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Conserved domains on  [gi|6042196|ref|NP_003784|]
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cathepsin F precursor [Homo sapiens]

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;
271-482 7.00e-90

Papain family cysteine protease;


:

Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 273.26  E-value: 7.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196    271 APPEWDWRSKGAVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSEQELLDCDKMDKACMGGLPSNAYSAIKNLGG 350
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTFNNGCNGGLPDNAFEYIKKNGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196    351 LETEDDYSYQGHMQSCNFSAEKAKVY-INDSVELSQN-EQKLAAWLAKRGPISVAINAFGM--QFYRHGISRPLRplCSP 426
Cdd:pfam00112  81 IVTESDYPYTAKDGTCKFKKSNSKVAkIKGYGDVPYNdEEALQAALAKNGPVSVAIDAYERdfQLYKSGVYKHTE--CGG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6042196    427 WLiDHAVLLVGYGNRSDVPFWAIKNSWGTDWGEKGYYYLHRGS-GACGVNTMASSAV 482
Cdd:pfam00112 159 EL-NHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVnNECGIASEASYPI 214
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 187-243 5.91e-15

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: 69.19  E-value: 5.91e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6042196     187 FKNFVITYNRTYESKEEARWRLSVFVNNMVRAQKIQALDRGTAQYGVTKFSDLTEEE 243
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNKKYEHSYKLGVNQFSDLTPEE 57
 
Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
271-482 7.00e-90

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 273.26  E-value: 7.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196    271 APPEWDWRSKGAVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSEQELLDCDKMDKACMGGLPSNAYSAIKNLGG 350
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTFNNGCNGGLPDNAFEYIKKNGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196    351 LETEDDYSYQGHMQSCNFSAEKAKVY-INDSVELSQN-EQKLAAWLAKRGPISVAINAFGM--QFYRHGISRPLRplCSP 426
Cdd:pfam00112  81 IVTESDYPYTAKDGTCKFKKSNSKVAkIKGYGDVPYNdEEALQAALAKNGPVSVAIDAYERdfQLYKSGVYKHTE--CGG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6042196    427 WLiDHAVLLVGYGNRSDVPFWAIKNSWGTDWGEKGYYYLHRGS-GACGVNTMASSAV 482
Cdd:pfam00112 159 EL-NHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVnNECGIASEASYPI 214
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
 272-481 3.19e-87

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: 266.03  E-value: 3.19e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196  272 PPEWDWRSKGAVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSEQELLDCDKM-DKACMGGLPSNAYSAIKNlGG 350
Cdd:cd02248   1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSgNNGCNGGNPDNAFEYVKN-GG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196  351 LETEDDYSYQGHMQSCNFSAEKAKVYINDSVELSQ-NEQKLAAWLAKRGPISVAINAFG-MQFYRHGISRPlrPLCSPWL 428
Cdd:cd02248  80 LASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPgDEEALKAALANYGPVSVAIDASSsFQFYKGGIYSG--PCCSNTN 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 6042196  429 IDHAVLLVGYGNRSDVPFWAIKNSWGTDWGEKGYYYLHRGSGACGVNTMASSA 481
Cdd:cd02248 158 LNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLCGIASYASYP 210
PTZ00203 PTZ00203
cathepsin L protease; Provisional
 184-483 3.12e-72

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 232.67  E-value: 3.12e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   184 ASIFKNFVITYNRTYESKEEARWRLSVFVNNMVRAQKIQAlDRGTAQYGVTKFSDLTEEEFRTIYLN-----TLLRKEPG 258
Cdd:PTZ00203  35 AALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQA-RNPHARFGITKFFDLSEAEFAARYLNgaayfAAAKQHAG 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   259 NKMKQAKSVGDLAPPEWDWRSKGAVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSEQELLDCDKMDKACMGGLP 338
Cdd:PTZ00203 114 QHYRKARADLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLM 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   339 SNAYS-AIKNLGG-LETEDDYSY---QGHMQSCNFSAEKAK-VYINDSVELSQNEQKLAAWLAKRGPISVAINAFGMQFY 412
Cdd:PTZ00203 194 LQAFEwVLRNMNGtVFTEKSYPYvsgNGDVPECSNSSELAPgARIDGYVSMESSERVMAAWLAKNGPISIAVDASSFMSY 273

