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Conserved domains on  [gi|1689781888|gb|TOY25122|]
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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 1.12e-116

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


:

Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 339.87  E-value: 1.12e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888   7 NAVLEQMKKDDISQMLVSDPTSIFYLTGVLIHPgERLLALYLNLNGnnklfinelfpvsedlgvEMVWFNDtqnpvEIIT 86
Cdd:COG0006     1 ARLRALMAEAGLDALLLTDPSNFAYLTGFRGSP-ERLAALLVTADG------------------EPVLFVD-----ELEA 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888  87 EHidknatmgvdknwparfllnlielgggsKFVNSSYIIDTLRMCKDEEEKELMRIASKLNDKAMEQLKATVSGELTEKQ 166
Cdd:COG0006    57 ER----------------------------ELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRPGVTERE 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 167 LVGKLSKIYEDLGTDGFSFDPIIGFGPNGANPHGEPGNALVKPGDAIILDIGCIKDNYCADMTRTVFYKEIPEKGREIFE 246
Cdd:COG0006   109 VAAELEAAMRRRGAEGPSFDTIVASGENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYE 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 247 IVLEANKRAEAIVKPGVRFCDIDAAARDYITEKGYGQYFTHRTGHSIGLEVHDKGDVSSINTDTVQPGMIFSIEPGIYLP 326
Cdd:COG0006   189 AVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAGYGEYFPHGTGHGVGLDVHEGPQISPGNDRPLEPGMVFTIEPGIYIP 268
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1689781888 327 GEFGVRIEDLVLVTEDGCEILNKHDKEICVV 357
Cdd:COG0006   269 GIGGVRIEDTVLVTEDGAEVLTRLPRELLEL 299
 
Name Accession Description Interval E-value
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
7-357 1.12e-116

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


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 339.87  E-value: 1.12e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888   7 NAVLEQMKKDDISQMLVSDPTSIFYLTGVLIHPgERLLALYLNLNGnnklfinelfpvsedlgvEMVWFNDtqnpvEIIT 86
Cdd:COG0006     1 ARLRALMAEAGLDALLLTDPSNFAYLTGFRGSP-ERLAALLVTADG------------------EPVLFVD-----ELEA 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888  87 EHidknatmgvdknwparfllnlielgggsKFVNSSYIIDTLRMCKDEEEKELMRIASKLNDKAMEQLKATVSGELTEKQ 166
Cdd:COG0006    57 ER----------------------------ELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRPGVTERE 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 167 LVGKLSKIYEDLGTDGFSFDPIIGFGPNGANPHGEPGNALVKPGDAIILDIGCIKDNYCADMTRTVFYKEIPEKGREIFE 246
Cdd:COG0006   109 VAAELEAAMRRRGAEGPSFDTIVASGENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYE 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 247 IVLEANKRAEAIVKPGVRFCDIDAAARDYITEKGYGQYFTHRTGHSIGLEVHDKGDVSSINTDTVQPGMIFSIEPGIYLP 326
Cdd:COG0006   189 AVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAGYGEYFPHGTGHGVGLDVHEGPQISPGNDRPLEPGMVFTIEPGIYIP 268
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1689781888 327 GEFGVRIEDLVLVTEDGCEILNKHDKEICVV 357
Cdd:COG0006   269 GIGGVRIEDTVLVTEDGAEVLTRLPRELLEL 299
APP-like cd01092
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
138-344 5.72e-106

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: 309.44  E-value: 5.72e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 138 ELMRIASKLNDKAMEQLKATVSGELTEKQLVGKLSKIYEDLGTDGFSFDPIIGFGPNGANPHGEPGNALVKPGDAIILDI 217
Cdd:cd01092     2 ELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKLGAEGPSFDTIVASGPNSALPHGVPSDRKIEEGDLVLIDF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 218 GCIKDNYCADMTRTVFYKEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDIDAAARDYITEKGYGQYFTHRTGHSIGLEV 297
Cdd:cd01092    82 GAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGYGEYFIHRTGHGVGLEV 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1689781888 298 HDKGDVSSINTDTVQPGMIFSIEPGIYLPGEFGVRIEDLVLVTEDGC 344
Cdd:cd01092   162 HEAPYISPGSDDVLEEGMVFTIEPGIYIPGKGGVRIEDDVLVTEDGC 208
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
138-341 4.66e-83

