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Conserved domains on  [gi|1527686809|gb|RRG70915|]
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aminopeptidase P family protein [Clostridioides difficile]

Protein Classification

M24 family metallopeptidase( domain architecture ID 11414248)

M24 family metallopeptidase cleaves amido-, imido- or amidino-containing bonds, exhibiting a fairly narrow substrate specificity compared to other metallo-aminopeptidases, possibly playing roles in regulation of biological processes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
7-357 3.18e-106

Xaa-Pro aminopeptidase [Amino acid transport and metabolism];


:

Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 313.29  E-value: 3.18e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809   7 VVELLETKGVDALYLTKKTNVNYISGFPD---EEAYAVICKDGN-FLVTDSRYMElaekvckdfeiinwhnfdrsvakav 82
Cdd:COG0006     3 LRALMAEAGLDALLLTDPSNFAYLTGFRGspeRLAALLVTADGEpVLFVDELEAE------------------------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809  83 ksvcdkvgikklgfertnivfdkyeelknliekdnGELIPTENIVETLRYVKDKDEIKNTRKACEIADKALEELIPHIKA 162
Cdd:COG0006    58 -----------------------------------RELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRP 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 163 GVSEIELATRLEYFMKMNGAQNIGFETILISGAKTSLLHGKPSDKIIEKGDFVLIDYGAMYNGYISDTTRTFIVGGASEK 242
Cdd:COG0006   103 GVTEREVAAELEAAMRRRGAEGPSFDTIVASGENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDE 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 243 QLEIYNLVKEAQNVGVENMKAGVHATIPDAEIRKVVKK--YEDYYYQGIGHGVGRDVHEEPFIGNYGDKIIEEGCIITME 320
Cdd:COG0006   183 QREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEagYGEYFPHGTGHGVGLDVHEGPQISPGNDRPLEPGMVFTIE 262
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1527686809 321 PGIYFPGWGGVRIEDTVLITKNGPERLTKFPKDLMIL 357
Cdd:COG0006   263 PGIYIPGIGGVRIEDTVLVTEDGAEVLTRLPRELLEL 299
 
Name Accession Description Interval E-value
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
7-357 3.18e-106

Xaa-Pro aminopeptidase [Amino acid transport and metabolism];


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 313.29  E-value: 3.18e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809   7 VVELLETKGVDALYLTKKTNVNYISGFPD---EEAYAVICKDGN-FLVTDSRYMElaekvckdfeiinwhnfdrsvakav 82
Cdd:COG0006     3 LRALMAEAGLDALLLTDPSNFAYLTGFRGspeRLAALLVTADGEpVLFVDELEAE------------------------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809  83 ksvcdkvgikklgfertnivfdkyeelknliekdnGELIPTENIVETLRYVKDKDEIKNTRKACEIADKALEELIPHIKA 162
Cdd:COG0006    58 -----------------------------------RELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRP 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 163 GVSEIELATRLEYFMKMNGAQNIGFETILISGAKTSLLHGKPSDKIIEKGDFVLIDYGAMYNGYISDTTRTFIVGGASEK 242
Cdd:COG0006   103 GVTEREVAAELEAAMRRRGAEGPSFDTIVASGENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDE 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 243 QLEIYNLVKEAQNVGVENMKAGVHATIPDAEIRKVVKK--YEDYYYQGIGHGVGRDVHEEPFIGNYGDKIIEEGCIITME 320
Cdd:COG0006   183 QREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEagYGEYFPHGTGHGVGLDVHEGPQISPGNDRPLEPGMVFTIE 262
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1527686809 321 PGIYFPGWGGVRIEDTVLITKNGPERLTKFPKDLMIL 357
Cdd:COG0006   263 PGIYIPGIGGVRIEDTVLVTEDGAEVLTRLPRELLEL 299
APP-like cd01092
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
139-344 9.98e-94

Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse hydrolysis of Xaa-Pro dipeptides and/or release of any N-terminal amino acid, including proline, that is linked with proline.


Pssm-ID: 238525 [Multi-domain]  Cd Length: 208  Bit Score: 278.24  E-value: 9.98e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 139 IKNTRKACEIADKALEELIPHIKAGVSEIELATRLEYFMKMNGAQNIGFETILISGAKTSLLHGKPSDKIIEKGDFVLID 218
Cdd:cd01092     1 IELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKLGAEGPSFDTIVASGPNSALPHGVPSDRKIEEGDLVLID 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 219 YGAMYNGYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVENMKAGVHATIPDAEIRKVV--KKYEDYYYQGIGHGVGRD 296
Cdd:cd01092    81 FGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIeeAGYGEYFIHRTGHGVGLE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1527686809 297 VHEEPFIGNYGDKIIEEGCIITMEPGIYFPGWGGVRIEDTVLITKNGP 344
Cdd:cd01092   161 VHEAPYISPGSDDVLEEGMVFTIEPGIYIPGKGGVRIEDDVLVTEDGC 208
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
143-341 2.46e-76

Metallopeptidase family M24; This family contains metallopeptidases. It also contains non-peptidase homologs such as the N terminal domain of Spt16 which is a histone H3-H4 binding module.


Pssm-ID: 459852 [Multi-domain]  Cd Length: 208  Bit Score: 234.06  E-value: 2.46e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 143 RKACEIADKALEELIPHIKAGVSEIELATRLEYF-MKMNGAQNIGFETILISGAKTSLLHGKPSDKIIEKGDFVLIDYGA 221
Cdd:pfam00557   4 RKAARIAAAALEAALAAIRPGVTERELAAELEAArLRRGGARGPAFPPIVASGPNAAIPHYIPNDRVLKPGDLVLIDVGA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 222 MYN-GYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVENMKAGVHATIPDAEIRKVVKK--YEDYYYQGIGHGVGRDVH 298
Cdd:pfam00557  84 EYDgGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEagLGEYFPHGLGHGIGLEVH 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1527686809 299 EEPFIGNYGDK-IIEEGCIITMEPGIYF-PGWGGVRIEDTVLITK 341
Cdd:pfam00557 164 EGPYISRGGDDrVLEPGMVFTIEPGIYFiPGWGGVRIEDTVLVTE 208
PRK09795 PRK09795
aminopeptidase; Provisional
1-356 5.75e-73

