Protein : Qrob_P0660200.2 Q. robur
Protein Identifier  ? Qrob_P0660200.2 Organism . Name  Quercus robur
Score  0.0 Score Type  egn
Protein Description  (M=2) 3.4.24.70 - Oligopeptidase A. Code Enzyme  EC:3.4.24.70
Gene Prediction Quality  validated Protein length 

Sequence

Length: 218  
Kegg Orthology  K01414
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0 Synonyms

3 GO Terms

Identifier Name Description
GO:0004222 metalloendopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
GO:0006508 proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
GO:0008237 metallopeptidase activity Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.

35 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pop:POPTR_0007s14960g 1 189 + 189 Gaps:4 27.45 703 64.25 2e-80 POPTRDRAFT_820137 hypothetical protein
blastp_kegg lcl|gmx:100776634 1 179 + 179 Gaps:4 23.25 787 65.03 2e-79 thimet oligopeptidase-like
blastp_kegg lcl|gmx:100780377 1 179 + 179 Gaps:4 23.25 787 65.03 2e-79 thimet oligopeptidase-like
blastp_kegg lcl|cit:102622997 1 179 + 179 Gaps:4 22.56 811 66.12 5e-79 thimet oligopeptidase-like
blastp_kegg lcl|cic:CICLE_v10024919mg 1 179 + 179 Gaps:4 22.85 801 65.57 4e-78 hypothetical protein
blastp_kegg lcl|tcc:TCM_000926 1 179 + 179 Gaps:4 23.64 774 64.48 3e-77 Zincin-like metalloproteases family protein
blastp_kegg lcl|mtr:MTR_5g030940 1 201 + 201 Gaps:4 21.11 971 57.56 5e-77 Oligopeptidase A
blastp_kegg lcl|rcu:RCOM_0230710 1 179 + 179 Gaps:4 23.46 780 63.93 7e-77 oligopeptidase A putative (EC:3.4.24.70)
blastp_kegg lcl|cam:101507357 1 179 + 179 Gaps:5 23.29 790 63.59 2e-76 oligopeptidase A-like
blastp_kegg lcl|ath:AT5G65620 1 179 + 179 Gaps:4 23.14 791 65.03 3e-76 organellar oligopeptidase A
blastp_pdb 1y79_1 1 177 + 177 Gaps:8 25.44 680 35.26 5e-23 mol:protein length:680 Peptidyl-Dipeptidase Dcp
blastp_pdb 1i1i_P 1 179 + 179 Gaps:15 26.14 681 34.27 2e-20 mol:protein length:681 NEUROLYSIN
blastp_pdb 2o3e_A 1 179 + 179 Gaps:15 26.25 678 34.27 2e-20 mol:protein length:678 Neurolysin
blastp_pdb 2o36_A 1 201 + 201 Gaps:5 29.67 674 29.50 3e-20 mol:protein length:674 Thimet oligopeptidase
blastp_pdb 1s4b_P 1 201 + 201 Gaps:5 29.67 674 29.50 3e-20 mol:protein length:674 Thimet oligopeptidase
blastp_uniprot_sprot sp|Q94AM1|OOPDA_ARATH 1 179 + 179 Gaps:4 23.14 791 65.03 1e-77 Organellar oligopeptidase A chloroplastic/mitochondrial OS Arabidopsis thaliana GN OOP PE 1 SV 1
blastp_uniprot_sprot sp|Q949P2|COPDA_ARATH 1 179 + 179 Gaps:4 26.11 701 62.30 4e-76 Probable cytosolic oligopeptidase A OS Arabidopsis thaliana GN CYOP PE 1 SV 1
blastp_uniprot_sprot sp|P44573|OPDA_HAEIN 1 217 + 217 Gaps:9 30.84 681 38.57 1e-39 Oligopeptidase A OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) GN prlC PE 3 SV 1
blastp_uniprot_sprot sp|P27298|OPDA_ECOLI 1 217 + 217 Gaps:9 30.88 680 37.14 2e-36 Oligopeptidase A OS Escherichia coli (strain K12) GN prlC PE 3 SV 3
blastp_uniprot_sprot sp|P27237|OPDA_SALTY 1 217 + 217 Gaps:9 30.88 680 36.67 6e-36 Oligopeptidase A OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GN prlC PE 1 SV 1
blastp_uniprot_sprot sp|P24171|DCP_ECOLI 1 177 + 177 Gaps:8 25.40 681 35.26 2e-22 Peptidyl-dipeptidase dcp OS Escherichia coli (strain K12) GN dcp PE 1 SV 4
blastp_uniprot_sprot sp|P27236|DCP_SALTY 1 177 + 177 Gaps:8 25.44 680 36.42 3e-22 Peptidyl-dipeptidase dcp OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GN dcp PE 1 SV 1
blastp_uniprot_sprot sp|Q54DD2|THOPL_DICDI 4 217 + 214 Gaps:12 31.20 673 32.86 1e-21 Thimet-like oligopeptidase OS Dictyostelium discoideum GN DDB_G0292362 PE 3 SV 1
blastp_uniprot_sprot sp|A2VDQ5|NEUL_BOVIN 1 179 + 179 Gaps:15 25.28 704 34.83 1e-21 Neurolysin mitochondrial OS Bos taurus GN NLN PE 2 SV 1
blastp_uniprot_sprot sp|Q1JPJ8|THOP1_BOVIN 1 177 + 177 Gaps:5 25.62 687 33.52 3e-21 Thimet oligopeptidase OS Bos taurus GN THOP1 PE 2 SV 3
