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.
|