aminopeptidase; Provisional


Pssm-ID: 182080 [Multi-domain]  Cd Length: 361  Bit Score: 230.59  E-value: 5.75e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809   1 MSRVKNVVELLETKGVDALYLTKKTNVNYISGFPDEEAYAVICKDGNFLVTDSRYMELAEKVCKDFEIinwHNFD--RSV 78
Cdd:PRK09795    1 MTLLASLRDWLKAQQLDAVLLSSRQNKQPHLGISTGSGYVVISRESAHILVDSRYYADVEARAQGYQL---HLLDatNTL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809  79 AKAVKSVCDKVGIKKLGFERTNIVFDKYEELKnliEKDNGELIPTEniVETLRYVKDKDEIKNTRKACEIADKALEELIP 158
Cdd:PRK09795   78 TTIVNQIIADEQLQTLGFEGQQVSWETAHRWQ---SELNAKLVSAT--PDVLRQIKTPEEVEKIRLACGIADRGAEHIRR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 159 HIKAGVSEIELATRLEYFMKMNGAQNIGFETILISGAKTSLLHGKPSDKIIEKGDFVLIDYGAMYNGYISDTTRTFIVGG 238
Cdd:PRK09795  153 FIQAGMSEREIAAELEWFMRQQGAEKASFDTIVASGWRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVNG 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 239 ASEKQ-----LEIYNLVKEAQNVGVENMKAGVHATIPDAEIRKVVKK--YEDYYYQGIGHGVGRDVHEEPFIGNYGDKII 311
Cdd:PRK09795  233 EGVSAeshplFNVYQIVLQAQLAAISAIRPGVRCQQVDDAARRVITEagYGDYFGHNTGHAIGIEVHEDPRFSPRDTTTL 312
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1527686809 312 EEGCIITMEPGIYFPGWGGVRIEDTVLITKNGPERLTKFPKDLMI 356
Cdd:PRK09795  313 QPGMLLTVEPGIYLPGQGGVRIEDVVLVTPQGAEVLYAMPKTVLL 357
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
132-349 7.26e-37

methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. Bacterial and organellar examples (type I) differ from eukaroytic and archaeal (type II) examples in lacking a region of approximately 60 amino acids between the 4th and 5th cobalt-binding ligands. This model describes type I. The role of this protein in general is to produce the mature form of cytosolic proteins by removing the N-terminal methionine. [Protein fate, Protein modification and repair]


Pssm-ID: 129591 [Multi-domain]  Cd Length: 247  Bit Score: 133.24  E-value: 7.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 132 YVKDKDEIKNTRKACEIADKALEELIPHIKAGVSEIELATRLEYFMKMNGAQN-----IGFETILISGAKTSLLHGKPSD 206
Cdd:TIGR00500   2 SLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPaflgyYGFPGSVCISVNEVVIHGIPDK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 207 KIIEKGDFVLIDYGAMYNGYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVENMKAGvhatIPDAEIRKVVKKY-EDYY 285
Cdd:TIGR00500  82 KVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPG----NRIGEIGAAIQKYaEAKG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 286 YQGI----GHGVGRDVHEEPFIGNYGDKI----IEEGCIITMEPGIYFPGWGGV-----------------RIEDTVLIT 340
Cdd:TIGR00500 158 FSVVreycGHGIGRKFHEEPQIPNYGKKFtnvrLKEGMVFTIEPMVNTGTEEITtaadgwtvktkdgslsaQFEHTIVIT 237

                  ....*....
gi 1527686809 341 KNGPERLTK 349
Cdd:TIGR00500 238 DNGPEILTE 246
 
Name Accession Description Interval E-value
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
7-357 3.18e-106

Xaa-Pro aminopeptidase [Amino acid transport and metabolism];


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 313.29  E-value: 3.18e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809   7 VVELLETKGVDALYLTKKTNVNYISGFPD---EEAYAVICKDGN-FLVTDSRYMElaekvckdfeiinwhnfdrsvakav 82
Cdd:COG0006     3 LRALMAEAGLDALLLTDPSNFAYLTGFRGspeRLAALLVTADGEpVLFVDELEAE------------------------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809  83 ksvcdkvgikklgfertnivfdkyeelknliekdnGELIPTENIVETLRYVKDKDEIKNTRKACEIADKALEELIPHIKA 162
Cdd:COG0006    58 -----------------------------------RELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRP 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 163 GVSEIELATRLEYFMKMNGAQNIGFETILISGAKTSLLHGKPSDKIIEKGDFVLIDYGAMYNGYISDTTRTFIVGGASEK 242
Cdd:COG0006   103 GVTEREVAAELEAAMRRRGAEGPSFDTIVASGENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDE 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 243 QLEIYNLVKEAQNVGVENMKAGVHATIPDAEIRKVVKK--YEDYYYQGIGHGVGRDVHEEPFIGNYGDKIIEEGCIITME 320
Cdd:COG0006   183 QREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEagYGEYFPHGTGHGVGLDVHEGPQISPGNDRPLEPGMVFTIE 262
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1527686809 321 PGIYFPGWGGVRIEDTVLITKNGPERLTKFPKDLMIL 357
Cdd:COG0006   263 PGIYIPGIGGVRIEDTVLVTEDGAEVLTRLPRELLEL 299
APP-like cd01092
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
139-344 9.98e-94

Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse hydrolysis of Xaa-Pro dipeptides and/or release of any N-terminal amino acid, including proline, that is linked with proline.


Pssm-ID: 238525 [Multi-domain]  Cd Length: 208  Bit Score: 278.24  E-value: 9.98e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 139 IKNTRKACEIADKALEELIPHIKAGVSEIELATRLEYFMKMNGAQNIGFETILISGAKTSLLHGKPSDKIIEKGDFVLID 218
Cdd:cd01092     1 IELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKLGAEGPSFDTIVASGPNSALPHGVPSDRKIEEGDLVLID 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 219 YGAMYNGYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVENMKAGVHATIPDAEIRKVV--KKYEDYYYQGIGHGVGRD 296
Cdd:cd01092    81 FGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIeeAGYGEYFIHRTGHGVGLE 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1527686809 297 VHEEPFIGNYGDKIIEEGCIITMEPGIYFPGWGGVRIEDTVLITKNGP 344
Cdd:cd01092   161 VHEAPYISPGSDDVLEEGMVFTIEPGIYIPGKGGVRIEDDVLVTEDGC 208
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
143-341 2.46e-76

Metallopeptidase family M24; This family contains metallopeptidases. It also contains non-peptidase homologs such as the N terminal domain of Spt16 which is a histone H3-H4 binding module.


