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Conserved domains on  [gi|414145857|pdb|4HPSC| ]
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Chain C, Crystal Structure Of A Pyrrolidone-Carboxylate Peptidase 1 (Target Id Nysgrc-012831) From Xenorhabdus Bovienii Ss-2004 In Space Group P21

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C15 cd00501
Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: ...
24-218 1.48e-98

Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: Enzymes responsible for cleaving pyroglutamate (pGlu) from the N-terminal end of specialized proteins. The N-terminal pGlu protects these proteins from proteolysis by other proteases until the pGlu is removed by a PGP. PGPs are cysteine proteases with a Cys-His-Glu/Asp catalytic triad. Type I PGPs are found in a wide variety of prokaryotes and eukaryotes. It is not clear whether the functional form is a monomer, a homodimer, or a homotetramer.


:

Pssm-ID: 238279  Cd Length: 194  Bit Score: 288.01  E-value: 1.48e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC        24 KTILVTAFDPFGGEAINPSWEAIKPLQGSQVFGANIEICQIPCIFDTSLEHLYAAVDKYQPELVISVGQAGGRTNITVER 103
Cdd:cd00501   1 KKVLVTGFGPFGGEPVNPSWEAVKELPKLILGGAEVVGLELPVVFQKAVEVLPELIEEHKPDLVIHVGLAGGRSTITIER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC       104 VAININDARIPDNAGNQPIDTPVIVDGPAAYFSRLPIKTMVNALNTAGIPASVSQTAGTFVCNHVMYGLLHYLAQNTPSV 183
Cdd:cd00501  81 VAINIDDARIPDNEGNQPIDEPIVPGGPAAYFSTLPVKAIVKALREAGIPARVSNDAGTYLCNHVYYGSLHESATRGPFI 160
                       170       180       190
                ....*....|....*....|....*....|....*
4HPSC       184 RGGFIHVPYLPEQAVkDGNQSSMTLMLMTLALKIA 218
Cdd:cd00501 161 RAGFIHVPYSPEQVA-DKGAPSMSLETILRALEAA 194
 
Name Accession Description Interval E-value
Peptidase_C15 cd00501
Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: ...
24-218 1.48e-98

Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: Enzymes responsible for cleaving pyroglutamate (pGlu) from the N-terminal end of specialized proteins. The N-terminal pGlu protects these proteins from proteolysis by other proteases until the pGlu is removed by a PGP. PGPs are cysteine proteases with a Cys-His-Glu/Asp catalytic triad. Type I PGPs are found in a wide variety of prokaryotes and eukaryotes. It is not clear whether the functional form is a monomer, a homodimer, or a homotetramer.


Pssm-ID: 238279  Cd Length: 194  Bit Score: 288.01  E-value: 1.48e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC        24 KTILVTAFDPFGGEAINPSWEAIKPLQGSQVFGANIEICQIPCIFDTSLEHLYAAVDKYQPELVISVGQAGGRTNITVER 103
Cdd:cd00501   1 KKVLVTGFGPFGGEPVNPSWEAVKELPKLILGGAEVVGLELPVVFQKAVEVLPELIEEHKPDLVIHVGLAGGRSTITIER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC       104 VAININDARIPDNAGNQPIDTPVIVDGPAAYFSRLPIKTMVNALNTAGIPASVSQTAGTFVCNHVMYGLLHYLAQNTPSV 183
Cdd:cd00501  81 VAINIDDARIPDNEGNQPIDEPIVPGGPAAYFSTLPVKAIVKALREAGIPARVSNDAGTYLCNHVYYGSLHESATRGPFI 160
                       170       180       190
                ....*....|....*....|....*....|....*
4HPSC       184 RGGFIHVPYLPEQAVkDGNQSSMTLMLMTLALKIA 218
Cdd:cd00501 161 RAGFIHVPYSPEQVA-DKGAPSMSLETILRALEAA 194
PRK13197 PRK13197
pyrrolidone-carboxylate peptidase; Provisional
23-228 2.16e-129