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: 251.01  E-value: 4.66e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 138 ELMRIASKLNDKAMEQLKATVSGELTEKQLVGKL-SKIYEDLGTDGFSFDPIIGFGPNGANPHGEPGNALVKPGDAIILD 216
Cdd:pfam00557   1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELeAARLRRGGARGPAFPPIVASGPNAAIPHYIPNDRVLKPGDLVLID 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 217 IGCI-KDNYCADMTRTVFYKEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDIDAAARDYITEKGYGQYFTHRTGHSIGL 295
Cdd:pfam00557  81 VGAEyDGGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGEYFPHGLGHGIGL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1689781888 296 EVHDKGDVSSINTDTV-QPGMIFSIEPGIY-LPGEFGVRIEDLVLVTE 341
Cdd:pfam00557 161 EVHEGPYISRGGDDRVlEPGMVFTIEPGIYfIPGWGGVRIEDTVLVTE 208
PRK09795 PRK09795
aminopeptidase; Provisional
116-358 2.95e-64

aminopeptidase; Provisional


Pssm-ID: 182080 [Multi-domain]  Cd Length: 361  Bit Score: 208.25  E-value: 2.95e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 116 SKFVNSSyiIDTLRMCKDEEEKELMRIASKLNDKAMEQLKATVSGELTEKQLVGKLSKIYEDLGTDGFSFDPIIGFGPNG 195
Cdd:PRK09795  114 AKLVSAT--PDVLRQIKTPEEVEKIRLACGIADRGAEHIRRFIQAGMSEREIAAELEWFMRQQGAEKASFDTIVASGWRG 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 196 ANPHGEPGNALVKPGDAIILDIGCIKDNYCADMTRTVFY--KEIPEKGREIF---EIVLEANKRAEAIVKPGVRFCDIDA 270
Cdd:PRK09795  192 ALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVngEGVSAESHPLFnvyQIVLQAQLAAISAIRPGVRCQQVDD 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 271 AARDYITEKGYGQYFTHRTGHSIGLEVHDKGDVSSINTDTVQPGMIFSIEPGIYLPGEFGVRIEDLVLVTEDGCEILNKH 350
Cdd:PRK09795  272 AARRVITEAGYGDYFGHNTGHAIGIEVHEDPRFSPRDTTTLQPGMLLTVEPGIYLPGQGGVRIEDVVLVTPQGAEVLYAM 351

                  ....*...
gi 1689781888 351 DKEICVVG 358
Cdd:PRK09795  352 PKTVLLTG 359
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
199-349 9.15e-21

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: 90.10  E-value: 9.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 199 HGEPGNALVKPGDAIILDIGCIKDNYCADMTRTVFYKEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDIDAAARDYITE 278
Cdd:TIGR00500  76 HGIPDKKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEA 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 279 KGYGQYFTHrTGHSIGLEVHDKGDV----SSINTDTVQPGMIFSIEPGIYLPGE-----------------FGVRIEDLV 337
Cdd:TIGR00500 156 KGFSVVREY-CGHGIGRKFHEEPQIpnygKKFTNVRLKEGMVFTIEPMVNTGTEeittaadgwtvktkdgsLSAQFEHTI 234
                         170
                  ....*....|..
gi 1689781888 338 LVTEDGCEILNK 349
Cdd:TIGR00500 235 VITDNGPEILTE 246
 
Name Accession Description Interval E-value
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
7-357 1.12e-116

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


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 339.87  E-value: 1.12e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888   7 NAVLEQMKKDDISQMLVSDPTSIFYLTGVLIHPgERLLALYLNLNGnnklfinelfpvsedlgvEMVWFNDtqnpvEIIT 86
Cdd:COG0006     1 ARLRALMAEAGLDALLLTDPSNFAYLTGFRGSP-ERLAALLVTADG------------------EPVLFVD-----ELEA 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888  87 EHidknatmgvdknwparfllnlielgggsKFVNSSYIIDTLRMCKDEEEKELMRIASKLNDKAMEQLKATVSGELTEKQ 166
Cdd:COG0006    57 ER----------------------------ELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRPGVTERE 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 167 LVGKLSKIYEDLGTDGFSFDPIIGFGPNGANPHGEPGNALVKPGDAIILDIGCIKDNYCADMTRTVFYKEIPEKGREIFE 246
Cdd:COG0006   109 VAAELEAAMRRRGAEGPSFDTIVASGENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYE 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 247 IVLEANKRAEAIVKPGVRFCDIDAAARDYITEKGYGQYFTHRTGHSIGLEVHDKGDVSSINTDTVQPGMIFSIEPGIYLP 326
Cdd:COG0006   189 AVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAGYGEYFPHGTGHGVGLDVHEGPQISPGNDRPLEPGMVFTIEPGIYIP 268
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1689781888 327 GEFGVRIEDLVLVTEDGCEILNKHDKEICVV 357
Cdd:COG0006   269 GIGGVRIEDTVLVTEDGAEVLTRLPRELLEL 299
APP-like cd01092
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
138-344 5.72e-106

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: 309.44  E-value: 5.72e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 138 ELMRIASKLNDKAMEQLKATVSGELTEKQLVGKLSKIYEDLGTDGFSFDPIIGFGPNGANPHGEPGNALVKPGDAIILDI 217
Cdd:cd01092     2 ELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKLGAEGPSFDTIVASGPNSALPHGVPSDRKIEEGDLVLIDF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 218 GCIKDNYCADMTRTVFYKEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDIDAAARDYITEKGYGQYFTHRTGHSIGLEV 297
Cdd:cd01092    82 GAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGYGEYFIHRTGHGVGLEV 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1689781888 298 HDKGDVSSINTDTVQPGMIFSIEPGIYLPGEFGVRIEDLVLVTEDGC 344
Cdd:cd01092   162 HEAPYISPGSDDVLEEGMVFTIEPGIYIPGKGGVRIEDDVLVTEDGC 208
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
138-341 4.66e-83

