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Conserved domains on  [gi|27465595|ref|NP_775155|]
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testin-2 precursor [Rattus norvegicus]

Protein Classification

C1 family peptidase( domain architecture ID 11276840)

C1 family peptidase (also called papain family protein) is a papain-like cysteine peptidase that catalyzes the hydrolysis of peptide bonds in substrates using a catalytic dyad of Cys and His residues

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_C1 pfam00112
Papain family cysteine protease;
114-332 7.42e-115

Papain family cysteine protease;


:

Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 331.04  E-value: 7.42e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595   114 VPKRVDWRQLGYVTPVKNQGHCASSWAFSATGSLEGQMFRKTERLIPLSEQNLLDCMGSNvtHGCSGGFMQYAFQYVKDN 193
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTFN--NGCNGGLPDNAFEYIKKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595   194 GGLATEESYPYRGQGRECRYHAENS-AANVRDFVQIP-GSEEALMKAVAKVGPISVAVDASHGSFQFYGSGIYYEPQCKR 271
Cdd:pfam00112  79 GGIVTESDYPYTAKDGTCKFKKSNSkVAKIKGYGDVPyNDEEALQAALAKNGPVSVAIDAYERDFQLYKSGVYKHTECGG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27465595   272 vHLNHAVLVVGYGFEgeesDGNSFWLVKNSWGEEWGMKGYMKLAKDWSNHCGIATYSTYPI 332
Cdd:pfam00112 159 -ELNHAVLLVGYGTE----NGVPYWIVKNSWGTDWGENGYFRIARGVNNECGIASEASYPI 214
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 29-87 9.87e-16

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.


:

Pssm-ID: 214853 [Multi-domain]  Cd Length: 57  Bit Score: 70.35  E-value: 9.87e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595     29 WNEWRTKHGKTYNMNEERLKR-AVWEKNFKMIELHNWEYlegRHDFTMAMNAFGDLTNIE 87
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRfAIFKENLKKIEEHNKKY---EHSYKLGVNQFSDLTPEE 57
 
Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
114-332 7.42e-115

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 331.04  E-value: 7.42e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595   114 VPKRVDWRQLGYVTPVKNQGHCASSWAFSATGSLEGQMFRKTERLIPLSEQNLLDCMGSNvtHGCSGGFMQYAFQYVKDN 193
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTFN--NGCNGGLPDNAFEYIKKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595   194 GGLATEESYPYRGQGRECRYHAENS-AANVRDFVQIP-GSEEALMKAVAKVGPISVAVDASHGSFQFYGSGIYYEPQCKR 271
Cdd:pfam00112  79 GGIVTESDYPYTAKDGTCKFKKSNSkVAKIKGYGDVPyNDEEALQAALAKNGPVSVAIDAYERDFQLYKSGVYKHTECGG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27465595   272 vHLNHAVLVVGYGFEgeesDGNSFWLVKNSWGEEWGMKGYMKLAKDWSNHCGIATYSTYPI 332
Cdd:pfam00112 159 -ELNHAVLLVGYGTE----NGVPYWIVKNSWGTDWGENGYFRIARGVNNECGIASEASYPI 214
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
 115-331 3.36e-110

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: 319.18  E-value: 3.36e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 115 PKRVDWRQLGYVTPVKNQGHCASSWAFSATGSLEGQMFRKTERLIPLSEQNLLDCMGSNvTHGCSGGFMQYAFQYVKdNG 194
Cdd:cd02248   1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSG-NNGCNGGNPDNAFEYVK-NG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 195 GLATEESYPYRGQGRECRYHAENSAANVRDFVQIP-GSEEALMKAVAKVGPISVAVDASHgSFQFYGSGIYYEPQCKRVH 273
Cdd:cd02248  79 GLASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPpGDEEALKAALANYGPVSVAIDASS-SFQFYKGGIYSGPCCSNTN 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27465595 274 LNHAVLVVGYGFEgeesDGNSFWLVKNSWGEEWGMKGYMKLAKDwSNHCGIATYSTYP 331
Cdd:cd02248 158 LNHAVLLVGYGTE----NGVDYWIVKNSWGTSWGEKGYIRIARG-SNLCGIASYASYP 210
Pept_C1 smart00645
Papain family cysteine protease;
114-331 1.23e-86