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6042196   413 RHGISRPlrplCSPWLIDHAVLLVGYGNRSDVPFWAIKNSWGTDWGEKGYYYLHRGSGACGVNTMASSAVV 483
Cdd:PTZ00203 274 HSGVLTS----CIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVTMGVNACLLTGYPVSVHV 340
Pept_C1 smart00645
Papain family cysteine protease;
271-482 4.45e-65

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 207.82  E-value: 4.45e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196     271 APPEWDWRSKGAVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSEQELLDCDKM-DKACMGGLPSNAYSAIKNLG 349
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGGgNCGCNGGLPDNAFEYIKKNG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196     350 GLETEDDYSYQGhmqscnfsaekakvyindsvelsqneqklaawlakrgpiSVAINAFGMQFYRHGISRPlrPLCSPWLI 429
Cdd:smart00645  81 GLETESCYPYTG---------------------------------------SVAIDASDFQFYKSGIYDH--PGCGSGTL 119

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 6042196     430 DHAVLLVGYGNRSD--VPFWAIKNSWGTDWGEKGYYYLHRGS-GACGVNTMASSAV 482
Cdd:smart00645 120 DHAVLIVGYGTEVEngKDYWIVKNSWGTDWGENGYFRIARGKnNECGIEASVASYP 175
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
272-465 2.22e-29

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 119.47  E-value: 2.22e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196  272 PPEWDWRSKgaVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSE--------QELLDCDKMDKACMGGLPSNAYS 343
Cdd:COG4870   5 PSSVDLRGY--VTPVKDQGSLGSCWAFATAAALESYLKKQAGAPGTSLDlselflynQARNGDGTEGTDDGGSSLRDALK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196  344 AIKNLGGLeTEDDYSYQGHMQSC---NFSAEKAKVY-INDSVELS--QNEQKLAAW---LAKRGPISVAINAF-GMQFYR 413
Cdd:COG4870  83 LLRWSGVV-PESDWPYDDSDFTSqpsAAAYADARNYkIQDYYRLPggGGATDLDAIkqaLAEGGPVVFGFYVYeSFYNYT 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 6042196  414 HGISRPlrPLCSPWLIDHAVLLVGYGNRSDVPFWAIKNSWGTDWGEKGYYYL 465
Cdd:COG4870 162 GGVYYP--TPGDASLGGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWI 211
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 187-243 5.91e-15

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: 69.19  E-value: 5.91e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6042196     187 FKNFVITYNRTYESKEEARWRLSVFVNNMVRAQKIQALDRGTAQYGVTKFSDLTEEE 243
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNKKYEHSYKLGVNQFSDLTPEE 57
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 187-244 6.60e-10

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: 54.57  E-value: 6.60e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6042196    187 FKNFVITYNRTYESKEEARWRLSVFVNNMVRAQKIQALDRGTAQYGVTKFSDLTEEEF 244
Cdd:pfam08246   1 FDDWMKKYGKSYRSEEEELYRFQIFKENLKRIEEHNSNGNVTYKLGLNKFADLTDEEF 58
 
Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
271-482 7.00e-90

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 273.26  E-value: 7.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196    271 APPEWDWRSKGAVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSEQELLDCDKMDKACMGGLPSNAYSAIKNLGG 350
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTFNNGCNGGLPDNAFEYIKKNGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196    351 LETEDDYSYQGHMQSCNFSAEKAKVY-INDSVELSQN-EQKLAAWLAKRGPISVAINAFGM--QFYRHGISRPLRplCSP 426
Cdd:pfam00112  81 IVTESDYPYTAKDGTCKFKKSNSKVAkIKGYGDVPYNdEEALQAALAKNGPVSVAIDAYERdfQLYKSGVYKHTE--CGG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6042196    427 WLiDHAVLLVGYGNRSDVPFWAIKNSWGTDWGEKGYYYLHRGS-GACGVNTMASSAV 482
Cdd:pfam00112 159 EL-NHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVnNECGIASEASYPI 214
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
 272-481 3.19e-87

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: 266.03  E-value: 3.19e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196  272 PPEWDWRSKGAVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSEQELLDCDKM-DKACMGGLPSNAYSAIKNlGG 350
Cdd:cd02248   1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSgNNGCNGGNPDNAFEYVKN-GG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196  351 LETEDDYSYQGHMQSCNFSAEKAKVYINDSVELSQ-NEQKLAAWLAKRGPISVAINAFG-MQFYRHGISRPlrPLCSPWL 428
Cdd:cd02248  80 LASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPgDEEALKAALANYGPVSVAIDASSsFQFYKGGIYSG--PCCSNTN 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 6042196  429 IDHAVLLVGYGNRSDVPFWAIKNSWGTDWGEKGYYYLHRGSGACGVNTMASSA 481
Cdd:cd02248 158 LNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLCGIASYASYP 210
PTZ00203 PTZ00203
cathepsin L protease; Provisional
 184-483 3.12e-72

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 232.67  E-value: 3.12e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   184 ASIFKNFVITYNRTYESKEEARWRLSVFVNNMVRAQKIQAlDRGTAQYGVTKFSDLTEEEFRTIYLN-----TLLRKEPG 258
Cdd:PTZ00203  35 AALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQA-RNPHARFGITKFFDLSEAEFAARYLNgaayfAAAKQHAG 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   259 NKMKQAKSVGDLAPPEWDWRSKGAVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSEQELLDCDKMDKACMGGLP 338
Cdd:PTZ00203 114 QHYRKARADLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLM 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   339 SNAYS-AIKNLGG-LETEDDYSY---QGHMQSCNFSAEKAK-VYINDSVELSQNEQKLAAWLAKRGPISVAINAFGMQFY 412
Cdd:PTZ00203 194 LQAFEwVLRNMNGtVFTEKSYPYvsgNGDVPECSNSSELAPgARIDGYVSMESSERVMAAWLAKNGPISIAVDASSFMSY 273

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6042196   413 RHGISRPlrplCSPWLIDHAVLLVGYGNRSDVPFWAIKNSWGTDWGEKGYYYLHRGSGACGVNTMASSAVV 483
Cdd:PTZ00203 274 HSGVLTS----CIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVTMGVNACLLTGYPVSVHV 340
Pept_C1 smart00645
Papain family cysteine protease;
271-482 4.45e-65

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 207.82  E-value: 4.45e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196     271 APPEWDWRSKGAVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSEQELLDCDKM-DKACMGGLPSNAYSAIKNLG 349
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGGgNCGCNGGLPDNAFEYIKKNG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196     350 GLETEDDYSYQGhmqscnfsaekakvyindsvelsqneqklaawlakrgpiSVAINAFGMQFYRHGISRPlrPLCSPWLI 429
Cdd:smart00645  81 GLETESCYPYTG---------------------------------------SVAIDASDFQFYKSGIYDH--PGCGSGTL 119

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 6042196     430 DHAVLLVGYGNRSD--VPFWAIKNSWGTDWGEKGYYYLHRGS-GACGVNTMASSAV 482
Cdd:smart00645 120 DHAVLIVGYGTEVEngKDYWIVKNSWGTDWGENGYFRIARGKnNECGIEASVASYP 175
PTZ00200 PTZ00200
cysteine proteinase; Provisional
 138-474 3.77e-48

