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Conserved domains on  [gi|515103|pdb|1CHM|B]
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Chain B, CREATINE AMIDINOHYDROLASE

Protein Classification

M24 family metallopeptidase( domain architecture ID 10473665)

M24 family metallopeptidase such as creatinase (also called creatine amidinohydrolase) that hydrolyzes creatine to sarcosine and urea

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Creatinase cd01090
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea.
 163-390 4.48e-172

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


:

Pssm-ID: 238523 [Multi-domain]  Cd Length: 228  Bit Score: 479.34  E-value: 4.48e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      163 HVMIRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAIADTFEDVELMDTWTWFQSGINTDGAHNPVTTRKVNKG 242
Cdd:cd01090   1 IALIRHGARIADIGGAAVVEAIREGVPEYEVALAGTQAMVREIAKTFPEVELMDTWTWFQSGINTDGAHNPVTNRKVQRG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      243 DILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYG 322
Cdd:cd01090  81 DILSLNCFPMIAGYYTALERTLFLDEVSDAHLKIWEANVAVHERGLELIKPGARCKDIAAELNEMYREHDLLRYRTFGYG 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1CHM_B      323 HSFGTLSHYYGREAGLELREDIDTVLEPGMVVSMEPMIMLPEGLPGAGGYREHDILIVNENGAENITK 390
Cdd:cd01090 161 HSFGVLSHYYGREAGLELREDIDTVLEPGMVVSMEPMIMLPEGQPGAGGYREHDILVINENGAENITG 228
Creatinase_N pfam01321
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ...
 26-157 9.32e-19

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: 81.58  E-value: 9.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B         26 RQARLRAHLAAENIDAAIFTSYHNINYYSDFlycSFGRPYALVVTEDDVISIsanIDGGQPWR--RTVGTDN--IVYTDW 101
Cdd:pfam01321   1 RLEKLRKLMEEKGLDAALVTSPENLRYLTGF---TGSRGLLLLVTADGALLL---VDALEYERaaAESAPDFdvVPYRDY 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
1CHM_B        102 QrdNYFAAIQQALPKARRIGIEHDHLNLQNRDKLAARYPDAELVDVAAACMRMRMI 157
Cdd:pfam01321  75 E--ALADLLKELGAGGKRVGFEADALTVAFYEALKEALPGAELVDVSGLIERLRMV 128
 
Name Accession Description Interval E-value
Creatinase cd01090
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea.
 163-390 4.48e-172

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


Pssm-ID: 238523 [Multi-domain]  Cd Length: 228  Bit Score: 479.34  E-value: 4.48e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      163 HVMIRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAIADTFEDVELMDTWTWFQSGINTDGAHNPVTTRKVNKG 242
Cdd:cd01090   1 IALIRHGARIADIGGAAVVEAIREGVPEYEVALAGTQAMVREIAKTFPEVELMDTWTWFQSGINTDGAHNPVTNRKVQRG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      243 DILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYG 322
Cdd:cd01090  81 DILSLNCFPMIAGYYTALERTLFLDEVSDAHLKIWEANVAVHERGLELIKPGARCKDIAAELNEMYREHDLLRYRTFGYG 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1CHM_B      323 HSFGTLSHYYGREAGLELREDIDTVLEPGMVVSMEPMIMLPEGLPGAGGYREHDILIVNENGAENITK 390
Cdd:cd01090 161 HSFGVLSHYYGREAGLELREDIDTVLEPGMVVSMEPMIMLPEGQPGAGGYREHDILVINENGAENITG 228
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
28-392 1.86e-67

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


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 215.84  E-value: 1.86e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       28 ARLRAHLAAENIDAAIFTSYHNINYYSDFlYCSFGRPYALVVTEDDvisisanidggqpwrrtvgtDNIVYTDWqrdnyf 107
Cdd:COG0006   1 ARLRALMAEAGLDALLLTDPSNFAYLTGF-RGSPERLAALLVTADG--------------------EPVLFVDE------ 53

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      108 aaiqqalpkarrigiehdhlnlqnrdklaaRYPDAELVDVAAACMRMRMIKSAEEHVMIRHGARIADIGGAAVVEALGDQ 187
Cdd:COG0006  54 ------------------------------LEAERELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRPG 103