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 257.90  E-value: 1.23e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595    114 VPKRVDWRQLGYVTPVKNQGHCASSWAFSATGSLEGQMFRKTERLIPLSEQNLLDCMGSNvTHGCSGGFMQYAFQYVKDN 193
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGGG-NCGCNGGLPDNAFEYIKKN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595    194 GGLATEESYPYRGqgrecryhaensaanvrdfvqipgseealmkavakvgpiSVAVDASHgsFQFYGSGIYYEPQCKRVH 273
Cdd:smart00645  80 GGLETESCYPYTG---------------------------------------SVAIDASD--FQFYKSGIYDHPGCGSGT 118

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 27465595    274 LNHAVLVVGYGFEGEesDGNSFWLVKNSWGEEWGMKGYMKLAKDWSNHCGI-ATYSTYP 331
Cdd:smart00645 119 LDHAVLIVGYGTEVE--NGKDYWIVKNSWGTDWGENGYFRIARGKNNECGIeASVASYP 175
PTZ00203 PTZ00203
cathepsin L protease; Provisional
 29-327 7.59e-63

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 203.39  E-value: 7.59e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595   29 WNEWRTKHGKTY-NMNEERLKRAVWEKNFKMIELHNWEYLEGRHDFTmamnAFGDLTNIEF-VKMMTGFQRQKIKKTHIF 106
Cdd:PTZ00203  38 FEEFKRTYQRAYgTLTEEQQRLANFERNLELMREHQARNPHARFGIT----KFFDLSEAEFaARYLNGAAYFAAAKQHAG 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595  107 QDHQ-----FLYVPKRVDWRQLGYVTPVKNQGHCASSWAFSATGSLEGQMFRKTERLIPLSEQNLLDCmgSNVTHGCSGG 181
Cdd:PTZ00203 114 QHYRkaradLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSC--DHVDNGCGGG 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595  182 FMQYAFQYVKDN--GGLATEESYPY---RGQGRECRYHAE-NSAANVRDFVQIPGSEEALMKAVAKVGPISVAVDAShgS 255
Cdd:PTZ00203 192 LMLQAFEWVLRNmnGTVFTEKSYPYvsgNGDVPECSNSSElAPGARIDGYVSMESSERVMAAWLAKNGPISIAVDAS--S 269

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27465595  256 FQFYGSGIYyePQCKRVHLNHAVLVVGYGFEGEEsdgnSFWLVKNSWGEEWGMKGYMKLAKDwSNHCGIATY 327
Cdd:PTZ00203 270 FMSYHSGVL--TSCIGEQLNHGVLLVGYNMTGEV----PYWVIKNSWGEDWGEKGYVRVTMG-VNACLLTGY 334
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
114-325 2.50e-41

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 149.13  E-value: 2.50e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 114 VPKRVDWRQlgYVTPVKNQGHCASSWAFSATGSLEGQMFRKTERL---IPLSEQNLLDCMGS-NVTHG--CSGGFMQYAF 187
Cdd:COG4870   4 LPSSVDLRG--YVTPVKDQGSLGSCWAFATAAALESYLKKQAGAPgtsLDLSELFLYNQARNgDGTEGtdDGGSSLRDAL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 188 QYVKDNGgLATEESYPYRGQGRECRYHAE--NSAANVR--DFVQIPGSE-----EALMKAVAKVGPISVAVDAsHGSFQF 258
Cdd:COG4870  82 KLLRWSG-VVPESDWPYDDSDFTSQPSAAayADARNYKiqDYYRLPGGGgatdlDAIKQALAEGGPVVFGFYV-YESFYN 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27465595 259 YGSGIYYEPQCKRVHLNHAVLVVGYgfegEESDGNSFWLVKNSWGEEWGMKGYMKLA-KDWSNHCGIA 325
Cdd:COG4870 160 YTGGVYYPTPGDASLGGHAVAIVGY----DDNYSDGAFIIKNSWGTGWGDNGYFWISyDDLLIGAGAA 223
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 29-87 9.87e-16

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.