rpsblast_cdd gnl|CDD|188995 3 177 + 175 Gaps:5 26.30 654 43.02 2e-61 cd06456 M3A_DCP Peptidase family M3 dipeptidyl carboxypeptidase (DCP). Peptidase family M3 dipeptidyl carboxypeptidase (DCP Dcp II peptidyl dipeptidase EC 3.4.15.5). This metal-binding M3A family also includes oligopeptidase A (OpdA EC 3.4.24.70) enzyme. DCP cleaves dipeptides off the C-termini of various peptides and proteins the smallest substrate being N-blocked tripeptides and unblocked tetrapeptides. DCP from E. coli is inhibited by the anti-hypertensive drug captopril an inhibitor of the mammalian angiotensin converting enzyme (ACE also called peptidyl dipeptidase A). Oligopeptidase A (OpdA) may play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. It can also cleave N-acetyl-L-Ala.
rpsblast_cdd gnl|CDD|189012 2 217 + 216 Gaps:10 35.25 590 37.02 1e-55 cd09605 M3A Peptidase M3A family includes Thimet oligopeptidase dipeptidyl carboxypeptidase and mitochondrial intermediate peptidase. The peptidase M3-like family also called neurolysin-like family is part of the "zincins" metallopeptidases and includes M3 M2 and M32 families of metallopeptidases. The M3 family is subdivided into two subfamilies: the widespread M3A which comprises a number of high-molecular mass endo- and exopeptidases from bacteria archaea protozoa fungi plants and animals and the small M3B whose members are enzymes primarily from bacteria. Well-known mammalian/eukaryotic M3A endopeptidases are the thimet oligopeptidase (TOP endopeptidase 3.4.24.15) neurolysin (alias endopeptidase 3.4.24.16) and the mitochondrial intermediate peptidase. The first two are intracellular oligopeptidases which act only on relatively short substrates of less than 20 amino acid residues while the latter cleaves N-terminal octapeptides from proteins during their import into the mitochondria. The M3A subfamily also contains several bacterial endopeptidases collectively called oligopeptidases A as well as a large number of bacterial carboxypeptidases called dipeptidyl peptidases (Dcp Dcp II peptidyl dipeptidase EC 3.4.15.5). The peptidases in the M3 family contain the HEXXH motif that forms the active site in conjunction with a C-terminally-located Glutamic acid (Glu) residue. A single zinc ion is ligated by the side-chains of the two Histidine (His) residues and the more C-terminal Glu. Most of the peptidases are synthesized without signal peptides or propeptides and function intracellularly. The structure of neurolysin shows similarities to those of angiotensin-converting enzyme (ACE peptidyl-dipeptidase A) peptidase unit 2 belonging to peptidase family M2. ACE is an enzyme responsible for cleavage of dipeptides from the C-termini of proteins notably converting angiotensin I to angiotensin II in mammals. There are similarities to the thermostable carboxypeptidases from Pyrococcus furiosus carboxypeptidase (PfuCP) and Thermus aquaticus (TaqCP) belonging to peptidase family M32. Little is known about function of this family including carboxypeptidases Taq and Pfu.
rpsblast_cdd gnl|CDD|30687 3 217 + 215 Gaps:10 30.31 683 39.61 2e-50 COG0339 Dcp Zn-dependent oligopeptidases [Amino acid transport and metabolism].
rpsblast_cdd gnl|CDD|182832 3 217 + 215 Gaps:9 30.59 680 37.50 5e-38 PRK10911 PRK10911 oligopeptidase A Provisional.
rpsblast_cdd gnl|CDD|188994 1 217 + 217 Gaps:11 32.97 637 35.24 2e-37 cd06455 M3A_TOP Peptidase M3 Thimet oligopeptidase (TOP) also includes neurolysin. Peptidase M3 Thimet oligopeptidase (TOP PZ-peptidase endo-oligopeptidase A endopeptidase 24.15 soluble metallo-endopeptidase EC 3.4.24.15) family also includes neurolysin (endopeptidase 24.16 microsomal endopeptidase mitochondrial oligopeptidase M neurotensin endopeptidase soluble angiotensin II-binding protein thimet oligopeptidase II) which hydrolyzes oligopeptides such as neurotensin bradykinin and dynorphin A. TOP and neurolysin are neuropeptidases expressed abundantly in the testis but also found in the liver lung and kidney. They are involved in the metabolism of neuropeptides under 20 amino acid residues long and cleave most bioactive peptides at the same sites but recognize different positions on some naturally occurring and synthetic peptides they cleave at distinct sites on the 13-residue bioactive peptide neurotensin which modulates central dopaminergic and cholinergic circuits. TOP has been shown to degrade peptides released by the proteasome limiting the extent of antigen presentation by major histocompatibility complex class I molecules and has been associated with amyloid protein precursor processing.