Pssm-ID: 459852 [Multi-domain]  Cd Length: 208  Bit Score: 234.06  E-value: 2.46e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 143 RKACEIADKALEELIPHIKAGVSEIELATRLEYF-MKMNGAQNIGFETILISGAKTSLLHGKPSDKIIEKGDFVLIDYGA 221
Cdd:pfam00557   4 RKAARIAAAALEAALAAIRPGVTERELAAELEAArLRRGGARGPAFPPIVASGPNAAIPHYIPNDRVLKPGDLVLIDVGA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 222 MYN-GYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVENMKAGVHATIPDAEIRKVVKK--YEDYYYQGIGHGVGRDVH 298
Cdd:pfam00557  84 EYDgGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEagLGEYFPHGLGHGIGLEVH 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1527686809 299 EEPFIGNYGDK-IIEEGCIITMEPGIYF-PGWGGVRIEDTVLITK 341
Cdd:pfam00557 164 EGPYISRGGDDrVLEPGMVFTIEPGIYFiPGWGGVRIEDTVLVTE 208
PRK09795 PRK09795
aminopeptidase; Provisional
1-356 5.75e-73

aminopeptidase; Provisional


Pssm-ID: 182080 [Multi-domain]  Cd Length: 361  Bit Score: 230.59  E-value: 5.75e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809   1 MSRVKNVVELLETKGVDALYLTKKTNVNYISGFPDEEAYAVICKDGNFLVTDSRYMELAEKVCKDFEIinwHNFD--RSV 78
Cdd:PRK09795    1 MTLLASLRDWLKAQQLDAVLLSSRQNKQPHLGISTGSGYVVISRESAHILVDSRYYADVEARAQGYQL---HLLDatNTL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809  79 AKAVKSVCDKVGIKKLGFERTNIVFDKYEELKnliEKDNGELIPTEniVETLRYVKDKDEIKNTRKACEIADKALEELIP 158
Cdd:PRK09795   78 TTIVNQIIADEQLQTLGFEGQQVSWETAHRWQ---SELNAKLVSAT--PDVLRQIKTPEEVEKIRLACGIADRGAEHIRR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 159 HIKAGVSEIELATRLEYFMKMNGAQNIGFETILISGAKTSLLHGKPSDKIIEKGDFVLIDYGAMYNGYISDTTRTFIVGG 238
Cdd:PRK09795  153 FIQAGMSEREIAAELEWFMRQQGAEKASFDTIVASGWRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVNG 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 239 ASEKQ-----LEIYNLVKEAQNVGVENMKAGVHATIPDAEIRKVVKK--YEDYYYQGIGHGVGRDVHEEPFIGNYGDKII 311
Cdd:PRK09795  233 EGVSAeshplFNVYQIVLQAQLAAISAIRPGVRCQQVDDAARRVITEagYGDYFGHNTGHAIGIEVHEDPRFSPRDTTTL 312
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1527686809 312 EEGCIITMEPGIYFPGWGGVRIEDTVLITKNGPERLTKFPKDLMI 356
Cdd:PRK09795  313 QPGMLLTVEPGIYLPGQGGVRIEDVVLVTPQGAEVLYAMPKTVLL 357
APP_MetAP cd01066
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
143-344 1.06e-60

A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as metallopeptidase family M24. This family of enzymes is able to cleave amido-, imido- and amidino-containing bonds. Members exibit relatively narrow substrate specificity compared to other metallo-aminopeptidases, suggesting they play roles in regulation of biological processes rather than general protein degradation.


Pssm-ID: 238514 [Multi-domain]  Cd Length: 207  Bit Score: 193.82  E-value: 1.06e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 143 RKACEIADKALEELIPHIKAGVSEIELATRLEYFMKMNGAQnIGFETILISGAKTSLLHGKPSDKIIEKGDFVLIDYGAM 222
Cdd:cd01066     5 RKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAGGY-PAGPTIVGSGARTALPHYRPDDRRLQEGDLVLVDLGGV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 223 YNGYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVENMKAGVHATIPDAEIRKVVKK--YEDYYYQGIGHGVGRDVHEE 300
Cdd:cd01066    84 YDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEhgLGPNFGHRTGHGIGLEIHEP 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1527686809 301 PFIGNYGDKIIEEGCIITMEPGIYFPGWGGVRIEDTVLITKNGP 344
Cdd:cd01066   164 PVLKAGDDTVLEPGMVFAVEPGLYLPGGGGVRIEDTVLVTEDGP 207
Prolidase cd01087
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ...
143-349 9.52e-51

Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline dipeptidase., imidodipeptidase, peptidase D, gamma-peptidase. Catalyses hydrolysis of Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-Pro.


Pssm-ID: 238520 [Multi-domain]  Cd Length: 243  Bit Score: 169.29  E-value: 9.52e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 143 RKACEIADKALEELIPHIKAGVSEIELATRLEYFMKMNGAQNiGFETILISGAKTSLLHGKPSDKIIEKGDFVLIDYGAM 222
Cdd:cd01087     5 RKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGARL-AYSYIVAAGSNAAILHYVHNDQPLKDGDLVLIDAGAE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 223 YNGYISDTTRTFIVGGA-SEKQLEIYNLVKEAQNVGVENMKAGV-HATIPDAEIRKVVKK-------------------Y 281
Cdd:cd01087    84 YGGYASDITRTFPVNGKfTDEQRELYEAVLAAQKAAIAACKPGVsYEDIHLLAHRVLAEGlkelgilkgdvdeivesgaY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 282 EDYYYQGIGHGVGRDVH--EEPFIGNYGDKIIEEGCIITMEPGIYFPGW----------GGVRIEDTVLITKNGPERLTK 349
Cdd:cd01087   164 AKFFPHGLGHYLGLDVHdvGGYLRYLRRARPLEPGMVITIEPGIYFIPDlldvpeyfrgGGIRIEDDVLVTEDGPENLTR 243
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
132-353 6.31e-40