Pssm-ID: 214853 [Multi-domain]  Cd Length: 57  Bit Score: 70.35  E-value: 9.87e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595     29 WNEWRTKHGKTYNMNEERLKR-AVWEKNFKMIELHNWEYlegRHDFTMAMNAFGDLTNIE 87
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRfAIFKENLKKIEEHNKKY---EHSYKLGVNQFSDLTPEE 57
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 29-88 6.74e-14

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 Swiss:Q70SU8. This family is classified as I29 by MEROPS.


Pssm-ID: 462410 [Multi-domain]  Cd Length: 58  Bit Score: 65.36  E-value: 6.74e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27465595    29 WNEWRTKHGKTYNMNEERLKR-AVWEKNFKMIELHNweyLEGRHDFTMAMNAFGDLTNIEF 88
Cdd:pfam08246   1 FDDWMKKYGKSYRSEEEELYRfQIFKENLKRIEEHN---SNGNVTYKLGLNKFADLTDEEF 58
 
Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
114-332 7.42e-115

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 331.04  E-value: 7.42e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595   114 VPKRVDWRQLGYVTPVKNQGHCASSWAFSATGSLEGQMFRKTERLIPLSEQNLLDCMGSNvtHGCSGGFMQYAFQYVKDN 193
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTFN--NGCNGGLPDNAFEYIKKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595   194 GGLATEESYPYRGQGRECRYHAENS-AANVRDFVQIP-GSEEALMKAVAKVGPISVAVDASHGSFQFYGSGIYYEPQCKR 271
Cdd:pfam00112  79 GGIVTESDYPYTAKDGTCKFKKSNSkVAKIKGYGDVPyNDEEALQAALAKNGPVSVAIDAYERDFQLYKSGVYKHTECGG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27465595   272 vHLNHAVLVVGYGFEgeesDGNSFWLVKNSWGEEWGMKGYMKLAKDWSNHCGIATYSTYPI 332
Cdd:pfam00112 159 -ELNHAVLLVGYGTE----NGVPYWIVKNSWGTDWGENGYFRIARGVNNECGIASEASYPI 214
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
 115-331 3.36e-110

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: 319.18  E-value: 3.36e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 115 PKRVDWRQLGYVTPVKNQGHCASSWAFSATGSLEGQMFRKTERLIPLSEQNLLDCMGSNvTHGCSGGFMQYAFQYVKdNG 194
Cdd:cd02248   1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSG-NNGCNGGNPDNAFEYVK-NG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 195 GLATEESYPYRGQGRECRYHAENSAANVRDFVQIP-GSEEALMKAVAKVGPISVAVDASHgSFQFYGSGIYYEPQCKRVH 273
Cdd:cd02248  79 GLASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPpGDEEALKAALANYGPVSVAIDASS-SFQFYKGGIYSGPCCSNTN 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27465595 274 LNHAVLVVGYGFEgeesDGNSFWLVKNSWGEEWGMKGYMKLAKDwSNHCGIATYSTYP 331
Cdd:cd02248 158 LNHAVLLVGYGTE----NGVDYWIVKNSWGTSWGEKGYIRIARG-SNLCGIASYASYP 210
Pept_C1 smart00645
Papain family cysteine protease;
114-331 1.23e-86

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 257.90  E-value: 1.23e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595    114 VPKRVDWRQLGYVTPVKNQGHCASSWAFSATGSLEGQMFRKTERLIPLSEQNLLDCMGSNvTHGCSGGFMQYAFQYVKDN 193
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGGG-NCGCNGGLPDNAFEYIKKN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595    194 GGLATEESYPYRGqgrecryhaensaanvrdfvqipgseealmkavakvgpiSVAVDASHgsFQFYGSGIYYEPQCKRVH 273
Cdd:smart00645  80 GGLETESCYPYTG---------------------------------------SVAIDASD--FQFYKSGIYDHPGCGSGT 118

