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Conserved domains on  [gi|1169087|sp|P43510|]
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RecName: Full=Cathepsin B-like cysteine proteinase 6; AltName: Full=Cysteine protease-related 6; Flags: Precursor

Protein Classification

C1 family peptidase( domain architecture ID 10119013)

C1 family peptidase such as cathepsin B, an endopeptidase that catalyzes the hydrolysis of proteins with broad specificity for peptide bonds; it preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates

CATH:  3.90.70.10
EC:  3.4.22.-
Gene Ontology:  GO:0008234|GO:0006508
MEROPS:  C1
PubMed:  12887050|11517925
SCOP:  4000859

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
106-355 3.58e-141

Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial nephritis antigen (TIN-Ag). Cathepsin B is a lysosomal papain-like cysteine peptidase which is expressed in all tissues and functions primarily as an exopeptidase through its carboxydipeptidyl activity. Together with other cathepsins, it is involved in the degradation of proteins, proenzyme activation, Ag processing, metabolism and apoptosis. Cathepsin B has been implicated in a number of human diseases such as cancer, rheumatoid arthritis, osteoporosis and Alzheimer's disease. The unique carboxydipeptidyl activity of cathepsin B is attributed to the presence of an occluding loop in its active site which favors the binding of the C-termini of substrate proteins. Some members of this group do not possess the occluding loop. TIN-Ag is an extracellular matrix basement protein which was originally identified as a target Ag involved in anti-tubular basement membrane antibody-mediated interstitial nephritis. It plays a role in renal tubulogenesis and is defective in hereditary tubulointerstitial disorders. TIN-Ag is exclusively expressed in kidney tissues.


:

Pssm-ID: 239111 [Multi-domain]  Cd Length: 236  Bit Score: 400.49  E-value: 3.58e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  106 PESFDSRDNWPKCDSIKVIRDQSSCGSCWAFGAVEAMSDRICIASHGELQVTLSADDLLSCCKSCGFGCNGGDPLAAWRY 185
Cdd:cd02620   1 PESFDAREKWPNCISIGEIRDQGNCGSCWAFSAVEAFSDRLCIQSNGKENVLLSAQDLLSCCSGCGDGCNGGYPDAAWKY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  186 WVKDGIVTGsnytannGCKPYPFPPCEHHSKKThfDPCPHDLYPTPKCEKKCvsdytDKTYSEDKFFGASAYGVKDDVEA 265
Cdd:cd02620  81 LTTTGVVTG-------GCQPYTIPPCGHHPEGP--PPCCGTPYCTPKCQDGC-----EKTYEEDKHKGKSAYSVPSDETD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  266 IQKELMTHGPLEIAFEVYEDFLNYDGGVYVHTGGKLGGGHAVKLIGWGIDDGIPYWTVANSWNTDWGEDGFFRILRGVDE 345
Cdd:cd02620 147 IMKEIMTNGPVQAAFTVYEDFLYYKSGVYQHTSGKQLGGHAVKIIGWGVENGVPYWLAANSWGTDWGENGYFRILRGSNE 226
                       250
                ....*....|
gi 1169087  346 CGIESGVVGG 355
Cdd:cd02620 227 CGIESEVVAG 236
 
Name Accession Description Interval E-value
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
106-355 3.58e-141

Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial nephritis antigen (TIN-Ag). Cathepsin B is a lysosomal papain-like cysteine peptidase which is expressed in all tissues and functions primarily as an exopeptidase through its carboxydipeptidyl activity. Together with other cathepsins, it is involved in the degradation of proteins, proenzyme activation, Ag processing, metabolism and apoptosis. Cathepsin B has been implicated in a number of human diseases such as cancer, rheumatoid arthritis, osteoporosis and Alzheimer's disease. The unique carboxydipeptidyl activity of cathepsin B is attributed to the presence of an occluding loop in its active site which favors the binding of the C-termini of substrate proteins. Some members of this group do not possess the occluding loop. TIN-Ag is an extracellular matrix basement protein which was originally identified as a target Ag involved in anti-tubular basement membrane antibody-mediated interstitial nephritis. It plays a role in renal tubulogenesis and is defective in hereditary tubulointerstitial disorders. TIN-Ag is exclusively expressed in kidney tissues.