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      188 VPEYEVALHATQAMVRAIADT--FEdvelmdtwTWFQSGINTDGAHNPVTTRKVNKGDILSLNCFPMIAGYYTALERTLF 265
Cdd:COG0006 104 VTEREVAAELEAAMRRRGAEGpsFD--------TIVASGENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVA 175

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      266 LDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGHSFGTLSHYYGReagleLREDID 345
Cdd:COG0006 176 VGEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAGYGEYFPHGTGHGVGLDVHEGPQ-----ISPGND 250

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
1CHM_B      346 TVLEPGMVVSMEPMIMlpegLPGAGGYREHDILIVNENGAENITKFP 392
Cdd:COG0006 251 RPLEPGMVFTIEPGIY----IPGIGGVRIEDTVLVTEDGAEVLTRLP 293
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 165-379 8.57e-34

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: 125.05  E-value: 8.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B        165 MIRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAiadtfEDVELMDTWTWFQSGINTDGAHNPVTTRKVNKGDI 244
Cdd:pfam00557   2 LMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRR-----GGARGPAFPPIVASGPNAAIPHYIPNDRVLKPGDL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B        245 LSLNCFPMIAGYYTA-LERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGH 323
Cdd:pfam00557  77 VLIDVGAEYDGGYCSdITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGEYFPHGLGH 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
1CHM_B        324 SFGTLSHyygrEAGLELREDIDTVLEPGMVVSMEPMIMLPeglPGAGGYR-EHDILI 379
Cdd:pfam00557 157 GIGLEVH----EGPYISRGGDDRVLEPGMVFTIEPGIYFI---PGWGGVRiEDTVLV 206
Creatinase_N pfam01321
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ...
 26-157 9.32e-19

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: 81.58  E-value: 9.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B         26 RQARLRAHLAAENIDAAIFTSYHNINYYSDFlycSFGRPYALVVTEDDVISIsanIDGGQPWR--RTVGTDN--IVYTDW 101
Cdd:pfam01321   1 RLEKLRKLMEEKGLDAALVTSPENLRYLTGF---TGSRGLLLLVTADGALLL---VDALEYERaaAESAPDFdvVPYRDY 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
1CHM_B        102 QrdNYFAAIQQALPKARRIGIEHDHLNLQNRDKLAARYPDAELVDVAAACMRMRMI 157
Cdd:pfam01321  75 E--ALADLLKELGAGGKRVGFEADALTVAFYEALKEALPGAELVDVSGLIERLRMV 128
PRK09795 PRK09795
aminopeptidase; Provisional
 147-392 1.23e-17

aminopeptidase; Provisional


Pssm-ID: 182080 [Multi-domain]  Cd Length: 361  Bit Score: 83.45  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       147 VAAACMRMRMIKSAEEHVMIRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAIAD--TFEdvelmdtwTWFQSG 224
Cdd:PRK09795 117 VSATPDVLRQIKTPEEVEKIRLACGIADRGAEHIRRFIQAGMSEREIAAELEWFMRQQGAEkaSFD--------TIVASG 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       225 INTDGAHNPVTTRKVNKGDILSLNCFPMIAGYYTALERTLFL---DHCSDDH--LRLWQVNVEVHEAGLKLIKPGARCSD 299
Cdd:PRK09795 189 WRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVngeGVSAESHplFNVYQIVLQAQLAAISAIRPGVRCQQ 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       300 I---ARELNEiflkhdvlqyrTFGYGHSFGtlsHYYGREAGLELREDI------DTVLEPGMVVSMEPMIMlpegLPGAG 370
Cdd:PRK09795 269 VddaARRVIT-----------EAGYGDYFG---HNTGHAIGIEVHEDPrfsprdTTTLQPGMLLTVEPGIY----LPGQG 330

                        250       260
                 ....*....|....*....|..
1CHM_B       371 GYREHDILIVNENGAENITKFP 392
Cdd:PRK09795 331 GVRIEDVVLVTPQGAEVLYAMP 352
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
 225-390 1.05e-09

