|
Name |
Accession |
Description |
Interval |
E-value |
| APP |
cd01085 |
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ... |
329-551 |
4.95e-143 |
|
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: 413.88 E-value: 4.95e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 329 GMRRAHIKDAVALCELFNWLEQEVPKGG-VTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPIPETNRTLS 407
Cdd:cd01085 1 GMRAAHIRDGVALVEFLAWLEQEVPKGEtITELSAADKLEEFRRQQKGYVGLSFDTISGFGPNGAIVHYSPTEESNRKIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 408 LDEVYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGT 487
Cdd:cd01085 81 PDGLYLIDSGGQYLDGTTDITRTVHLGEPTAEQKRDYTLVLKGHIALARAKFPKGTTGSQLDALARQPLWKAGLDYGHGT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18777778 488 GHGVGSFLNVHEGPCGIsYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPAKTKYNF 551
Cdd:cd01085 161 GHGVGSFLNVHEGPQSI-SPAPNNVPLKAGMILSNEPGYYKEGKYGIRIENLVLVVEAETTEFG 223
|
|
| Creatinase_N_2 |
pfam16189 |
Creatinase/Prolidase N-terminal domain; |
157-326 |
2.37e-65 |
|
Creatinase/Prolidase N-terminal domain; :
Pssm-ID: 465053 Cd Length: 159 Bit Score: 211.20 E-value: 2.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 157 DRPERPCKPLLTLGLDYTGISWKEKVADLRLKMAERSIVWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLERIMLF 236
Cdd:pfam16189 1 DRPALPANPVFVLPLKYAGESAAEKLARLREALKEKGADALVLSALDEIAWLLNLRGSDVPYNPVFLSYALVTDDEATLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 237 IDGDRIDaPGVKQHLlldlgleAEYKIQVLPYKSILSELKTLCADlsprEKVWV-SDKASYAVSEAIPKDHRCCMPYTPI 315
Cdd:pfam16189 81 VDPEKLS-DEVRAHL-------EENGVEIRPYDDIYEDLAALAAG----KKVLLdPSRTSYALYSALPAGAKVVEAPSPI 148
|
170
....*....|.
gi 18777778 316 CIAKAVKNSAE 326
Cdd:pfam16189 149 TLMKAVKNETE 159
|
|
| Peptidase_M24_C |
pfam16188 |
C-terminal region of peptidase_M24; This is a short region at the C-terminus of a number of ... |
557-619 |
9.16e-26 |
|
C-terminal region of peptidase_M24; This is a short region at the C-terminus of a number of metallo-peptidases of the M24 family. :
Pssm-ID: 465052 Cd Length: 63 Bit Score: 100.18 E-value: 9.16e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18777778 557 LTFEPLTLVPIQTKMIDVDALTDKECDWLNSYHQTCRDVIGKELQTQGrqEALEWLLRETEPI 619
Cdd:pfam16188 3 LGFETLTLVPIDRKLIDVSLLTEEEIEWLNAYHARVREKLSPLLEEEE--DALEWLKRATRPI 63
|
|
| Creatinase_N |
pfam01321 |
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ... |
10-154 |
1.09e-09 |
|
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: 56.54 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 10 LRQLRQAMRNSEcvaepIQAYIIPSGDahqseyiapcdcRRAFVSGFDGSAGTAI-ITEEHAAMWTD-GRYFLQAAKQmd 87
Cdd:pfam01321 2 LEKLRKLMEEKG-----LDAALVTSPE------------NLRYLTGFTGSRGLLLlVTADGALLLVDaLEYERAAAES-- 62
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18777778 88 nnWTLMKM-GLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAghHLVPVkENLVDKI 154
Cdd:pfam01321 63 --APDFDVvPYRDYEALADLLKELGAGGKRVGFEADALTVAFYEALKEALPGA--ELVDV-SGLIERL 125
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| APP |