Pssm-ID: 239111 [Multi-domain]  Cd Length: 236  Bit Score: 400.49  E-value: 3.58e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  106 PESFDSRDNWPKCDSIKVIRDQSSCGSCWAFGAVEAMSDRICIASHGELQVTLSADDLLSCCKSCGFGCNGGDPLAAWRY 185
Cdd:cd02620   1 PESFDAREKWPNCISIGEIRDQGNCGSCWAFSAVEAFSDRLCIQSNGKENVLLSAQDLLSCCSGCGDGCNGGYPDAAWKY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  186 WVKDGIVTGsnytannGCKPYPFPPCEHHSKKThfDPCPHDLYPTPKCEKKCvsdytDKTYSEDKFFGASAYGVKDDVEA 265
Cdd:cd02620  81 LTTTGVVTG-------GCQPYTIPPCGHHPEGP--PPCCGTPYCTPKCQDGC-----EKTYEEDKHKGKSAYSVPSDETD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  266 IQKELMTHGPLEIAFEVYEDFLNYDGGVYVHTGGKLGGGHAVKLIGWGIDDGIPYWTVANSWNTDWGEDGFFRILRGVDE 345
Cdd:cd02620 147 IMKEIMTNGPVQAAFTVYEDFLYYKSGVYQHTSGKQLGGHAVKIIGWGVENGVPYWLAANSWGTDWGENGYFRILRGSNE 226
                       250
                ....*....|
gi 1169087  346 CGIESGVVGG 355
Cdd:cd02620 227 CGIESEVVAG 236
Peptidase_C1 pfam00112
Papain family cysteine protease;
105-356 1.19e-85

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 258.63  E-value: 1.19e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087    105 IPESFDSRDNWpkcdSIKVIRDQSSCGSCWAFGAVEAMSDRICIASHGelQVTLSADDLLSCCKSCgFGCNGGDPLAAWR 184
Cdd:pfam00112   1 LPESFDWREKG----AVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGK--LVSLSEQQLVDCDTFN-NGCNGGLPDNAFE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087    185 YWVKD-GIVTGSNYtanngckPYPfppcEHHSKkthfdpcphdlyptpkCEKKCVSDYtdktYSEDKFFGASAYGvkdDV 263
Cdd:pfam00112  74 YIKKNgGIVTESDY-------PYT----AKDGT----------------CKFKKSNSK----VAKIKGYGDVPYN---DE 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087    264 EAIQKELMTHGPLEIAFEVYE-DFLNYDGGVYVHTGGKLGGGHAVKLIGWGIDDGIPYWTVANSWNTDWGEDGFFRILRG 342
Cdd:pfam00112 120 EALQAALAKNGPVSVAIDAYErDFQLYKSGVYKHTECGGELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARG 199
                         250
                  ....*....|....*
gi 1169087    343 VD-ECGIESGVVGGI 356
Cdd:pfam00112 200 VNnECGIASEASYPI 214
Pept_C1 smart00645
Papain family cysteine protease;
105-356 7.37e-60

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 191.26  E-value: 7.37e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087     105 IPESFDSRDNWpkCDSIkvIRDQSSCGSCWAFGAVEAMSDRICIASHGelQVTLSADDLLSCCKSCGFGCNGGDPLAAWR 184
Cdd:smart00645   1 LPESFDWRKKG--AVTP--VKDQGQCGSCWAFSATGALEGRYCIKTGK--LVSLSEQQLVDCSGGGNCGCNGGLPDNAFE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087     185 YWVKDGivtgsnYTANNGCKPYPFppcehhskkthfdpcphdlyptpkcekkcvsdytdktysedkffgasaygvkddve 264
Cdd:smart00645  75 YIKKNG------GLETESCYPYTG-------------------------------------------------------- 92
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087     265 aiqkelmthgpleIAFEVYEDFLNYDGGVYVHTG-GKLGGGHAVKLIGWG--IDDGIPYWTVANSWNTDWGEDGFFRILR 341
Cdd:smart00645  93 -------------SVAIDASDFQFYKSGIYDHPGcGSGTLDHAVLIVGYGteVENGKDYWIVKNSWGTDWGENGYFRIAR 159
                          250
                   ....*....|....*.
gi 1169087     342 GVD-ECGIESGVVGGI 356
Cdd:smart00645 160 GKNnECGIEASVASYP 175
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
104-339 2.04e-32

Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 126.02  E-value: 2.04e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  104 DIPESFDSRDNWPKcdsikvIRDQSSCGSCWAFGAVEAM-SDRICIASHGELQVTLSADDLLSC----CKSCGFGCNGGD 178
Cdd:COG4870   3 ALPSSVDLRGYVTP------VKDQGSLGSCWAFATAAALeSYLKKQAGAPGTSLDLSELFLYNQarngDGTEGTDDGGSS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  179 PLAAWRYWVKDGIVTGSNYtanngckPYPfppcehhskkthfdpcphdlyptpkcEKKCVSDYTDKTYSEDKFFGASAY- 257
Cdd:COG4870  77 LRDALKLLRWSGVVPESDW-------PYD--------------------------DSDFTSQPSAAAYADARNYKIQDYy 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  258 -----GVKDDVEAIQKELMTHGPLEIAFEVYEDFLNYDGGVYVHT-GGKLGGGHAVKLIGWgiDDGIP--YWTVANSWNT 329
Cdd:COG4870 124 rlpggGGATDLDAIKQALAEGGPVVFGFYVYESFYNYTGGVYYPTpGDASLGGHAVAIVGY--DDNYSdgAFIIKNSWGT 201
                       250
                ....*....|
gi 1169087  330 DWGEDGFFRI 339
Cdd:COG4870 202 GWGDNGYFWI 211
PTZ00200 PTZ00200
cysteine proteinase; Provisional
95-361 1.04e-29

