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Conserved domains on  [gi|8393218|ref|NP_058793|]
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dipeptidyl peptidase 1 precursor [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C1A_CathepsinC cd02621
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ...
230-459 3.45e-124

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  Cd Length: 243  Bit Score: 365.17  E-value: 3.45e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  230 LPESWDWRNVR-GINFVSPVRNQESCGSCYSFASLGMLEARIRILTNN----SQTPILSPQEVVSCSPYAQGCDGGFPYL 304
Cdd:cd02621   1 LPKSFDWGDVNnGFNYVSPVRNQGGCGSCYAFASVYALEARIMIASNKtdplGQQPILSPQHVLSCSQYSQGCDGGFPFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  305 IaGKYAQDFGVVEENCFPYTA-TDAPCK-PKENCLRYYSSEYYYVGGFYGGCNEALMKLELVKHGPMAVAFEVHDDFLHY 382
Cdd:cd02621  81 V-GKFAEDFGIVTEDYFPYTAdDDRPCKaSPSECRRYYFSDYNYVGGCYGCTNEDEMKWEIYRNGPIVVAFEVYSDFDFY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  383 HSGIYHHT-------GLSDPFNPFELTNHAVLLVGYGKDPVTGLDYWIVKNSWGSQWGESGYFRIRRGTDECAIESIAMA 455
Cdd:cd02621 160 KEGVYHHTdndevsdGDNDNFNPFELTNHAVLLVGWGEDEIKGEKYWIVKNSWGSSWGEKGYFKIRRGTNECGIESQAVF 239

                ....
gi 8393218  456 AIPI 459
Cdd:cd02621 240 AYPI 243
CathepsinC_exc pfam08773
Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological ...
26-138 3.12e-62

Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological activator of a group of serine proteases. This domain corresponds to the exclusion domain whose structure excludes the approach of a polypeptide apart from its termini. It forms an enclosed beta barrel structure composed from 8 anti-parallel beta strands. Based on a structural comparison and interaction data, it is suggested that the exclusion domain originates from a metallo-protease inhibitor.


:

Pssm-ID: 312344  Cd Length: 117  Bit Score: 200.96  E-value: 3.12e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218     26 TPANCTYPDLLGTWVFQVGPRHPRSHINCSVMEP----TEEKVVIHLKKLDTAYDEVGNSGYFTLIYNQGFEIVLNDYKW 101
Cdd:pfam08773   1 TPVNCTYEDIVGTWKFQVGKGGGDKRVNCSHMGPdnfnPSKTVTVHLLKPNVVIDELGNTGFWTLIYNQGFEVVINNRKY 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 8393218    102 FAFFKYEVKGSRAISYCHETMTGWVHDVLGRNWACFV 138
Cdd:pfam08773  81 FAFFKYKKNGSNVTSYCNETLPGWYHDVLGRNWACFR 117
Pox_I6 super family cl28439
Poxvirus I6-like family; This family includes I6 proteins as well as the related F5L proteins.
168-204 5.78e-03

Poxvirus I6-like family; This family includes I6 proteins as well as the related F5L proteins.


The actual alignment was detected with superfamily member pfam04595:

Pssm-ID: 333259  Cd Length: 320  Bit Score: 38.48  E-value: 5.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 8393218    168 YSHNHNFVKAINS---VQKSWTATTYEEYEKLSIRDLIRR 204
Cdd:pfam04595  14 YCNENLFNKPENTlddVSKSLLILESFKYEKYVISGLIKI 53
 
Name Accession Description Interval E-value
Peptidase_C1A_CathepsinC cd02621
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ...
230-459 3.45e-124

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  Cd Length: 243  Bit Score: 365.17  E-value: 3.45e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  230 LPESWDWRNVR-GINFVSPVRNQESCGSCYSFASLGMLEARIRILTNN----SQTPILSPQEVVSCSPYAQGCDGGFPYL 304
Cdd:cd02621   1 LPKSFDWGDVNnGFNYVSPVRNQGGCGSCYAFASVYALEARIMIASNKtdplGQQPILSPQHVLSCSQYSQGCDGGFPFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  305 IaGKYAQDFGVVEENCFPYTA-TDAPCK-PKENCLRYYSSEYYYVGGFYGGCNEALMKLELVKHGPMAVAFEVHDDFLHY 382
Cdd:cd02621  81 V-GKFAEDFGIVTEDYFPYTAdDDRPCKaSPSECRRYYFSDYNYVGGCYGCTNEDEMKWEIYRNGPIVVAFEVYSDFDFY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  383 HSGIYHHT-------GLSDPFNPFELTNHAVLLVGYGKDPVTGLDYWIVKNSWGSQWGESGYFRIRRGTDECAIESIAMA 455
Cdd:cd02621 160 KEGVYHHTdndevsdGDNDNFNPFELTNHAVLLVGWGEDEIKGEKYWIVKNSWGSSWGEKGYFKIRRGTNECGIESQAVF 239