pyrrolidone-carboxylate peptidase; Provisional


Pssm-ID: 237299  Cd Length: 215  Bit Score: 366.89  E-value: 2.16e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC         23 MKTILVTAFDPFGGEAINPSWEAIKPLQGSQVFGANIEICQIPCIFDTSLEHLYAAVDKYQPELVISVGQAGGRTNITVE 102
Cdd:PRK13197   1 MMKILVTGFDPFGGEKINPSWEAVKQLPGKEIGGAEIIKRQLPTVFGKSAEVLKEAIEEVQPDAVICIGQAGGRTDITPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC        103 RVAININDARIPDNAGNQPIDTPVIVDGPAAYFSRLPIKTMVNALNTAGIPASVSQTAGTFVCNHVMYGLLHYLAQNTPS 182
Cdd:PRK13197  81 RVAINIDDARIPDNEGNQPIDEPIVEDGPAAYFSTLPIKAMVKAIREAGIPASVSNTAGTFVCNHVMYGLLHLLDKKYPN 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
4HPSC        183 VRGGFIHVPYLPEQAVKDGNQSSMTLMLMTLALKIAIETAWKNTSD 228
Cdd:PRK13197 161 IRAGFIHIPYLPEQAVNKPGTPSMSLEDIVRGLELAIEAIVENEDD 206
Pcp COG2039
Pyrrolidone-carboxylate peptidase (N-terminal pyroglutamyl peptidase) [Posttranslational ...
24-228 5.62e-107

Pyrrolidone-carboxylate peptidase (N-terminal pyroglutamyl peptidase) [Posttranslational modification, protein turnover, chaperones]


Pssm-ID: 224950  Cd Length: 207  Bit Score: 309.64  E-value: 5.62e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC        24 KTILVTAFDPFGGEAINPSWEAIKPLQGSQVFGANIEICQIPCIFDTSLEHLYAAVDKYQPELVISVGQAGGRTNITVER 103
Cdd:COG2039   1 MKVLVTGFEPFGGEPINPSWEAVKELNGRIIGGAEVKGRILPVVFKKSIDALVQAIAEVQPDLVLAIGQAGGRTKITPER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC       104 VAININDARIPDNAGNQPIDTPVIVDGPAAYFSRLPIKTMVNALNTAGIPASVSQTAGTFVCNHVMYGLLHYLAQNTPSV 183
Cdd:COG2039  81 VAINVDDARIPDNAGNQPIDEPIDPDGPAAYFSTLPVKAMVQAIREAGIPASVSNSAGTYVCNHVMYGLLHHLAKKGPPV 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
4HPSC       184 RGGFIHVPYLPEQAVKDGNQSSMTLMLMTLALKIAIETAWKNTSD 228
Cdd:COG2039 161 RAGFIHVPYLPEQAARKPNTPSMSLDTIVRGVRAAIEAILRQKDD 205
Peptidase_C15 pfam01470
Pyroglutamyl peptidase;
23-223 2.30e-101

Pyroglutamyl peptidase;


Pssm-ID: 250642  Cd Length: 203  Bit Score: 295.42  E-value: 2.30e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC          23 MKtILVTAFDPFGGEAINPSWEAIKPLQGSQVFGANIEICQIPCIFDTSLEHLYAAVDKYQPELVISVGQAGGRTNITVE 102
Cdd:pfam01470   1 MK-VLVTGFEPFGGDPINPAWEAAKQLDGRTIGGATIVGRILPTSFKKAAEVLQQAIAEIKPDIVIALGQAPGRSAITVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC         103 RVAININDARIPDNAGNQPIDTPVIVDGPAAYFSRLPIKTMVNALNTAGIPASVSQTAGTFVCNHVMYGLLHYLAQNTPS 182
Cdd:pfam01470  80 RVAINIDDARIPDNDGYQPIDEPIVPDGPAAYFATLPVKAMVKAMREAGIPAAVSNTAGTFVCNHVMYLLLHHSAKKGPP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
4HPSC         183 VRGGFIHVPYLPEQAVKDGNQSSMTLMLMTLALKIAIETAW 223
Cdd:pfam01470 160 VRAGFIHVPYLPEQVVDKPNTPSMSLDTIVAGVTAAIEAAL 200
pyro_pdase TIGR00504
pyroglutamyl-peptidase I; Alternate names include pyroglutamate aminopeptidase, ...
26-228 2.45e-94

