENKNSSWKSE 540 SLSRLHLATV DQNGKHLCLH KDYNSSFVVT SKCICINDDS LCLDDPQSQW FQLVFPHEKN 600 MKHQWSSGRI VPCHGTDPGS IPGWYLEREK SFVFQTLWNG RFYKLEREKK QIRRRRRKME 660 NLVNSFSVLE LDADDSTIQP LSLPSGSSGK KANGKALPVK IEKQDQHNPY LSDYRLPLVW 720 IDLEMTGLNI ELDRILEIAC IITDGNLTKS VEGPDLVIHQ TKECLDGMGE WCKSHHAASG 780 LTKKVLQSTI SEREAEEQVI EFVKKHVGGT YKPLLAGNSI YVDLQYMKKY MPELAGIFSH 840 VVVDVSSISA LCIRWYPKDQ KKVPTKQKRH RALDDIRESI EELKYYKANI FKPKAENTLS 900 QMPTPEPPQT IDLDKDQGDN VQKKKKRKVR EAATKNVSNA DDPNAEDPGK RKPCRPKSWV 960 WDHFIKEKGR AMCKWCKNAS YAADSHNSGT SNLSTHLRKQ CKKFPKHLDP NYDPNQTILS 1020 LQDSKGTSSN STIVAVHFDV DVSRQALARM IIVDELPFSF VENEGFRYFM SVTQPRLPLP 1080 GRLAIARDCL NLYTSEKHKL RNMFTKANQS VCLTTDTWTS VQNINYMVLT AHFIDQDWKM 1140 HKRILNFCPI TSHKGEVIGK KFEKCLEGWM IDKVFTITVD NASSNDLAIS YLKNRMEDWN 1200 SHPLKGEHLH VRCCAHILNL VVGDGLKSKD MHSSISKIRN AVRYVRGSAS RLDRFKICIK 1260 EARIQDKSTV QYDCPTRWNS TYLMLESALK FQKAFKRLGE KCVEYAMLEG GVPNNVDWDN 1320 AKCFVKFLKL FFEITKKVSG STYVTSSTYF MEHCKILGGF NAWMGCHKDD PILANMATKM 1380 TAKYSKYWGD VAKMNMLVFI AVIFYPRRKF QFINWGLNKY YEKEVADSLC DKVKEALNKM 1440 FESYSRFSNK EDVDDQFEKD MDQDPNLSQT EVDIYLSEPR EKKNPDFDIL NWWKVNSTKY 1500 PTLGLIARDI LAMPISTVAS ESAFSTGGRV LSCYRSSLTY VSWNLKNNKS D* 1560 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00479 | EXOIII | 2.0e-24 | 718 | 891 | 189 | + exonuclease domain in DNA-polymerase alpha and epsilon chain, ribonuclease T and other exonucleases. | ||
pfam00929 | RNase_T | 6.0e-30 | 719 | 883 | 167 | + Exonuclease. This family includes a variety of exonuclease proteins, such as ribonuclease T and the epsilon subunit of DNA polymerase III.; | ||
COG1949 | Orn | 3.0e-70 | 717 | 896 | 180 | + Oligoribonuclease (3'->5' exoribonuclease) [RNA processing and modification] | ||
PRK05359 | PRK05359 | 1.0e-78 | 718 | 893 | 176 | + oligoribonuclease; Provisional | ||
cd06135 | Orn | 3.0e-86 | 718 | 891 | 174 | + DEDDh 3'-5' exonuclease domain of oligoribonuclease and similar proteins. Oligoribonuclease (Orn) is a DEDDh-type DnaQ-like 3'-5' exoribonuclease that is responsible for degrading small oligoribonucleotides to mononucleotides. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. Orn is essential for Escherichia coli survival. The human homolog, also called Sfn (small fragment nuclease), is able to hydrolyze short single-stranded RNA and DNA oligomers. It plays a role in cellular nucleotide recycling. |
Gene Ontology | |
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GO Term | Description |
GO:0003677 | DNA binding |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
GO:0046983 | protein dimerization activity |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ABD32354.1 | 0 | 83 | 594 | 5 | 531 | Glycoside hydrolase, family 5; Ricin B-related lectin [Medicago truncatula] |
GenBank | ACX85638.1 | 0 | 949 | 1539 | 20 | 637 | putative transposase [Cucumis melo] |
RefSeq | XP_002272386.1 | 0 | 84 | 594 | 8 | 527 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002272422.1 | 0 | 72 | 594 | 80 | 610 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002509879.1 | 0 | 107 | 594 | 32 | 531 | hydrolase, hydrolyzing O-glycosyl compounds, 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 | 1j9a_A | 3.00018e-42 | 718 | 892 | 10 | 182 | A Chain A, Oligoribonuclease |
PDB | 2igi_B | 3.99931e-42 | 718 | 892 | 7 | 179 | A Chain A, Crystal Structure Of E. Coli Oligoribonuclease |
PDB | 2igi_A | 3.99931e-42 | 718 | 892 | 7 | 179 | A Chain A, Crystal Structure Of E. Coli Oligoribonuclease |
PDB | 1yta_D | 3.99931e-42 | 718 | 892 | 7 | 179 | A Chain A, Crystal Structure Of Oligoribonuclease, The Lone Essential Exoribonuclease In Escherichia Coli |
PDB | 1yta_C | 3.99931e-42 | 718 | 892 | 7 | 179 | A Chain A, Crystal Structure Of Oligoribonuclease, The Lone Essential Exoribonuclease In Escherichia Coli |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
CN824957 | 238 | 661 | 896 | 0 |
FK019042 | 240 | 662 | 898 | 0 |
AW126172 | 168 | 709 | 876 | 0 |
GO338111 | 265 | 346 | 594 | 0 |
FK021220 | 227 | 662 | 885 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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