                ....
gi 8393218  456 AIPI 459
Cdd:cd02621 240 AYPI 243
Peptidase_C1 pfam00112
Papain family cysteine protease;
230-457 2.92e-74

Papain family cysteine protease;


Pssm-ID: 306594  Cd Length: 214  Bit Score: 235.52  E-value: 2.92e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218    230 LPESWDWRNVrgiNFVSPVRNQESCGSCYSFASLGMLEARIRILTNNSqtPILSPQEVVSCSPYAQGCDGGFPYLiAGKY 309
Cdd:pfam00112   1 LPESFDWREK---GAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKL--VSLSEQQLVDCDTFNNGCNGGLPDN-AFEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218    310 AQDF-GVVEENCFPYTATDAPCKPKENclRYYSSEYYYVGGFYGGCNEALMKlELVKHGPMAVAFEV-HDDFLHYHSGIY 387
Cdd:pfam00112  75 IKKNgGIVTESDYPYTAHDGTCKFKKS--NNKVAKIKGYGDVPYNDEEALQA-ALAKNGPVSVAIDAyEDDFQLYKSGVY 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8393218    388 HHTGLSDPFNpfeltnHAVLLVGYGKDPvtGLDYWIVKNSWGSQWGESGYFRIRRGTD-ECAIESIAMAAI 457
Cdd:pfam00112 152 KHTSCGGELN------HAVLIVGYGVEN--GVPYWIVKNSWGTDWGENGYFRIARGVNnECGIASEASYPI 214
Pept_C1 smart00645
Papain family cysteine protease;
230-458 8.56e-64

Papain family cysteine protease;


Pssm-ID: 214761  Cd Length: 175  Bit Score: 207.05  E-value: 8.56e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218     230 LPESWDWRNVrgiNFVSPVRNQESCGSCYSFASLGMLEARIRILTNNSqtPILSPQEVVSCS-PYAQGCDGGFPYLiAGK 308
Cdd:smart00645   1 LPESFDWRKK---GAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKL--VSLSEQQLVDCSgGGNCGCNGGLPDN-AFE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218     309 YAQDFGVVE-ENCFPYTAtdapckpkenclryysseyyyvggfyggcnealmklelvkhgpmaVAFEVHDDFLHYHSGIY 387
Cdd:smart00645  75 YIKKNGGLEtESCYPYTG---------------------------------------------SVAIDASDFQFYKSGIY 109
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8393218     388 HHTGLSDpfnpfELTNHAVLLVGYGKDPVTGLDYWIVKNSWGSQWGESGYFRIRRGTD-ECAIESIaMAAIP 458
Cdd:smart00645 110 DHPGCGS-----GTLDHAVLIVGYGTEVENGKDYWIVKNSWGTDWGENGYFRIARGKNnECGIEAS-VASYP 175
CathepsinC_exc pfam08773
Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological ...
26-138 3.12e-62

Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological activator of a group of serine proteases. This domain corresponds to the exclusion domain whose structure excludes the approach of a polypeptide apart from its termini. It forms an enclosed beta barrel structure composed from 8 anti-parallel beta strands. Based on a structural comparison and interaction data, it is suggested that the exclusion domain originates from a metallo-protease inhibitor.


Pssm-ID: 312344  Cd Length: 117  Bit Score: 200.96  E-value: 3.12e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218     26 TPANCTYPDLLGTWVFQVGPRHPRSHINCSVMEP----TEEKVVIHLKKLDTAYDEVGNSGYFTLIYNQGFEIVLNDYKW 101
Cdd:pfam08773   1 TPVNCTYEDIVGTWKFQVGKGGGDKRVNCSHMGPdnfnPSKTVTVHLLKPNVVIDELGNTGFWTLIYNQGFEVVINNRKY 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 8393218    102 FAFFKYEVKGSRAISYCHETMTGWVHDVLGRNWACFV 138
Cdd:pfam08773  81 FAFFKYKKNGSNVTSYCNETLPGWYHDVLGRNWACFR 117
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
22-462 1.40e-45