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: 58.51  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B        225 INTDGAHNPVTTRKVNKGDILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIAREL 304
Cdd:TIGR00500  70 VNEVVIHGIPDKKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAI 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B        305 NEIFLKHDVLQYRTFGyGHSFG-------TLSHYYGREAGLelredidtVLEPGMVVSMEPMIML--------------- 362
Cdd:TIGR00500 150 QKYAEAKGFSVVREYC-GHGIGrkfheepQIPNYGKKFTNV--------RLKEGMVFTIEPMVNTgteeittaadgwtvk 220

                         170       180
                  ....*....|....*....|....*....
1CHM_B        363 -PEGLPGAggYREHDILIVnENGAENITK 390
Cdd:TIGR00500 221 tKDGSLSA--QFEHTIVIT-DNGPEILTE 246
 
Name Accession Description Interval E-value
Creatinase cd01090
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea.
 163-390 4.48e-172

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


Pssm-ID: 238523 [Multi-domain]  Cd Length: 228  Bit Score: 479.34  E-value: 4.48e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      163 HVMIRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAIADTFEDVELMDTWTWFQSGINTDGAHNPVTTRKVNKG 242
Cdd:cd01090   1 IALIRHGARIADIGGAAVVEAIREGVPEYEVALAGTQAMVREIAKTFPEVELMDTWTWFQSGINTDGAHNPVTNRKVQRG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      243 DILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYG 322
Cdd:cd01090  81 DILSLNCFPMIAGYYTALERTLFLDEVSDAHLKIWEANVAVHERGLELIKPGARCKDIAAELNEMYREHDLLRYRTFGYG 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1CHM_B      323 HSFGTLSHYYGREAGLELREDIDTVLEPGMVVSMEPMIMLPEGLPGAGGYREHDILIVNENGAENITK 390
Cdd:cd01090 161 HSFGVLSHYYGREAGLELREDIDTVLEPGMVVSMEPMIMLPEGQPGAGGYREHDILVINENGAENITG 228
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
28-392 1.86e-67

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


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 215.84  E-value: 1.86e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       28 ARLRAHLAAENIDAAIFTSYHNINYYSDFlYCSFGRPYALVVTEDDvisisanidggqpwrrtvgtDNIVYTDWqrdnyf 107
Cdd:COG0006   1 ARLRALMAEAGLDALLLTDPSNFAYLTGF-RGSPERLAALLVTADG--------------------EPVLFVDE------ 53

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      108 aaiqqalpkarrigiehdhlnlqnrdklaaRYPDAELVDVAAACMRMRMIKSAEEHVMIRHGARIADIGGAAVVEALGDQ 187
Cdd:COG0006  54 ------------------------------LEAERELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRPG 103

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      188 VPEYEVALHATQAMVRAIADT--FEdvelmdtwTWFQSGINTDGAHNPVTTRKVNKGDILSLNCFPMIAGYYTALERTLF 265
Cdd:COG0006 104 VTEREVAAELEAAMRRRGAEGpsFD--------TIVASGENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVA 175

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      266 LDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGHSFGTLSHYYGReagleLREDID 345
Cdd:COG0006 176 VGEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAGYGEYFPHGTGHGVGLDVHEGPQ-----ISPGND 250

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
1CHM_B      346 TVLEPGMVVSMEPMIMlpegLPGAGGYREHDILIVNENGAENITKFP 392
Cdd:COG0006 251 RPLEPGMVFTIEPGIY----IPGIGGVRIEDTVLVTEDGAEVLTRLP 293
APP_MetAP cd01066
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
 165-385 1.44e-46

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: 158.77  E-value: 1.44e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      165 MIRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAIAdtfedveLMDTWTWFQSGINTDGAHNPVTTRKVNKGDI 244
Cdd:cd01066   3 RLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAGG-------YPAGPTIVGSGARTALPHYRPDDRRLQEGDL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      245 LSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGHS 324
Cdd:cd01066  76 VLVDLGGVYDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLGPNFGHRTGHG 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
1CHM_B      325 FGTLSHYYGReagleLREDIDTVLEPGMVVSMEPMImlpeGLPGAGGYREHDILIVNENGA 385
Cdd:cd01066 156 IGLEIHEPPV-----LKAGDDTVLEPGMVFAVEPGL----YLPGGGGVRIEDTVLVTEDGP 207
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 165-379 8.57e-34