pyroglutamyl-peptidase I; Alternate names include pyroglutamate aminopeptidase, pyrrolidone-carboxylate peptidase, and 5-oxoprolyl-peptidase. It removes pyroglutamate (pyrrolidone-carboxylate, a modified glutamine) that can otherwise block hydrolysis of a polypeptide at the amino end, and so can be extremely useful in the biochemical studies of proteins. The biological role in the various species in which it is found is not fully understood. The enzyme appears to be a homodimer. It does not closely resemble any other peptidases [Protein fate, Degradation of proteins, peptides, and glycopeptides].


Pssm-ID: 129595  Cd Length: 212  Bit Score: 277.88  E-value: 2.45e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC          26 ILVTAFDPFGGEAINPSWEAIKPLQGSQVfGANIEICQIPCIFDTSLEHLYAAVDKYQPELVISVGQAGGRTNITVERVA 105
Cdd:TIGR00504   2 VLLTGFEPFGVDPVNPSWEAAEELDGRTI-GATVVAEILPNTFFEAIEALQQAIDEIEPDIVIMLGLAPGRSMITVERVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC         106 ININDARIPDNAGNQPIDTPVIVDGPAAYFSRLPIKTMVNALNTAGIPASVSQTAGTFVCNHVMYGLLHYLAQNTPSVRG 185
Cdd:TIGR00504  81 INVNDARIPDNAGEQPIDEPIVPDGPAAYFATLPVRAMVLAMKKAGIPADVSYTAGTFVCNHLMYGLLHHLAQKGLPVRA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
4HPSC         186 GFIHVPYLPEQAVKDGNQSSMTLMLMTLALKIAIETAWKNTSD 228
Cdd:TIGR00504 161 GFIHVPYLPSQVALKHGVPSMSLDTAVAGVTIAIETAIRQSAD 203
 
Name Accession Description Interval E-value
Peptidase_C15 cd00501
Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: ...
24-218 1.48e-98

Pyroglutamyl peptidase (PGP) type I, also known as pyrrolidone carboxyl peptidase (pcp) type I: Enzymes responsible for cleaving pyroglutamate (pGlu) from the N-terminal end of specialized proteins. The N-terminal pGlu protects these proteins from proteolysis by other proteases until the pGlu is removed by a PGP. PGPs are cysteine proteases with a Cys-His-Glu/Asp catalytic triad. Type I PGPs are found in a wide variety of prokaryotes and eukaryotes. It is not clear whether the functional form is a monomer, a homodimer, or a homotetramer.


Pssm-ID: 238279  Cd Length: 194  Bit Score: 288.01  E-value: 1.48e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC        24 KTILVTAFDPFGGEAINPSWEAIKPLQGSQVFGANIEICQIPCIFDTSLEHLYAAVDKYQPELVISVGQAGGRTNITVER 103
Cdd:cd00501   1 KKVLVTGFGPFGGEPVNPSWEAVKELPKLILGGAEVVGLELPVVFQKAVEVLPELIEEHKPDLVIHVGLAGGRSTITIER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC       104 VAININDARIPDNAGNQPIDTPVIVDGPAAYFSRLPIKTMVNALNTAGIPASVSQTAGTFVCNHVMYGLLHYLAQNTPSV 183
Cdd:cd00501  81 VAINIDDARIPDNEGNQPIDEPIVPGGPAAYFSTLPVKAIVKALREAGIPARVSNDAGTYLCNHVYYGSLHESATRGPFI 160
                       170       180       190
                ....*....|....*....|....*....|....*
4HPSC       184 RGGFIHVPYLPEQAVkDGNQSSMTLMLMTLALKIA 218
Cdd:cd00501 161 RAGFIHVPYSPEQVA-DKGAPSMSLETILRALEAA 194
PRK13197 PRK13197
pyrrolidone-carboxylate peptidase; Provisional
23-228 2.16e-129