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 119.03  E-value: 1.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087    95 LSKTKDLDLDI-------PESFDsrdnWPKCDSIKVIRDQSS-CGSCWAF---GAVEAMsdricIASHGELQVTLSADDL 163
Cdd:PTZ00200 217 LKKAKNTDEDVkdpskitGEGLD----WRRADAVTKVKDQGLnCGSCWAFssvGSVESL-----YKIYRDKSVDLSEQEL 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087   164 LSCCKSCGfGCNGGDPLAAWRYWVKDGIVTGSNYtanngckPYpfppcehHSKkthfdpcphdlyptpkcEKKCVSDYTD 243
Cdd:PTZ00200 288 VNCDTKSQ-GCSGGYPDTALEYVKNKGLSSSSDV-------PY-------LAK-----------------DGKCVVSSTK 335
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087   244 KTYSEDKFFgasAYGvKDdveaIQKELMTHGPLEIAFEVYEDFLNYDGGVYvhtGGKLGGG--HAVKLIGWGIDD--GIP 319
Cdd:PTZ00200 336 KVYIDSYLV---AKG-KD----VLNKSLVISPTVVYIAVSRELLKYKSGVY---NGECGKSlnHAVLLVGEGYDEktKKR 404
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 1169087   320 YWTVANSWNTDWGEDGFFRILR---GVDECGIESgvVGGIPKLNS 361
Cdd:PTZ00200 405 YWIIKNSWGTDWGENGYMRLERtneGTDKCGILT--VGLTPVFYS 447
 
Name Accession Description Interval E-value
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
106-355 3.58e-141

Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial nephritis antigen (TIN-Ag). Cathepsin B is a lysosomal papain-like cysteine peptidase which is expressed in all tissues and functions primarily as an exopeptidase through its carboxydipeptidyl activity. Together with other cathepsins, it is involved in the degradation of proteins, proenzyme activation, Ag processing, metabolism and apoptosis. Cathepsin B has been implicated in a number of human diseases such as cancer, rheumatoid arthritis, osteoporosis and Alzheimer's disease. The unique carboxydipeptidyl activity of cathepsin B is attributed to the presence of an occluding loop in its active site which favors the binding of the C-termini of substrate proteins. Some members of this group do not possess the occluding loop. TIN-Ag is an extracellular matrix basement protein which was originally identified as a target Ag involved in anti-tubular basement membrane antibody-mediated interstitial nephritis. It plays a role in renal tubulogenesis and is defective in hereditary tubulointerstitial disorders. TIN-Ag is exclusively expressed in kidney tissues.


Pssm-ID: 239111 [Multi-domain]  Cd Length: 236  Bit Score: 400.49  E-value: 3.58e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  106 PESFDSRDNWPKCDSIKVIRDQSSCGSCWAFGAVEAMSDRICIASHGELQVTLSADDLLSCCKSCGFGCNGGDPLAAWRY 185
Cdd:cd02620   1 PESFDAREKWPNCISIGEIRDQGNCGSCWAFSAVEAFSDRLCIQSNGKENVLLSAQDLLSCCSGCGDGCNGGYPDAAWKY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  186 WVKDGIVTGsnytannGCKPYPFPPCEHHSKKThfDPCPHDLYPTPKCEKKCvsdytDKTYSEDKFFGASAYGVKDDVEA 265
Cdd:cd02620  81 LTTTGVVTG-------GCQPYTIPPCGHHPEGP--PPCCGTPYCTPKCQDGC-----EKTYEEDKHKGKSAYSVPSDETD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  266 IQKELMTHGPLEIAFEVYEDFLNYDGGVYVHTGGKLGGGHAVKLIGWGIDDGIPYWTVANSWNTDWGEDGFFRILRGVDE 345
Cdd:cd02620 147 IMKEIMTNGPVQAAFTVYEDFLYYKSGVYQHTSGKQLGGHAVKIIGWGVENGVPYWLAANSWGTDWGENGYFRILRGSNE 226
                       250
                ....*....|
gi 1169087  346 CGIESGVVGG 355
Cdd:cd02620 227 CGIESEVVAG 236
Peptidase_C1 pfam00112
Papain family cysteine protease;
105-356 1.19e-85