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 27465595    274 LNHAVLVVGYGFEGEesDGNSFWLVKNSWGEEWGMKGYMKLAKDWSNHCGI-ATYSTYP 331
Cdd:smart00645 119 LDHAVLIVGYGTEVE--NGKDYWIVKNSWGTDWGENGYFRIARGKNNECGIeASVASYP 175
PTZ00203 PTZ00203
cathepsin L protease; Provisional
 29-327 7.59e-63

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 203.39  E-value: 7.59e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595   29 WNEWRTKHGKTY-NMNEERLKRAVWEKNFKMIELHNWEYLEGRHDFTmamnAFGDLTNIEF-VKMMTGFQRQKIKKTHIF 106
Cdd:PTZ00203  38 FEEFKRTYQRAYgTLTEEQQRLANFERNLELMREHQARNPHARFGIT----KFFDLSEAEFaARYLNGAAYFAAAKQHAG 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595  107 QDHQ-----FLYVPKRVDWRQLGYVTPVKNQGHCASSWAFSATGSLEGQMFRKTERLIPLSEQNLLDCmgSNVTHGCSGG 181
Cdd:PTZ00203 114 QHYRkaradLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSC--DHVDNGCGGG 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595  182 FMQYAFQYVKDN--GGLATEESYPY---RGQGRECRYHAE-NSAANVRDFVQIPGSEEALMKAVAKVGPISVAVDAShgS 255
Cdd:PTZ00203 192 LMLQAFEWVLRNmnGTVFTEKSYPYvsgNGDVPECSNSSElAPGARIDGYVSMESSERVMAAWLAKNGPISIAVDAS--S 269

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27465595  256 FQFYGSGIYyePQCKRVHLNHAVLVVGYGFEGEEsdgnSFWLVKNSWGEEWGMKGYMKLAKDwSNHCGIATY 327
Cdd:PTZ00203 270 FMSYHSGVL--TSCIGEQLNHGVLLVGYNMTGEV----PYWVIKNSWGEDWGEKGYVRVTMG-VNACLLTGY 334
PTZ00021 PTZ00021
falcipain-2; Provisional
 36-333 1.43e-55

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 188.06  E-value: 1.43e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595   36 HGKTYNMNEERLKR-AVWEKNFKMIELHNWE----YLEGrhdftmaMNAFGDLTNIEF-VKMMT----GFQRQKIKKTHI 105
Cdd:PTZ00021 176 HGKKYQTPDEMQQRyLSFVENLAKINAHNNKenvlYKKG-------MNRFGDLSFEEFkKKYLTlksfDFKSNGKKSPRV 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595  106 --FQDHQFLYVPK-------RVDWRQLGYVTPVKNQGHCASSWAFSATGSLEGQ-MFRKTErLIPLSEQNLLDCMGSNvt 175
Cdd:PTZ00021 249 inYDDVIKKYKPKdatfdhaKYDWRLHNGVTPVKDQKNCGSCWAFSTVGVVESQyAIRKNE-LVSLSEQELVDCSFKN-- 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595  176 HGCSGGFMQYAFQYVKDNGGLATEESYPYRGQGRE-CRYHAENSAANVRDFVQIPgsEEALMKAVAKVGPISVAVDASHg 254
Cdd:PTZ00021 326 NGCYGGLIPNAFEDMIELGGLCSEDDYPYVSDTPElCNIDRCKEKYKIKSYVSIP--EDKFKEAIRFLGPISVSIAVSD- 402

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595  255 SFQFYGSGIyYEPQCKRvHLNHAVLVVGYGFE---GEESDGNS---FWLVKNSWGEEWGMKGYMKLAKDWSNH---CGIA 325
Cdd:PTZ00021 403 DFAFYKGGI-FDGECGE-EPNHAVILVGYGMEeiyNSDTKKMEkryYYIIKNSWGESWGEKGFIRIETDENGLmktCSLG 480


