|
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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 163 HVMIRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAIADTFEDVELMDTWTWFQSGINTDGAHNPVTTRKVNKG 242
Cdd:cd01090 1 IALIRHGARIADIGGAAVVEAIREGVPEYEVALAGTQAMVREIAKTFPEVELMDTWTWFQSGINTDGAHNPVTNRKVQRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 243 DILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYG 322
Cdd:cd01090 81 DILSLNCFPMIAGYYTALERTLFLDEVSDAHLKIWEANVAVHERGLELIKPGARCKDIAAELNEMYREHDLLRYRTFGYG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 28 ARLRAHLAAENIDAAIFTSYHNINYYSDFlYCSFGRPYALVVTEDDvisisanidggqpwrrtvgtDNIVYTDWqrdnyf 107
Cdd:COG0006 1 ARLRALMAEAGLDALLLTDPSNFAYLTGF-RGSPERLAALLVTADG--------------------EPVLFVDE------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 108 aaiqqalpkarrigiehdhlnlqnrdklaaRYPDAELVDVAAACMRMRMIKSAEEHVMIRHGARIADIGGAAVVEALGDQ 187
Cdd:COG0006 54 ------------------------------LEAERELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRPG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 188 VPEYEVALHATQAMVRAIADT--FEdvelmdtwTWFQSGINTDGAHNPVTTRKVNKGDILSLNCFPMIAGYYTALERTLF 265
Cdd:COG0006 104 VTEREVAAELEAAMRRRGAEGpsFD--------TIVASGENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 266 LDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGHSFGTLSHYYGReagleLREDID 345
Cdd:COG0006 176 VGEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAGYGEYFPHGTGHGVGLDVHEGPQ-----ISPGND 250
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 165 MIRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAiadtfEDVELMDTWTWFQSGINTDGAHNPVTTRKVNKGDI 244
Cdd:pfam00557 2 LMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRR-----GGARGPAFPPIVASGPNAAIPHYIPNDRVLKPGDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 245 LSLNCFPMIAGYYTA-LERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGH 323
Cdd:pfam00557 77 VLIDVGAEYDGGYCSdITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGEYFPHGLGH 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 26 RQARLRAHLAAENIDAAIFTSYHNINYYSDFlycSFGRPYALVVTEDDVISIsanIDGGQPWR--RTVGTDN--IVYTDW 101
Cdd:pfam01321 1 RLEKLRKLMEEKGLDAALVTSPENLRYLTGF---TGSRGLLLLVTADGALLL---VDALEYERaaAESAPDFdvVPYRDY 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 147 VAAACMRMRMIKSAEEHVMIRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAIAD--TFEdvelmdtwTWFQSG 224
Cdd:PRK09795 117 VSATPDVLRQIKTPEEVEKIRLACGIADRGAEHIRRFIQAGMSEREIAAELEWFMRQQGAEkaSFD--------TIVASG 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 225 INTDGAHNPVTTRKVNKGDILSLNCFPMIAGYYTALERTLFL---DHCSDDH--LRLWQVNVEVHEAGLKLIKPGARCSD 299
Cdd:PRK09795 189 WRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVngeGVSAESHplFNVYQIVLQAQLAAISAIRPGVRCQQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 300 I---ARELNEiflkhdvlqyrTFGYGHSFGtlsHYYGREAGLELREDI------DTVLEPGMVVSMEPMIMlpegLPGAG 370
Cdd:PRK09795 269 VddaARRVIT-----------EAGYGDYFG---HNTGHAIGIEVHEDPrfsprdTTTLQPGMLLTVEPGIY----LPGQG 330
|
250 260
....*....|....*....|..
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 225 INTDGAHNPVTTRKVNKGDILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIAREL 304
Cdd:TIGR00500 70 VNEVVIHGIPDKKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 305 NEIFLKHDVLQYRTFGyGHSFG-------TLSHYYGREAGLelredidtVLEPGMVVSMEPMIML--------------- 362
Cdd:TIGR00500 150 QKYAEAKGFSVVREYC-GHGIGrkfheepQIPNYGKKFTNV--------RLKEGMVFTIEPMVNTgteeittaadgwtvk 220
|
170 180
....*....|....*....|....*....