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 258.63  E-value: 1.19e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087    105 IPESFDSRDNWpkcdSIKVIRDQSSCGSCWAFGAVEAMSDRICIASHGelQVTLSADDLLSCCKSCgFGCNGGDPLAAWR 184
Cdd:pfam00112   1 LPESFDWREKG----AVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGK--LVSLSEQQLVDCDTFN-NGCNGGLPDNAFE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087    185 YWVKD-GIVTGSNYtanngckPYPfppcEHHSKkthfdpcphdlyptpkCEKKCVSDYtdktYSEDKFFGASAYGvkdDV 263
Cdd:pfam00112  74 YIKKNgGIVTESDY-------PYT----AKDGT----------------CKFKKSNSK----VAKIKGYGDVPYN---DE 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087    264 EAIQKELMTHGPLEIAFEVYE-DFLNYDGGVYVHTGGKLGGGHAVKLIGWGIDDGIPYWTVANSWNTDWGEDGFFRILRG 342
Cdd:pfam00112 120 EALQAALAKNGPVSVAIDAYErDFQLYKSGVYKHTECGGELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARG 199
                         250
                  ....*....|....*
gi 1169087    343 VD-ECGIESGVVGGI 356
Cdd:pfam00112 200 VNnECGIASEASYPI 214
Pept_C1 smart00645
Papain family cysteine protease;
105-356 7.37e-60

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 191.26  E-value: 7.37e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087     105 IPESFDSRDNWpkCDSIkvIRDQSSCGSCWAFGAVEAMSDRICIASHGelQVTLSADDLLSCCKSCGFGCNGGDPLAAWR 184
Cdd:smart00645   1 LPESFDWRKKG--AVTP--VKDQGQCGSCWAFSATGALEGRYCIKTGK--LVSLSEQQLVDCSGGGNCGCNGGLPDNAFE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087     185 YWVKDGivtgsnYTANNGCKPYPFppcehhskkthfdpcphdlyptpkcekkcvsdytdktysedkffgasaygvkddve 264
Cdd:smart00645  75 YIKKNG------GLETESCYPYTG-------------------------------------------------------- 92
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087     265 aiqkelmthgpleIAFEVYEDFLNYDGGVYVHTG-GKLGGGHAVKLIGWG--IDDGIPYWTVANSWNTDWGEDGFFRILR 341
Cdd:smart00645  93 -------------SVAIDASDFQFYKSGIYDHPGcGSGTLDHAVLIVGYGteVENGKDYWIVKNSWGTDWGENGYFRIAR 159
                          250
                   ....*....|....*.
gi 1169087     342 GVD-ECGIESGVVGGI 356
Cdd:smart00645 160 GKNnECGIEASVASYP 175
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
106-353 1.27e-55

Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) similar to papain, including the mammalian CPs (cathepsins B, C, F, H, L, K, O, S, V, X and W). Papain is an endopeptidase with specific substrate preferences, primarily for bulky hydrophobic or aromatic residues at the S2 subsite, a hydrophobic pocket in papain that accommodates the P2 sidechain of the substrate (the second residue away from the scissile bond). Most members of the papain subfamily are endopeptidases. Some exceptions to this rule can be explained by specific details of the catalytic domains like the occluding loop in cathepsin B which confers an additional carboxydipeptidyl activity and the mini-chain of cathepsin H resulting in an N-terminal exopeptidase activity. Papain-like CPs have different functions in various organisms. Plant CPs are used to mobilize storage proteins in seeds. Parasitic CPs act extracellularly to help invade tissues and cells, to hatch or to evade the host immune system. Mammalian CPs are primarily lysosomal enzymes with the exception of cathepsin W, which is retained in the endoplasmic reticulum. They are responsible for protein degradation in the lysosome. Papain-like CPs are synthesized as inactive proenzymes with N-terminal propeptide regions, which are removed upon activation. In addition to its inhibitory role, the propeptide is required for proper folding of the newly synthesized enzyme and its stabilization in denaturing pH conditions. Residues within the propeptide region also play a role in the transport of the proenzyme to lysosomes or acidified vesicles. Also included in this subfamily are proteins classified as non-peptidase homologs, which lack peptidase activity or have missing active site residues.


Pssm-ID: 239068 [Multi-domain]  Cd Length: 210  Bit Score: 181.67  E-value: 1.27e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  106 PESFDSRDNwpkcDSIKVIRDQSSCGSCWAFGAVEAMSDRICIAsHGELqVTLSADDLLSCCKSCGFGCNGGDPLAAWRY 185
Cdd:cd02248   1 PESVDWREK----GAVTPVKDQGSCGSCWAFSTVGALEGAYAIK-TGKL-VSLSEQQLVDCSTSGNNGCNGGNPDNAFEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  186 WVKDGIVTGSNY--TANNG-CKpypFPPCEHHSKkthfdpcphdlyptpkcekkcVSDYTDKTYSedkffgasaygvkdD 262
Cdd:cd02248  75 VKNGGLASESDYpyTGKDGtCK---YNSSKVGAK---------------------ITGYSNVPPG--------------D 116
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  263 VEAIQKELMTHGPLEIAFEVYEDFLNYDGGVYVH-TGGKLGGGHAVKLIGWGIDDGIPYWTVANSWNTDWGEDGFFRILR 341
Cdd:cd02248 117 EEALKAALANYGPVSVAIDASSSFQFYKGGIYSGpCCSNTNLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIAR 196
                       250
                ....*....|..
gi 1169087  342 GVDECGIESGVV 353
Cdd:cd02248 197 GSNLCGIASYAS 208
Peptidase_C1A_CathepsinC cd02621
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ...
106-357 6.64e-45

Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine peptidase with chloride dependency and dipeptidyl aminopeptidase activity, resulting from its tetrameric structure which limits substrate access. Each subunit of the tetramer is composed of three peptides: the heavy and light chains, which together adopts the papain fold and forms the catalytic domain; and the residual propeptide region, which forms a beta barrel and points towards the substrate's N-terminus. The subunit composition is the result of the unique characteristic of procathepsin C maturation involving the cleavage of the catalytic domain and the non-autocatalytic excision of an activation peptide within its propeptide region. By removing N-terminal dipeptide extensions, cathepsin C activates granule serine peptidases (granzymes) involved in cell-mediated apoptosis, inflammation and tissue remodelling. Loss-of-function mutations in cathepsin C are associated with Papillon-Lefevre and Haim-Munk syndromes, rare diseases characterized by hyperkeratosis and early-onset periodontitis. Cathepsin C is widely expressed in many tissues with high levels in lung, kidney and placenta. It is also highly expressed in cytotoxic lymphocytes and mature myeloid cells.


Pssm-ID: 239112 [Multi-domain]  Cd Length: 243  Bit Score: 154.85  E-value: 6.64e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  106 PESFDSRDNWPKCDSIKVIRDQSSCGSCWAFGAVEAMSDRICIASHGELQVT----LSADDLLSCCKScGFGCNGGDPLA 181
Cdd:cd02621   2 PKSFDWGDVNNGFNYVSPVRNQGGCGSCYAFASVYALEARIMIASNKTDPLGqqpiLSPQHVLSCSQY-SQGCDGGFPFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  182 AWRYWVKDGIVTgsnytanNGCKPYpfppcehhskkthfdpcphdlypTPKCEKKCVSDYTDKT--YSEDKFFGASAYGV 259
Cdd:cd02621  81 VGKFAEDFGIVT-------EDYFPY-----------------------TADDDRPCKASPSECRryYFSDYNYVGGCYGC 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  260 KDDVEaIQKELMTHGPLEIAFEVYEDFLNYDGGVYVHTGGKLGGG-------------HAVKLIGWGIDD--GIPYWTVA 324
Cdd:cd02621 131 TNEDE-MKWEIYRNGPIVVAFEVYSDFDFYKEGVYHHTDNDEVSDgdndnfnpfeltnHAVLLVGWGEDEikGEKYWIVK 209
                       250       260       270
                ....*....|....*....|....*....|...
gi 1169087  325 NSWNTDWGEDGFFRILRGVDECGIESGVVGGIP 357
Cdd:cd02621 210 NSWGSSWGEKGYFKIRRGTNECGIESQAVFAYP 242
Peptidase_C1A_CathepsinX cd02698
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ...
105-358 3.25e-39

Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase activity. It can also act as a carboxydipeptidase, like cathepsin B, but has been shown to preferentially cleave substrates through a monopeptidyl carboxypeptidase pathway. The propeptide region of cathepsin X, the shortest among papain-like peptidases, is covalently attached to the active site cysteine in the inactive form of the enzyme. Little is known about the biological function of cathepsin X. Some studies point to a role in early tumorigenesis. A more recent study indicates that cathepsin X expression is restricted to immune cells suggesting a role in phagocytosis and the regulation of the immune response.


Pssm-ID: 239149  Cd Length: 239  Bit Score: 139.86  E-value: 3.25e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  105 IPESFDSRDNwPKCDSIKVIRDQ---SSCGSCWAFGAVEAMSDRICIASHGEL-QVTLSADDLLSCckSCGFGCNGGDPL 180
Cdd:cd02698   1 LPKSWDWRNV-NGVNYVSPTRNQhipQYCGSCWAHGSTSALADRINIARKGAWpSVYLSVQVVIDC--AGGGSCHGGDPG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  181 AAWRYWVKDGIV--TGSNYTANNG-CKPypFPPCehhskKThfdpCphdlypTPKCEKKCVSDYTdkTYSedkffgASAY 257
Cdd:cd02698  78 GVYEYAHKHGIPdeTCNPYQAKDGeCNP--FNRC-----GT----C------NPFGECFAIKNYT--LYF------VSDY 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  258 GVKDDVEAIQKELMTHGPLEIAFEVYEDFLNYDGGVYVHTGGKLGGGHAVKLIGWGIDD-GIPYWTVANSWNTDWGEDGF 336
Cdd:cd02698 133 GSVSGRDKMMAEIYARGPISCGIMATEALENYTGGVYKEYVQDPLINHIISVAGWGVDEnGVEYWIVRNSWGEPWGERGW 212
                       250       260
                ....*....|....*....|....*..
gi 1169087  337 FRILRGV-----DECGIESGVVGGIPK 358
Cdd:cd02698 213 FRIVTSSykgarYNLAIEEDCAWADPI 239
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
104-339 2.04e-32

Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 126.02  E-value: 2.04e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  104 DIPESFDSRDNWPKcdsikvIRDQSSCGSCWAFGAVEAM-SDRICIASHGELQVTLSADDLLSC----CKSCGFGCNGGD 178
Cdd:COG4870   3 ALPSSVDLRGYVTP------VKDQGSLGSCWAFATAAALeSYLKKQAGAPGTSLDLSELFLYNQarngDGTEGTDDGGSS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  179 PLAAWRYWVKDGIVTGSNYtanngckPYPfppcehhskkthfdpcphdlyptpkcEKKCVSDYTDKTYSEDKFFGASAY- 257
Cdd:COG4870  77 LRDALKLLRWSGVVPESDW-------PYD--------------------------DSDFTSQPSAAAYADARNYKIQDYy 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  258 -----GVKDDVEAIQKELMTHGPLEIAFEVYEDFLNYDGGVYVHT-GGKLGGGHAVKLIGWgiDDGIP--YWTVANSWNT 329
Cdd:COG4870 124 rlpggGGATDLDAIKQALAEGGPVVFGFYVYESFYNYTGGVYYPTpGDASLGGHAVAIVGY--DDNYSdgAFIIKNSWGT 201
                       250
                ....*....|
gi 1169087  330 DWGEDGFFRI 339
Cdd:COG4870 202 GWGDNGYFWI 211
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
124-339 7.99e-31

C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; composed of two subfamilies of cysteine peptidases (CPs), C1A (papain) and C1B (bleomycin hydrolase). Papain-like enzymes are mostly endopeptidases with some exceptions like cathepsins B, C, H and X, which are exopeptidases. Papain-like CPs have different functions in various organisms. Plant CPs are used to mobilize storage proteins in seeds while mammalian CPs are primarily lysosomal enzymes responsible for protein degradation in the lysosome. Papain-like CPs are synthesized as inactive proenzymes with N-terminal propeptide regions, which are removed upon activation. Bleomycin hydrolase (BH) is a CP that detoxifies bleomycin by hydrolysis of an amide group. It acts as a carboxypeptidase on its C-terminus to convert itself into an aminopeptidase and peptide ligase. BH is found in all tissues in mammals as well as in many other eukaryotes. It forms a hexameric ring barrel structure with the active sites imbedded in the central channel. Some members of the C1 family are proteins classified as non-peptidase homologs which lack peptidase activity or have missing active site residues.


Pssm-ID: 239110 [Multi-domain]  Cd Length: 223  Bit Score: 117.23  E-value: 7.99e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  124 IRDQSSCGSCWAFGAVEAMSDRICIASHGELQVTLSADDLLSC----CKSCGFGCNGGDPLAAWRY-WVKDGIVTGSNYt 198
Cdd:cd02619  12 VKNQGSRGSCWAFASAYALESAYRIKGGEDEYVDLSPQYLYICandeCLGINGSCDGGGPLSALLKlVALKGIPPEEDY- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087  199 aNNGCKPYPFPPCEHhskkthfdpcphdlyPTPKCEKKCVSDYtdktYSEDKFfgasaygvkdDVEAIQKELMTHGPLEI 278
Cdd:cd02619  91 -PYGAESDGEEPKSE---------------AALNAAKVKLKDY----RRVLKN----------NIEDIKEALAKGGPVVA 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169087  279 AFEVYEDFLNYDGG------VYVHTGGKLGGGHAVKLIGWGID--DGIPYWTVANSWNTDWGEDGFFRI 339
Cdd:cd02619 141 GFDVYSGFDRLKEGiiyeeiVYLLYEDGDLGGHAVVIVGYDDNyvEGKGAFIVKNSWGTDWGDNGYGRI 209
PTZ00200 PTZ00200
cysteine proteinase; Provisional
95-361 1.04e-29