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 141.30  E-value: 6.31e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 132 YVKDKDEIKNTRKACEIADKALEELIPHIKAGVSEIELATRLEYFMKMNGAqnigfetilISGAK----------TSL-- 199
Cdd:COG0024     2 EIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHGA---------IPAFLgyygfpksicTSVne 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 200 --LHGKPSDKIIEKGDFVLIDYGAMYNGYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVENMKAGVHatIPD--AEIR 275
Cdd:COG0024    73 vvVHGIPSDRVLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNR--LGDigHAIQ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 276 KVVKKY-----EDYyyqgIGHGVGRDVHEEPFIGNYGDK----IIEEGCIITMEP-------GIYFP--GWgGVRIED-- 335
Cdd:COG0024   151 SYAESNgysvvREF----VGHGIGREMHEEPQVPNYGRPgrgpRLKPGMVLAIEPminagtpEVKVLddGW-TVVTKDgs 225
                         250       260
                  ....*....|....*....|....*
gi 1527686809 336 -------TVLITKNGPERLTKFPKD 353
Cdd:COG0024   226 lsaqfehTVAVTEDGPEILTLPDGG 250
PRK05716 PRK05716
methionine aminopeptidase; Validated
133-353 3.42e-38

methionine aminopeptidase; Validated


Pssm-ID: 235576 [Multi-domain]  Cd Length: 252  Bit Score: 136.80  E-value: 3.42e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 133 VKDKDEIKNTRKACEIADKALEELIPHIKAGVSEIELatrleyfmkmngaQNIGFETILISGAKTSLL------------ 200
Cdd:PRK05716    5 IKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKEL-------------DRIAEEYIRDQGAIPAPLgyhgfpksicts 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 201 ------HGKPSDKIIEKGDFVLIDYGAMYNGYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVENMKAGVHATIPDAEI 274
Cdd:PRK05716   72 vnevvcHGIPSDKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 275 RKVVKKY-----EDYyyqgIGHGVGRDVHEEPFIGNYGDK----IIEEGCIITMEP----GIYFP-----GWGGV----- 331
Cdd:PRK05716  152 QKYAEAEgfsvvREY----CGHGIGRKFHEEPQIPHYGAPgdgpVLKEGMVFTIEPminaGKREVktlkdGWTVVtkdgs 227
                         250       260
                  ....*....|....*....|....*
gi 1527686809 332 ---RIEDTVLITKNGPERLTKFPKD 353
Cdd:PRK05716  228 lsaQYEHTVAVTEDGPEILTLRPEE 252
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
132-349 7.26e-37

methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. Bacterial and organellar examples (type I) differ from eukaroytic and archaeal (type II) examples in lacking a region of approximately 60 amino acids between the 4th and 5th cobalt-binding ligands. This model describes type I. The role of this protein in general is to produce the mature form of cytosolic proteins by removing the N-terminal methionine. [Protein fate, Protein modification and repair]


Pssm-ID: 129591 [Multi-domain]  Cd Length: 247  Bit Score: 133.24  E-value: 7.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 132 YVKDKDEIKNTRKACEIADKALEELIPHIKAGVSEIELATRLEYFMKMNGAQN-----IGFETILISGAKTSLLHGKPSD 206
Cdd:TIGR00500   2 SLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHGAKPaflgyYGFPGSVCISVNEVVIHGIPDK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 207 KIIEKGDFVLIDYGAMYNGYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVENMKAGvhatIPDAEIRKVVKKY-EDYY 285
Cdd:TIGR00500  82 KVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPG----NRIGEIGAAIQKYaEAKG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 286 YQGI----GHGVGRDVHEEPFIGNYGDKI----IEEGCIITMEPGIYFPGWGGV-----------------RIEDTVLIT 340
Cdd:TIGR00500 158 FSVVreycGHGIGRKFHEEPQIPNYGKKFtnvrLKEGMVFTIEPMVNTGTEEITtaadgwtvktkdgslsaQFEHTIVIT 237

                  ....*....
gi 1527686809 341 KNGPERLTK 349
Cdd:TIGR00500 238 DNGPEILTE 246
MetAP1 cd01086
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
139-349 2.47e-36

Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and Peptidase M. Catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.


Pssm-ID: 238519 [Multi-domain]  Cd Length: 238  Bit Score: 131.46  E-value: 2.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 139 IKNTRKACEIADKALEELIPHIKAGVSEIELATRLEYFMKMNGAQ-----NIGFE-TILISGAKTsLLHGKPSDKIIEKG 212
Cdd:cd01086     1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEHGAYpaplgYYGFPkSICTSVNEV-VCHGIPDDRVLKDG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 213 DFVLIDYGAMYNGYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVENMKAGVHATIPDAEIRKVVKKY-----EDYyyq 287
Cdd:cd01086    80 DIVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNgysvvREF--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 288 gIGHGVGRDVHEEPFIGNYGDK----IIEEGCIITMEP----GIYFP-----GWGGV--------RIEDTVLITKNGPER 346
Cdd:cd01086   157 -GGHGIGRKFHEEPQIPNYGRPgtgpKLKPGMVFTIEPminlGTYEVvtlpdGWTVVtkdgslsaQFEHTVLITEDGPEI 235

                  ...
gi 1527686809 347 LTK 349
Cdd:cd01086   236 LTL 238
PRK10879 PRK10879
proline aminopeptidase P II; Provisional
100-348 3.84e-33

proline aminopeptidase P II; Provisional


Pssm-ID: 182804 [Multi-domain]  Cd Length: 438  Bit Score: 127.92  E-value: 3.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 100 NIVFDKYEEL-----KNLieKDNGELIPTENIVETLRYVKDKDEIKNTRKACEIADKALEELIPHIKAGVSEIELATRLE 174
Cdd:PRK10879  137 EIVFSALEKLrkgsrQNL--TAPATLTDWRPWVHEMRLFKSPEEIAVLRRAGEISALAHTRAMEKCRPGMFEYQLEGEIH 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 175 YFMKMNGAQNIGFETILISGAKTSLLHGKPSDKIIEKGDFVLIDYGAMYNGYISDTTRTFIVGGA-SEKQLEIYNLVKEA 253
Cdd:PRK10879  215 HEFNRHGARYPSYNTIVGSGENGCILHYTENESEMRDGDLVLIDAGCEYKGYAGDITRTFPVNGKfTPAQREIYDIVLES 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 254 QNVGVENMKAG------------------VHATIPDAEIRKVV--KKYEDYYYQGIGHGVGRDVHEepfIGNYG---DKI 310
Cdd:PRK10879  295 LETSLRLYRPGtsirevtgevvrimvsglVKLGILKGDVDQLIaeNAHRPFFMHGLSHWLGLDVHD---VGVYGqdrSRI 371
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1527686809 311 IEEGCIITMEPGIY----------FPGWgGVRIEDTVLITKNGPERLT 348
Cdd:PRK10879  372 LEPGMVLTVEPGLYiapdadvpeqYRGI-GIRIEDDIVITETGNENLT 418
PRK12896 PRK12896
methionine aminopeptidase; Reviewed
133-348 1.26e-28