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 171.80  E-value: 3.77e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   138 KSAFTQGSAMISSLSQNHP----DNRNETFSSVISLLNEDPLSQDLPVKMASI--FKNFVITYNRTYESKEEARWRLSVF 211
Cdd:PTZ00200  71 KMVKSFKSDLEEHIDKDFPrldkSKRDSYVDELTRLFKDGYISDDPKLEFEVYleFEEFNKKYNRKHATHAERLNRFLTF 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   212 VNNM--VRAQKiqaldrGTAQY--GVTKFSDLTEEEFRTIY---------------LNTLLRKEPG----NKMKQAKS-- 266
Cdd:PTZ00200 151 RNNYleVKSHK------GDEPYskEINKFSDLTEEEFRKLFpvikvppksnstshnNDFKARHVSNptylKNLKKAKNtd 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   267 --VGD---LAPPEWDWRSKGAVTKVKDQG-MCGSCWAFSVTGNVEGQWFLNQGTLLSLSEQELLDCDKMDKACMGGLPSN 340
Cdd:PTZ00200 225 edVKDpskITGEGLDWRRADAVTKVKDQGlNCGSCWAFSSVGSVESLYKIYRDKSVDLSEQELVNCDTKSQGCSGGYPDT 304

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   341 AYSAIKNlGGLETEDDYSYQGHMQSCNFSAEKaKVYINDSVELSQNE--QKLAAWlakrGPISVAINA---FGMqfYRHG 415
Cdd:PTZ00200 305 ALEYVKN-KGLSSSSDVPYLAKDGKCVVSSTK-KVYIDSYLVAKGKDvlNKSLVI----SPTVVYIAVsreLLK--YKSG 376

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6042196   416 IsrpLRPLCSPWLiDHAVLLV--GYGNRSDVPFWAIKNSWGTDWGEKGYYYLHR---GSGACGV 474
Cdd:PTZ00200 377 V---YNGECGKSL-NHAVLLVgeGYDEKTKKRYWIIKNSWGTDWGENGYMRLERtneGTDKCGI 436
PTZ00021 PTZ00021
falcipain-2; Provisional
 187-462 2.24e-47

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 170.72  E-value: 2.24e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   187 FKNFVITYNRTYESKEEARWRLSVFVNNmvrAQKIQALD-RGTAQY--GVTKFSDLTEEEFRTIYLN-------TLLRKE 256
Cdd:PTZ00021 169 FYLFIKEHGKKYQTPDEMQQRYLSFVEN---LAKINAHNnKENVLYkkGMNRFGDLSFEEFKKKYLTlksfdfkSNGKKS 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   257 PG--------NKMKQAKSVGDLAppEWDWRSKGAVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSEQELLDCDK 328
Cdd:PTZ00021 246 PRvinyddviKKYKPKDATFDHA--KYDWRLHNGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVDCSF 323

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   329 MDKACMGGLPSNAYSAIKNLGGLETEDDYSYQGHM-QSCNFSAEKAKVYINDSVELSQNEQKLAawLAKRGPISVAINA- 406
Cdd:PTZ00021 324 KNNGCYGGLIPNAFEDMIELGGLCSEDDYPYVSDTpELCNIDRCKEKYKIKSYVSIPEDKFKEA--IRFLGPISVSIAVs 401

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6042196   407 --FGmqFYRHGIsrpLRPLCSPWLiDHAVLLVGYGNRSDVP----------FWAIKNSWGTDWGEKGY 462
Cdd:PTZ00021 402 ddFA--FYKGGI---FDGECGEEP-NHAVILVGYGMEEIYNsdtkkmekryYYIIKNSWGESWGEKGF 463
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
 274-465 6.72e-30