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 119.03  E-value: 1.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087    95 LSKTKDLDLDI-------PESFDsrdnWPKCDSIKVIRDQSS-CGSCWAF---GAVEAMsdricIASHGELQVTLSADDL 163
Cdd:PTZ00200 217 LKKAKNTDEDVkdpskitGEGLD----WRRADAVTKVKDQGLnCGSCWAFssvGSVESL-----YKIYRDKSVDLSEQEL 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087   164 LSCCKSCGfGCNGGDPLAAWRYWVKDGIVTGSNYtanngckPYpfppcehHSKkthfdpcphdlyptpkcEKKCVSDYTD 243
Cdd:PTZ00200 288 VNCDTKSQ-GCSGGYPDTALEYVKNKGLSSSSDV-------PY-------LAK-----------------DGKCVVSSTK 335
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087   244 KTYSEDKFFgasAYGvKDdveaIQKELMTHGPLEIAFEVYEDFLNYDGGVYvhtGGKLGGG--HAVKLIGWGIDD--GIP 319
Cdd:PTZ00200 336 KVYIDSYLV---AKG-KD----VLNKSLVISPTVVYIAVSRELLKYKSGVY---NGECGKSlnHAVLLVGEGYDEktKKR 404
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 1169087   320 YWTVANSWNTDWGEDGFFRILR---GVDECGIESgvVGGIPKLNS 361
Cdd:PTZ00200 405 YWIIKNSWGTDWGENGYMRLERtneGTDKCGILT--VGLTPVFYS 447
PTZ00203 PTZ00203
cathepsin L protease; Provisional
93-346 1.18e-28

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 114.41  E-value: 1.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087    93 QHLSKTK-DLDLdIPESFDsrdnWPKCDSIKVIRDQSSCGSCWAFGAVEAMSDRICIASHGelQVTLSADDLLSCcKSCG 171
Cdd:PTZ00203 114 QHYRKARaDLSA-VPDAVD----WREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHK--LVRLSEQQLVSC-DHVD 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087   172 FGCNGGDPLAAWRYWVKD--GIV-TGSNY--TANNGckpyPFPPCEHHSkkthfdpcphDLYPTPKcekkcVSDYTDKTY 246
Cdd:PTZ00203 186 NGCGGGLMLQAFEWVLRNmnGTVfTEKSYpyVSGNG----DVPECSNSS----------ELAPGAR-----IDGYVSMES 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087   247 SEDkffgasaygvkddveAIQKELMTHGPLEIAFEVyEDFLNYDGGVYVHTGGKlGGGHAVKLIGWGIDDGIPYWTVANS 326
Cdd:PTZ00203 247 SER---------------VMAAWLAKNGPISIAVDA-SSFMSYHSGVLTSCIGE-QLNHGVLLVGYNMTGEVPYWVIKNS 309
                        250       260
                 ....*....|....*....|
gi 1169087   327 WNTDWGEDGFFRILRGVDEC 346
Cdd:PTZ00203 310 WGEDWGEKGYVRVTMGVNAC 329
PTZ00049 PTZ00049
cathepsin C-like protein; Provisional
16-350 7.28e-24

cathepsin C-like protein; Provisional


Pssm-ID: 240244 [Multi-domain]  Cd Length: 693  Bit Score: 103.49  E-value: 7.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087    16 CACNDNlESVLDKYRNREIDSEAAELDGDDLIDYVNENQNlwtakkqrrfSSVYGENDKAKWGLMGVNHVRLSVKgkqhl 95
Cdd:PTZ00049 310 CPCNKD-EHVQDEVNLGDSDQPVSPVSPVSLMQLGNTNFL----------AHVHGSDATNEMDLENYEDTEKAPH----- 373
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087    96 sktKDLDLD-IPESFDSRDNWPKCDSIKVIRDQSSCGSCWAFGAVEAMSDRICIASHGEL-QVTLSA-DDLLS--CCKSC 170
Cdd:PTZ00049 374 ---RELEIDeLPKNFTWGDPFNNNTREYDVTNQLLCGSCYIASQMYAFKRRIEIALTKNLdKKYLNNfDDLLSiqTVLSC 450
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087   171 GF---GCNGGDPLAAWRYWVKDGIVTGS--NYTANNGCKPYP---FPPCEHHSKKTHFDPCPHDLYPTPKC----EKKCV 238
Cdd:PTZ00049 451 SFydqGCNGGFPYLVSKMAKLQGIPLDKvfPYTATEQTCPYQvdqSANSMNGSANLRQINAVFFSSETQSDmhadFEAPI 530
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087   239 SDYTDKTYSEDKFFGASAYGVK--DDVEAIQKELMTHGPLEIAFEVYEDFLNYDGGVYV----------------HTG-G 299
Cdd:PTZ00049 531 SSEPARWYAKDYNYIGGCYGCNqcNGEKIMMNEIYRNGPIVASFEASPDFYDYADGVYYvedfpharrctvdlpkHNGvY 610
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 1169087   300 KLGG----GHAVKLIGWGID--DGIP--YWTVANSWNTDWGEDGFFRILRGVDECGIES 350
Cdd:PTZ00049 611 NITGwekvNHAIVLVGWGEEeiNGKLykYWIGRNSWGKNWGKEGYFKIIRGKNFSGIES 669
PTZ00021 PTZ00021
falcipain-2; Provisional
97-339 2.14e-17