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: 251.01  E-value: 4.66e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 138 ELMRIASKLNDKAMEQLKATVSGELTEKQLVGKL-SKIYEDLGTDGFSFDPIIGFGPNGANPHGEPGNALVKPGDAIILD 216
Cdd:pfam00557   1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELeAARLRRGGARGPAFPPIVASGPNAAIPHYIPNDRVLKPGDLVLID 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 217 IGCI-KDNYCADMTRTVFYKEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDIDAAARDYITEKGYGQYFTHRTGHSIGL 295
Cdd:pfam00557  81 VGAEyDGGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGEYFPHGLGHGIGL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1689781888 296 EVHDKGDVSSINTDTV-QPGMIFSIEPGIY-LPGEFGVRIEDLVLVTE 341
Cdd:pfam00557 161 EVHEGPYISRGGDDRVlEPGMVFTIEPGIYfIPGWGGVRIEDTVLVTE 208
APP_MetAP cd01066
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
138-344 1.16e-64

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: 204.22  E-value: 1.16e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 138 ELMRIASKLNDKAMEQLKATVSGELTEKQLVGKLSKIYEDLGtDGFSFDPIIGFGPNGANPHGEPGNALVKPGDAIILDI 217
Cdd:cd01066     2 ARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAG-GYPAGPTIVGSGARTALPHYRPDDRRLQEGDLVLVDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 218 GCIKDNYCADMTRTVFYKEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDIDAAARDYITEKGYGQYFTHRTGHSIGLEV 297
Cdd:cd01066    81 GGVYDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLGPNFGHRTGHGIGLEI 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1689781888 298 HDKGDVSSINTDTVQPGMIFSIEPGIYLPGEFGVRIEDLVLVTEDGC 344
Cdd:cd01066   161 HEPPVLKAGDDTVLEPGMVFAVEPGLYLPGGGGVRIEDTVLVTEDGP 207
PRK09795 PRK09795
aminopeptidase; Provisional
116-358 2.95e-64

aminopeptidase; Provisional


Pssm-ID: 182080 [Multi-domain]  Cd Length: 361  Bit Score: 208.25  E-value: 2.95e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 116 SKFVNSSyiIDTLRMCKDEEEKELMRIASKLNDKAMEQLKATVSGELTEKQLVGKLSKIYEDLGTDGFSFDPIIGFGPNG 195
Cdd:PRK09795  114 AKLVSAT--PDVLRQIKTPEEVEKIRLACGIADRGAEHIRRFIQAGMSEREIAAELEWFMRQQGAEKASFDTIVASGWRG 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 196 ANPHGEPGNALVKPGDAIILDIGCIKDNYCADMTRTVFY--KEIPEKGREIF---EIVLEANKRAEAIVKPGVRFCDIDA 270
Cdd:PRK09795  192 ALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVngEGVSAESHPLFnvyQIVLQAQLAAISAIRPGVRCQQVDD 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 271 AARDYITEKGYGQYFTHRTGHSIGLEVHDKGDVSSINTDTVQPGMIFSIEPGIYLPGEFGVRIEDLVLVTEDGCEILNKH 350
Cdd:PRK09795  272 AARRVITEAGYGDYFGHNTGHAIGIEVHEDPRFSPRDTTTLQPGMLLTVEPGIYLPGQGGVRIEDVVLVTPQGAEVLYAM 351

                  ....*...
gi 1689781888 351 DKEICVVG 358
Cdd:PRK09795  352 PKTVLLTG 359
Prolidase cd01087
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ...
138-347 5.26e-45

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: 154.65  E-value: 5.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 138 ELMRIASKLNDKAMEQLKATVSGELTEKQLVGKLSKIYEDLGTDGfSFDPIIGFGPNGANPHGEPGNALVKPGDAIILDI 217
Cdd:cd01087     2 ELMRKACDISAEAHRAAMKASRPGMSEYELEAEFEYEFRSRGARL-AYSYIVAAGSNAAILHYVHNDQPLKDGDLVLIDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 218 GCIKDNYCADMTRTvfykeIPEKG------REIFEIVLEANKRAEAIVKPGVRFCDIDAAARDYITE--------KG--- 280
Cdd:cd01087    81 GAEYGGYASDITRT-----FPVNGkftdeqRELYEAVLAAQKAAIAACKPGVSYEDIHLLAHRVLAEglkelgilKGdvd 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 281 -------YGQYFTHRTGHSIGLEVHDKGDVSSIN--TDTVQPGMIFSIEPGIYLPGEF----------GVRIEDLVLVTE 341
Cdd:cd01087   156 eivesgaYAKFFPHGLGHYLGLDVHDVGGYLRYLrrARPLEPGMVITIEPGIYFIPDLldvpeyfrggGIRIEDDVLVTE 235