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: 116.46  E-value: 6.72e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196  274 EWDWRSKGaVTKVKDQGMCGSCWAFSVTGNVE-------GQWFLNQGTLLSLSEQELLDCDKMDKACMGGLPSNAYSAIK 346
Cdd:cd02619   1 SVDLRPLR-LTPVKNQGSRGSCWAFASAYALEsayrikgGEDEYVDLSPQYLYICANDECLGINGSCDGGGPLSALLKLV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196  347 NLGGLETEDDYSYQGHMQSCNFSAEK----AKVYIND-SVELSQNEQKLAAWLAKRGPISVAINAFGMQFYRHGISRPLR 421
Cdd:cd02619  80 ALKGIPPEEDYPYGAESDGEEPKSEAalnaAKVKLKDyRRVLKNNIEDIKEALAKGGPVVAGFDVYSGFDRLKEGIIYEE 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 6042196  422 PL----CSPWLIDHAVLLVGYG--NRSDVPFWAIKNSWGTDWGEKGYYYL 465
Cdd:cd02619 160 IVyllyEDGDLGGHAVVIVGYDdnYVEGKGAFIVKNSWGTDWGDNGYGRI 209
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
272-465 2.22e-29

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 119.47  E-value: 2.22e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196  272 PPEWDWRSKgaVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSE--------QELLDCDKMDKACMGGLPSNAYS 343
Cdd:COG4870   5 PSSVDLRGY--VTPVKDQGSLGSCWAFATAAALESYLKKQAGAPGTSLDlselflynQARNGDGTEGTDDGGSSLRDALK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196  344 AIKNLGGLeTEDDYSYQGHMQSC---NFSAEKAKVY-INDSVELS--QNEQKLAAW---LAKRGPISVAINAF-GMQFYR 413
Cdd:COG4870  83 LLRWSGVV-PESDWPYDDSDFTSqpsAAAYADARNYkIQDYYRLPggGGATDLDAIkqaLAEGGPVVFGFYVYeSFYNYT 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 6042196  414 HGISRPlrPLCSPWLIDHAVLLVGYGNRSDVPFWAIKNSWGTDWGEKGYYYL 465
Cdd:COG4870 162 GGVYYP--TPGDASLGGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWI 211
Peptidase_C1A_CathepsinC cd02621
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ...
 272-481 2.92e-27

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: 109.40  E-value: 2.92e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196  272 PPEWDWRSKGA----VTKVKDQGMCGSCWAFSVTGNVEGQ-----WFLNQ-GTLLSLSEQELLDCDKMDKACMGGLPsna 341
Cdd:cd02621   2 PKSFDWGDVNNgfnyVSPVRNQGGCGSCYAFASVYALEARimiasNKTDPlGQQPILSPQHVLSCSQYSQGCDGGFP--- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196  342 YSAIK--NLGGLETEDDYSYQGHMQS-CNFSAEKAKVY-------------INDSVELsQNEqklaawLAKRGPISVAIN 405
Cdd:cd02621  79 FLVGKfaEDFGIVTEDYFPYTADDDRpCKASPSECRRYyfsdynyvggcygCTNEDEM-KWE------IYRNGPIVVAFE 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196  406 AFG-MQFYRHGI---------SRPLRPLCSPW-LIDHAVLLVGYG--NRSDVPFWAIKNSWGTDWGEKGYYYLHRGSGAC 472
Cdd:cd02621 152 VYSdFDFYKEGVyhhtdndevSDGDNDNFNPFeLTNHAVLLVGWGedEIKGEKYWIVKNSWGSSWGEKGYFKIRRGTNEC 231


                ....*....
gi 6042196  473 GVNTMASSA 481
Cdd:cd02621 232 GIESQAVFA 240
Peptidase_C1A_CathepsinX cd02698
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ...
 272-469 7.89e-21

