Protein : Qrob_P0019960.2 Q. robur

Protein Identifier  ? Qrob_P0019960.2 Organism . Name  Quercus robur
Score  99.0 Score Type  egn
Protein Description  (M=1) 3.4.24.16 - Neurolysin. Code Enzyme  EC:3.4.24.16
Gene Prediction Quality  validated Protein length 

Sequence

Length: 674  
Kegg Orthology  K01392

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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.

36 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|rcu:RCOM_1081460 12 673 + 662 Gaps:28 97.32 709 74.06 0.0 oligopeptidase putative (EC:3.4.24.16)
blastp_kegg lcl|cic:CICLE_v10033657mg 3 673 + 671 Gaps:31 99.00 703 74.86 0.0 hypothetical protein
blastp_kegg lcl|cit:102612794 3 673 + 671 Gaps:31 99.00 703 74.71 0.0 neurolysin mitochondrial-like
blastp_kegg lcl|pmum:103321960 1 673 + 673 Gaps:34 100.00 707 72.70 0.0 probable thimet oligopeptidase
blastp_kegg lcl|tcc:TCM_010744 2 673 + 672 Gaps:29 98.87 707 72.96 0.0 Zincin-like metalloproteases family protein
blastp_kegg lcl|pper:PRUPE_ppa002154mg 1 673 + 673 Gaps:35 100.00 708 72.60 0.0 hypothetical protein
blastp_kegg lcl|fve:101295009 1 673 + 673 Gaps:37 100.00 710 70.28 0.0 neurolysin mitochondrial-like
blastp_kegg lcl|pop:POPTR_0010s06460g 7 672 + 666 Gaps:31 98.17 710 75.47 0.0 POPTRDRAFT_565929 peptidase M3 family protein
blastp_kegg lcl|mdm:103452091 33 673 + 641 Gaps:28 94.49 708 73.09 0.0 probable thimet oligopeptidase
blastp_kegg lcl|cmo:103487749 7 673 + 667 Gaps:31 98.30 704 69.94 0.0 probable thimet oligopeptidase
blastp_pdb 1i1i_P 49 668 + 620 Gaps:38 96.33 681 36.89 5e-136 mol:protein length:681 NEUROLYSIN
blastp_pdb 2o3e_A 49 668 + 620 Gaps:38 96.76 678 36.89 1e-135 mol:protein length:678 Neurolysin
blastp_pdb 2o36_A 50 669 + 620 Gaps:43 97.18 674 35.11 1e-128 mol:protein length:674 Thimet oligopeptidase
blastp_pdb 1s4b_P 50 669 + 620 Gaps:43 97.18 674 35.11 1e-128 mol:protein length:674 Thimet oligopeptidase
blastp_pdb 1y79_1 131 669 + 539 Gaps:65 86.76 680 25.93 9e-44 mol:protein length:680 Peptidyl-Dipeptidase Dcp
blastp_uniprot_sprot sp|F4HTQ1|MPRO1_ARATH 2 673 + 672 Gaps:30 98.87 710 61.54 0.0 Probable thimet oligopeptidase OS Arabidopsis thaliana GN At1g67690 PE 3 SV 1
blastp_uniprot_sprot sp|Q02038|NEUL_PIG 49 668 + 620 Gaps:40 93.18 704 37.20 3e-137 Neurolysin mitochondrial OS Sus scrofa GN NLN PE 1 SV 1
blastp_uniprot_sprot sp|P42675|NEUL_RABIT 49 668 + 620 Gaps:38 93.18 704 36.89 4e-135 Neurolysin mitochondrial OS Oryctolagus cuniculus GN NLN PE 1 SV 1
blastp_uniprot_sprot sp|Q91YP2|NEUL_MOUSE 49 668 + 620 Gaps:38 93.18 704 37.04 5e-135 Neurolysin mitochondrial OS Mus musculus GN Nln PE 2 SV 1
blastp_uniprot_sprot sp|P42676|NEUL_RAT 49 668 + 620 Gaps:38 93.18 704 36.89 5e-135 Neurolysin mitochondrial OS Rattus norvegicus GN Nln PE 1 SV 1
blastp_uniprot_sprot sp|Q9BYT8|NEUL_HUMAN 49 668 + 620 Gaps:38 93.18 704 36.43 2e-134 Neurolysin mitochondrial OS Homo sapiens GN NLN PE 1 SV 1
blastp_uniprot_sprot sp|A2VDQ5|NEUL_BOVIN 49 668 + 620 Gaps:38 93.18 704 36.59 3e-134 Neurolysin mitochondrial OS Bos taurus GN NLN PE 2 SV 1
blastp_uniprot_sprot sp|Q5R9V6|NEUL_PONAB 49 668 + 620 Gaps:38 93.18 704 36.13 5e-133 Neurolysin mitochondrial OS Pongo abelii GN NLN PE 2 SV 1
blastp_uniprot_sprot sp|P52888|THOP1_HUMAN 50 669 + 620 Gaps:43 95.07 689 35.11 1e-127 Thimet oligopeptidase OS Homo sapiens GN THOP1 PE 1 SV 2
blastp_uniprot_sprot sp|Q8C1A5|THOP1_MOUSE 48 668 + 621 Gaps:46 95.92 687 35.05 2e-126 Thimet oligopeptidase OS Mus musculus GN Thop1 PE 1 SV 1
rpsblast_cdd gnl|CDD|188994 62 668 + 607 Gaps:32 100.00 637 41.29 0.0 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.
rpsblast_cdd gnl|CDD|189012 66 664 + 599 Gaps:93 98.64 590 34.71 1e-139 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 55 664 + 610 Gaps:51 95.61 683 30.93 1e-101 COG0339 Dcp Zn-dependent oligopeptidases [Amino acid transport and metabolism].
rpsblast_cdd gnl|CDD|188995 66 663 + 598 Gaps:92 97.86 654 31.09 8e-93 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|201794 253 668 + 416 Gaps:50 99.56 450 33.71 2e-78 pfam01432 Peptidase_M3 Peptidase family M3. This is the Thimet oligopeptidase family large family of mammalian and bacterial oligopeptidases that cleave medium sized peptides. The group also contains mitochondrial intermediate peptidase which is encoded by nuclear DNA but functions within the mitochondria to remove the leader sequence.

14 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Phobius 1 13 13 SIGNAL_PEPTIDE_N_REGION none N-terminal region of a signal peptide. none
Gene3D 178 372 195 G3DSA:1.10.1370.10 none none IPR024077
Gene3D 528 668 141 G3DSA:1.10.1370.10 none none IPR024077
Phobius 26 33 8 SIGNAL_PEPTIDE_C_REGION none C-terminal region of a signal peptide. none
PANTHER 48 668 621 PTHR11804 none none none
PANTHER 48 668 621 PTHR11804:SF40 none none none
Phobius 1 33 33 SIGNAL_PEPTIDE none Signal peptide region none
Phobius 34 673 640 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Gene3D 382 527 146 G3DSA:3.40.390.10 none none IPR024079
Phobius 14 25 12 SIGNAL_PEPTIDE_H_REGION none Hydrophobic region of a signal peptide. none
Gene3D 47 177 131 G3DSA:1.20.1050.40 none none IPR024080
Pfam 256 574 319 PF01432 none Peptidase family M3 IPR001567
Pfam 581 667 87 PF01432 none Peptidase family M3 IPR001567
SUPERFAMILY 53 666 614 SSF55486 none none none

1 Localization

Analysis Start End Length
TMHMM 13 35 22

0 Qtllist

0 Targeting