cd01085 |
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ... |
329-551 |
4.95e-143 |
|
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: 413.88 E-value: 4.95e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 329 GMRRAHIKDAVALCELFNWLEQEVPKGG-VTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPIPETNRTLS 407
Cdd:cd01085 1 GMRAAHIRDGVALVEFLAWLEQEVPKGEtITELSAADKLEEFRRQQKGYVGLSFDTISGFGPNGAIVHYSPTEESNRKIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 408 LDEVYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGT 487
Cdd:cd01085 81 PDGLYLIDSGGQYLDGTTDITRTVHLGEPTAEQKRDYTLVLKGHIALARAKFPKGTTGSQLDALARQPLWKAGLDYGHGT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18777778 488 GHGVGSFLNVHEGPCGIsYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPAKTKYNF 551
Cdd:cd01085 161 GHGVGSFLNVHEGPQSI-SPAPNNVPLKAGMILSNEPGYYKEGKYGIRIENLVLVVEAETTEFG 223
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
183-566 |
5.55e-72 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 233.94 E-value: 5.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 183 ADLRLKMAERSIVWFVVTALDEIAWLFNLRGSdvehnPVFFSYAIIGLE-RIMLFIDGdridapgvkqhllldlgLEAEY 261
Cdd:COG0006 1 ARLRALMAEAGLDALLLTDPSNFAYLTGFRGS-----PERLAALLVTADgEPVLFVDE-----------------LEAER 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 262 KIQVLPykSILSELKtlcadlsprekvwvsdkasyavseaipkdhrccmpytpiciakAVKNSAESAGMRRAHIKDAVAL 341
Cdd:COG0006 59 ELVDAS--DLLEELR-------------------------------------------AIKSPEEIELMRKAARIADAAH 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 342 CELFNWLEQevpkgGVTEISAADKAEEFRRQQaDFVDLSFPTISSTGPNGAIIHYAPipeTNRTLSLDEVYLIDSGAQYK 421
Cdd:COG0006 94 EAALAALRP-----GVTEREVAAELEAAMRRR-GAEGPSFDTIVASGENAAIPHYTP---TDRPLKPGDLVLIDAGAEYD 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 422 DGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVfPTGTKGHLLDSFARSALWDSGL--DYLHGTGHGVGsfLNVHE 499
Cdd:COG0006 165 GYTSDITRTVAVGEPSDEQREIYEAVLEAQEAAIAAL-KPGVTGGEVDAAARDVLAEAGYgeYFPHGTGHGVG--LDVHE 241
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18777778 500 GPcgiSYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPAKtkynfnnrgsltFEPLTLVP 566
Cdd:COG0006 242 GP---QISPGNDRPLEPGMVFTIEPGIYIPGIGGVRIEDTVLVTEDG------------AEVLTRLP 293
|
|
| Creatinase_N_2 |
pfam16189 |
Creatinase/Prolidase N-terminal domain; |
157-326 |
2.37e-65 |
|
Creatinase/Prolidase N-terminal domain;
Pssm-ID: 465053 Cd Length: 159 Bit Score: 211.20 E-value: 2.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 157 DRPERPCKPLLTLGLDYTGISWKEKVADLRLKMAERSIVWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLERIMLF 236
Cdd:pfam16189 1 DRPALPANPVFVLPLKYAGESAAEKLARLREALKEKGADALVLSALDEIAWLLNLRGSDVPYNPVFLSYALVTDDEATLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 237 IDGDRIDaPGVKQHLlldlgleAEYKIQVLPYKSILSELKTLCADlsprEKVWV-SDKASYAVSEAIPKDHRCCMPYTPI 315
Cdd:pfam16189 81 VDPEKLS-DEVRAHL-------EENGVEIRPYDDIYEDLAALAAG----KKVLLdPSRTSYALYSALPAGAKVVEAPSPI 148
|
170
....*....|.