pyrrolidone-carboxylate peptidase; Provisional


Pssm-ID: 237299  Cd Length: 215  Bit Score: 366.89  E-value: 2.16e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC         23 MKTILVTAFDPFGGEAINPSWEAIKPLQGSQVFGANIEICQIPCIFDTSLEHLYAAVDKYQPELVISVGQAGGRTNITVE 102
Cdd:PRK13197   1 MMKILVTGFDPFGGEKINPSWEAVKQLPGKEIGGAEIIKRQLPTVFGKSAEVLKEAIEEVQPDAVICIGQAGGRTDITPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC        103 RVAININDARIPDNAGNQPIDTPVIVDGPAAYFSRLPIKTMVNALNTAGIPASVSQTAGTFVCNHVMYGLLHYLAQNTPS 182
Cdd:PRK13197  81 RVAINIDDARIPDNEGNQPIDEPIVEDGPAAYFSTLPIKAMVKAIREAGIPASVSNTAGTFVCNHVMYGLLHLLDKKYPN 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
4HPSC        183 VRGGFIHVPYLPEQAVKDGNQSSMTLMLMTLALKIAIETAWKNTSD 228
Cdd:PRK13197 161 IRAGFIHIPYLPEQAVNKPGTPSMSLEDIVRGLELAIEAIVENEDD 206
Pcp COG2039
Pyrrolidone-carboxylate peptidase (N-terminal pyroglutamyl peptidase) [Posttranslational ...
24-228 5.62e-107

Pyrrolidone-carboxylate peptidase (N-terminal pyroglutamyl peptidase) [Posttranslational modification, protein turnover, chaperones]


Pssm-ID: 224950  Cd Length: 207  Bit Score: 309.64  E-value: 5.62e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC        24 KTILVTAFDPFGGEAINPSWEAIKPLQGSQVFGANIEICQIPCIFDTSLEHLYAAVDKYQPELVISVGQAGGRTNITVER 103
Cdd:COG2039   1 MKVLVTGFEPFGGEPINPSWEAVKELNGRIIGGAEVKGRILPVVFKKSIDALVQAIAEVQPDLVLAIGQAGGRTKITPER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC       104 VAININDARIPDNAGNQPIDTPVIVDGPAAYFSRLPIKTMVNALNTAGIPASVSQTAGTFVCNHVMYGLLHYLAQNTPSV 183
Cdd:COG2039  81 VAINVDDARIPDNAGNQPIDEPIDPDGPAAYFSTLPVKAMVQAIREAGIPASVSNSAGTYVCNHVMYGLLHHLAKKGPPV 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
4HPSC       184 RGGFIHVPYLPEQAVKDGNQSSMTLMLMTLALKIAIETAWKNTSD 228
Cdd:COG2039 161 RAGFIHVPYLPEQAARKPNTPSMSLDTIVRGVRAAIEAILRQKDD 205
Peptidase_C15 pfam01470
Pyroglutamyl peptidase;
23-223 2.30e-101

Pyroglutamyl peptidase;


Pssm-ID: 250642  Cd Length: 203  Bit Score: 295.42  E-value: 2.30e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC          23 MKtILVTAFDPFGGEAINPSWEAIKPLQGSQVFGANIEICQIPCIFDTSLEHLYAAVDKYQPELVISVGQAGGRTNITVE 102
Cdd:pfam01470   1 MK-VLVTGFEPFGGDPINPAWEAAKQLDGRTIGGATIVGRILPTSFKKAAEVLQQAIAEIKPDIVIALGQAPGRSAITVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC         103 RVAININDARIPDNAGNQPIDTPVIVDGPAAYFSRLPIKTMVNALNTAGIPASVSQTAGTFVCNHVMYGLLHYLAQNTPS 182
Cdd:pfam01470  80 RVAINIDDARIPDNDGYQPIDEPIVPDGPAAYFATLPVKAMVKAMREAGIPAAVSNTAGTFVCNHVMYLLLHHSAKKGPP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
4HPSC         183 VRGGFIHVPYLPEQAVKDGNQSSMTLMLMTLALKIAIETAW 223
Cdd:pfam01470 160 VRAGFIHVPYLPEQVVDKPNTPSMSLDTIVAGVTAAIEAAL 200
pyro_pdase TIGR00504
pyroglutamyl-peptidase I; Alternate names include pyroglutamate aminopeptidase, ...
26-228 2.45e-94