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: 91.32  E-value: 7.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196  272 PPEWDWRSKGAV---TKVKDQGM---CGSCWAFSVTG------NVEGQwflNQGTLLSLSEQELLDCDKMDkACMGGLPS 339
Cdd:cd02698   2 PKSWDWRNVNGVnyvSPTRNQHIpqyCGSCWAHGSTSaladriNIARK---GAWPSVYLSVQVVIDCAGGG-SCHGGDPG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196  340 NAYSAIKNlGGLETEDDYSYQGH---------------MQSCNFSAEKAKVYINDSVELSqNEQKLAAWLAKRGPISVAI 404
Cdd:cd02698  78 GVYEYAHK-HGIPDETCNPYQAKdgecnpfnrcgtcnpFGECFAIKNYTLYFVSDYGSVS-GRDKMMAEIYARGPISCGI 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6042196  405 NAFGMQF-YRHGI--SRPLRPLcspwlIDHAVLLVGYGNRSD-VPFWAIKNSWGTDWGEKGYYYLHRGS 469
Cdd:cd02698 156 MATEALEnYTGGVykEYVQDPL-----INHIISVAGWGVDENgVEYWIVRNSWGEPWGERGWFRIVTSS 219
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
 286-473 2.12e-19

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: 86.94  E-value: 2.12e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196  286 VKDQGMCGSCWAFSVTGNVEGQWFLnQGTLLSLSEQELLD----CDKMDKACMGGLPSNAYSAIKNLGgLETEDDYSY-- 359
Cdd:cd02620  19 IRDQGNCGSCWAFSAVEAFSDRLCI-QSNGKENVLLSAQDllscCSGCGDGCNGGYPDAAWKYLTTTG-VVTGGCQPYti 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196  360 --QGHMQSCNFSAE-----------------KAKVYINDSVE-LSQNEQKLAAWLAKRGPISVAINA---FGMqfYRHGI 416
Cdd:cd02620  97 ppCGHHPEGPPPCCgtpyctpkcqdgcektyEEDKHKGKSAYsVPSDETDIMKEIMTNGPVQAAFTVyedFLY--YKSGV 174

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6042196  417 SRPLRplcSPWLIDHAVLLVGYGNRSDVPFWAIKNSWGTDWGEKGYYYLHRGSGACG 473
Cdd:cd02620 175 YQHTS---GKQLGGHAVKIIGWGVENGVPYWLAANSWGTDWGENGYFRILRGSNECG 228
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 187-243 5.91e-15

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: 69.19  E-value: 5.91e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6042196     187 FKNFVITYNRTYESKEEARWRLSVFVNNMVRAQKIQALDRGTAQYGVTKFSDLTEEE 243
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNKKYEHSYKLGVNQFSDLTPEE 57
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 187-244 6.60e-10

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: 54.57  E-value: 6.60e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6042196    187 FKNFVITYNRTYESKEEARWRLSVFVNNMVRAQKIQALDRGTAQYGVTKFSDLTEEEF 244
Cdd:pfam08246   1 FDDWMKKYGKSYRSEEEELYRFQIFKENLKRIEEHNSNGNVTYKLGLNKFADLTDEEF 58
PTZ00049 PTZ00049
cathepsin C-like protein; Provisional
 286-478 9.14e-08

cathepsin C-like protein; Provisional


Pssm-ID: 240244 [Multi-domain]  Cd Length: 693  Bit Score: 54.57  E-value: 9.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   286 VKDQGMCGSCWAFS------------VTGNVEGQWFLNqgTLLSLSEQELLDCDKMDKACMGGLPSnAYSAIKNLGGLET 353
Cdd:PTZ00049 400 VTNQLLCGSCYIASqmyafkrrieiaLTKNLDKKYLNN--FDDLLSIQTVLSCSFYDQGCNGGFPY-LVSKMAKLQGIPL 476

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   354 EDDYSYQGHMQSCNFSAEKAKVYINDSVELSQNEQKL---------------------AAWLAK---------------- 396
Cdd:PTZ00049 477 DKVFPYTATEQTCPYQVDQSANSMNGSANLRQINAVFfssetqsdmhadfeapissepARWYAKdynyiggcygcnqcng 556