gi 18777778 316 CIAKAVKNSAE 326
Cdd:pfam16189 149 TLMKAVKNETE 159
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
328-544 |
1.20e-62 |
|
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: 205.94 E-value: 1.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 328 AGMRRAHIKDAVALCELFNWLeqevpKGGVTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPipeTNRTLS 407
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAI-----RPGVTERELAAELEAARLRRGGARGPAFPPIVASGPNAAIPHYIP---NDRVLK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 408 LDEVYLIDSGAQYKDG-TTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPtGTKGHLLDSFARSALWDSGLD--YL 484
Cdd:pfam00557 73 PGDLVLIDVGAEYDGGyCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKP-GVTGGDVDAAAREVLEEAGLGeyFP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18777778 485 HGTGHGVGsfLNVHEGPcgISYKTFSDEPLEAGMIVTDEPGYYE-DGAFGIRIENVVLVVP 544
Cdd:pfam00557 152 HGLGHGIG--LEVHEGP--YISRGGDDRVLEPGMVFTIEPGIYFiPGWGGVRIEDTVLVTE 208
|
|
| Peptidase_M24_C |
pfam16188 |
C-terminal region of peptidase_M24; This is a short region at the C-terminus of a number of ... |
557-619 |
9.16e-26 |
|
C-terminal region of peptidase_M24; This is a short region at the C-terminus of a number of metallo-peptidases of the M24 family.
Pssm-ID: 465052 Cd Length: 63 Bit Score: 100.18 E-value: 9.16e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18777778 557 LTFEPLTLVPIQTKMIDVDALTDKECDWLNSYHQTCRDVIGKELQTQGrqEALEWLLRETEPI 619
Cdd:pfam16188 3 LGFETLTLVPIDRKLIDVSLLTEEEIEWLNAYHARVREKLSPLLEEEE--DALEWLKRATRPI 63
|
|
| PRK09795 |
PRK09795 |
aminopeptidase; Provisional |
356-544 |
4.75e-19 |
|
aminopeptidase; Provisional
Pssm-ID: 182080 [Multi-domain] Cd Length: 361 Bit Score: 89.23 E-value: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 356 GVTEISAADKAEEFRRQQADfVDLSFPTISSTGPNGAIIHYAPipeTNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHF-- 433
Cdd:PRK09795 157 GMSEREIAAELEWFMRQQGA-EKASFDTIVASGWRGALPHGKA---SDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVng 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 434 -GTPTAYEKECFTY--VLKGHIAVSAAVFPtGTKGHLLDSFARSALWDSGL-DYL-HGTGHGVGsfLNVHEGPcgiSYKT 508
Cdd:PRK09795 233 eGVSAESHPLFNVYqiVLQAQLAAISAIRP-GVRCQQVDDAARRVITEAGYgDYFgHNTGHAIG--IEVHEDP---RFSP 306
|
170 180 190
....*....|....*....|....*....|....*.