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 83.28  E-value: 2.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087    97 KTKDLDLDiPESFDsrdnWPKCDSIKVIRDQSSCGSCWAFGAVEAMSDRICIASHgELqVTLSADDLLSCCKScGFGCNG 176
Cdd:PTZ00021 259 KPKDATFD-HAKYD----WRLHNGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKN-EL-VSLSEQELVDCSFK-NNGCYG 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087   177 GD-PLAAWRYWVKDGIVTGSNYtanngckPYpfppcehhskkthFDPCPHdlyptpKCE-KKCVSDYTDKTY---SEDKF 251
Cdd:PTZ00021 331 GLiPNAFEDMIELGGLCSEDDY-------PY-------------VSDTPE------LCNiDRCKEKYKIKSYvsiPEDKF 384
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087   252 fgasaygvkddVEAIQkelmTHGPLEIAFEVYEDFLNYDGGVYvhtGGKLGG--GHAVKLIGWGIDDGIP---------- 319
Cdd:PTZ00021 385 -----------KEAIR----FLGPISVSIAVSDDFAFYKGGIF---DGECGEepNHAVILVGYGMEEIYNsdtkkmekry 446
                        250       260
                 ....*....|....*....|
gi 1169087   320 YWTVANSWNTDWGEDGFFRI 339
Cdd:PTZ00021 447 YYIIKNSWGESWGEKGFIRI 466
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
130-354 7.99e-17

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381 [Multi-domain]  Cd Length: 548  Bit Score: 81.86  E-value: 7.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087   130 CGSCWAFGAVEAMSDRICIASHGE----LQVTLSADDLLSCCKScGFGCNGGDPLAAWRYWVKDGIVTgsnytanngckp 205
Cdd:PTZ00364 232 CNSSYVEAALAAMMARVMVASNRTdplgQQTFLSARHVLDCSQY-GQGCAGGFPEEVGKFAETFGILT------------ 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087   206 ypfppcehhskkthfdpcpHDLYPTPKCEKKCVSdYTDKTYSEDK--FFGA-----SAYGVKDDVEAIQKELMTHGPLEI 278
Cdd:PTZ00364 299 -------------------TDSYYIPYDSGDGVE-RACKTRRPSRryYFTNygplgGYYGAVTDPDEIIWEIYRHGPVPA 358
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087   279 AFEVYEDFLNYDGGVYVHTGGKLGG-------------------GHAVKLIGWGIDD-GIPYWTVANSWNT--DWGEDGF 336
Cdd:PTZ00364 359 SVYANSDWYNCDENSTEDVRYVSLDdystasadrplrhyfasnvNHTVLIIGWGTDEnGGDYWLVLDPWGSrrSWCDGGT 438
                        250
                 ....*....|....*...
gi 1169087   337 FRILRGVDECGIESGVVG 354
Cdd:PTZ00364 439 RKIARGVNAYNIESEVVV 456
PTZ00462 PTZ00462
Serine-repeat antigen protein; Provisional
47-339 8.26e-06

Serine-repeat antigen protein; Provisional


Pssm-ID: 185641 [Multi-domain]  Cd Length: 1004  Bit Score: 48.13  E-value: 8.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087     47 IDYVNENQNLWTAKKQRRFSSVYGENDKAKWGlMGVNHVRLSVKGKQHLSKTKDLDLDIPESFDSR-DNWPKCDSIKVIR 125
Cdd:PTZ00462  470 IEYFNEHEKLNEEKKRKIYDDKDSPEDKDNKG-KDIIHIDKTIEKEDTLKYDNNDKMFCNKEFCNRlKDENNCISKIQIE 548
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087    126 DQSSCGSCWAFGAVEAMSDRICIAshGELQVTLSADDLLSCCKS-----CGFGCNggdPLAAWRYWVKDGIVTG-SNYTA 199
Cdd:PTZ00462  549 DQGNCAISWIFASKYHLETIKCMK--GYEPHAISALYIANCSKGehkdrCDEGSN---PLEFLQIIEDNGFLPAdSNYLY 623
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169087    200 N-----NGCkpypfPPCEHH--SKKTHFDPCPHDlyptpKCEKKCVSDYTDKTYSEDKFfgasaygvKDDVEA----IQK 268
Cdd:PTZ00462  624 NytkvgEDC-----PDEEDHwmNLLDHGKILNHN-----KKEPNSLDGKAYRAYESEHF--------HDKMDAfikiIKD 685
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169087    269 ELMTHGPLeIAFEVYEDFLNYD--GGVYVHTGGKLGGGHAVKLIGWG-----IDDGIPYWTVANSWNTDWGEDGFFRI 339
Cdd:PTZ00462  686 EIMNKGSV-IAYIKAENVLGYEfnGKKVQNLCGDDTADHAVNIVGYGnyindEDEKKSYWIVRNSWGKYWGDEGYFKV 762
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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