|
| Spot ID | Accession number | Description | Score (%) | Coverage (%) | Theoretical MW (kDa)/IP | Function | Reference |
|
| SUSMJ-5204 | JAC59075.1 (GenBank) | Microplusin-like 2, partial (Rhipicephalus microplus) | 495.58 | 31.63 | 10.7/6.98 | Antimicrobial peptide isolated from the cattle tick R. microplus. Its copper-chelating ability is putatively responsible for its bacteriostatic effect. | [32] |
|
| SUSMJ-6205 | JAC59122.1 (GenBank) | Hemelipoprotein HeLp2, partial (Rhipicephalus microplus) | 29.67 | 5.99 | 30.5/6.65 | Protein involved in heme transports from hemolymph to tissues, suggesting to be an essential adaptation to the loss of the heme synthesis pathway | [33] |
|
| SUSMJ-6208 | JAP78009.1 (GenBank) | Hypothetical protein (Rhipicephalus appendiculatus) | 7.25 | 20.12 | 18.9/6.77 | Protein binding to EGF. The functional significance of EGF domains in what appears to be unrelated proteins is not yet clear. However, a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted | [34] |
|
| SUSMJ-6302 | JAC59082.1 (GenBank)
JAC59119.1 (GenBank) | Secreted protein 33, partial (Rhipicephalus microplus)
Secreted protein 27, partial (Rhipicephalus microplus) | 10.08
8.31 | 3.83
3.86 | 37.8/7.99
37.4/7.28 | Leucine-rich repeat domain, L domain-like. Leucine-rich repeats (LRR) consist of 2-45 motifs of 20-30 amino acids in length that generally fold into an arc or horseshoe shape. LRRs occur in proteins ranging from viruses to eukaryotes, and appear to provide a structural framework for the formation of protein-protein interactions. Proteins containing LRRs include tyrosine kinase receptors, cell-adhesion molecules, virulence factors, and extracellular matrix-binding glycoproteins, and are involved in a variety of biological processes, including signal transduction, cell adhesion, DNA repair, recombination, transcription, RNA processing, disease resistance, apoptosis, and immune response | [35–38] |
|
| SUSMJ-6304 | JAC59079.1 (GenBank) | Secreted protein 36, partial (Rhipicephalus microplus) | 23.30 | 16.26 | 21.6/7.12 | Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of superoxide radicals to molecular oxygen. | [32] |
| JAC59082.1 (GenBank) | Secreted protein 33, partial (Rhipicephalus microplus) | 16.45 | 3.83 | 37.8/7.99 | Uncharacterized.
The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. Reported by Tirloni 2014. | [3] |
| De novo | 100% identity to phospholipases | | 100 | --- | Phospholipase-mediated phospholipid hydrolysis leads to the production of lipid mediators or second messengers that affect signal transduction, thus regulating a variety of physiologic and pathophysiologic processes. | [39] |
|
| SMJ-7106 | P02070 (UniProtKB/Swiss-Prot)
2QSP (PDB)
2EU1 (PDB) |
Hemoglobin subunit beta OS=Bos Taurus GN=HBB PE=1 SV=1 (HBB_BOVIN)
C Chain C, Bovine hemoglobin At Ph 5.7
D Chain D, Crystal structure determination of goat hemoglobin (Capra hircus) at 3 Angstrom resolution |
1919.94
163.98
1288.43 |
82.76
78.72
55.17 |
15.9/7.59
15.0/8.44
16.0/7.30 | Haemoglobins (Hb) function is transport oxygen in blood plasma, and binds oxygen in the reduced [Fe(II)] state. (Hb) tetramer of two alpha and two beta chains, although embryonic and foetal forms can substitute the alpha or beta chain for ones with higher oxygen affinity, such as gamma, delta, epsilon or zeta chains. Hb transports oxygen from lungs to other tissues in vertebrates. Hb proteins are also present in unicellular organisms where they act as enzymes or sensors. | [40–42] |
|
| RESSA-3008 | JAC59001.1 (GenBank) | TIL domain-containing protein 2 (Rhipicephalus microplus) | 1193.73 | 52.94 | 9.2/5.77 | Different analyses carried out show that thia protein contains a domain 25 -81 TIL (trypsin inhibitory-like) This domain is found in proteinase inhibitors, as well as in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9. | [3] |
| ACV83329.1 (GenBank) | Serine proteinase inhibitor precursor (Rhipicephalus microplus) | 872.04 | 67.06 | 9.3/6.24 | Serpin family members have activity as inhibitors of serine proteinases, and serve in regulation of proteinase-mediated, such as inflammatory, and the immune response with consequent pathology in deficiency state. | [43] |
ABH10604.1
(GenBank) | Neutrophil elastase inhibitor (Rhipicephalus microplus) | 210.52 | 21.15 | 11.5/6.51 | In ticks, these inhibitors (due to their properties) play a role in the feeding process, however the crucial role is still unclear. | [44] |
|
| RESSA-5214 | JAC59087.1 (GenBank) | Secreted protein 31, partial (Rhipicephalus microplus) | 17.73 | 2 | 15.6/6.52 | Unknown. Reported by Tirloni 2014. | [45] |
|