                 ....*...
gi 27465595  326 TYSTYPIV 333
Cdd:PTZ00021 481 TEAYVPLI 488
PTZ00200 PTZ00200
cysteine proteinase; Provisional
 20-332 6.45e-50

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 172.19  E-value: 6.45e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595   20 TPDPSLD----VEWNEWRTKHGKTYNMNEERLKRAV-WEKNFKMIELHnweylEGRHDFTMAMNAFGDLTNIEFVKM--- 91
Cdd:PTZ00200 113 SDDPKLEfevyLEFEEFNKKYNRKHATHAERLNRFLtFRNNYLEVKSH-----KGDEPYSKEINKFSDLTEEEFRKLfpv 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595   92 MTGFQRQKIKKTH------IFQDHQFL-------------YVPKRV-----DWRQLGYVTPVKNQG-HCASSWAFSATGS 146
Cdd:PTZ00200 188 IKVPPKSNSTSHNndfkarHVSNPTYLknlkkakntdedvKDPSKItgeglDWRRADAVTKVKDQGlNCGSCWAFSSVGS 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595  147 LEGQMFRKTERLIPLSEQNLLDCMGSNvtHGCSGGFMQYAFQYVKdNGGLATEESYPYRGQGRECRYHAensaanvRDFV 226
Cdd:PTZ00200 268 VESLYKIYRDKSVDLSEQELVNCDTKS--QGCSGGYPDTALEYVK-NKGLSSSSDVPYLAKDGKCVVSS-------TKKV 337

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595  227 QIPGSEEALMKAVAK----VGPISVAVDASHgSFQFYGSGIYYEPqCKrVHLNHAVLVVGYGFEgeESDGNSFWLVKNSW 302
Cdd:PTZ00200 338 YIDSYLVAKGKDVLNkslvISPTVVYIAVSR-ELLKYKSGVYNGE-CG-KSLNHAVLLVGEGYD--EKTKKRYWIIKNSW 412

                        330       340       350
                 ....*....|....*....|....*....|..
gi 27465595  303 GEEWGMKGYMKLA--KDWSNHCGIATYSTYPI 332
Cdd:PTZ00200 413 GTDWGENGYMRLErtNEGTDKCGILTVGLTPV 444
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
114-325 2.50e-41

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 149.13  E-value: 2.50e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 114 VPKRVDWRQlgYVTPVKNQGHCASSWAFSATGSLEGQMFRKTERL---IPLSEQNLLDCMGS-NVTHG--CSGGFMQYAF 187
Cdd:COG4870   4 LPSSVDLRG--YVTPVKDQGSLGSCWAFATAAALESYLKKQAGAPgtsLDLSELFLYNQARNgDGTEGtdDGGSSLRDAL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 188 QYVKDNGgLATEESYPYRGQGRECRYHAE--NSAANVR--DFVQIPGSE-----EALMKAVAKVGPISVAVDAsHGSFQF 258
Cdd:COG4870  82 KLLRWSG-VVPESDWPYDDSDFTSQPSAAayADARNYKiqDYYRLPGGGgatdlDAIKQALAEGGPVVFGFYV-YESFYN 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27465595 259 YGSGIYYEPQCKRVHLNHAVLVVGYgfegEESDGNSFWLVKNSWGEEWGMKGYMKLA-KDWSNHCGIA 325
Cdd:COG4870 160 YTGGVYYPTPGDASLGGHAVAIVGY----DDNYSDGAFIIKNSWGTGWGDNGYFWISyDDLLIGAGAA 223
Peptidase_C1A_CathepsinC cd02621
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ...
 115-332 1.67e-37