5 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 3 177 175 PTHR11804:SF39 none none none
SUPERFAMILY 2 200 199 SSF55486 none none none
Gene3D 7 157 151 G3DSA:3.40.390.10 none none IPR024079
PANTHER 3 177 175 PTHR11804 none none none
Pfam 2 201 200 PF01432 none Peptidase family M3 IPR001567

0 Localization

11 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran2_2015_nEpis_3P Qrob_Chr12 12 s_1AOES6_1466 s_1B0DDG_1094 28,97 28,55 30,1 lod 3.6 8.4
Bourran2_2014_nP_A4 Qrob_Chr11 11 s_1B58GB_1413 s_1A5BYY_1671 11,15 0 42,38 lod 1,8913 4,5
Bourran2_2002_QTL16_peak_Bud_burst_A4 Qrob_Chr11 11 s_A9OIA_166 s_1C6WBF_114 21,23 2,83 42,83 lod 5,1 7,2
Bourran2_2015_nSeqBC_3P Qrob_Chr11 11 s_1DG9PM_867 s_1BZ083_1312 26,06 25,47 27,72 lod 3.6 7.1
Champenoux_2015_nSecLBD_3P Qrob_Chr11 11 s_1DG9PM_867 s_1BZ083_1312 25,78 25,47 27,72 lod 6.3 16.6
Bourran2_2014_nP_3P Qrob_Chr11 11 v_11486_194 s_1AT3E_2335 7,9 0,09 30,09 lod 2,3636 5
Bourran2_2014_nPriBD_3P Qrob_Chr11 11 v_11486_194 s_1AT3E_2335 5,54 0,4 20,6 lod 2,6345 5,9
Bourran1_2003_QTL6_peak_Bud_burst_A4 Qrob_Chr11 11 v_12066_307 s_1A9FKZ_348 3,59 0 20,89 lod 3,4 9,4
PM_1999_QTL17_peak_Bud_burst_3P Qrob_Chr11 11 s_1A9FKZ_348 v_11486_883 4,8 0 24,8 lod 3,5 6,2
Bourran2_2014_vEpiBC*_3P Qrob_Chr11 11 s_1A5GRX_415 v_4456_500 9,37 0 19,27 lod 3,513 9,3
NancyGreenhouseCO2_2001_ambient_elevated_leaf_cellulose_QTL1_d13Cf Qrob_Chr11 11 s_1A9FKZ_348 v_7268_36 13.33 3,98 19,87 lod 29.1377 0.18

0 Targeting