                  ....*.
gi 1689781888 342 DGCEIL 347
Cdd:cd01087   236 DGPENL 241
PRK10879 PRK10879
proline aminopeptidase P II; Provisional
128-347 3.89e-32

proline aminopeptidase P II; Provisional


Pssm-ID: 182804 [Multi-domain]  Cd Length: 438  Bit Score: 124.84  E-value: 3.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 128 LRMCKDEEEKELMR----IASKLNDKAMEQLKATvsgeLTEKQLVGKLSKIYEDLGTDGFSFDPIIGFGPNGANPHGEPG 203
Cdd:PRK10879  170 MRLFKSPEEIAVLRrageISALAHTRAMEKCRPG----MFEYQLEGEIHHEFNRHGARYPSYNTIVGSGENGCILHYTEN 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 204 NALVKPGDAIILDIGCIKDNYCADMTRT--VFYKEIPEKgREIFEIVLEANKRAEAIVKPGVRFCDIDAAA--------- 272
Cdd:PRK10879  246 ESEMRDGDLVLIDAGCEYKGYAGDITRTfpVNGKFTPAQ-REIYDIVLESLETSLRLYRPGTSIREVTGEVvrimvsglv 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 273 ---------RDYITEKGYGQYFTHRTGHSIGLEVHDKGDVSSINTDTVQPGMIFSIEPGIYL------PGEF---GVRIE 334
Cdd:PRK10879  325 klgilkgdvDQLIAENAHRPFFMHGLSHWLGLDVHDVGVYGQDRSRILEPGMVLTVEPGLYIapdadvPEQYrgiGIRIE 404
                         250
                  ....*....|...
gi 1689781888 335 DLVLVTEDGCEIL 347
Cdd:PRK10879  405 DDIVITETGNENL 417
APP cd01085
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ...
158-343 4.25e-30

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: 114.58  E-value: 4.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 158 VSGELTEKQLVGKL------SKIYEDLgtdgfSFDPIIGFGPNGANPHGEP---GNALVKPGDAIILDIGcikDNYC--- 225
Cdd:cd01085    26 KGETITELSAADKLeefrrqQKGYVGL-----SFDTISGFGPNGAIVHYSPteeSNRKISPDGLYLIDSG---GQYLdgt 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 226 ADMTRTVFYKEIPEKGREIFEIVLEANKR-AEAIVKPGVRFCDIDAAARDYITEKG--YGqyftHRTGHSIG--LEVHD- 299
Cdd:cd01085    98 TDITRTVHLGEPTAEQKRDYTLVLKGHIAlARAKFPKGTTGSQLDALARQPLWKAGldYG----HGTGHGVGsfLNVHEg 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1689781888 300 -KGDVSSINTDTVQPGMIFSIEPGIYLPGEFGVRIEDLVLVTEDG 343
Cdd:cd01085   174 pQSISPAPNNVPLKAGMILSNEPGYYKEGKYGIRIENLVLVVEAE 218
MetAP1 cd01086
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
199-347 1.37e-22

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: 94.87  E-value: 1.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 199 HGEPGNALVKPGDAIILDIGCIKDNYCADMTRTVFYKEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDIDAAARDYITE 278
Cdd:cd01086    68 HGIPDDRVLKDGDIVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEK 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 279 KGYG---QYfthrTGHSIGLEVHDKGDV---SSINTDTV-QPGMIFSIEPGIYL-----------------PGEFGVRIE 334
Cdd:cd01086   148 NGYSvvrEF----GGHGIGRKFHEEPQIpnyGRPGTGPKlKPGMVFTIEPMINLgtyevvtlpdgwtvvtkDGSLSAQFE 223
                         170
                  ....*....|...
gi 1689781888 335 DLVLVTEDGCEIL 347
Cdd:cd01086   224 HTVLITEDGPEIL 236
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
132-353 1.52e-22

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 94.69  E-value: 1.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 132 KDEEEKELMRIASKLNDKAMEQLKATVSGELTEKQLvgklSKIYED-----------LGTDGFSF-------DPIIgfgp 193
Cdd:COG0024     4 KTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLEL----DRIAEEfirdhgaipafLGYYGFPKsictsvnEVVV---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 194 nganpHGEPGNALVKPGDAIILDIGCIKDNYCADMTRTVFYKEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDIDAAAR 273
Cdd:COG0024    76 -----HGIPSDRVLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 274 DYITEKGYG---QYfthrTGHSIGLEVHDKGDVSsiNTDT------VQPGMIFSIEPGIYLpGEFGVRIED--------- 335
Cdd:COG0024   151 SYAESNGYSvvrEF----VGHGIGREMHEEPQVP--NYGRpgrgprLKPGMVLAIEPMINA-GTPEVKVLDdgwtvvtkd 223
                         250       260
                  ....*....|....*....|....*..
gi 1689781888 336 ---------LVLVTEDGCEILNKHDKE 353
Cdd:COG0024   224 gslsaqfehTVAVTEDGPEILTLPDGG 250
Creatinase_N pfam01321
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ...
5-131 4.89e-22