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 163 HVMIRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAIADTFEDVELMDTWTWFQSGINTDGAHNPVTTRKVNKG 242
Cdd:cd01090 1 IALIRHGARIADIGGAAVVEAIREGVPEYEVALAGTQAMVREIAKTFPEVELMDTWTWFQSGINTDGAHNPVTNRKVQRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 243 DILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYG 322
Cdd:cd01090 81 DILSLNCFPMIAGYYTALERTLFLDEVSDAHLKIWEANVAVHERGLELIKPGARCKDIAAELNEMYREHDLLRYRTFGYG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 28 ARLRAHLAAENIDAAIFTSYHNINYYSDFlYCSFGRPYALVVTEDDvisisanidggqpwrrtvgtDNIVYTDWqrdnyf 107
Cdd:COG0006 1 ARLRALMAEAGLDALLLTDPSNFAYLTGF-RGSPERLAALLVTADG--------------------EPVLFVDE------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 108 aaiqqalpkarrigiehdhlnlqnrdklaaRYPDAELVDVAAACMRMRMIKSAEEHVMIRHGARIADIGGAAVVEALGDQ 187
Cdd:COG0006 54 ------------------------------LEAERELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRPG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 188 VPEYEVALHATQAMVRAIADT--FEdvelmdtwTWFQSGINTDGAHNPVTTRKVNKGDILSLNCFPMIAGYYTALERTLF 265
Cdd:COG0006 104 VTEREVAAELEAAMRRRGAEGpsFD--------TIVASGENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 266 LDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGHSFGTLSHYYGReagleLREDID 345
Cdd:COG0006 176 VGEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAGYGEYFPHGTGHGVGLDVHEGPQ-----ISPGND 250
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 165 MIRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAIAdtfedveLMDTWTWFQSGINTDGAHNPVTTRKVNKGDI 244
Cdd:cd01066 3 RLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAGG-------YPAGPTIVGSGARTALPHYRPDDRRLQEGDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 245 LSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGHS 324
Cdd:cd01066 76 VLVDLGGVYDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLGPNFGHRTGHG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 165 MIRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAiadtfEDVELMDTWTWFQSGINTDGAHNPVTTRKVNKGDI 244
Cdd:pfam00557 2 LMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRR-----GGARGPAFPPIVASGPNAAIPHYIPNDRVLKPGDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 245 LSLNCFPMIAGYYTA-LERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGH 323
Cdd:pfam00557 77 VLIDVGAEYDGGYCSdITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGEYFPHGLGH 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 166 IRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAIAD--TFEdvelmdtwTWFQSGINTDGAHNPVTTRKVNKGD 243
Cdd:cd01092 4 LRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKLGAEgpSFD--------TIVASGPNSALPHGVPSDRKIEEGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 244 ILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGH 323
Cdd:cd01092 76 LVLIDFGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGYGEYFIHRTGH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 26 RQARLRAHLAAENIDAAIFTSYHNINYYSDFlycSFGRPYALVVTEDDVISIsanIDGGQPWR--RTVGTDN--IVYTDW 101
Cdd:pfam01321 1 RLEKLRKLMEEKGLDAALVTSPENLRYLTGF---TGSRGLLLLVTADGALLL---VDALEYERaaAESAPDFdvVPYRDY 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 147 VAAACMRMRMIKSAEEHVMIRHGARIADIGGAAVVEALGDQVPEYEVALHATQAMVRAIAD--TFEdvelmdtwTWFQSG 224
Cdd:PRK09795 117 VSATPDVLRQIKTPEEVEKIRLACGIADRGAEHIRRFIQAGMSEREIAAELEWFMRQQGAEkaSFD--------TIVASG 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 225 INTDGAHNPVTTRKVNKGDILSLNCFPMIAGYYTALERTLFL---DHCSDDH--LRLWQVNVEVHEAGLKLIKPGARCSD 299
Cdd:PRK09795 189 WRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVngeGVSAESHplFNVYQIVLQAQLAAISAIRPGVRCQQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 300 I---ARELNEiflkhdvlqyrTFGYGHSFGtlsHYYGREAGLELREDI------DTVLEPGMVVSMEPMIMlpegLPGAG 370
Cdd:PRK09795 269 VddaARRVIT-----------EAGYGDYFG---HNTGHAIGIEVHEDPrfsprdTTTLQPGMLLTVEPGIY----LPGQG 330
|
250 260
....*....|....*....|..