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: 125.05  E-value: 8.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B        165 MIRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAiadtfEDVELMDTWTWFQSGINTDGAHNPVTTRKVNKGDI 244
Cdd:pfam00557   2 LMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRR-----GGARGPAFPPIVASGPNAAIPHYIPNDRVLKPGDL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B        245 LSLNCFPMIAGYYTA-LERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGH 323
Cdd:pfam00557  77 VLIDVGAEYDGGYCSdITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGEYFPHGLGH 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
1CHM_B        324 SFGTLSHyygrEAGLELREDIDTVLEPGMVVSMEPMIMLPeglPGAGGYR-EHDILI 379
Cdd:pfam00557 157 GIGLEVH----EGPYISRGGDDRVLEPGMVFTIEPGIYFI---PGWGGVRiEDTVLV 206
APP-like cd01092
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
 166-385 3.33e-23

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: 96.42  E-value: 3.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      166 IRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAIAD--TFEdvelmdtwTWFQSGINTDGAHNPVTTRKVNKGD 243
Cdd:cd01092   4 LRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKLGAEgpSFD--------TIVASGPNSALPHGVPSDRKIEEGD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      244 ILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGH 323
Cdd:cd01092  76 LVLIDFGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGYGEYFIHRTGH 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1CHM_B      324 SFGTLSHYYGReagleLREDIDTVLEPGMVVSMEPMIMlpegLPGAGGYREHDILIVNENGA 385
Cdd:cd01092 156 GVGLEVHEAPY-----ISPGSDDVLEEGMVFTIEPGIY----IPGKGGVRIEDDVLVTEDGC 208
Creatinase_N pfam01321
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ...
 26-157 9.32e-19

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: 81.58  E-value: 9.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B         26 RQARLRAHLAAENIDAAIFTSYHNINYYSDFlycSFGRPYALVVTEDDVISIsanIDGGQPWR--RTVGTDN--IVYTDW 101
Cdd:pfam01321   1 RLEKLRKLMEEKGLDAALVTSPENLRYLTGF---TGSRGLLLLVTADGALLL---VDALEYERaaAESAPDFdvVPYRDY 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
1CHM_B        102 QrdNYFAAIQQALPKARRIGIEHDHLNLQNRDKLAARYPDAELVDVAAACMRMRMI 157
Cdd:pfam01321  75 E--ALADLLKELGAGGKRVGFEADALTVAFYEALKEALPGAELVDVSGLIERLRMV 128
PRK09795 PRK09795
aminopeptidase; Provisional
 147-392 1.23e-17

aminopeptidase; Provisional


Pssm-ID: 182080 [Multi-domain]  Cd Length: 361  Bit Score: 83.45  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       147 VAAACMRMRMIKSAEEHVMIRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAIAD--TFEdvelmdtwTWFQSG 224
Cdd:PRK09795 117 VSATPDVLRQIKTPEEVEKIRLACGIADRGAEHIRRFIQAGMSEREIAAELEWFMRQQGAEkaSFD--------TIVASG 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       225 INTDGAHNPVTTRKVNKGDILSLNCFPMIAGYYTALERTLFL---DHCSDDH--LRLWQVNVEVHEAGLKLIKPGARCSD 299
Cdd:PRK09795 189 WRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVngeGVSAESHplFNVYQIVLQAQLAAISAIRPGVRCQQ 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       300 I---ARELNEiflkhdvlqyrTFGYGHSFGtlsHYYGREAGLELREDI------DTVLEPGMVVSMEPMIMlpegLPGAG 370
Cdd:PRK09795 269 VddaARRVIT-----------EAGYGDYFG---HNTGHAIGIEVHEDPrfsprdTTTLQPGMLLTVEPGIY----LPGQG 330

                        250       260
                 ....*....|....*....|..
1CHM_B       371 GYREHDILIVNENGAENITKFP 392
Cdd:PRK09795 331 GVRIEDVVLVTPQGAEVLYAMP 352
MetAP1 cd01086
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 242-390 1.54e-10

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: 60.97  E-value: 1.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      242 GDILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGy 321
Cdd:cd01086  79 GDIVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFG- 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      322 GHSFGTLSH------YYGREaglelreDIDTVLEPGMVVSMEPMI--------MLPEG--LPGAGGYR----EHDILIVn 381
Cdd:cd01086 158 GHGIGRKFHeepqipNYGRP-------GTGPKLKPGMVFTIEPMInlgtyevvTLPDGwtVVTKDGSLsaqfEHTVLIT- 229