methionine aminopeptidase; Reviewed


Pssm-ID: 237252 [Multi-domain]  Cd Length: 255  Bit Score: 111.47  E-value: 1.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 133 VKDKDEIKNTRKACEIADKALEELIPHIKAGVSEIELATRLEYFMKMNGAQN-----IGF-ETILISgAKTSLLHGKPSD 206
Cdd:PRK12896   10 IKSPRELEKMRKIGRIVATALKEMGKAVEPGMTTKELDRIAEKRLEEHGAIPspegyYGFpGSTCIS-VNEEVAHGIPGP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 207 KIIEKGDFVLIDYGAMYNGYISDTTRTFIVGGASEkqlEIYNLV---KEAQNVGVENMKAGVHATIPDAEIRKVVKKY-- 281
Cdd:PRK12896   89 RVIKDGDLVNIDVSAYLDGYHGDTGITFAVGPVSE---EAEKLCrvaEEALWAGIKQVKAGRPLNDIGRAIEDFAKKNgy 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 282 ---EDYyyqgIGHGVGRDVHEEP-FIGNYGDK----IIEEGCIITMEP----GIYF-----PGWG--------GVRIEDT 336
Cdd:PRK12896  166 svvRDL----TGHGVGRSLHEEPsVILTYTDPlpnrLLRPGMTLAVEPflnlGAKDaetldDGWTvvtpdkslSAQFEHT 241
                         250
                  ....*....|..
gi 1527686809 337 VLITKNGPERLT 348
Cdd:PRK12896  242 VVVTRDGPEILT 253
Creatinase_N pfam01321
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ...
3-133 6.54e-28

Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic domains from creatinase and prolidase. The exact function of this domain is uncertain.


Pssm-ID: 460159  Cd Length: 128  Bit Score: 105.85  E-value: 6.54e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809   3 RVKNVVELLETKGVDALYLTKKTNVNYISGFPDEEAYA-VICKDGNFLVTD-SRYMELAEKVCKDFEIINWHNFdRSVAK 80
Cdd:pfam01321   1 RLEKLRKLMEEKGLDAALVTSPENLRYLTGFTGSRGLLlLVTADGALLLVDaLEYERAAAESAPDFDVVPYRDY-EALAD 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1527686809  81 AVKSVCdkVGIKKLGFERTNIVFDKYEELKNLIEKDngELIPTENIVETLRYV 133
Cdd:pfam01321  80 LLKELG--AGGKRVGFEADALTVAFYEALKEALPGA--ELVDVSGLIERLRMV 128
APP cd01085
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ...
164-343 6.02e-27

X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline aminopeptidase, aminopeptidase P, and aminoacylproline aminopeptidase. Catalyses release of any N-terminal amino acid, including proline, that is linked with proline, even from a dipeptide or tripeptide.


Pssm-ID: 238518 [Multi-domain]  Cd Length: 224  Bit Score: 106.11  E-value: 6.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 164 VSEIELATRLEYFMKMNGAQ-NIGFETILISGAKTSLLHGKP---SDKIIEKGDFVLIDYGAMYNGYISDTTRTFIVGGA 239
Cdd:cd01085    30 ITELSAADKLEEFRRQQKGYvGLSFDTISGFGPNGAIVHYSPteeSNRKISPDGLYLIDSGGQYLDGTTDITRTVHLGEP 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 240 SEKQLEIYNLVKEAqNVGVENMK--AGVHATIPDAEIRKVVKKYEDYYYQGIGHGVGR--DVHEEP--FIGNYGDKIIEE 313
Cdd:cd01085   110 TAEQKRDYTLVLKG-HIALARAKfpKGTTGSQLDALARQPLWKAGLDYGHGTGHGVGSflNVHEGPqsISPAPNNVPLKA 188
                         170       180       190
                  ....*....|....*....|....*....|
gi 1527686809 314 GCIITMEPGIYFPGWGGVRIEDTVLITKNG 343
Cdd:cd01085   189 GMILSNEPGYYKEGKYGIRIENLVLVVEAE 218
PRK15173 PRK15173
peptidase; Provisional
72-355 1.55e-21

peptidase; Provisional


Pssm-ID: 185095 [Multi-domain]  Cd Length: 323  Bit Score: 93.63  E-value: 1.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809  72 HNFDRSVAKAVKSVCD---------KVGIKKLGFErTNIVFDKYEELKNLIeKDNGELIPTENIVETLRYVKDKDEIKNT 142
Cdd:PRK15173   27 NNKERPIGPPIESVCNilkdalndaRVLNKKIAID-LNIMSNGGKRVIDAV-MPNVDFVDSSSIFNELRVIKSPWEIKRL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 143 RKACEIADKALEELIPHIKAGVSEIELATRLEYFMKMNGAQNIGFETILISGAKTS--LLhgkPSDKIIEKGDFVLIDYG 220
Cdd:PRK15173  105 RKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSKSETHFSRFHLISVGADFSpkLI---PSNTKACSGDLIKFDCG 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 221 AMYNGYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVENMKAGVHATIPDAEIRKVVKK--YEDYYYQGIGHGVG--RD 296
Cdd:PRK15173  182 VDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKsgLPNYNRGHLGHGNGvfLG 261
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1527686809 297 VHEEPFIGNYGDKIIEEGCIITMEPGIYFPGWGGVRIEDTVLITKNGPERLTKFPKDLM 355
Cdd:PRK15173  262 LEESPFVSTHATESFTSGMVLSLETPYYGYNLGSIMIEDMILINKEGIEFLSKLPRDLV 320
PRK14575 PRK14575
putative peptidase; Provisional
72-355 7.07e-21

putative peptidase; Provisional


Pssm-ID: 173039 [Multi-domain]  Cd Length: 406  Bit Score: 92.85  E-value: 7.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809  72 HNFDRSVAKAVKSVCD---------KVGIKKLGFErTNIVFDKYEELKNLIeKDNGELIPTENIVETLRYVKDKDEIKNT 142
Cdd:PRK14575  110 NNKERPIGPPIESVCNilkdalndaRVLNKKIAID-LNIMSNGGKRVIDAV-MPNVDFVDSSSIFNELRVIKSPWEIKRL 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 143 RKACEIADKALEELIPHIKAGVSEIELATRLEYFMKMNGAQNIGFETILISGAKTS--LLhgkPSDKIIEKGDFVLIDYG 220
Cdd:PRK14575  188 RKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSKSETHFSRFHLISVGADFSpkLI---PSNTKACSGDLIKFDCG 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 221 AMYNGYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVENMKAGVHATIPDAEIRKVVKK--YEDYYYQGIGHGVG--RD 296
Cdd:PRK14575  265 VDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKsgLPNYNRGHLGHGNGvfLG 344
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1527686809 297 VHEEPFIGNYGDKIIEEGCIITMEPGIYFPGWGGVRIEDTVLITKNGPERLTKFPKDLM 355
Cdd:PRK14575  345 LEESPFVSTHATESFTSGMVLSLETPYYGYNLGSIMIEDMILINKEGIEFLSKLPRDLV 403
PRK12897 PRK12897
type I methionyl aminopeptidase;
133-350 2.85e-20

type I methionyl aminopeptidase;