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381  Cd Length: 548  Bit Score: 168.15  E-value: 1.40e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218    22 VSSDTPANCTYPDLLGTWVFQV-GPRHPRSH--INC-SVMEPTEEKVVIHLKKLDTAYDEVGNSGYFTLIYNQGFEIVLN 97
Cdd:PTZ00364  11 LSEYTPARCLSDQYLGLWSFTItKFKYLKTNdrVECpASISSRVTKLIVTLMPNGAAQEQGGATGRWTPVYNHGFEIRIA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218    98 DYKWFAFFKYE-------VKGSRAISYCHETMtGWV--HDVLGRNWACFVGKKMANHSEKVYvNVahlgglqekyserly 168
Cdd:PTZ00364  91 GLVYLFISAWAeipneghYKVSSRCDKSQPGM-GWAtkQGIQPRSQACLYASLIKPLINTNV-NI--------------- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   169 sHNHNFVKAINSVQKSWTATTYEEYEKLSirdlirrsghSGRILRPKPAPITDEIQQQI-LSLPESWDWRNVRGINFVSP 247
Cdd:PTZ00364 154 -HYVQRPGPVNPRRLPVLVPTGDPYSKSR----------SARKAKTASFGFRQSFSHQLgDPPPAAWSWGDVGGASFLPA 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   248 VRNQ---ESCGSCYSFASLGMLEARIRILTNNS----QTPILSPQEVVSCSPYAQGCDGGFPYLIaGKYAQDFGVVEENC 320
Cdd:PTZ00364 223 APPAspgRGCNSSYVEAALAAMMARVMVASNRTdplgQQTFLSARHVLDCSQYGQGCAGGFPEEV-GKFAETFGILTTDS 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   321 F--PYTATDA---PCKPKENCLRYYSSEYYYVGGFYGGCNEAL-MKLELVKHGPMAVAFEVHDD-----------FLHYH 383
Cdd:PTZ00364 302 YyiPYDSGDGverACKTRRPSRRYYFTNYGPLGGYYGAVTDPDeIIWEIYRHGPVPASVYANSDwyncdenstedVRYVS 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   384 SGIYHHTGLSDPFNPF--ELTNHAVLLVGYGKDPVTGlDYWIVKNSWGSQ--WGESGYFRIRRGTDECAIES--IAMAAI 457
Cdd:PTZ00364 382 LDDYSTASADRPLRHYfaSNVNHTVLIIGWGTDENGG-DYWLVLDPWGSRrsWCDGGTRKIARGVNAYNIESevVVMYWA 460

                 ....*
gi 8393218   458 PIPKL 462
Cdd:PTZ00364 461 PYPDV 465
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
228-440 5.03e-14

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


Pssm-ID: 227207  Cd Length: 372  Bit Score: 73.33  E-value: 5.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  228 LSLPESWDWRNVRGinfVSPVRNQESCGSCYSFASLGMLE-------ARIRILTNNSQTPILSPQEVVSCSPYAQG---- 296
Cdd:COG4870  97 ASLPSYFDRRDEGK---VSPVKDQGSGGSCWAFATTRSLEsylnpesAWDFSENNMKNLLGVPYEKGFDYTSNDGGnadm 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  297 ------CDGGFPYLIAGKYAqDFGVVEENCFPYTATDAPCKPKENCLRYYSSEyyyvggfyggcNEALMKLELVKHGPmA 370
Cdd:COG4870 174 saayltEWSGPVYETDDPYS-ENSYFSPTNLPVTKHVQEAQIIPSRKKYLDNG-----------NIKAMFGFYGAVSS-S 240
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8393218  371 VAFEVHDDFLHYHSGIYHHTGlsdpfnpfELTNHAVLLVGY--------GKDPVTGLDYWIVKNSWGSQWGESGYFRI 440
Cdd:COG4870 241 MYIDATNSLGICIPYPYVDSG--------ENWGHAVLIVGYddsfdinnFKYGPPGDGAFIIKNSWGTNWGENGYFWI 310
Pox_I6 pfam04595
Poxvirus I6-like family; This family includes I6 proteins as well as the related F5L proteins.
168-204 5.78e-03

Poxvirus I6-like family; This family includes I6 proteins as well as the related F5L proteins.