                ....*....
1CHM_B      382 ENGAENITK 390
Cdd:cd01086 230 EDGPEILTL 238
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
 225-390 1.05e-09

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: 58.51  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B        225 INTDGAHNPVTTRKVNKGDILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIAREL 304
Cdd:TIGR00500  70 VNEVVIHGIPDKKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAI 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B        305 NEIFLKHDVLQYRTFGyGHSFG-------TLSHYYGREAGLelredidtVLEPGMVVSMEPMIML--------------- 362
Cdd:TIGR00500 150 QKYAEAKGFSVVREYC-GHGIGrkfheepQIPNYGKKFTNV--------RLKEGMVFTIEPMVNTgteeittaadgwtvk 220

                         170       180
                  ....*....|....*....|....*....
1CHM_B        363 -PEGLPGAggYREHDILIVnENGAENITK 390
Cdd:TIGR00500 221 tKDGSLSA--QFEHTIVIT-DNGPEILTE 246
PRK14576 PRK14576
putative endopeptidase; Provisional
 107-391 5.31e-09

putative endopeptidase; Provisional


Pssm-ID: 173040 [Multi-domain]  Cd Length: 405  Bit Score: 57.72  E-value: 5.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       107 FAAIQQALPKA----RRIGIEHDHLNLQNRDKLAARYPDAELVDVAAACMRMRMIKSAEEHVMIRHGARIADIGGAAVVE 182
Cdd:PRK14576 123 FSLVKNALEDAgvldKTIAIELQAMSNGGKGVLDKVAPGLKLVDSTALFNEIRMIKSPWEIEHLRKSAEITEYGIASAAK 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       183 ALGDQVPEYEVALHATQAMVRAIADTFEDVELMDTWTWFQSGINTDgahnpvtTRKVNKGDILSLNCFPMIAGYYTALER 262
Cdd:PRK14576 203 KIRVGCTAAELTAAFKAAVMSFPETNFSRFNLISVGDNFSPKIIAD-------TTPAKVGDLIKFDCGIDVAGYGADLAR 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       263 TLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGHSFGTlshYYGREAGLELRE 342
Cdd:PRK14576 276 TFVLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVFDSTMAVIKTSGLPHYNRGHLGHGDGV---FLGLEEVPFVST 352

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
1CHM_B       343 DIDTVLEPGMVVSMEPmimlPEGLPGAGGYREHDILIVNENGAENITKF 391
Cdd:PRK14576 353 QATETFCPGMVLSLET----PYYGIGVGSIMLEDMILITDSGFEFLSKL 397
PRK15173 PRK15173
peptidase; Provisional
 110-392 7.84e-09

peptidase; Provisional


Pssm-ID: 185095 [Multi-domain]  Cd Length: 323  Bit Score: 56.65  E-value: 7.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       110 IQQALPKAR----RIGIEHDHLNLQNRDKLAARYPDAELVDVAAACMRMRMIKSAEEHVMIRHGARIADIGGAAVVEALG 185
Cdd:PRK15173  44 LKDALNDARvlnkKIAIDLNIMSNGGKRVIDAVMPNVDFVDSSSIFNELRVIKSPWEIKRLRKSAEITEYGITEASKLIR 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       186 DQVPEYEVALHATQAMVRAIADTFEDVELMDTWTWFQSGINtdgahnPVTTrKVNKGDILSLNCFPMIAGYYTALERTLF 265
Cdd:PRK15173 124 VGCTSAELTAAYKAAVMSKSETHFSRFHLISVGADFSPKLI------PSNT-KACSGDLIKFDCGVDVDGYGADIARTFV 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       266 LDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGHSFGTlshYYGREAGLELREDID 345
Cdd:PRK15173 197 VGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSGLPNYNRGHLGHGNGV---FLGLEESPFVSTHAT 273

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
1CHM_B       346 TVLEPGMVVSMEPmimlPEGLPGAGGYREHDILIVNENGAENITKFP 392
Cdd:PRK15173 274 ESFTSGMVLSLET----PYYGYNLGSIMIEDMILINKEGIEFLSKLP 316
Prolidase cd01087
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ...
 270-390 1.13e-08