Pssm-ID: 171806  Cd Length: 248  Bit Score: 88.55  E-value: 2.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 133 VKDKDEIKNTRKACEIADKALEELIPHIKAGVSEIELATRLEYFMKMNGAQNI-----GFETILISGAKTSLLHGKPSDK 207
Cdd:PRK12897    4 IKTKNEIDLMHESGKLLASCHREIAKIMKPGITTKEINTFVEAYLEKHGATSEqkgynGYPYAICASVNDEMCHAFPADV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 208 IIEKGDFVLIDYGAMYNGYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVENMKAGVHAtipdAEIRKVVKKY------ 281
Cdd:PRK12897   84 PLTEGDIVTIDMVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNRV----GDIGYAIESYvanegf 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 282 ---EDYyyqgIGHGVGRDVHEEPFIGNYGDK----IIEEGCIITMEP----GIYFP-----GWGG--------VRIEDTV 337
Cdd:PRK12897  160 svaRDF----TGHGIGKEIHEEPAIFHFGKQgqgpELQEGMVITIEPivnvGMRYSkvdlnGWTArtmdgklsAQYEHTI 235
                         250
                  ....*....|...
gi 1527686809 338 LITKNGPERLTKF 350
Cdd:PRK12897  236 AITKDGPIILTKL 248
PRK12318 PRK12318
methionyl aminopeptidase;
133-348 8.06e-19

methionyl aminopeptidase;


Pssm-ID: 183434 [Multi-domain]  Cd Length: 291  Bit Score: 85.26  E-value: 8.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 133 VKDKDEIKNTRKACEIADKALEELIPHIKAGVSEIELATRLEYFMKMNGA----QNIG---FETILISGAKTSLLHGKPS 205
Cdd:PRK12318   43 IKTPEQIEKIRKACQVTARILDALCEAAKEGVTTNELDELSRELHKEYNAipapLNYGsppFPKTICTSLNEVICHGIPN 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 206 DKIIEKGDFVLIDYGAMYNGYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVENMKAGvhatIPDAEIRKVVKKYEDYY 285
Cdd:PRK12318  123 DIPLKNGDIMNIDVSCIVDGYYGDCSRMVMIGEVSEIKKKVCQASLECLNAAIAILKPG----IPLYEIGEVIENCADKY 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 286 -----YQGIGHGVGRDVHEEPFIGNYGDK---IIEEGCIITMEP--------GIYFP----------GWGGVRIEDTVLI 339
Cdd:PRK12318  199 gfsvvDQFVGHGVGIKFHENPYVPHHRNSskiPLAPGMIFTIEPminvgkkeGVIDPinhweartcdNQPSAQWEHTILI 278

                  ....*....
gi 1527686809 340 TKNGPERLT 348
Cdd:PRK12318  279 TETGYEILT 287
MetAP2 cd01088
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
143-321 9.17e-18

Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and peptidase M. Catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.


Pssm-ID: 238521 [Multi-domain]  Cd Length: 291  Bit Score: 82.30  E-value: 9.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 143 RKACEIADKALEELIPHIKAGVSEIELATRLEYFMKMNGAQnIGFETILisgaktSLLH-------GKPSDKIIEKGDFV 215
Cdd:cd01088     5 REAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELGAG-PAFPVNL------SINEcaahytpNAGDDTVLKEGDVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 216 LIDYGAMYNGYISDTTRTFIVGGASEKQLEIynlVKEAQNVGVENMKAGVHATIPDAEIRKVVkkyEDYYYQGI----GH 291
Cdd:cd01088    78 KLDFGAHVDGYIADSAFTVDFDPKYDDLLEA---AKEALNAAIKEAGPDVRLGEIGEAIEEVI---ESYGFKPIrnltGH 151
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1527686809 292 GVGR-DVHEEPFIGNY---GDKIIEEGCIITMEP 321
Cdd:cd01088   152 SIERyRLHAGKSIPNVkggEGTRLEEGDVYAIEP 185
PRK14576 PRK14576
putative endopeptidase; Provisional
10-354 2.57e-16

putative endopeptidase; Provisional


Pssm-ID: 173040 [Multi-domain]  Cd Length: 405  Bit Score: 79.67  E-value: 2.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809  10 LLETKGVDALYLTKKTNVNYISGFPD---------EEAYAVICKDGNF--------LVTDSRYMELAEKVCKDFEII--- 69
Cdd:PRK14576   19 VMEREGIDALVVTVCDNFYYLTGFASffmytfrhtGAAVAIMFRDANIpsqiimneFEAASTHFDMPNSVLKTFPVWvdv 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809  70 ----NWHNF----DRSVAKAVKSVcdkVGIKKLGFERTNiVFDKYEELKnLIEKDNG------------ELIPTENIVET 129
Cdd:PRK14576   99 ddprNPHHHykkrDRPIGPPVEAV---FSLVKNALEDAG-VLDKTIAIE-LQAMSNGgkgvldkvapglKLVDSTALFNE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 130 LRYVKDKDEIKNTRKACEIADKALEELIPHIKAGVSEIELATRLEYFMKMNGAQNIGFETILISGAKTSLlHGKPSDKII 209
Cdd:PRK14576  174 IRMIKSPWEIEHLRKSAEITEYGIASAAKKIRVGCTAAELTAAFKAAVMSFPETNFSRFNLISVGDNFSP-KIIADTTPA 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 210 EKGDFVLIDYGAMYNGYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVENMKAGVH-ATIPDAEIRKVVKKYEDYYYQG 288
Cdd:PRK14576  253 KVGDLIKFDCGIDVAGYGADLARTFVLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKlKAVFDSTMAVIKTSGLPHYNRG 332
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1527686809 289 -IGHGVG--RDVHEEPFIGNYGDKIIEEGCIITMEPGIYFPGWGGVRIEDTVLITKNGPERLTKFPKDL 354
Cdd:PRK14576  333 hLGHGDGvfLGLEEVPFVSTQATETFCPGMVLSLETPYYGIGVGSIMLEDMILITDSGFEFLSKLDRDL 401
PRK13607 PRK13607
proline dipeptidase; Provisional
216-348 4.98e-14

proline dipeptidase; Provisional


Pssm-ID: 237444 [Multi-domain]  Cd Length: 443  Bit Score: 72.62  E-value: 4.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 216 LIDYGAMYNGYISDTTRTFivggASEKQLEIYNLVK---EAQNVGVENMKAGV---------HatipdAEIRKVVKKY-- 281
Cdd:PRK13607  244 LIDAGAEYNGYAADITRTY----AAKEDNDFAALIKdvnKEQLALIATMKPGVsyvdlhiqmH-----QRIAKLLRKFqi 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 282 ------EDYYYQGI---------GHGVGRDVH------------------EEPFIGNygDKIIEEGCIITMEPGIYF--- 325
Cdd:PRK13607  315 vtglseEAMVEQGItspffphglGHPLGLQVHdvagfmqddrgthlaapeKHPYLRC--TRVLEPGMVLTIEPGLYFids 392
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1527686809 326 -----------------------PgWGGVRIEDTVLITKNGPERLT 348
Cdd:PRK13607  393 llaplregpfskhfnwqkidalkP-FGGIRIEDNVVVHENGVENMT 437
Creatinase cd01090
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea.
139-349 8.53e-14

Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea.