Pssm-ID: 252691  Cd Length: 320  Bit Score: 38.48  E-value: 5.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 8393218    168 YSHNHNFVKAINS---VQKSWTATTYEEYEKLSIRDLIRR 204
Cdd:pfam04595  14 YCNENLFNKPENTlddVSKSLLILESFKYEKYVISGLIKI 53
 
Name Accession Description Interval E-value
Peptidase_C1A_CathepsinC cd02621
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ...
230-459 3.45e-124

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  Cd Length: 243  Bit Score: 365.17  E-value: 3.45e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  230 LPESWDWRNVR-GINFVSPVRNQESCGSCYSFASLGMLEARIRILTNN----SQTPILSPQEVVSCSPYAQGCDGGFPYL 304
Cdd:cd02621   1 LPKSFDWGDVNnGFNYVSPVRNQGGCGSCYAFASVYALEARIMIASNKtdplGQQPILSPQHVLSCSQYSQGCDGGFPFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  305 IaGKYAQDFGVVEENCFPYTA-TDAPCK-PKENCLRYYSSEYYYVGGFYGGCNEALMKLELVKHGPMAVAFEVHDDFLHY 382
Cdd:cd02621  81 V-GKFAEDFGIVTEDYFPYTAdDDRPCKaSPSECRRYYFSDYNYVGGCYGCTNEDEMKWEIYRNGPIVVAFEVYSDFDFY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  383 HSGIYHHT-------GLSDPFNPFELTNHAVLLVGYGKDPVTGLDYWIVKNSWGSQWGESGYFRIRRGTDECAIESIAMA 455
Cdd:cd02621 160 KEGVYHHTdndevsdGDNDNFNPFELTNHAVLLVGWGEDEIKGEKYWIVKNSWGSSWGEKGYFKIRRGTNECGIESQAVF 239

                ....
gi 8393218  456 AIPI 459
Cdd:cd02621 240 AYPI 243
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
231-454 8.95e-79

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  Cd Length: 210  Bit Score: 247.15  E-value: 8.95e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  231 PESWDWRNVrgiNFVSPVRNQESCGSCYSFASLGMLEARIRILTNNsqTPILSPQEVVSCSPYA-QGCDGGFPYlIAGKY 309
Cdd:cd02248   1 PESVDWREK---GAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGK--LVSLSEQQLVDCSTSGnNGCNGGNPD-NAFEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  310 AQDFGVVEENCFPYTATDAPCKPKENCLRYYSSEYYYVGGFyggcNEALMKLELVKHGPMAVAFEVHDDFLHYHSGIYHH 389
Cdd:cd02248  75 VKNGGLASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPG----DEEALKAALANYGPVSVAIDASSSFQFYKGGIYSG 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8393218  390 tglsdPFNPFELTNHAVLLVGYGKDPvtGLDYWIVKNSWGSQWGESGYFRIRRGTDECAIESIAM 454
Cdd:cd02248 151 -----PCCSNTNLNHAVLLVGYGTEN--GVDYWIVKNSWGTSWGEKGYIRIARGSNLCGIASYAS 208
Peptidase_C1 pfam00112
Papain family cysteine protease;
230-457 2.92e-74

Papain family cysteine protease;


Pssm-ID: 306594  Cd Length: 214  Bit Score: 235.52  E-value: 2.92e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218    230 LPESWDWRNVrgiNFVSPVRNQESCGSCYSFASLGMLEARIRILTNNSqtPILSPQEVVSCSPYAQGCDGGFPYLiAGKY 309
Cdd:pfam00112   1 LPESFDWREK---GAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKL--VSLSEQQLVDCDTFNNGCNGGLPDN-AFEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218    310 AQDF-GVVEENCFPYTATDAPCKPKENclRYYSSEYYYVGGFYGGCNEALMKlELVKHGPMAVAFEV-HDDFLHYHSGIY 387
Cdd:pfam00112  75 IKKNgGIVTESDYPYTAHDGTCKFKKS--NNKVAKIKGYGDVPYNDEEALQA-ALAKNGPVSVAIDAyEDDFQLYKSGVY 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8393218    388 HHTGLSDPFNpfeltnHAVLLVGYGKDPvtGLDYWIVKNSWGSQWGESGYFRIRRGTD-ECAIESIAMAAI 457
Cdd:pfam00112 152 KHTSCGGELN------HAVLIVGYGVEN--GVPYWIVKNSWGTDWGENGYFRIARGVNnECGIASEASYPI 214
Pept_C1 smart00645
Papain family cysteine protease;
230-458 8.56e-64

Papain family cysteine protease;