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: 55.27  E-value: 1.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      270 SDDHLRLWQVNVEVHEAGLKLIKPGARCSDI----ARELNEIFLKHDVL-----------QYRTFgYGHSfgtLSHYYGR 334
Cdd:cd01087 102 TDEQRELYEAVLAAQKAAIAACKPGVSYEDIhllaHRVLAEGLKELGILkgdvdeivesgAYAKF-FPHG---LGHYLGL 177

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1CHM_B      335 E----AGLELREDIDTVLEPGMVVSMEPMIMLPEGLPGA------GGYR-EHDILiVNENGAENITK 390
Cdd:cd01087 178 DvhdvGGYLRYLRRARPLEPGMVITIEPGIYFIPDLLDVpeyfrgGGIRiEDDVL-VTEDGPENLTR 243
PRK05716 PRK05716
methionine aminopeptidase; Validated
 237-390 1.19e-08

methionine aminopeptidase; Validated


Pssm-ID: 235576 [Multi-domain]  Cd Length: 252  Bit Score: 55.53  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       237 RKVNKGDILSLNCFPMIAGYY--TAleRTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVL 314
Cdd:PRK05716  84 KVLKEGDIVNIDVTVIKDGYHgdTS--RTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGFS 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       315 QYRTFGyGHSFGT-------LSHYYGREAGlelredidTVLEPGMVVSMEPMI--------MLPEG--LPGAGGYR---- 373
Cdd:PRK05716 162 VVREYC-GHGIGRkfheepqIPHYGAPGDG--------PVLKEGMVFTIEPMInagkrevkTLKDGwtVVTKDGSLsaqy 232

                        170
                 ....*....|....*..
1CHM_B       374 EHDILIVnENGAENITK 390
Cdd:PRK05716 233 EHTVAVT-EDGPEILTL 248
PRK14575 PRK14575
putative peptidase; Provisional
 110-392 1.51e-08

putative peptidase; Provisional


Pssm-ID: 173039 [Multi-domain]  Cd Length: 406  Bit Score: 56.25  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       110 IQQALPKAR----RIGIEHDHLNLQNRDKLAARYPDAELVDVAAACMRMRMIKSAEEHVMIRHGARIADIGGAAVVEALG 185
Cdd:PRK14575 127 LKDALNDARvlnkKIAIDLNIMSNGGKRVIDAVMPNVDFVDSSSIFNELRVIKSPWEIKRLRKSAEITEYGITEASKLIR 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       186 DQVPEYEVALHATQAMVRAIADTFEDVELMDTWTWFQSGINtdgahnPVTTrKVNKGDILSLNCFPMIAGYYTALERTLF 265
Cdd:PRK14575 207 VGCTSAELTAAYKAAVMSKSETHFSRFHLISVGADFSPKLI------PSNT-KACSGDLIKFDCGVDVDGYGADIARTFV 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       266 LDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGHSFGTlshYYGREAGLELREDID 345
Cdd:PRK14575 280 VGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSGLPNYNRGHLGHGNGV---FLGLEESPFVSTHAT 356

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
1CHM_B       346 TVLEPGMVVSMEPmimlPEGLPGAGGYREHDILIVNENGAENITKFP 392
Cdd:PRK14575 357 ESFTSGMVLSLET----PYYGYNLGSIMIEDMILINKEGIEFLSKLP 399
PLN03158 PLN03158
methionine aminopeptidase; Provisional
 237-395 3.19e-08

methionine aminopeptidase; Provisional


Pssm-ID: 215607 [Multi-domain]  Cd Length: 396  Bit Score: 55.23  E-value: 3.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       237 RKVNKGDILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARcsdiARELNEIFLKHDV--- 313
Cdd:PLN03158 216 RKLEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEASRQLVKCTYECLEKAIAIVKPGVR----YREVGEVINRHATmsg 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       314 LQYRTFGYGHSFGTLSH------YYGREAGLelredidTVLEPGMVVSMEPMI--------MLPEGLPG--AGGYR---- 373
Cdd:PLN03158 292 LSVVKSYCGHGIGELFHcapnipHYARNKAV-------GVMKAGQVFTIEPMInagvwrdrMWPDGWTAvtADGKRsaqf 364