gi 18777778 509 FSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVP 544
Cdd:PRK09795 307 RDTTTLQPGMLLTVEPGIYLPGQGGVRIEDVVLVTP 342
|
|
| Creatinase_N |
pfam01321 |
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ... |
10-154 |
1.09e-09 |
|
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: 56.54 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 10 LRQLRQAMRNSEcvaepIQAYIIPSGDahqseyiapcdcRRAFVSGFDGSAGTAI-ITEEHAAMWTD-GRYFLQAAKQmd 87
Cdd:pfam01321 2 LEKLRKLMEEKG-----LDAALVTSPE------------NLRYLTGFTGSRGLLLlVTADGALLLVDaLEYERAAAES-- 62
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18777778 88 nnWTLMKM-GLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAghHLVPVkENLVDKI 154
Cdd:pfam01321 63 --APDFDVvPYRDYEALADLLKELGAGGKRVGFEADALTVAFYEALKEALPGA--ELVDV-SGLIERL 125
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| APP |
cd01085 |
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ... |
329-551 |
4.95e-143 |
|
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: 413.88 E-value: 4.95e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 329 GMRRAHIKDAVALCELFNWLEQEVPKGG-VTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPIPETNRTLS 407
Cdd:cd01085 1 GMRAAHIRDGVALVEFLAWLEQEVPKGEtITELSAADKLEEFRRQQKGYVGLSFDTISGFGPNGAIVHYSPTEESNRKIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 408 LDEVYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGT 487
Cdd:cd01085 81 PDGLYLIDSGGQYLDGTTDITRTVHLGEPTAEQKRDYTLVLKGHIALARAKFPKGTTGSQLDALARQPLWKAGLDYGHGT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18777778 488 GHGVGSFLNVHEGPCGIsYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPAKTKYNF 551
Cdd:cd01085 161 GHGVGSFLNVHEGPQSI-SPAPNNVPLKAGMILSNEPGYYKEGKYGIRIENLVLVVEAETTEFG 223
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
183-566 |
5.55e-72 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 233.94 E-value: 5.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 183 ADLRLKMAERSIVWFVVTALDEIAWLFNLRGSdvehnPVFFSYAIIGLE-RIMLFIDGdridapgvkqhllldlgLEAEY 261
Cdd:COG0006 1 ARLRALMAEAGLDALLLTDPSNFAYLTGFRGS-----PERLAALLVTADgEPVLFVDE-----------------LEAER 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 262 KIQVLPykSILSELKtlcadlsprekvwvsdkasyavseaipkdhrccmpytpiciakAVKNSAESAGMRRAHIKDAVAL 341
Cdd:COG0006 59 ELVDAS--DLLEELR-------------------------------------------AIKSPEEIELMRKAARIADAAH 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 342 CELFNWLEQevpkgGVTEISAADKAEEFRRQQaDFVDLSFPTISSTGPNGAIIHYAPipeTNRTLSLDEVYLIDSGAQYK 421
Cdd:COG0006 94 EAALAALRP-----GVTEREVAAELEAAMRRR-GAEGPSFDTIVASGENAAIPHYTP---TDRPLKPGDLVLIDAGAEYD 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 422 DGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVfPTGTKGHLLDSFARSALWDSGL--DYLHGTGHGVGsfLNVHE 499
Cdd:COG0006 165 GYTSDITRTVAVGEPSDEQREIYEAVLEAQEAAIAAL-KPGVTGGEVDAAARDVLAEAGYgeYFPHGTGHGVG--LDVHE 241
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18777778 500 GPcgiSYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPAKtkynfnnrgsltFEPLTLVP 566
Cdd:COG0006 242 GP---QISPGNDRPLEPGMVFTIEPGIYIPGIGGVRIEDTVLVTEDG------------AEVLTRLP 293
|
|
| Creatinase_N_2 |
pfam16189 |
Creatinase/Prolidase N-terminal domain; |
157-326 |
2.37e-65 |
|
Creatinase/Prolidase N-terminal domain;
Pssm-ID: 465053 Cd Length: 159 Bit Score: 211.20 E-value: 2.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 157 DRPERPCKPLLTLGLDYTGISWKEKVADLRLKMAERSIVWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLERIMLF 236
Cdd:pfam16189 1 DRPALPANPVFVLPLKYAGESAAEKLARLREALKEKGADALVLSALDEIAWLLNLRGSDVPYNPVFLSYALVTDDEATLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 237 IDGDRIDaPGVKQHLlldlgleAEYKIQVLPYKSILSELKTLCADlsprEKVWV-SDKASYAVSEAIPKDHRCCMPYTPI 315
Cdd:pfam16189 81 VDPEKLS-DEVRAHL-------EENGVEIRPYDDIYEDLAALAAG----KKVLLdPSRTSYALYSALPAGAKVVEAPSPI 148
|
170
....*....|.