Pssm-ID: 214761  Cd Length: 175  Bit Score: 207.05  E-value: 8.56e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218     230 LPESWDWRNVrgiNFVSPVRNQESCGSCYSFASLGMLEARIRILTNNSqtPILSPQEVVSCS-PYAQGCDGGFPYLiAGK 308
Cdd:smart00645   1 LPESFDWRKK---GAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKL--VSLSEQQLVDCSgGGNCGCNGGLPDN-AFE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218     309 YAQDFGVVE-ENCFPYTAtdapckpkenclryysseyyyvggfyggcnealmklelvkhgpmaVAFEVHDDFLHYHSGIY 387
Cdd:smart00645  75 YIKKNGGLEtESCYPYTG---------------------------------------------SVAIDASDFQFYKSGIY 109
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8393218     388 HHTGLSDpfnpfELTNHAVLLVGYGKDPVTGLDYWIVKNSWGSQWGESGYFRIRRGTD-ECAIESIaMAAIP 458
Cdd:smart00645 110 DHPGCGS-----GTLDHAVLIVGYGTEVENGKDYWIVKNSWGTDWGENGYFRIARGKNnECGIEAS-VASYP 175
CathepsinC_exc pfam08773
Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological ...
26-138 3.12e-62

Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological activator of a group of serine proteases. This domain corresponds to the exclusion domain whose structure excludes the approach of a polypeptide apart from its termini. It forms an enclosed beta barrel structure composed from 8 anti-parallel beta strands. Based on a structural comparison and interaction data, it is suggested that the exclusion domain originates from a metallo-protease inhibitor.


Pssm-ID: 312344  Cd Length: 117  Bit Score: 200.96  E-value: 3.12e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218     26 TPANCTYPDLLGTWVFQVGPRHPRSHINCSVMEP----TEEKVVIHLKKLDTAYDEVGNSGYFTLIYNQGFEIVLNDYKW 101
Cdd:pfam08773   1 TPVNCTYEDIVGTWKFQVGKGGGDKRVNCSHMGPdnfnPSKTVTVHLLKPNVVIDELGNTGFWTLIYNQGFEVVINNRKY 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 8393218    102 FAFFKYEVKGSRAISYCHETMTGWVHDVLGRNWACFV 138
Cdd:pfam08773  81 FAFFKYKKNGSNVTSYCNETLPGWYHDVLGRNWACFR 117
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
231-456 2.27e-61

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  Cd Length: 236  Bit Score: 202.89  E-value: 2.27e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  231 PESWD----WRNVRGINfvsPVRNQESCGSCYSFASLGMLEARIRILTNNSQTPILSPQEVVSCSPYAQ-GCDGGFPyLI 305
Cdd:cd02620   1 PESFDarekWPNCISIG---EIRDQGNCGSCWAFSAVEAFSDRLCIQSNGKENVLLSAQDLLSCCSGCGdGCNGGYP-DA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  306 AGKYAQDFGVVEENCFPYTatDAPCKPKENCLRYYSSEYYYVGGFYGGC-------------------NEALMKLELVKH 366
Cdd:cd02620  77 AWKYLTTTGVVTGGCQPYT--IPPCGHHPEGPPPCCGTPYCTPKCQDGCektyeedkhkgksaysvpsDETDIMKEIMTN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  367 GPMAVAFEVHDDFLHYHSGIYHHTGLSdpfnpfELTNHAVLLVGYGKDpvTGLDYWIVKNSWGSQWGESGYFRIRRGTDE 446
Cdd:cd02620 155 GPVQAAFTVYEDFLYYKSGVYQHTSGK------QLGGHAVKIIGWGVE--NGVPYWLAANSWGTDWGENGYFRILRGSNE 226
                       250
                ....*....|
gi 8393218  447 CAIESIAMAA 456
Cdd:cd02620 227 CGIESEVVAG 236
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
233-444 7.14e-54

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  Cd Length: 223  Bit Score: 182.71  E-value: 7.14e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  233 SWDWRNVRginfVSPVRNQESCGSCYSFASLGMLEARIRILTNNSQTPILSPQEVVS-----CSPYAQGCDGGFPYLIAG 307
Cdd:cd02619   1 SVDLRPLR----LTPVKNQGSRGSCWAFASAYALESAYRIKGGEDEYVDLSPQYLYIcandeCLGINGSCDGGGPLSALL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  308 KYAQDFGVVEENCFPYTATDAPCKPKEN--------CLRYYSSEYYYvggfyggcNEALMKLELVKHGPMAVAFEVHDDF 379
Cdd:cd02619  77 KLVALKGIPPEEDYPYGAESDGEEPKSEaalnaakvKLKDYRRVLKN--------NIEDIKEALAKGGPVVAGFDVYSGF 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8393218  380 LHYHSGIYHHTGLSDPFNPFELTNHAVLLVGYGKDPVTGLDYWIVKNSWGSQWGESGYFRIRRGT 444
Cdd:cd02619 149 DRLKEGIIYEEIVYLLYEDGDLGGHAVVIVGYDDNYVEGKGAFIVKNSWGTDWGDNGYGRISYED 213
Peptidase_C1A_CathepsinX cd02698
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ...
230-459 4.03e-52