                        170       180
                 ....*....|....*....|...
1CHM_B       374 EHdILIVNENGAENIT-KFPYGP 395
Cdd:PLN03158 365 EH-TLLVTETGVEVLTaRLPSSP 386
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
237-394 1.79e-07

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 51.93  E-value: 1.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      237 RKVNKGDILSLNCFPMIAGYY--TAleRTLFLDHCSDDHLRLwqvnVEV-HEA---GLKLIKPGARCSDIARELNEIFLK 310
Cdd:COG0024  82 RVLKDGDIVNIDVGAILDGYHgdSA--RTFVVGEVSPEARRL----VEVtEEAlyaGIAAAKPGNRLGDIGHAIQSYAES 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B      311 HD--VLqyRTFGyGHSFGT-------LSHYYGREAGLELRedidtvlePGMVVSMEPMIMlpeglpgAGGYR-------- 373
Cdd:COG0024 156 NGysVV--REFV-GHGIGRemheepqVPNYGRPGRGPRLK--------PGMVLAIEPMIN-------AGTPEvkvlddgw 217

                       170       180       190
                ....*....|....*....|....*....|....
1CHM_B      374 -------------EHDILIVnENGAENITKFPYG 394
Cdd:COG0024 218 tvvtkdgslsaqfEHTVAVT-EDGPEILTLPDGG 250
PRK12896 PRK12896
methionine aminopeptidase; Reviewed
 225-389 3.21e-06

methionine aminopeptidase; Reviewed


Pssm-ID: 237252 [Multi-domain]  Cd Length: 255  Bit Score: 48.29  E-value: 3.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       225 INTDGAHNPVTTRKVNKGDILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIAREl 304
Cdd:PRK12896  77 VNEEVAHGIPGPRVIKDGDLVNIDVSAYLDGYHGDTGITFAVGPVSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRA- 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       305 neiflkhdVLQY-RTFGY-------GHSFGT--------LSHYYgreaglelREDIDTVLEPGMVVSMEPMIMLpeglpG 368
Cdd:PRK12896 156 --------IEDFaKKNGYsvvrdltGHGVGRslheepsvILTYT--------DPLPNRLLRPGMTLAVEPFLNL-----G 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
1CHM_B       369 AGGYR-------------------EHDILiVNENGAENIT 389
Cdd:PRK12896 215 AKDAEtlddgwtvvtpdkslsaqfEHTVV-VTRDGPEILT 253
PRK10879 PRK10879
proline aminopeptidase P II; Provisional
 285-389 5.16e-04

proline aminopeptidase P II; Provisional


Pssm-ID: 182804 [Multi-domain]  Cd Length: 438  Bit Score: 42.02  E-value: 5.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       285 EAGLKLIKPGARCSDIARELNEIF---------LKHDVLQ------YRTF---GYGHSFGTLSH---YYGreaglelrED 343
Cdd:PRK10879 296 ETSLRLYRPGTSIREVTGEVVRIMvsglvklgiLKGDVDQliaenaHRPFfmhGLSHWLGLDVHdvgVYG--------QD 367

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
1CHM_B       344 IDTVLEPGMVVSMEPMIML------PEGLPGAGGYREHDILIvNENGAENIT 389
Cdd:PRK10879 368 RSRILEPGMVLTVEPGLYIapdadvPEQYRGIGIRIEDDIVI-TETGNENLT 418
PRK12318 PRK12318
methionyl aminopeptidase;
242-360 1.16e-03

methionyl aminopeptidase;


Pssm-ID: 183434 [Multi-domain]  Cd Length: 291  Bit Score: 40.57  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CHM_B       242 GDILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHD---VLQYRT 318
Cdd:PRK12318 129 GDIMNIDVSCIVDGYYGDCSRMVMIGEVSEIKKKVCQASLECLNAAIAILKPGIPLYEIGEVIENCADKYGfsvVDQFVG 208

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
1CHM_B       319 FGYG---HSFGTLSHYYGREAGLelredidtvLEPGMVVSMEPMI 360
Cdd:PRK12318 209 HGVGikfHENPYVPHHRNSSKIP---------LAPGMIFTIEPMI 244
 
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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