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: 90.06  E-value: 4.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888   5 RLNAVLEQMKKDDISQMLVSDPTSIFYLTGVlihPGERLLALYLNLNGnNKLFINELFPVS----EDLGVEMVWFNDTQN 80
Cdd:pfam01321   1 RLEKLRKLMEEKGLDAALVTSPENLRYLTGF---TGSRGLLLLVTADG-ALLLVDALEYERaaaeSAPDFDVVPYRDYEA 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1689781888  81 PVEIITEHIDKNATMGVDKNW-PARFLLNLIELGGGSKFVNSSYIIDTLRMC 131
Cdd:pfam01321  77 LADLLKELGAGGKRVGFEADAlTVAFYEALKEALPGAELVDVSGLIERLRMV 128
PRK05716 PRK05716
methionine aminopeptidase; Validated
131-353 2.86e-21

methionine aminopeptidase; Validated


Pssm-ID: 235576 [Multi-domain]  Cd Length: 252  Bit Score: 91.35  E-value: 2.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 131 CKDEEEKELMRIASKLNDKAMEQLKATVSGELTEKQLvgklSKIYEDLGTDgfsfdpiigfgpNGANP------------ 198
Cdd:PRK05716    5 IKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKEL----DRIAEEYIRD------------QGAIPaplgyhgfpksi 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 199 ---------HGEPGNALVKPGDAIILDIGCIKDNYCADMTRTVFYKEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDID 269
Cdd:PRK05716   69 ctsvnevvcHGIPSDKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 270 AAARDYITEKGYG---QYfthrTGHSIGLEVHDKGDV---SSINTDTV-QPGMIFSIEPGIYLpGEFGVRI--------- 333
Cdd:PRK05716  149 HAIQKYAEAEGFSvvrEY----CGHGIGRKFHEEPQIphyGAPGDGPVlKEGMVFTIEPMINA-GKREVKTlkdgwtvvt 223
                         250       260
                  ....*....|....*....|....*....
gi 1689781888 334 ---------EDLVLVTEDGCEILNKHDKE 353
Cdd:PRK05716  224 kdgslsaqyEHTVAVTEDGPEILTLRPEE 252
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
199-349 9.15e-21

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: 90.10  E-value: 9.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 199 HGEPGNALVKPGDAIILDIGCIKDNYCADMTRTVFYKEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDIDAAARDYITE 278
Cdd:TIGR00500  76 HGIPDKKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEA 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 279 KGYGQYFTHrTGHSIGLEVHDKGDV----SSINTDTVQPGMIFSIEPGIYLPGE-----------------FGVRIEDLV 337
Cdd:TIGR00500 156 KGFSVVREY-CGHGIGRKFHEEPQIpnygKKFTNVRLKEGMVFTIEPMVNTGTEeittaadgwtvktkdgsLSAQFEHTI 234
                         170
                  ....*....|..
gi 1689781888 338 LVTEDGCEILNK 349
Cdd:TIGR00500 235 VITDNGPEILTE 246
PRK12318 PRK12318
methionyl aminopeptidase;
132-352 1.63e-20

methionyl aminopeptidase;


Pssm-ID: 183434 [Multi-domain]  Cd Length: 291  Bit Score: 90.26  E-value: 1.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 132 KDEEEKELMRIASKLNDKAMEQL-KATVSGELTEK--QLVGKLSKIYE----DLGTDGFSFDPIIGFGPNGANPHGEPGN 204
Cdd:PRK12318   44 KTPEQIEKIRKACQVTARILDALcEAAKEGVTTNEldELSRELHKEYNaipaPLNYGSPPFPKTICTSLNEVICHGIPND 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 205 ALVKPGDAIILDIGCIKDNYCADMTRTVFYKEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDIDAAARDYITEKGYG-- 282
Cdd:PRK12318  124 IPLKNGDIMNIDVSCIVDGYYGDCSRMVMIGEVSEIKKKVCQASLECLNAAIAILKPGIPLYEIGEVIENCADKYGFSvv 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 283 -QYfthrTGHSIGLEVHDKGDVS---SINTDTVQPGMIFSIEPGIYLPGEFGV------------------RIEDLVLVT 340
Cdd:PRK12318  204 dQF----VGHGVGIKFHENPYVPhhrNSSKIPLAPGMIFTIEPMINVGKKEGVidpinhweartcdnqpsaQWEHTILIT 279
                         250
                  ....*....|..
gi 1689781888 341 EDGCEILNKHDK 352
Cdd:PRK12318  280 ETGYEILTLLDK 291
PRK14576 PRK14576
putative endopeptidase; Provisional
109-354 4.83e-20