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: 178.38  E-value: 4.03e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  230 LPESWDWRNVRGINFVSPVRNQ---ESCGSCYSFASLGMLEARIRILTNNSQTPI-LSPQEVVSCSPyAQGCDGGFPyLI 305
Cdd:cd02698   1 LPKSWDWRNVNGVNYVSPTRNQhipQYCGSCWAHGSTSALADRINIARKGAWPSVyLSVQVVIDCAG-GGSCHGGDP-GG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  306 AGKYAQDFGVVEENCFPYTATDAPCKPKENC---------------LRYYSSEYYYVGgfyggcNEALMKLELVKHGPMA 370
Cdd:cd02698  79 VYEYAHKHGIPDETCNPYQAKDGECNPFNRCgtcnpfgecfaiknyTLYFVSDYGSVS------GRDKMMAEIYARGPIS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  371 VAFEVHDDFLHYHSGIYHHtglsdpFNPFELTNHAVLLVGYGKDpVTGLDYWIVKNSWGSQWGESGYFRIRRGT-----D 445
Cdd:cd02698 153 CGIMATEALENYTGGVYKE------YVQDPLINHIISVAGWGVD-ENGVEYWIVRNSWGEPWGERGWFRIVTSSykgarY 225
                       250
                ....*....|....
gi 8393218  446 ECAIESIAMAAIPI 459
Cdd:cd02698 226 NLAIEEDCAWADPI 239
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
22-462 1.40e-45

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381  Cd Length: 548  Bit Score: 168.15  E-value: 1.40e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218    22 VSSDTPANCTYPDLLGTWVFQV-GPRHPRSH--INC-SVMEPTEEKVVIHLKKLDTAYDEVGNSGYFTLIYNQGFEIVLN 97
Cdd:PTZ00364  11 LSEYTPARCLSDQYLGLWSFTItKFKYLKTNdrVECpASISSRVTKLIVTLMPNGAAQEQGGATGRWTPVYNHGFEIRIA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218    98 DYKWFAFFKYE-------VKGSRAISYCHETMtGWV--HDVLGRNWACFVGKKMANHSEKVYvNVahlgglqekyserly 168
Cdd:PTZ00364  91 GLVYLFISAWAeipneghYKVSSRCDKSQPGM-GWAtkQGIQPRSQACLYASLIKPLINTNV-NI--------------- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   169 sHNHNFVKAINSVQKSWTATTYEEYEKLSirdlirrsghSGRILRPKPAPITDEIQQQI-LSLPESWDWRNVRGINFVSP 247
Cdd:PTZ00364 154 -HYVQRPGPVNPRRLPVLVPTGDPYSKSR----------SARKAKTASFGFRQSFSHQLgDPPPAAWSWGDVGGASFLPA 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   248 VRNQ---ESCGSCYSFASLGMLEARIRILTNNS----QTPILSPQEVVSCSPYAQGCDGGFPYLIaGKYAQDFGVVEENC 320
Cdd:PTZ00364 223 APPAspgRGCNSSYVEAALAAMMARVMVASNRTdplgQQTFLSARHVLDCSQYGQGCAGGFPEEV-GKFAETFGILTTDS 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   321 F--PYTATDA---PCKPKENCLRYYSSEYYYVGGFYGGCNEAL-MKLELVKHGPMAVAFEVHDD-----------FLHYH 383
Cdd:PTZ00364 302 YyiPYDSGDGverACKTRRPSRRYYFTNYGPLGGYYGAVTDPDeIIWEIYRHGPVPASVYANSDwyncdenstedVRYVS 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   384 SGIYHHTGLSDPFNPF--ELTNHAVLLVGYGKDPVTGlDYWIVKNSWGSQ--WGESGYFRIRRGTDECAIES--IAMAAI 457
Cdd:PTZ00364 382 LDDYSTASADRPLRHYfaSNVNHTVLIIGWGTDENGG-DYWLVLDPWGSRrsWCDGGTRKIARGVNAYNIESevVVMYWA 460