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: 134.05  E-value: 1.67e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 115 PKRVDWRQLG----YVTPVKNQGHCASSWAFSATGSLEGQMFRKTERLIP------LSEQNLLDCmgSNVTHGCSGGFMQ 184
Cdd:cd02621   2 PKSFDWGDVNngfnYVSPVRNQGGCGSCYAFASVYALEARIMIASNKTDPlgqqpiLSPQHVLSC--SQYSQGCDGGFPF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 185 YAFQYVKDNGgLATEESYPYRGQG-RECRYHAENSaanVR----DFVQIPG-----SEEALMKAVAKVGPISVAVDAsHG 254
Cdd:cd02621  80 LVGKFAEDFG-IVTEDYFPYTADDdRPCKASPSEC---RRyyfsDYNYVGGcygctNEDEMKWEIYRNGPIVVAFEV-YS 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 255 SFQFYGSGIYY---------EPQCKRVH---LNHAVLVVGYGfeGEESDGNSFWLVKNSWGEEWGMKGYMKLAKDwSNHC 322
Cdd:cd02621 155 DFDFYKEGVYHhtdndevsdGDNDNFNPfelTNHAVLLVGWG--EDEIKGEKYWIVKNSWGSSWGEKGYFKIRRG-TNEC 231

                       250
                ....*....|..
gi 27465595 323 GIATYST--YPI 332
Cdd:cd02621 232 GIESQAVfaYPI 243
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
 118-327 9.97e-36

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: 129.17  E-value: 9.97e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 118 VDWRQLgYVTPVKNQGHCASSWAFSATGSLEGQMFRKTER--LIPLSEQNLLDCMGSNV---THGCSGGFMQYAFQYVKD 192
Cdd:cd02619   2 VDLRPL-RLTPVKNQGSRGSCWAFASAYALESAYRIKGGEdeYVDLSPQYLYICANDEClgiNGSCDGGGPLSALLKLVA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 193 NGGLATEESYPYRGQ--GRECRYHAENSAANVR--DFVQI-PGSEEALMKAVAKVGPISVAVDAsHGSFQFYGSGIYYEP 267
Cdd:cd02619  81 LKGIPPEEDYPYGAEsdGEEPKSEAALNAAKVKlkDYRRVlKNNIEDIKEALAKGGPVVAGFDV-YSGFDRLKEGIIYEE 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27465595 268 Q-----CKRVHLNHAVLVVGYGFEgeESDGNSFWLVKNSWGEEWGMKGYMKL-AKDWSNHCGIATY 327
Cdd:cd02619 160 IvyllyEDGDLGGHAVVIVGYDDN--YVEGKGAFIVKNSWGTDWGDNGYGRIsYEDVYEMTFGANV 223
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
 117-324 6.39e-35

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: 127.39  E-value: 6.39e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 117 RVDWRQLGYVTPVKNQGHCASSWAFSATGSLegqmfrkTERL---------IPLSEQNLLDCMGSNvTHGCSGGFMQYAF 187
Cdd:cd02620   7 REKWPNCISIGEIRDQGNCGSCWAFSAVEAF-------SDRLciqsngkenVLLSAQDLLSCCSGC-GDGCNGGYPDAAW 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 188 QYVKDNGgLATEESYPY------------------RGQGRECRYHAENSAANVRDFV----QIPGSEEALMKAVAKVGPI 245
Cdd:cd02620  79 KYLTTTG-VVTGGCQPYtippcghhpegpppccgtPYCTPKCQDGCEKTYEEDKHKGksaySVPSDETDIMKEIMTNGPV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 246 SVAVDAsHGSFQFYGSGIYyepqckrVHLN------HAVLVVGYGFEgeesDGNSFWLVKNSWGEEWGMKGYMKLAKDwS 319
Cdd:cd02620 158 QAAFTV-YEDFLYYKSGVY-------QHTSgkqlggHAVKIIGWGVE----NGVPYWLAANSWGTDWGENGYFRILRG-S 224


                ....*
gi 27465595 320 NHCGI 324
Cdd:cd02620 225 NECGI 229
Peptidase_C1A_CathepsinX cd02698
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ...
 114-315 7.71e-35