putative endopeptidase; Provisional


Pssm-ID: 173040 [Multi-domain]  Cd Length: 405  Bit Score: 90.46  E-value: 4.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 109 LIELGGGSKFVNSSYIIDTLRMCKDEEEKELMRIASKLNDKAMEQLKATVSGELTEKQLVGKLSKIYEDLGTDGFSFDPI 188
Cdd:PRK14576  155 LDKVAPGLKLVDSTALFNEIRMIKSPWEIEHLRKSAEITEYGIASAAKKIRVGCTAAELTAAFKAAVMSFPETNFSRFNL 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 189 IGFGPNgANPHGEPGNALVKPGDAIILDIGCIKDNYCADMTRTVFYKEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDI 268
Cdd:PRK14576  235 ISVGDN-FSPKIIADTTPAKVGDLIKFDCGIDVAGYGADLARTFVLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAV 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 269 DAAARDYITEKGYGQYFTHRTGHSIG--LEVHDKGDVSSINTDTVQPGMIFSIEPGIYLPGEFGVRIEDLVLVTEDGCEI 346
Cdd:PRK14576  314 FDSTMAVIKTSGLPHYNRGHLGHGDGvfLGLEEVPFVSTQATETFCPGMVLSLETPYYGIGVGSIMLEDMILITDSGFEF 393

                  ....*...
gi 1689781888 347 LNKHDKEI 354
Cdd:PRK14576  394 LSKLDRDL 401
PRK15173 PRK15173
peptidase; Provisional
118-354 1.94e-19

peptidase; Provisional


Pssm-ID: 185095 [Multi-domain]  Cd Length: 323  Bit Score: 87.85  E-value: 1.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 118 FVNSSYIIDTLRMCKDEEEKELMRIASKLNDKAMEQLKATVSGELTEKQLVGKLSKIYEDLGTDGFSFDPIIGFGPNgAN 197
Cdd:PRK15173   82 FVDSSSIFNELRVIKSPWEIKRLRKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSKSETHFSRFHLISVGAD-FS 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 198 PHGEPGNALVKPGDAIILDIGCIKDNYCADMTRTVFYKEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDIDAAARDYIT 277
Cdd:PRK15173  161 PKLIPSNTKACSGDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIK 240
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1689781888 278 EKGYGQYFTHRTGHSIG--LEVHDKGDVSSINTDTVQPGMIFSIEPGIYLPGEFGVRIEDLVLVTEDGCEILNKHDKEI 354
Cdd:PRK15173  241 KSGLPNYNRGHLGHGNGvfLGLEESPFVSTHATESFTSGMVLSLETPYYGYNLGSIMIEDMILINKEGIEFLSKLPRDL 319
PRK14575 PRK14575
putative peptidase; Provisional
2-354 2.22e-19

putative peptidase; Provisional


Pssm-ID: 173039 [Multi-domain]  Cd Length: 406  Bit Score: 88.61  E-value: 2.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888   2 KAQRLNAVLEQ----MKKDDISQMLVSDPTSIFYLTGVLI-------HPGERLLALYLNLNGNNKLFINELFPVS----- 65
Cdd:PRK14575    5 KKEHLNTVSRKlrtiMERDNIDAVIVTTCDNFYHVTGILSffmytfrNTGTAIAVVFRDVKIPSLIIMNEFEAASltldm 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888  66 --EDLGVEMVWFnDTQNPVEI-----------ITEHIDKNATMGVDKNWPARFL-------LNLIELGG---------GS 116
Cdd:PRK14575   85 pnAELKTFPVWV-DVDDPFNMrdsannnkerpIGPPIESVCNILKDALNDARVLnkkiaidLNIMSNGGkrvidavmpNV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 117 KFVNSSYIIDTLRMCKDEEEKELMRIASKLNDKAMEQLKATVSGELTEKQLVGKLSKIYEDLGTDGFSFDPIIGFGPNgA 196
Cdd:PRK14575  164 DFVDSSSIFNELRVIKSPWEIKRLRKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSKSETHFSRFHLISVGAD-F 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 197 NPHGEPGNALVKPGDAIILDIGCIKDNYCADMTRTVFYKEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDIDAAARDYI 276
Cdd:PRK14575  243 SPKLIPSNTKACSGDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVI 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 277 TEKGYGQYFTHRTGHSIG--LEVHDKGDVSSINTDTVQPGMIFSIEPGIYLPGEFGVRIEDLVLVTEDGCEILNKHDKEI 354
Cdd:PRK14575  323 KKSGLPNYNRGHLGHGNGvfLGLEESPFVSTHATESFTSGMVLSLETPYYGYNLGSIMIEDMILINKEGIEFLSKLPRDL 402
PRK12896 PRK12896
methionine aminopeptidase; Reviewed
132-347 5.45e-18