                 ....*
gi 8393218   458 PIPKL 462
Cdd:PTZ00364 461 PYPDV 465
PTZ00200 PTZ00200
cysteine proteinase; Provisional
231-457 3.31e-45

cysteine proteinase; Provisional


Pssm-ID: 240310  Cd Length: 448  Bit Score: 165.25  E-value: 3.31e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   231 PESWDWRNVRGinfVSPVRNQ-ESCGSCYSFASLGMLEARIRILTNNSQTpiLSPQEVVSCSPYAQGCDGGFPYLiAGKY 309
Cdd:PTZ00200 235 GEGLDWRRADA---VTKVKDQgLNCGSCWAFSSVGSVESLYKIYRDKSVD--LSEQELVNCDTKSQGCSGGYPDT-ALEY 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   310 AQDFGVVEENCFPYTATDAPCKPKENCLRYYSSeyyyvgGFYGGCNEALMKLELVkhGPMAVAFEVHDDFLHYHSGIYhh 389
Cdd:PTZ00200 309 VKNKGLSSSSDVPYLAKDGKCVVSSTKKVYIDS------YLVAKGKDVLNKSLVI--SPTVVYIAVSRELLKYKSGVY-- 378
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8393218   390 TG-LSDPFNpfeltnHAVLLVGYGKDPVTGLDYWIVKNSWGSQWGESGYFRIRR---GTDECAIESIAMAAI 457
Cdd:PTZ00200 379 NGeCGKSLN------HAVLLVGEGYDEKTKKRYWIIKNSWGTDWGENGYMRLERtneGTDKCGILTVGLTPV 444
PTZ00049 PTZ00049
cathepsin C-like protein; Provisional
226-454 9.54e-43

cathepsin C-like protein; Provisional


Pssm-ID: 240244  Cd Length: 693  Bit Score: 160.89  E-value: 9.54e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   226 QILSLPESWDWRNVRGIN-FVSPVRNQESCGSCYSFASLGMLEARIRI---------LTNNSQTpILSPQEVVSCSPYAQ 295
Cdd:PTZ00049 377 EIDELPKNFTWGDPFNNNtREYDVTNQLLCGSCYIASQMYAFKRRIEIaltknldkkYLNNFDD-LLSIQTVLSCSFYDQ 455
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   296 GCDGGFPYLIaGKYAQDFGVVEENCFPYTATDAPC---------------KPKENCLRYYSSEYYYVGGFYGG------- 353
Cdd:PTZ00049 456 GCNGGFPYLV-SKMAKLQGIPLDKVFPYTATEQTCpyqvdqsansmngsaNLRQINAVFFSSETQSDMHADFEapissep 534
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   354 ----------------CN----EALMKLELVKHGPMAVAFEVHDDFLHYHSGIY----------------HHTGLSDpFN 397
Cdd:PTZ00049 535 arwyakdynyiggcygCNqcngEKIMMNEIYRNGPIVASFEASPDFYDYADGVYyvedfpharrctvdlpKHNGVYN-IT 613
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 8393218   398 PFELTNHAVLLVGYGKDPVTG--LDYWIVKNSWGSQWGESGYFRIRRGTDECAIESIAM 454
Cdd:PTZ00049 614 GWEKVNHAIVLVGWGEEEINGklYKYWIGRNSWGKNWGKEGYFKIIRGKNFSGIESQSL 672
PTZ00203 PTZ00203
cathepsin L protease; Provisional
229-456 7.32e-35

cathepsin L protease; Provisional


Pssm-ID: 185513  Cd Length: 348  Bit Score: 134.06  E-value: 7.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   229 SLPESWDWRNvRGInfVSPVRNQESCGSCYSFASLGMLEARIRILTNNSQTpiLSPQEVVSCSPYAQGCDGG-----FPY 303
Cdd:PTZ00203 125 AVPDAVDWRE-KGA--VTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVR--LSEQQLVSCDHVDNGCGGGlmlqaFEW 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   304 LIAGKYAqdfGVVEENCFPYTAT--DAPckpkeNCLRyySSEYYYVGG----FYGGCNEALMKLELVKHGPMAVAFEVhD 377
Cdd:PTZ00203 200 VLRNMNG---TVFTEKSYPYVSGngDVP-----ECSN--SSELAPGARidgyVSMESSERVMAAWLAKNGPISIAVDA-S 268
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8393218   378 DFLHYHSGIYHHTglsdpfnPFELTNHAVLLVGYGKdpVTGLDYWIVKNSWGSQWGESGYFRIRRGTDECAIESIAMAA 456
Cdd:PTZ00203 269 SFMSYHSGVLTSC-------IGEQLNHGVLLVGYNM--TGEVPYWVIKNSWGEDWGEKGYVRVTMGVNACLLTGYPVSV 338
PTZ00021 PTZ00021
falcipain-2; Provisional
189-446 4.22e-33