gi 18777778 316 CIAKAVKNSAE 326
Cdd:pfam16189 149 TLMKAVKNETE 159
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
328-544 |
1.20e-62 |
|
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: 205.94 E-value: 1.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 328 AGMRRAHIKDAVALCELFNWLeqevpKGGVTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPipeTNRTLS 407
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAI-----RPGVTERELAAELEAARLRRGGARGPAFPPIVASGPNAAIPHYIP---NDRVLK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 408 LDEVYLIDSGAQYKDG-TTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPtGTKGHLLDSFARSALWDSGLD--YL 484
Cdd:pfam00557 73 PGDLVLIDVGAEYDGGyCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKP-GVTGGDVDAAAREVLEEAGLGeyFP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18777778 485 HGTGHGVGsfLNVHEGPcgISYKTFSDEPLEAGMIVTDEPGYYE-DGAFGIRIENVVLVVP 544
Cdd:pfam00557 152 HGLGHGIG--LEVHEGP--YISRGGDDRVLEPGMVFTIEPGIYFiPGWGGVRIEDTVLVTE 208
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
333-542 |
3.09e-41 |
|
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: 148.43 E-value: 3.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 333 AHIKDAVAL-CELFNWLEqEVPKGGVTEISAADKAE-EFRRQQADfvDLSFPTISSTGPNGAIIHYAPipeTNRTLSLDE 410
Cdd:cd01092 2 ELLRKAARIaDKAFEELL-EFIKPGMTEREVAAELEyFMRKLGAE--GPSFDTIVASGPNSALPHGVP---SDRKIEEGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 411 VYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPtGTKGHLLDSFARSALWDSGL-DYL-HGTG 488
Cdd:cd01092 76 LVLIDFGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKP-GVTAKEVDKAARDVIEEAGYgEYFiHRTG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 18777778 489 HGVGsfLNVHEGPcGISykTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLV 542
Cdd:cd01092 155 HGVG--LEVHEAP-YIS--PGSDDVLEEGMVFTIEPGIYIPGKGGVRIEDDVLV 203
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
328-547 |
9.86e-36 |
|
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: 133.35 E-value: 9.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 328 AGMRRAHIKDAVALCELFNWLeqevpKGGVTEISAAdkAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPipeTNRTLS 407
Cdd:cd01066 2 ARLRKAAEIAEAAMAAAAEAI-----RPGVTEAEVA--AAIEQALRAAGGYPAGPTIVGSGARTALPHYRP---DDRRLQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 408 LDEVYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPtGTKGHLLDSFARSALWDSGL--DYLH 485
Cdd:cd01066 72 EGDLVLVDLGGVYDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALRP-GVTAEEVDAAAREVLEEHGLgpNFGH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18777778 486 GTGHGVGsfLNVHEGPcgiSYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPAKT 547
Cdd:cd01066 151 RTGHGIG--LEIHEPP---VLKAGDDTVLEPGMVFAVEPGLYLPGGGGVRIEDTVLVTEDGP 207
|
|
| Peptidase_M24_C |
pfam16188 |
C-terminal region of peptidase_M24; This is a short region at the C-terminus of a number of ... |
557-619 |
9.16e-26 |
|
C-terminal region of peptidase_M24; This is a short region at the C-terminus of a number of metallo-peptidases of the M24 family.