pyroglutamyl-peptidase I; Alternate names include pyroglutamate aminopeptidase, pyrrolidone-carboxylate peptidase, and 5-oxoprolyl-peptidase. It removes pyroglutamate (pyrrolidone-carboxylate, a modified glutamine) that can otherwise block hydrolysis of a polypeptide at the amino end, and so can be extremely useful in the biochemical studies of proteins. The biological role in the various species in which it is found is not fully understood. The enzyme appears to be a homodimer. It does not closely resemble any other peptidases [Protein fate, Degradation of proteins, peptides, and glycopeptides].


Pssm-ID: 129595  Cd Length: 212  Bit Score: 277.88  E-value: 2.45e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC          26 ILVTAFDPFGGEAINPSWEAIKPLQGSQVfGANIEICQIPCIFDTSLEHLYAAVDKYQPELVISVGQAGGRTNITVERVA 105
Cdd:TIGR00504   2 VLLTGFEPFGVDPVNPSWEAAEELDGRTI-GATVVAEILPNTFFEAIEALQQAIDEIEPDIVIMLGLAPGRSMITVERVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC         106 ININDARIPDNAGNQPIDTPVIVDGPAAYFSRLPIKTMVNALNTAGIPASVSQTAGTFVCNHVMYGLLHYLAQNTPSVRG 185
Cdd:TIGR00504  81 INVNDARIPDNAGEQPIDEPIVPDGPAAYFATLPVRAMVLAMKKAGIPADVSYTAGTFVCNHLMYGLLHHLAQKGLPVRA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
4HPSC         186 GFIHVPYLPEQAVKDGNQSSMTLMLMTLALKIAIETAWKNTSD 228
Cdd:TIGR00504 161 GFIHVPYLPSQVALKHGVPSMSLDTAVAGVTIAIETAIRQSAD 203
PRK13194 PRK13194
pyrrolidone-carboxylate peptidase; Provisional
23-222 4.36e-62

pyrrolidone-carboxylate peptidase; Provisional


Pssm-ID: 183887  Cd Length: 208  Bit Score: 195.10  E-value: 4.36e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC         23 MKtILVTAFDPFGGEAINPSWEAIKPLQGSQVFGANIEICQIPCIFDTSLEHLYAAVDKYQPELVISVGQAGGRTNITVE 102
Cdd:PRK13194   1 MK-VLVTGFEPFGGDKKNPTMDIVKALDGKKIGDAKVFGRVLPVSFKRAREELEKVLDEIKPDITINLGLAPGRTHISVE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC        103 RVAININDARIPDNAGNQPIDTPVIVDGPAAYFSRLPIKTMVNALNTAGIPASVSQTAGTFVCNHVMYGLLHYLAQNTPS 182
Cdd:PRK13194  80 RVAVNAIDARIPDNDGEKPEDEPIVEGAPAAYFATLPTREIVEELKKNGIPAVLSYSAGTYLCNYVMYLTLHHSATKGYP 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
4HPSC        183 VRGGFIHVPYLPEQAV----KDGNQSSMTLMLMTLALKIAIETA 222
Cdd:PRK13194 160 KMAGFIHVPYTPDQVIekigKGKNTPSMCLEMEIEAVKIAIRVA 203
PRK13195 PRK13195
pyrrolidone-carboxylate peptidase; Provisional
23-228 2.27e-46

