blastp_kegg |
lcl|pper:PRUPE_ppa007441mg
|
27 |
126 |
+ |
100 |
Gaps:1 |
26.98 |
367 |
66.67 |
5e-32 |
hypothetical protein
|
blastp_kegg |
lcl|pmum:103321308
|
27 |
126 |
+ |
100 |
Gaps:1 |
27.05 |
366 |
65.66 |
2e-31 |
cysteine proteinase 15A-like
|
blastp_kegg |
lcl|mdm:103450429
|
31 |
124 |
+ |
94 |
Gaps:1 |
25.48 |
365 |
69.89 |
2e-30 |
cysteine proteinase 15A
|
blastp_kegg |
lcl|cam:101501911
|
34 |
126 |
+ |
93 |
Gaps:3 |
25.41 |
362 |
66.30 |
4e-30 |
cysteine proteinase 15A-like
|
blastp_kegg |
lcl|pop:POPTR_0002s03020g
|
26 |
124 |
+ |
99 |
Gaps:3 |
26.70 |
367 |
65.31 |
5e-30 |
POPTRDRAFT_816035 hypothetical protein
|
blastp_kegg |
lcl|fve:101294426
|
26 |
126 |
+ |
101 |
none |
27.67 |
365 |
62.38 |
8e-30 |
cysteine proteinase 15A-like
|
blastp_kegg |
lcl|pxb:103928316
|
34 |
124 |
+ |
91 |
Gaps:1 |
24.59 |
366 |
70.00 |
3e-29 |
cysteine proteinase 15A
|
blastp_kegg |
lcl|mtr:MTR_1g023210
|
35 |
126 |
+ |
92 |
Gaps:3 |
25.00 |
364 |
65.93 |
3e-29 |
Cysteine proteinase
|
blastp_kegg |
lcl|vvi:100250475
|
35 |
126 |
+ |
92 |
Gaps:3 |
23.99 |
371 |
68.54 |
5e-29 |
cysteine proteinase RD19a-like
|
blastp_kegg |
lcl|gmx:100778716
|
26 |
126 |
+ |
101 |
Gaps:1 |
27.32 |
366 |
61.00 |
7e-29 |
cysteine proteinase 15A-like
|
blastp_pdb |
3f75_P
|
54 |
127 |
+ |
74 |
none |
69.81 |
106 |
36.49 |
6e-07 |
mol:protein length:106 Cathepsin L propeptide
|
blastp_uniprot_sprot |
sp|P25804|CYSP_PEA
|
34 |
126 |
+ |
93 |
Gaps:3 |
25.34 |
363 |
61.96 |
1e-29 |
Cysteine proteinase 15A OS Pisum sativum PE 1 SV 1
|
blastp_uniprot_sprot |
sp|Q10716|CYSP1_MAIZE
|
35 |
129 |
+ |
95 |
none |
25.61 |
371 |
58.95 |
1e-27 |
Cysteine proteinase 1 OS Zea mays GN CCP1 PE 2 SV 1
|
blastp_uniprot_sprot |
sp|P43295|A494_ARATH
|
27 |
123 |
+ |
97 |
Gaps:2 |
26.32 |
361 |
57.89 |
5e-25 |
Probable cysteine proteinase A494 OS Arabidopsis thaliana GN At2g21430 PE 2 SV 2
|
blastp_uniprot_sprot |
sp|P43296|RD19A_ARATH
|
31 |
123 |
+ |
93 |
Gaps:2 |
24.73 |
368 |
57.14 |
1e-22 |
Cysteine proteinase RD19a OS Arabidopsis thaliana GN RD19A PE 2 SV 1
|
blastp_uniprot_sprot |
sp|P14658|CYSP_TRYBB
|
53 |
129 |
+ |
77 |
Gaps:12 |
19.78 |
450 |
38.20 |
2e-09 |
Cysteine proteinase OS Trypanosoma brucei brucei PE 1 SV 1
|
blastp_uniprot_sprot |
sp|P25779|CYSP_TRYCR
|
53 |
119 |
+ |
67 |
Gaps:4 |
15.20 |
467 |
39.44 |
4e-07 |
Cruzipain OS Trypanosoma cruzi PE 1 SV 1
|
blastp_uniprot_sprot |
sp|Q9TST1|CATW_FELCA
|
39 |
119 |
+ |
81 |
Gaps:1 |
21.93 |
374 |
35.37 |
9e-07 |
Cathepsin W OS Felis catus GN CTSW PE 2 SV 2
|
blastp_uniprot_sprot |
sp|P35591|CYSP1_LEIPI
|
58 |
117 |
+ |
60 |
Gaps:1 |
17.23 |
354 |
44.26 |
1e-06 |
Cysteine proteinase 1 OS Leishmania pifanoi GN CYS1 PE 2 SV 2
|
blastp_uniprot_sprot |
sp|P25775|LMCPA_LEIME
|
58 |
117 |
+ |
60 |
Gaps:1 |
17.23 |
354 |
44.26 |
1e-06 |
Cysteine proteinase A OS Leishmania mexicana GN LMCPA PE 2 SV 1
|
blastp_uniprot_sprot |
sp|P56202|CATW_HUMAN
|
52 |
115 |
+ |
64 |
Gaps:1 |
17.29 |
376 |
43.08 |
2e-06 |
Cathepsin W OS Homo sapiens GN CTSW PE 1 SV 2
|
rpsblast_cdd |
gnl|CDD|197916
|
59 |
114 |
+ |
56 |
Gaps:1 |
100.00 |
57 |
42.11 |
1e-10 |
smart00848 Inhibitor_I29 Cathepsin propeptide inhibitor domain (I29). This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin. This family is classified as I29 by MEROPS. Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins these are referred to as either simple or compound inhibitors respectively. In many cases they are synthesised as part of a larger precursor protein either as a prepropeptide or as an N-terminal domain associated with an inactive peptidase or zymogen. This domain prevents access of the substrate to the active site. Removal of the N-terminal inhibitor domain either by interaction with a second peptidase or by autocatalytic cleavage activates the zymogen. Other inhibitors interact direct with proteinases using a simple noncovalent lock and key mechanism while yet others use a conformational change-based trapping mechanism that depends on their structural and thermodynamic properties.
|
rpsblast_cdd |
gnl|CDD|203889
|
59 |
115 |
+ |
57 |
Gaps:1 |
100.00 |
58 |
41.38 |
1e-08 |
pfam08246 Inhibitor_I29 Cathepsin propeptide inhibitor domain (I29). This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin. This family is classified as I29 by MEROPS.
|
rpsblast_cdd |
gnl|CDD|185513
|
59 |
115 |
+ |
57 |
none |
16.38 |
348 |
40.35 |
2e-07 |
PTZ00203 PTZ00203 cathepsin L protease Provisional.
|
rpsblast_kog |
gnl|CDD|36755
|
26 |
145 |
+ |
120 |
Gaps:1 |
32.53 |
372 |
37.19 |
2e-19 |
KOG1542 KOG1542 KOG1542 Cysteine proteinase Cathepsin F [Posttranslational modification protein turnover chaperones].
|