Pssm-ID: 465052 Cd Length: 63 Bit Score: 100.18 E-value: 9.16e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18777778 557 LTFEPLTLVPIQTKMIDVDALTDKECDWLNSYHQTCRDVIGKELQTQGrqEALEWLLRETEPI 619
Cdd:pfam16188 3 LGFETLTLVPIDRKLIDVSLLTEEEIEWLNAYHARVREKLSPLLEEEE--DALEWLKRATRPI 63
|
|
| PRK09795 |
PRK09795 |
aminopeptidase; Provisional |
356-544 |
4.75e-19 |
|
aminopeptidase; Provisional
Pssm-ID: 182080 [Multi-domain] Cd Length: 361 Bit Score: 89.23 E-value: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 356 GVTEISAADKAEEFRRQQADfVDLSFPTISSTGPNGAIIHYAPipeTNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHF-- 433
Cdd:PRK09795 157 GMSEREIAAELEWFMRQQGA-EKASFDTIVASGWRGALPHGKA---SDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVng 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 434 -GTPTAYEKECFTY--VLKGHIAVSAAVFPtGTKGHLLDSFARSALWDSGL-DYL-HGTGHGVGsfLNVHEGPcgiSYKT 508
Cdd:PRK09795 233 eGVSAESHPLFNVYqiVLQAQLAAISAIRP-GVRCQQVDDAARRVITEAGYgDYFgHNTGHAIG--IEVHEDP---RFSP 306
|
170 180 190
....*....|....*....|....*....|....*.
gi 18777778 509 FSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVP 544
Cdd:PRK09795 307 RDTTTLQPGMLLTVEPGIYLPGQGGVRIEDVVLVTP 342
|
|
| Prolidase |
cd01087 |
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ... |
368-542 |
3.48e-18 |
|
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: 84.16 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 368 EFRRQQADfvdLSFPTISSTGPNGAIIHYApipETNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHF-GTPTAYEKECFTY 446
Cdd:cd01087 38 EFRSRGAR---LAYSYIVAAGSNAAILHYV---HNDQPLKDGDLVLIDAGAEYGGYASDITRTFPVnGKFTDEQRELYEA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 447 VLKGHIAVSAAVFPtGTK---GHLL-DSFARSALWDSGLD----------------YLHGTGHGVGsfLNVHEgpCGISY 506
Cdd:cd01087 112 VLAAQKAAIAACKP-GVSyedIHLLaHRVLAEGLKELGILkgdvdeivesgayakfFPHGLGHYLG--LDVHD--VGGYL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 18777778 507 KTFS-DEPLEAGMIVTDEPGYY---EDGAF-------GIRIENVVLV 542
Cdd:cd01087 187 RYLRrARPLEPGMVITIEPGIYfipDLLDVpeyfrggGIRIEDDVLV 233
|
|
| PRK10879 |
PRK10879 |
proline aminopeptidase P II; Provisional |
322-542 |
1.15e-11 |
|
proline aminopeptidase P II; Provisional
Pssm-ID: 182804 [Multi-domain] Cd Length: 438 Bit Score: 67.06 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 322 KNSAESAGMRRA-------HIKdAVALCE--LFNW-LEQEVpkggvteisaadkAEEFRRQQADFVdlSFPTISSTGPNG 391
Cdd:PRK10879 174 KSPEEIAVLRRAgeisalaHTR-AMEKCRpgMFEYqLEGEI-------------HHEFNRHGARYP--SYNTIVGSGENG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 392 AIIHYApipETNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHF-GTPTAYEKECFTYVLKGhIAVSAAVFPTGT------- 463
Cdd:PRK10879 238 CILHYT---ENESEMRDGDLVLIDAGCEYKGYAGDITRTFPVnGKFTPAQREIYDIVLES-LETSLRLYRPGTsirevtg 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 464 ----------------KG---HLLDSFARSALwdsgldYLHGTGHGVGsfLNVHEgpCGiSYKTFSDEPLEAGMIVTDEP 524
Cdd:PRK10879 314 evvrimvsglvklgilKGdvdQLIAENAHRPF------FMHGLSHWLG--LDVHD--VG-VYGQDRSRILEPGMVLTVEP 382
|
250 260
....*....|....*....|....*..