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: 127.14  E-value: 7.71e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 114 VPKRVDWRQL---GYVTPVKNQ---GHCASSWAFSATGSLEGQMF--RKTER-LIPLSEQNLLDCMGSNvthGCSGGFMQ 184
Cdd:cd02698   1 LPKSWDWRNVngvNYVSPTRNQhipQYCGSCWAHGSTSALADRINiaRKGAWpSVYLSVQVVIDCAGGG---SCHGGDPG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595 185 YAFQYVKDNGgLATEESYPYRGQGREC-RYHAENSA--------------ANVRDFVQIPGsEEALMKAVAKVGPISVAV 249
Cdd:cd02698  78 GVYEYAHKHG-IPDETCNPYQAKDGECnPFNRCGTCnpfgecfaiknytlYFVSDYGSVSG-RDKMMAEIYARGPISCGI 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27465595 250 DAsHGSFQFYGSGIYYEPQcKRVHLNHAVLVVGYGfegEESDGNSFWLVKNSWGEEWGMKGYMKLA 315
Cdd:cd02698 156 MA-TEALENYTGGVYKEYV-QDPLINHIISVAGWG---VDENGVEYWIVRNSWGEPWGERGWFRIV 216
PTZ00049 PTZ00049
cathepsin C-like protein; Provisional
 129-330 4.42e-17

cathepsin C-like protein; Provisional


Pssm-ID: 240244 [Multi-domain]  Cd Length: 693  Bit Score: 81.92  E-value: 4.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595  129 VKNQGHCASSWAFSA------------TGSLEGQMFRKTERLipLSEQNLLDCmgSNVTHGCSGGFMQYAFQYVKDNG-- 194
Cdd:PTZ00049 400 VTNQLLCGSCYIASQmyafkrrieialTKNLDKKYLNNFDDL--LSIQTVLSC--SFYDQGCNGGFPYLVSKMAKLQGip 475

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595  195 ------GLATEESYPYR----------------------GQGRECRYHA--ENSAAN------VRDFVQIPG-------- 230
Cdd:PTZ00049 476 ldkvfpYTATEQTCPYQvdqsansmngsanlrqinavffSSETQSDMHAdfEAPISSeparwyAKDYNYIGGcygcnqcn 555

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595  231 SEEALMKAVAKVGPISVAVDAShGSFQFYGSGIYY---EPQCKRV-----------------HLNHAVLVVGYGFEGEES 290
Cdd:PTZ00049 556 GEKIMMNEIYRNGPIVASFEAS-PDFYDYADGVYYvedFPHARRCtvdlpkhngvynitgweKVNHAIVLVGWGEEEING 634

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 27465595  291 DGNSFWLVKNSWGEEWGMKGYMKLAKDwSNHCGIATYSTY 330
Cdd:PTZ00049 635 KLYKYWIGRNSWGKNWGKEGYFKIIRG-KNFSGIESQSLF 673
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 29-87 9.87e-16

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.


Pssm-ID: 214853 [Multi-domain]  Cd Length: 57  Bit Score: 70.35  E-value: 9.87e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595     29 WNEWRTKHGKTYNMNEERLKR-AVWEKNFKMIELHNWEYlegRHDFTMAMNAFGDLTNIE 87
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRfAIFKENLKKIEEHNKKY---EHSYKLGVNQFSDLTPEE 57
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
 115-329 1.30e-14

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381 [Multi-domain]  Cd Length: 548  Bit Score: 74.54  E-value: 1.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595  115 PKRVDWRQLG---YVTPVKNQGH---CASSWAFSATGSLEGQMFRKTERLIP------LSEQNLLDCmgSNVTHGCSGGF 182
Cdd:PTZ00364 206 PAAWSWGDVGgasFLPAAPPASPgrgCNSSYVEAALAAMMARVMVASNRTDPlgqqtfLSARHVLDC--SQYGQGCAGGF 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595  183 MQYAFQYVKDNGGLATEESY-PYRgQGRECRYHAENSAANVRDFV----QIPG------SEEALMKAVAKVGPISVAVDA 251
Cdd:PTZ00364 284 PEEVGKFAETFGILTTDSYYiPYD-SGDGVERACKTRRPSRRYYFtnygPLGGyygavtDPDEIIWEIYRHGPVPASVYA 362