falcipain-2; Provisional


Pssm-ID: 240232  Cd Length: 489  Bit Score: 130.66  E-value: 4.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   189 TYEEYEK--LSIR--DLIRRSGHSGR-------ILRPKPApitDEIQQQilslpESWDWRNVRGinfVSPVRNQESCGSC 257
Cdd:PTZ00021 222 SFEEFKKkyLTLKsfDFKSNGKKSPRvinyddvIKKYKPK---DATFDH-----AKYDWRLHNG---VTPVKDQKNCGSC 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   258 YSFASLGMLEARIRILTNnsQTPILSPQEVVSCSPYAQGCDGGFPYLIAGKYAQDFGVVEENCFPYTAtDAP-------C 330
Cdd:PTZ00021 291 WAFSTVGVVESQYAIRKN--ELVSLSEQELVDCSFKNNGCYGGLIPNAFEDMIELGGLCSEDDYPYVS-DTPelcnidrC 367
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218   331 KPKENCLRYYSSEYYYVggfyggcNEALMKLelvkhGPMAVAFEVHDDFLHYHSGIYHHTGLSDPfnpfeltNHAVLLVG 410
Cdd:PTZ00021 368 KEKYKIKSYVSIPEDKF-------KEAIRFL-----GPISVSIAVSDDFAFYKGGIFDGECGEEP-------NHAVILVG 428
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 8393218   411 YGK----DPVTGLD----YWIVKNSWGSQWGESGYFRIRrgTDE 446
Cdd:PTZ00021 429 YGMeeiyNSDTKKMekryYYIIKNSWGESWGEKGFIRIE--TDE 470
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
228-440 5.03e-14

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


Pssm-ID: 227207  Cd Length: 372  Bit Score: 73.33  E-value: 5.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  228 LSLPESWDWRNVRGinfVSPVRNQESCGSCYSFASLGMLE-------ARIRILTNNSQTPILSPQEVVSCSPYAQG---- 296
Cdd:COG4870  97 ASLPSYFDRRDEGK---VSPVKDQGSGGSCWAFATTRSLEsylnpesAWDFSENNMKNLLGVPYEKGFDYTSNDGGnadm 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393218  297 ------CDGGFPYLIAGKYAqDFGVVEENCFPYTATDAPCKPKENCLRYYSSEyyyvggfyggcNEALMKLELVKHGPmA 370
Cdd:COG4870 174 saayltEWSGPVYETDDPYS-ENSYFSPTNLPVTKHVQEAQIIPSRKKYLDNG-----------NIKAMFGFYGAVSS-S 240
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8393218  371 VAFEVHDDFLHYHSGIYHHTGlsdpfnpfELTNHAVLLVGY--------GKDPVTGLDYWIVKNSWGSQWGESGYFRI 440
Cdd:COG4870 241 MYIDATNSLGICIPYPYVDSG--------ENWGHAVLIVGYddsfdinnFKYGPPGDGAFIIKNSWGTNWGENGYFWI 310
PTZ00462 PTZ00462
Serine-repeat antigen protein; Provisional
403-461 7.00e-08

Serine-repeat antigen protein; Provisional


Pssm-ID: 185641  Cd Length: 1004  Bit Score: 54.68  E-value: 7.00e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8393218    403 NHAVLLVGYGK---DPVTGLDYWIVKNSWGSQWGESGYFRIRR-GTDECA---IESIAMAAIPIPK 461
Cdd:PTZ00462  722 DHAVNIVGYGNyinDEDEKKSYWIVRNSWGKYWGDEGYFKVDMyGPSHCEdnfIHSVVIFNIDLPK 787
Pox_I6 pfam04595
Poxvirus I6-like family; This family includes I6 proteins as well as the related F5L proteins.
168-204 5.78e-03

Poxvirus I6-like family; This family includes I6 proteins as well as the related F5L proteins.


Pssm-ID: 252691  Cd Length: 320  Bit Score: 38.48  E-value: 5.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 8393218    168 YSHNHNFVKAINS---VQKSWTATTYEEYEKLSIRDLIRR 204
Cdd:pfam04595  14 YCNENLFNKPENTlddVSKSLLILESFKYEKYVISGLIKI 53
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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