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 242 GDILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGy 321
Cdd:cd01086 79 GDIVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFG- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 322 GHSFGTLSH------YYGREaglelreDIDTVLEPGMVVSMEPMI--------MLPEG--LPGAGGYR----EHDILIVn 381
Cdd:cd01086 158 GHGIGRKFHeepqipNYGRP-------GTGPKLKPGMVFTIEPMInlgtyevvTLPDGwtVVTKDGSLsaqfEHTVLIT- 229
|
....*....
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 225 INTDGAHNPVTTRKVNKGDILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIAREL 304
Cdd:TIGR00500 70 VNEVVIHGIPDKKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 305 NEIFLKHDVLQYRTFGyGHSFG-------TLSHYYGREAGLelredidtVLEPGMVVSMEPMIML--------------- 362
Cdd:TIGR00500 150 QKYAEAKGFSVVREYC-GHGIGrkfheepQIPNYGKKFTNV--------RLKEGMVFTIEPMVNTgteeittaadgwtvk 220
|
170 180
....*....|....*....|....*....
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 107 FAAIQQALPKA----RRIGIEHDHLNLQNRDKLAARYPDAELVDVAAACMRMRMIKSAEEHVMIRHGARIADIGGAAVVE 182
Cdd:PRK14576 123 FSLVKNALEDAgvldKTIAIELQAMSNGGKGVLDKVAPGLKLVDSTALFNEIRMIKSPWEIEHLRKSAEITEYGIASAAK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 183 ALGDQVPEYEVALHATQAMVRAIADTFEDVELMDTWTWFQSGINTDgahnpvtTRKVNKGDILSLNCFPMIAGYYTALER 262
Cdd:PRK14576 203 KIRVGCTAAELTAAFKAAVMSFPETNFSRFNLISVGDNFSPKIIAD-------TTPAKVGDLIKFDCGIDVAGYGADLAR 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 263 TLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGHSFGTlshYYGREAGLELRE 342
Cdd:PRK14576 276 TFVLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVFDSTMAVIKTSGLPHYNRGHLGHGDGV---FLGLEEVPFVST 352
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 110 IQQALPKAR----RIGIEHDHLNLQNRDKLAARYPDAELVDVAAACMRMRMIKSAEEHVMIRHGARIADIGGAAVVEALG 185
Cdd:PRK15173 44 LKDALNDARvlnkKIAIDLNIMSNGGKRVIDAVMPNVDFVDSSSIFNELRVIKSPWEIKRLRKSAEITEYGITEASKLIR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 186 DQVPEYEVALHATQAMVRAIADTFEDVELMDTWTWFQSGINtdgahnPVTTrKVNKGDILSLNCFPMIAGYYTALERTLF 265
Cdd:PRK15173 124 VGCTSAELTAAYKAAVMSKSETHFSRFHLISVGADFSPKLI------PSNT-KACSGDLIKFDCGVDVDGYGADIARTFV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 266 LDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGHSFGTlshYYGREAGLELREDID 345
Cdd:PRK15173 197 VGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSGLPNYNRGHLGHGNGV---FLGLEESPFVSTHAT 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 270 SDDHLRLWQVNVEVHEAGLKLIKPGARCSDI----ARELNEIFLKHDVL-----------QYRTFgYGHSfgtLSHYYGR 334
Cdd:cd01087 102 TDEQRELYEAVLAAQKAAIAACKPGVSYEDIhllaHRVLAEGLKELGILkgdvdeivesgAYAKF-FPHG---LGHYLGL 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 237 RKVNKGDILSLNCFPMIAGYY--TAleRTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVL 314
Cdd:PRK05716 84 KVLKEGDIVNIDVTVIKDGYHgdTS--RTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGFS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 315 QYRTFGyGHSFGT-------LSHYYGREAGlelredidTVLEPGMVVSMEPMI--------MLPEG--LPGAGGYR---- 373
Cdd:PRK05716 162 VVREYC-GHGIGRkfheepqIPHYGAPGDG--------PVLKEGMVFTIEPMInagkrevkTLKDGwtVVTKDGSLsaqy 232
|
170
....*....|....*..