pyrrolidone-carboxylate peptidase; Provisional


Pssm-ID: 171894  Cd Length: 222  Bit Score: 155.19  E-value: 2.27e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC         23 MKTILVTAFDPFGGEAINPSWEAIKPLQGSQVFGANIEICQIPCIFDTSLEHLYAAVDKYQPELVISVGQAGGRTNITVE 102
Cdd:PRK13195   1 MSKVLVTGFGPYGVTPVNPAQLTAEELDGRTIAGATVISRIVPNTFFESIAAAQQAIAEIEPALVIMLGEYPGRSMITVE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC        103 RVAININDAR---IPDNAGNQPIDTPVIVDGPAAYFSRLPIKTMVNALNTAGIPASVSQTAGTFVCNHVMYGLLHYLAQN 179
Cdd:PRK13195  81 RLAQNVNDCGrygLADCAGRVLVGEPTDPAGPVAYHATVPVRAMVLAMRKAGVPADVSDAAGTFVCNHLMYGVLHHLAQK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
4HPSC        180 TPSVRGGFIHVPYLPEQAVKDGNQS--SMTLMLMTLALKIAIETAWKNTSD 228
Cdd:PRK13195 161 GLPVRAGWIHLPCLPSVAALDHNLGvpSMSVQTAVAGVTAGIEAAIRQSAD 211
PRK13196 PRK13196
pyrrolidone-carboxylate peptidase; Provisional
23-221 8.01e-46

pyrrolidone-carboxylate peptidase; Provisional


Pssm-ID: 171895  Cd Length: 211  Bit Score: 153.22  E-value: 8.01e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC         23 MKTILVTAFDPFGGEAINPSWEAIKPLQGSQVFGANIEICQIPCIFDTSLEHLYAAVDKYQPELVISVGQAGGRTNITVE 102
Cdd:PRK13196   1 MPTLLLTGFEPFHTHPVNPSAQAAQALNGEQAGALRVHSALLPVEPRAAMAALSRLLDELQPSAVLLTGLAAGRPQVTLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC        103 RVAININDARIPDNAGNQPIDTPVIV--DGPAAYFSRLPIKTMVNALNTAGIPASVSQTAGTFVCNHVMYGLLHYLAQ-N 179
Cdd:PRK13196  81 RVAVNVMDFSIPDNAGQTYRDTPVCTepDAPAAYLSTLPLRAILAAWHDAGIPGHISNTAGLYVCNFVLYHALHQLHLrG 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
4HPSC        180 TPSVRGGFIHVPYLPEQAVK-DGNQSSMTLM---LMTLALKIAIET 221
Cdd:PRK13196 161 RAEVPCGFLHVPANAQVALAvAGDRPPLPYLpqeEITRAVRVAAET 206
PRK13193 PRK13193
pyrrolidone-carboxylate peptidase; Provisional
25-228 6.07e-35

pyrrolidone-carboxylate peptidase; Provisional


Pssm-ID: 237298  Cd Length: 209  Bit Score: 125.04  E-value: 6.07e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC         25 TILVTAFDPFGGEAINPSWEAIKPLQGSQVFGANIEICQIPCIFDTSLEHLYAAVDKYQPELVISVGQAGGRTNITVERV 104
Cdd:PRK13193   2 TVLLFGFEPFLEYKENPSQLIVEALNGSTILKEEVKGVILPVEYEKIEDLIVTKIREMKPILTLGIGVAPGRAKITPEKI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HPSC        105 AININDARIPDNAGNQPIDTPVIVDGPAAYFSRLPIKTMVNALNTAGIPASVSQTAGTFVCNHVMYGLLHYlAQNTPSvR 184
Cdd:PRK13193  82 AINYKYSREGDNAGKKYKGEKIDPLGQDGIFTNIPVEDLVDLLNENGIPAELSLSAGSYLCNNAMYIIIRE-ARKYNS-L 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
4HPSC        185 GGFIHVPYLPEQAVK-DGNQSSMTLMLMTLALKIAIETAWKNTSD 228
Cdd:PRK13193 160 GGFIHVPLHESYAARiQRPIPSMSLDTMIRGIRLSMEFILTNKKE 204
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • 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 et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • 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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