Pssm-ID: 238523 [Multi-domain]  Cd Length: 228  Bit Score: 69.87  E-value: 8.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 139 IKNTRKACEIADKALEELIphiKAGVSEIELATRLEYFMKMNGAQNIGFE------TILISGAKTSLLHGKPSDKIIEKG 212
Cdd:cd01090     4 IRHGARIADIGGAAVVEAI---REGVPEYEVALAGTQAMVREIAKTFPEVelmdtwTWFQSGINTDGAHNPVTNRKVQRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 213 DFVLIDYGAMYNGYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVENMKAGVHATIPDAEIRKVVKKYEDYYYQ--GIG 290
Cdd:cd01090    81 DILSLNCFPMIAGYYTALERTLFLDEVSDAHLKIWEANVAVHERGLELIKPGARCKDIAAELNEMYREHDLLRYRtfGYG 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1527686809 291 HGVGRDVHEepfignYG-----------DKIIEEGCIITMEPGIYF----PGWGGVRIEDTVLITKNGPERLTK 349
Cdd:cd01090   161 HSFGVLSHY------YGreaglelrediDTVLEPGMVVSMEPMIMLpegqPGAGGYREHDILVINENGAENITG 228
PLN03158 PLN03158
methionine aminopeptidase; Provisional
124-349 1.31e-13

methionine aminopeptidase; Provisional


Pssm-ID: 215607 [Multi-domain]  Cd Length: 396  Bit Score: 71.41  E-value: 1.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 124 ENIVEtlryVKDKDEIKNTRKACEIADKALEELIPHIKAGVSEIEL------AT--------RLEYFMkmngaqnigFET 189
Cdd:PLN03158  132 QHSVE----IKTPEQIQRMRETCRIAREVLDAAARAIKPGVTTDEIdrvvheATiaaggypsPLNYHF---------FPK 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 190 ILISGAKTSLLHGKPSDKIIEKGDFVLIDYGAMYNGYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVENMKAGV---- 265
Cdd:PLN03158  199 SCCTSVNEVICHGIPDARKLEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEASRQLVKCTYECLEKAIAIVKPGVryre 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 266 -------HATIPDAEirkVVKKYedyyyqgIGHGVGRDVHEEPFIGNYGDK----IIEEGCIITMEPGI--------YFP 326
Cdd:PLN03158  279 vgevinrHATMSGLS---VVKSY-------CGHGIGELFHCAPNIPHYARNkavgVMKAGQVFTIEPMInagvwrdrMWP 348
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1527686809 327 -GWGGV--------RIEDTVLITKNGPERLTK 349
Cdd:PLN03158  349 dGWTAVtadgkrsaQFEHTLLVTETGVEVLTA 380
PRK07281 PRK07281
methionyl aminopeptidase;
196-348 6.05e-09

methionyl aminopeptidase;


Pssm-ID: 180918  Cd Length: 286  Bit Score: 56.39  E-value: 6.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 196 KTSLLHGKPSDKI---IEKGDF----VLIDYGAMYNGYISDTTRTFIVGGASEKQLEIYNLVKEAQNVGVEnmKAGVHAT 268
Cdd:PRK07281   96 KVDMVLSEPLDKSivdVSKLNFdnveQMKKYTESYRGGLADSCWAYAVGTPSDEVKNLMDVTKEAMYRGIE--QAVVGNR 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 269 IPDaeIRKVVKKYEDYYYQGI-----GHGVGRDVHEEPFIGNYGDK----IIEEGCIITMEPGIYFPGW----------- 328
Cdd:PRK07281  174 IGD--IGAAIQEYAESRGYGVvrdlvGHGVGPTMHEEPMVPNYGTAgrglRLREGMVLTIEPMINTGTWeidtdmktgwa 251
                         170       180
                  ....*....|....*....|....*..
gi 1527686809 329 -----GGV--RIEDTVLITKNGPERLT 348
Cdd:PRK07281  252 hktldGGLscQYEHQFVITKDGPVILT 278
met_pdase_II TIGR00501
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ...
144-321 8.42e-09

methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. Bacterial and organellar examples (type I) differ from eukaroytic and archaeal (type II) examples in lacking a region of approximately 60 amino acids between the 4th and 5th cobalt-binding ligands. The role of this protein in general is to produce the mature amino end of cytosolic proteins by removing the N-terminal methionine. This model describes type II, among which the eukaryotic members typically have an N-terminal extension not present in archaeal members. It can act cotranslationally. The enzyme from rat has been shown to associate with translation initiation factor 2 (IF-2) and may have a role in translational regulation. [Protein fate, Protein modification and repair]


Pssm-ID: 129592  Cd Length: 295  Bit Score: 55.95  E-value: 8.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 144 KACEIADKALEELIPHIKAGVSEIELATRLEYFMKMNGAQNiGFETILISGAKTSLLHGKPSDK-IIEKGDFVLIDYGAM 222
Cdd:TIGR00501  10 EAGKIHSKVRREAADRIVPGVKLLEVAEFVENRIRELGAEP-AFPCNISINECAAHFTPKAGDKtVFKDGDVVKLDLGAH 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 223 YNGYISDTTRTFIVGGASEkqlEIYNLVKEAQNVGVENMKAGVHATipdaEIRKVVKK-YEDYYYQGI----GHGVGR-D 296
Cdd:TIGR00501  89 VDGYIADTAITVDLGDQYD---NLVKAAKDALYTAIKEIRAGVRVG----EIGKAIQEvIESYGVKPIsnltGHSMAPyR 161
                         170       180
                  ....*....|....*....|....*...
gi 1527686809 297 VHEEPFIGNYGDK---IIEEGCIITMEP 321
Cdd:TIGR00501 162 LHGGKSIPNVKERdttKLEEGDVVAIEP 189
COG5406 COG5406
Nucleosome binding factor SPN, SPT16 subunit [Transcription, Replication, recombination and ...
187-352 8.45e-05