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595  252 SHGSFQ----FYGSGIYYEPQCKRV-------------HLNHAVLVVGYgfeGEESDGNSFWLVKNSWGEE--WGMKGYM 312
Cdd:PTZ00364 363 NSDWYNcdenSTEDVRYVSLDDYSTasadrplrhyfasNVNHTVLIIGW---GTDENGGDYWLVLDPWGSRrsWCDGGTR 439

                        250
                 ....*....|....*..
gi 27465595  313 KLAKDwSNHCGIATYST 329
Cdd:PTZ00364 440 KIARG-VNAYNIESEVV 455
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 29-88 6.74e-14

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 Swiss:Q70SU8. This family is classified as I29 by MEROPS.


Pssm-ID: 462410 [Multi-domain]  Cd Length: 58  Bit Score: 65.36  E-value: 6.74e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27465595    29 WNEWRTKHGKTYNMNEERLKR-AVWEKNFKMIELHNweyLEGRHDFTMAMNAFGDLTNIEF 88
Cdd:pfam08246   1 FDDWMKKYGKSYRSEEEELYRfQIFKENLKRIEEHN---SNGNVTYKLGLNKFADLTDEEF 58
PTZ00462 PTZ00462
Serine-repeat antigen protein; Provisional
 129-322 4.73e-13

Serine-repeat antigen protein; Provisional


Pssm-ID: 185641 [Multi-domain]  Cd Length: 1004  Bit Score: 70.09  E-value: 4.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595   129 VKNQGHCASSWAFSATGSLEGQMFRKTERLIPLSEQNLLDCMGSNVTHGCSGGFMQYAF-QYVKDNGGLATEESYPYR-- 205
Cdd:PTZ00462  547 IEDQGNCAISWIFASKYHLETIKCMKGYEPHAISALYIANCSKGEHKDRCDEGSNPLEFlQIIEDNGFLPADSNYLYNyt 626

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27465595   206 GQGREC---------------------------------RYHAENSAANVRDFVQIPGSEealmkaVAKVGPISVAVDAS 252
Cdd:PTZ00462  627 KVGEDCpdeedhwmnlldhgkilnhnkkepnsldgkayrAYESEHFHDKMDAFIKIIKDE------IMNKGSVIAYIKAE 700

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27465595   253 HG-SFQFYGSGIyyEPQCKRVHLNHAVLVVGYG-FEGEESDGNSFWLVKNSWGEEWGMKGYMKLAKDWSNHC 322
Cdd:PTZ00462  701 NVlGYEFNGKKV--QNLCGDDTADHAVNIVGYGnYINDEDEKKSYWIVRNSWGKYWGDEGYFKVDMYGPSHC 770
Peptidase_C1_2 pfam03051
Peptidase C1-like family; This family is closely related to the Peptidase_C1 family pfam00112, ...
 274-318 1.62e-03

Peptidase C1-like family; This family is closely related to the Peptidase_C1 family pfam00112, containing several prokaryotic and eukaryotic aminopeptidases and bleomycin hydrolases.


Pssm-ID: 397262  Cd Length: 438  Bit Score: 40.02  E-value: 1.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 27465595   274 LNHAVLVVGYGfegEESDGNSF-WLVKNSWGEEWGMKGYMKLAKDW 318
Cdd:pfam03051 359 MTHAMVLTGVD---EDDDGKPTkWKVENSWGEDSGEKGYFVMSDDW 401
PepC COG3579
Aminopeptidase C [Amino acid transport and metabolism];
274-318 1.66e-03

Aminopeptidase C [Amino acid transport and metabolism];


Pssm-ID: 442798 [Multi-domain]  Cd Length: 440  Bit Score: 39.86  E-value: 1.66e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 27465595 274 LNHAVLVVGYGFEgeeSDGNS-FWLVKNSWGEEWGMKGYMKLAKDW 318
Cdd:COG3579 361 DTHAMVITGVDLD---QNGKPtRWKVENSWGDDNGYKGYFYMSDAW 403
 
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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