gi 18777778 525 GYY---------EDGAFGIRIENVVLV 542
Cdd:PRK10879 383 GLYiapdadvpeQYRGIGIRIEDDIVI 409
|
|
| Creatinase_N |
pfam01321 |
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ... |
10-154 |
1.09e-09 |
|
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: 56.54 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 10 LRQLRQAMRNSEcvaepIQAYIIPSGDahqseyiapcdcRRAFVSGFDGSAGTAI-ITEEHAAMWTD-GRYFLQAAKQmd 87
Cdd:pfam01321 2 LEKLRKLMEEKG-----LDAALVTSPE------------NLRYLTGFTGSRGLLLlVTADGALLLVDaLEYERAAAES-- 62
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18777778 88 nnWTLMKM-GLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAghHLVPVkENLVDKI 154
Cdd:pfam01321 63 --APDFDVvPYRDYEALADLLKELGAGGKRVGFEADALTVAFYEALKEALPGA--ELVDV-SGLIERL 125
|
|
| PRK15173 |
PRK15173 |
peptidase; Provisional |
359-542 |
7.12e-07 |
|
peptidase; Provisional
Pssm-ID: 185095 [Multi-domain] Cd Length: 323 Bit Score: 51.64 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 359 EISAADKAEEFRRQQADFVDLSFPTIsstgpnGAIIHYAPIPETNRTLSLDEVYLiDSGAQYKDGTTDVTRTMHFGTPTA 438
Cdd:PRK15173 130 ELTAAYKAAVMSKSETHFSRFHLISV------GADFSPKLIPSNTKACSGDLIKF-DCGVDVDGYGADIARTFVVGEPPE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 439 YEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSfARSALWDSGL-DYLHG-TGHGVGSFLNVHEGPCgisYKTFSDEPLEA 516
Cdd:PRK15173 203 ITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDS-TMEVIKKSGLpNYNRGhLGHGNGVFLGLEESPF---VSTHATESFTS 278
|
170 180
....*....|....*....|....*.
gi 18777778 517 GMIVTDEPGYYEDGAFGIRIENVVLV 542
Cdd:PRK15173 279 GMVLSLETPYYGYNLGSIMIEDMILI 304
|
|
| PRK14575 |
PRK14575 |
putative peptidase; Provisional |
359-542 |
1.22e-06 |
|
putative peptidase; Provisional
Pssm-ID: 173039 [Multi-domain] Cd Length: 406 Bit Score: 51.25 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 359 EISAADKAEEFRRQQADFVDLSFPTIsstgpnGAIIHYAPIPETNRTLSLDEVYLiDSGAQYKDGTTDVTRTMHFGTPTA 438
Cdd:PRK14575 213 ELTAAYKAAVMSKSETHFSRFHLISV------GADFSPKLIPSNTKACSGDLIKF-DCGVDVDGYGADIARTFVVGEPPE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 439 YEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSfARSALWDSGL-DYLHG-TGHGVGSFLNVHEGPcgiSYKTFSDEPLEA 516
Cdd:PRK14575 286 ITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDS-TMEVIKKSGLpNYNRGhLGHGNGVFLGLEESP---FVSTHATESFTS 361
|
170 180
....*....|....*....|....*.
gi 18777778 517 GMIVTDEPGYYEDGAFGIRIENVVLV 542
Cdd:PRK14575 362 GMVLSLETPYYGYNLGSIMIEDMILI 387
|
|
| PRK14576 |
PRK14576 |
putative endopeptidase; Provisional |
415-542 |
1.84e-04 |
|
putative endopeptidase; Provisional
Pssm-ID: 173040 [Multi-domain] Cd Length: 405 Bit Score: 44.24 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18777778 415 DSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSfARSALWDSGLDYLH--GTGHGVG 492
Cdd:PRK14576 261 DCGIDVAGYGADLARTFVLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVFDS-TMAVIKTSGLPHYNrgHLGHGDG 339
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 18777778 493 SFLNVHEGPcgiSYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLV 542
Cdd:PRK14576 340 VFLGLEEVP---FVSTQATETFCPGMVLSLETPYYGIGVGSIMLEDMILI 386
|
|
|