methionine aminopeptidase; Reviewed


Pssm-ID: 237252 [Multi-domain]  Cd Length: 255  Bit Score: 82.19  E-value: 5.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 132 KDEEEKELMRIASKLNDKAMEQLKATVSGELTEKQLVGKLSKIYED-------LGTDGF------SFDPIIGfgpnganp 198
Cdd:PRK12896   11 KSPRELEKMRKIGRIVATALKEMGKAVEPGMTTKELDRIAEKRLEEhgaipspEGYYGFpgstciSVNEEVA-------- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 199 HGEPGNALVKPGDAIILDIGCIKDNYCADMTRTVFYKEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDIDAAARDYITE 278
Cdd:PRK12896   83 HGIPGPRVIKDGDLVNIDVSAYLDGYHGDTGITFAVGPVSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAIEDFAKK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 279 KGYgQYFTHRTGHSIGLEVHDkgDVSSINT-------DTVQPGMIFSIEPGIYL-----------------PGEFGVRIE 334
Cdd:PRK12896  163 NGY-SVVRDLTGHGVGRSLHE--EPSVILTytdplpnRLLRPGMTLAVEPFLNLgakdaetlddgwtvvtpDKSLSAQFE 239
                         250
                  ....*....|...
gi 1689781888 335 DLVLVTEDGCEIL 347
Cdd:PRK12896  240 HTVVVTRDGPEIL 252
Creatinase cd01090
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea.
192-345 3.44e-16

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


Pssm-ID: 238523 [Multi-domain]  Cd Length: 228  Bit Score: 76.81  E-value: 3.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 192 GPNGANPHGEPGNALVKPGDaiILDIGC---IKDNYCAdMTRTVFYKEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDI 268
Cdd:cd01090    62 GINTDGAHNPVTNRKVQRGD--ILSLNCfpmIAGYYTA-LERTLFLDEVSDAHLKIWEANVAVHERGLELIKPGARCKDI 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 269 DAAARDYITEKGYGQYFTHRTGHSIGLEVHDKGDVSSI----NTDTV-QPGMIFSIEPGIYL----PGEFGVRIEDLVLV 339
Cdd:cd01090   139 AAELNEMYREHDLLRYRTFGYGHSFGVLSHYYGREAGLelreDIDTVlEPGMVVSMEPMIMLpegqPGAGGYREHDILVI 218

                  ....*.
gi 1689781888 340 TEDGCE 345
Cdd:cd01090   219 NENGAE 224
PRK13607 PRK13607
proline dipeptidase; Provisional
224-345 2.17e-12

proline dipeptidase; Provisional


Pssm-ID: 237444 [Multi-domain]  Cd Length: 443  Bit Score: 67.61  E-value: 2.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 224 YCADMTRTVFYKEipekgREIFEIVLEANKRAE----AIVKPGVRFCDIDAAA--------RDY----------ITEKGY 281
Cdd:PRK13607  254 YAADITRTYAAKE-----DNDFAALIKDVNKEQlaliATMKPGVSYVDLHIQMhqriakllRKFqivtglseeaMVEQGI 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 282 GQ-YFTHRTGHSIGLEVHD--------KGDVSSI--------NTDTVQPGMIFSIEPGIY---------LPGEF------ 329
Cdd:PRK13607  329 TSpFFPHGLGHPLGLQVHDvagfmqddRGTHLAApekhpylrCTRVLEPGMVLTIEPGLYfidsllaplREGPFskhfnw 408
                         170       180
                  ....*....|....*....|....*.
gi 1689781888 330 ----------GVRIEDLVLVTEDGCE 345
Cdd:PRK13607  409 qkidalkpfgGIRIEDNVVVHENGVE 434
CDC68-like cd01091
Related to aminopeptidase P and aminopeptidase M, a member of this domain family is present in ...
121-347 4.09e-11

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: 62.36  E-value: 4.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 121 SSYIIDTLRMCKDEEEKELmriASKLNDKAMEQLKatvsgelTEKQLVGKLSKIYEDLgtdgfSFDPIIGFGPNGANPhg 200
Cdd:cd01091    16 KKFFVDEVEEIIDQEKKVT---HSKLSDKVEKAIE-------DKKKYKAKLDPEQLDW-----CYPPIIQSGGNYDLL-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 201 epGNALVKpgDAIILDIGCI-------KDNYCADMTRTVFYKEIPEKgREIFEIVLEANKRAEAIVKPGVRFCDIDAAAR 273
Cdd:cd01091    79 --KSSSSS--DKLLYHFGVIicslgarYKSYCSNIARTFLIDPTSEQ-QKNYNFLLALQEEILKELKPGAKLSDVYQKTL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 274 DYITEKG--YGQYFTHRTGHSIGLEVHDKG-DVSSINTDTVQPGMIFSIEPGIY-LPGE---------FGVRIEDLVLVT 340
Cdd:cd01091   154 DYIKKKKpeLEPNFTKNLGFGIGLEFRESSlIINAKNDRKLKKGMVFNLSIGFSnLQNPepkdkesktYALLLSDTILVT 233