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   397 ----------RGPISVAINAFGMQF-YRHGI----SRPLRPLC-------------SPW-LIDHAVLLVGYG----NRSD 443
Cdd:PTZ00049 557 ekimmneiyrNGPIVASFEASPDFYdYADGVyyveDFPHARRCtvdlpkhngvyniTGWeKVNHAIVLVGWGeeeiNGKL 636

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 6042196   444 VPFWAIKNSWGTDWGEKGYYYLHRGSGACGVNTMA 478
Cdd:PTZ00049 637 YKYWIGRNSWGKNWGKEGYFKIIRGKNFSGIESQS 671
PTZ00462 PTZ00462
Serine-repeat antigen protein; Provisional
 403-463 3.20e-06

Serine-repeat antigen protein; Provisional


Pssm-ID: 185641 [Multi-domain]  Cd Length: 1004  Bit Score: 50.06  E-value: 3.20e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6042196    403 AINAFGMQFYrhgiSRPLRPLCSPWLIDHAVLLVGYGNRSD-----VPFWAIKNSWGTDWGEKGYY 463
Cdd:PTZ00462  699 AENVLGYEFN----GKKVQNLCGDDTADHAVNIVGYGNYINdedekKSYWIVRNSWGKYWGDEGYF 760
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
 266-476 6.18e-05

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381 [Multi-domain]  Cd Length: 548  Bit Score: 45.65  E-value: 6.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   266 SVGDLAPPEWDWRSKGAVT---KVKDQG---MCGSCWAFSVTGNVEGQWFLNQ------GTLLSLSEQELLDCDKMDKAC 333
Cdd:PTZ00364 200 QLGDPPPAAWSWGDVGGASflpAAPPASpgrGCNSSYVEAALAAMMARVMVASnrtdplGQQTFLSARHVLDCSQYGQGC 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   334 MGGLPSNAYSAIKNLGGLeTEDDY-----SYQGHMQSCNFSAEKAKVYINDSVEL-----SQNEQKLAAW-LAKRGPISV 402
Cdd:PTZ00364 280 AGGFPEEVGKFAETFGIL-TTDSYyipydSGDGVERACKTRRPSRRYYFTNYGPLggyygAVTDPDEIIWeIYRHGPVPA 358

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6042196   403 AINAFGMQFYRHGIS------------------RPLRPLCSPWLiDHAVLLVGYG-NRSDVPFWAIKNSWGT--DWGEKG 461
Cdd:PTZ00364 359 SVYANSDWYNCDENStedvryvslddystasadRPLRHYFASNV-NHTVLIIGWGtDENGGDYWLVLDPWGSrrSWCDGG 437

                        250
                 ....*....|....*
gi 6042196   462 YYYLHRGSGACGVNT 476
Cdd:PTZ00364 438 TRKIARGVNAYNIES 452
PepC COG3579
Aminopeptidase C [Amino acid transport and metabolism];
430-464 1.46e-04

Aminopeptidase C [Amino acid transport and metabolism];


Pssm-ID: 442798 [Multi-domain]  Cd Length: 440  Bit Score: 44.09  E-value: 1.46e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 6042196  430 DHAVLLVGY-----GNrsdVPFWAIKNSWGTDWGEKGYYY 464
Cdd:COG3579 362 THAMVITGVdldqnGK---PTRWKVENSWGDDNGYKGYFY 398
Peptidase_C1_2 pfam03051
Peptidase C1-like family; This family is closely related to the Peptidase_C1 family pfam00112, ...
 428-463 7.39e-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: 38.86  E-value: 7.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 6042196    428 LIDHAVLLVGYGNRSD--VPFWAIKNSWGTDWGEKGYY 463
Cdd:pfam03051 358 LMTHAMVLTGVDEDDDgkPTKWKVENSWGEDSGEKGYF 395
 
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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