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 110 IQQALPKAR----RIGIEHDHLNLQNRDKLAARYPDAELVDVAAACMRMRMIKSAEEHVMIRHGARIADIGGAAVVEALG 185
Cdd:PRK14575 127 LKDALNDARvlnkKIAIDLNIMSNGGKRVIDAVMPNVDFVDSSSIFNELRVIKSPWEIKRLRKSAEITEYGITEASKLIR 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 186 DQVPEYEVALHATQAMVRAIADTFEDVELMDTWTWFQSGINtdgahnPVTTrKVNKGDILSLNCFPMIAGYYTALERTLF 265
Cdd:PRK14575 207 VGCTSAELTAAYKAAVMSKSETHFSRFHLISVGADFSPKLI------PSNT-KACSGDLIKFDCGVDVDGYGADIARTFV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 266 LDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHDVLQYRTFGYGHSFGTlshYYGREAGLELREDID 345
Cdd:PRK14575 280 VGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSGLPNYNRGHLGHGNGV---FLGLEESPFVSTHAT 356
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 237 RKVNKGDILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARcsdiARELNEIFLKHDV--- 313
Cdd:PLN03158 216 RKLEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEASRQLVKCTYECLEKAIAIVKPGVR----YREVGEVINRHATmsg 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 314 LQYRTFGYGHSFGTLSH------YYGREAGLelredidTVLEPGMVVSMEPMI--------MLPEGLPG--AGGYR---- 373
Cdd:PLN03158 292 LSVVKSYCGHGIGELFHcapnipHYARNKAV-------GVMKAGQVFTIEPMInagvwrdrMWPDGWTAvtADGKRsaqf 364
|
170 180
....*....|....*....|...
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 237 RKVNKGDILSLNCFPMIAGYY--TAleRTLFLDHCSDDHLRLwqvnVEV-HEA---GLKLIKPGARCSDIARELNEIFLK 310
Cdd:COG0024 82 RVLKDGDIVNIDVGAILDGYHgdSA--RTFVVGEVSPEARRL----VEVtEEAlyaGIAAAKPGNRLGDIGHAIQSYAES 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 311 HD--VLqyRTFGyGHSFGT-------LSHYYGREAGLELRedidtvlePGMVVSMEPMIMlpeglpgAGGYR-------- 373
Cdd:COG0024 156 NGysVV--REFV-GHGIGRemheepqVPNYGRPGRGPRLK--------PGMVLAIEPMIN-------AGTPEvkvlddgw 217
|
170 180 190
....*....|....*....|....*....|....
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 225 INTDGAHNPVTTRKVNKGDILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIAREl 304
Cdd:PRK12896 77 VNEEVAHGIPGPRVIKDGDLVNIDVSAYLDGYHGDTGITFAVGPVSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRA- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 305 neiflkhdVLQY-RTFGY-------GHSFGT--------LSHYYgreaglelREDIDTVLEPGMVVSMEPMIMLpeglpG 368
Cdd:PRK12896 156 --------IEDFaKKNGYsvvrdltGHGVGRslheepsvILTYT--------DPLPNRLLRPGMTLAVEPFLNL-----G 214
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 285 EAGLKLIKPGARCSDIARELNEIF---------LKHDVLQ------YRTF---GYGHSFGTLSH---YYGreaglelrED 343
Cdd:PRK10879 296 ETSLRLYRPGTSIREVTGEVVRIMvsglvklgiLKGDVDQliaenaHRPFfmhGLSHWLGLDVHdvgVYG--------QD 367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 515103 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515103 242 GDILSLNCFPMIAGYYTALERTLFLDHCSDDHLRLWQVNVEVHEAGLKLIKPGARCSDIARELNEIFLKHD---VLQYRT 318
Cdd:PRK12318 129 GDIMNIDVSCIVDGYYGDCSRMVMIGEVSEIKKKVCQASLECLNAAIAILKPGIPLYEIGEVIENCADKYGfsvVDQFVG 208
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 515103 319 FGYG---HSFGTLSHYYGREAGLelredidtvLEPGMVVSMEPMI 360
Cdd:PRK12318 209 HGVGikfHENPYVPHHRNSSKIP---------LAPGMIFTIEPMI 244
|
|
|