                  ....*..
gi 1689781888 341 EDGCEIL 347
Cdd:cd01091   234 EDEPAIV 240
COG5406 COG5406
Nucleosome binding factor SPN, SPT16 subunit [Transcription, Replication, recombination and ...
92-322 1.92e-10

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: 62.34  E-value: 1.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888   92 NATMGVDKNWPARFLLNLIELGGGSKFVNS--SYIIDTLRMCKDEEEKelmRIASKLNDKaMEQLKATVSGElteKQLVG 169
Cdd:COG5406    159 DVSLGLSKMFLTKDAEEIANCRASSAASSVlmRYFVKEMEMLWDGAFK---ITHGKLSDL-MESLIDDVEFF---QTKSL 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888  170 KLSKIYEDLGTdgFSFDPIIGFGPNGANPHGEPGNALVKPGDAIILDIGCIKDNYCADMTRTVFYKEIPEKGREiFEIVL 249
Cdd:COG5406    232 KLGDIDLDQLE--WCYTPIIQSGGSIDLTPSAFSFPMELTGDVVLLSIGIRYNGYCSNMSRTILTDPDSEQQKN-YEFLY 308
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1689781888  250 EANKRAEAIVKPGVRFCDIDAAARDYITEKG--YGQYFTHRTGHSIGLEVHDKGDVSSINTDTV-QPGMIFSIEPG 322
Cdd:COG5406    309 MLQKYILGLVRPGTDSGIIYSEAEKYISSNGpeLGPNFIYNVGLMIGIEFRSSQKPFNVKNGRVlQAGCIFNISLG 384
PLN03158 PLN03158
methionine aminopeptidase; Provisional
199-349 9.67e-10

methionine aminopeptidase; Provisional


Pssm-ID: 215607 [Multi-domain]  Cd Length: 396  Bit Score: 59.47  E-value: 9.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 199 HGEPGNALVKPGDAIILDIGCIKDNYCADMTRTVFYKEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDIDAAARDYITE 278
Cdd:PLN03158  210 HGIPDARKLEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEASRQLVKCTYECLEKAIAIVKPGVRYREVGEVINRHATM 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 279 KGYgQYFTHRTGHSIGLEVHDKGDVSSINTD----TVQPGMIFSIEPGI--------YLP---------GEFGVRIEDLV 337
Cdd:PLN03158  290 SGL-SVVKSYCGHGIGELFHCAPNIPHYARNkavgVMKAGQVFTIEPMInagvwrdrMWPdgwtavtadGKRSAQFEHTL 368
                         170
                  ....*....|..
gi 1689781888 338 LVTEDGCEILNK 349
Cdd:PLN03158  369 LVTETGVEVLTA 380
MetAP2 cd01088
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
207-321 2.23e-05

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: 45.70  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 207 VKPGDAIILDIGCIKDNYCADMTRTVfykEIPEKGREIFEIVLEANKRAEAIVKPGVRFCDIDAAARDYITEKGYgQYFT 286
Cdd:cd01088    71 LKEGDVVKLDFGAHVDGYIADSAFTV---DFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIESYGF-KPIR 146
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1689781888 287 HRTGHSIG-LEVHDkG----DVSSINTDTVQPGMIFSIEP 321
Cdd:cd01088   147 NLTGHSIErYRLHA-GksipNVKGGEGTRLEEGDVYAIEP 185
PRK12897 PRK12897
type I methionyl aminopeptidase;
132-349 1.86e-04

type I methionyl aminopeptidase;


Pssm-ID: 171806  Cd Length: 248  Bit Score: 42.33  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 132 KDEEEKELMRIASKLNDKAMEQLKATVSGELTEKQL-------VGKLSKIYEDLGTDGFSFdpIIGFGPNGANPHGEPGN 204
Cdd:PRK12897    5 KTKNEIDLMHESGKLLASCHREIAKIMKPGITTKEIntfveayLEKHGATSEQKGYNGYPY--AICASVNDEMCHAFPAD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 205 ALVKPGDAIILDIGCIKDNYCADMTRTVFYKEIPEKGREIFEIVLEANKRA--EAIVkpGVRFCDIDAAARDYITEKGYg 282
Cdd:PRK12897   83 VPLTEGDIVTIDMVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGidQAVI--GNRVGDIGYAIESYVANEGF- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689781888 283 QYFTHRTGHSIGLEVHDKGDVSSINTD----TVQPGMIFSIEPGI-----------------YLPGEFGVRIEDLVLVTE 341
Cdd:PRK12897  160 SVARDFTGHGIGKEIHEEPAIFHFGKQgqgpELQEGMVITIEPIVnvgmryskvdlngwtarTMDGKLSAQYEHTIAITK 239

                  ....*...
gi 1689781888 342 DGCEILNK 349
Cdd:PRK12897  240 DGPIILTK 247
 
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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