Nucleosome binding factor SPN, SPT16 subunit [Transcription, Replication, recombination and repair, Chromatin structure and dynamics];


Pssm-ID: 227693 [Multi-domain]  Cd Length: 1001  Bit Score: 44.62  E-value: 8.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809  187 FETILISGAKTSLLHGKPSDKIIEKGDFVLIDYGAMYNGYISDTTRTFIVGGASEKQLEiYNLVKEAQNVGVENMKAGVH 266
Cdd:COG5406    245 YTPIIQSGGSIDLTPSAFSFPMELTGDVVLLSIGIRYNGYCSNMSRTILTDPDSEQQKN-YEFLYMLQKYILGLVRPGTD 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809  267 ATIPDAEIRKVVKK----YEDYYYQGIGHGVGRDVHEEPFIGNY-GDKIIEEGCIITMEPGI------YFPGWGGVRIED 335
Cdd:COG5406    324 SGIIYSEAEKYISSngpeLGPNFIYNVGLMIGIEFRSSQKPFNVkNGRVLQAGCIFNISLGFgnlinpHPKNNYALLLID 403
                          170
                   ....*....|....*..
gi 1527686809  336 TVLITKNGPERLTKFPK 352
Cdd:COG5406    404 TEQISLSNPIVFTDSPK 420
PA2G4-like cd01089
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ...
143-348 7.02e-04

Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family members have been implicated in cell cycle control.


Pssm-ID: 238522  Cd Length: 228  Bit Score: 40.39  E-value: 7.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 143 RKACEIADKALEELIPHIKAGVSEIELATR-----LEYFMKM-----NGAQNIGFETIlISGAKTsLLHGKP----SDKI 208
Cdd:cd01089     5 KTAGQIANKVLKQVISLCVPGAKVVDLCEKgdkliLEELGKVykkekKLEKGIAFPTC-ISVNNC-VCHFSPlksdATYT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 209 IEKGDFVLIDYGAMYNGYISDTTRTFIVGGASEKQLE--IYNLVKEAQNVgvenMKAGVHATIP---DAEIRKVV-KKYE 282
Cdd:cd01089    83 LKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAETPVTgkKADVIAAAHYA----LEAALRLLRPgnqNSDITEAIqKVIV 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1527686809 283 DYYYQGI----GHGVGRDVHEepfiGNYGDKIIE---EGCIITMEPGIYFPGWGGVRIEDTVLITKNGPERLT 348
Cdd:cd01089   159 DYGCTPVegvlSHQLKRVVSS----GEGKAKLVEcvkHGLLFPYPVLYEKEGEVVAQFKLTVLLTPNGVTVLT 227
CDC68-like cd01091
Related to aminopeptidase P and aminopeptidase M, a member of this domain family is present in ...
190-347 7.77e-04

Related to aminopeptidase P and aminopeptidase M, a member of this domain family is present in cell division control protein 68, a transcription factor.


Pssm-ID: 238524 [Multi-domain]  Cd Length: 243  Bit Score: 40.41  E-value: 7.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 190 ILISGAKTSLL-HGKPSDKIIEKGDFVLIDYGAMYNGYISDTTRTFIVgGASEKQLEIYNLVKEAQNVGVENMKAGvhAT 268
Cdd:cd01091    68 IIQSGGNYDLLkSSSSSDKLLYHFGVIICSLGARYKSYCSNIARTFLI-DPTSEQQKNYNFLLALQEEILKELKPG--AK 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 269 IPDA------EIRKVVKKYEDYYYQGIGHGVGRDVHEEPF-IGNYGDKIIEEGCIITMEPGI---------------Yfp 326
Cdd:cd01091   145 LSDVyqktldYIKKKKPELEPNFTKNLGFGIGLEFRESSLiINAKNDRKLKKGMVFNLSIGFsnlqnpepkdkesktY-- 222
                         170       180
                  ....*....|....*....|.
gi 1527686809 327 gwgGVRIEDTVLITKNGPERL 347
Cdd:cd01091   223 ---ALLLSDTILVTEDEPAIV 240
PTZ00053 PTZ00053
methionine aminopeptidase 2; Provisional
137-282 9.12e-04

methionine aminopeptidase 2; Provisional


Pssm-ID: 240246 [Multi-domain]  Cd Length: 470  Bit Score: 40.85  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 137 DEIKNTRKACEIADKALEELIPHIKAGVSEIELATRLE----YFMKMNGAQ-NIGFETILisgaktSLLH------GKPS 205
Cdd:PTZ00053  156 EQYQDLRRAAEVHRQVRRYAQSVIKPGVKLIDICERIEsksrELIEADGLKcGWAFPTGC------SLNHcaahytPNTG 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 206 DK-IIEKGDFVLIDYGAMYNGYISDTTRTFIVGGASEKQLEIynlVKEAQNVGVENmkAGVHATIPD--AEIRKVVKKYE 282
Cdd:PTZ00053  230 DKtVLTYDDVCKLDFGTHVNGRIIDCAFTVAFNPKYDPLLQA---TKDATNTGIKE--AGIDVRLSDigAAIQEVIESYE 304
crvDNA_42K TIGR00495
42K curved DNA binding protein; Proteins identified by this model have been identified in a ...
145-244 9.37e-04

42K curved DNA binding protein; Proteins identified by this model have been identified in a number of species as a nuclear (but not nucleolar) protein with a cell cycle dependence. Various names given to members of this family have included cell cycle protein p38-2G4, DNA-binding protein GBP16, and proliferation-associated protein 1. This protein is closely related to methionine aminopeptidase, a cobolt-binding protein. [Unknown function, General]


Pssm-ID: 273105  Cd Length: 390  Bit Score: 41.03  E-value: 9.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1527686809 145 ACEIADKALEELIPHIKAGVSEIELATRLEYFMKMNGA----------QNIGFETIlIS----GAKTSLLHGKPsDKIIE 210
Cdd:TIGR00495  26 AGEIANNVLKSVVEACSPGAKVVDICEKGDAFIMEETAkifkkekemeKGIAFPTC-ISvnncVGHFSPLKSDQ-DYILK 103
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1527686809 211 KGDFVLIDYGAMYNGYISDTTRTFIVGGASEKQL 244
Cdd:TIGR00495 104 EGDVVKIDLGCHIDGFIALVAHTFVVGVAQEEPV 137
 
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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