|
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 ... |
314-532 |
1.65e-123 |
|
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: 364.19 E-value: 1.65e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 314 LKASHVRDAVAVIQYLVWLEKNVPKG-TVDEFSGAEHIDQLRRNENFSSGPSFETISASGLNAALAHYSPTKELHRKLSL 392
Cdd:cd01085 2 MRAAHIRDGVALVEFLAWLEQEVPKGeTITELSAADKLEEFRRQQKGYVGLSFDTISGFGPNGAIVHYSPTEESNRKISP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 393 DEMYLVDSGGQYWDGTTDITRTVHWGTPTAFQKEAYTRVLMGNIDLSRLVFPAATSGRVVEAFARRALWEVGLNYGHGTG 472
Cdd:cd01085 82 DGLYLIDSGGQYLDGTTDITRTVHLGEPTAEQKRDYTLVLKGHIALARAKFPKGTTGSQLDALARQPLWKAGLDYGHGTG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806523 473 HGIGNFLCVHEWPVG--FQYNNMAMAKGMFTSIEPGYYQDGEFGIRLEDVALVVEAKTKYPG 532
Cdd:cd01085 162 HGVGSFLNVHEGPQSisPAPNNVPLKAGMILSNEPGYYKEGKYGIRIENLVLVVEAETTEFG 223
|
|
| Creatinase_N_2 |
pfam16189 |
Creatinase/Prolidase N-terminal domain; |
144-310 |
4.35e-62 |
|
Creatinase/Prolidase N-terminal domain;
:
Pssm-ID: 465053 Cd Length: 159 Bit Score: 202.72 E-value: 4.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 144 ERPPVPSQPIYALPKEFTGSTWQEKVSAIRSYMQNHTmaPTGVLLSALDETAWLFNLRSSDIPYNPFFYSYTLLTDSSIR 223
Cdd:pfam16189 1 DRPALPANPVFVLPLKYAGESAAEKLARLREALKEKG--ADALVLSALDEIAWLLNLRGSDVPYNPVFLSYALVTDDEAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 224 LFVNKSRFSLETLQYLNTNctlpmCVQLEDYSQIRDGVKAYASGnVKILIGISYTTYGVYDVIPKEKLVTETYSPVMLIK 303
Cdd:pfam16189 79 LFVDPEKLSDEVRAHLEEN-----GVEIRPYDDIYEDLAALAAG-KKVLLDPSRTSYALYSALPAGAKVVEAPSPITLMK 152
|
....*..
gi 1958806523 304 AVKNSKE 310
Cdd:pfam16189 153 AVKNETE 159
|
|
| Peptidase_M24_C |
pfam16188 |
C-terminal region of peptidase_M24; This is a short region at the C-terminus of a number of ... |
533-597 |
1.16e-22 |
|
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: 91.32 E-value: 1.16e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806523 533 TYLTFELVSFVPYDRNLIDVSLLSPEQLQYLNRYYQTIRENIGPELQRRQllEEFAWLERHTEPL 597
Cdd:pfam16188 1 PFLGFETLTLVPIDRKLIDVSLLTEEEIEWLNAYHARVREKLSPLLEEEE--DALEWLKRATRPI 63
|
|
| Creatinase_N |
pfam01321 |
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ... |
2-126 |
1.15e-16 |
|
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: 76.57 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 2 RLAALRQQMEKSNLSAYIIPDtdahmseyigkhDERRAWISGFTGSAGTA-VVTKKKAAVWTD-SRYWTQAeRQMDCNWE 79
Cdd:pfam01321 1 RLEKLRKLMEEKGLDAALVTS------------PENLRYLTGFTGSRGLLlLVTADGALLLVDaLEYERAA-AESAPDFD 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958806523 80 LHKEVSISSIVAWILAEVPDGENVGFDPFLFSVGSWENYDQELQDSN 126
Cdd:pfam01321 68 VVPYRDYEALADLLKELGAGGKRVGFEADALTVAFYEALKEALPGAE 114
|
|
| |
|
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 ... |
314-532 |
1.65e-123 |
|
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: 364.19 E-value: 1.65e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 314 LKASHVRDAVAVIQYLVWLEKNVPKG-TVDEFSGAEHIDQLRRNENFSSGPSFETISASGLNAALAHYSPTKELHRKLSL 392
Cdd:cd01085 2 MRAAHIRDGVALVEFLAWLEQEVPKGeTITELSAADKLEEFRRQQKGYVGLSFDTISGFGPNGAIVHYSPTEESNRKISP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 393 DEMYLVDSGGQYWDGTTDITRTVHWGTPTAFQKEAYTRVLMGNIDLSRLVFPAATSGRVVEAFARRALWEVGLNYGHGTG 472
Cdd:cd01085 82 DGLYLIDSGGQYLDGTTDITRTVHLGEPTAEQKRDYTLVLKGHIALARAKFPKGTTGSQLDALARQPLWKAGLDYGHGTG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806523 473 HGIGNFLCVHEWPVG--FQYNNMAMAKGMFTSIEPGYYQDGEFGIRLEDVALVVEAKTKYPG 532
Cdd:cd01085 162 HGVGSFLNVHEGPQSisPAPNNVPLKAGMILSNEPGYYKEGKYGIRIENLVLVVEAETTEFG 223
|
|
| Creatinase_N_2 |
pfam16189 |
Creatinase/Prolidase N-terminal domain; |
144-310 |
4.35e-62 |
|
Creatinase/Prolidase N-terminal domain;
Pssm-ID: 465053 Cd Length: 159 Bit Score: 202.72 E-value: 4.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 144 ERPPVPSQPIYALPKEFTGSTWQEKVSAIRSYMQNHTmaPTGVLLSALDETAWLFNLRSSDIPYNPFFYSYTLLTDSSIR 223
Cdd:pfam16189 1 DRPALPANPVFVLPLKYAGESAAEKLARLREALKEKG--ADALVLSALDEIAWLLNLRGSDVPYNPVFLSYALVTDDEAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 224 LFVNKSRFSLETLQYLNTNctlpmCVQLEDYSQIRDGVKAYASGnVKILIGISYTTYGVYDVIPKEKLVTETYSPVMLIK 303
Cdd:pfam16189 79 LFVDPEKLSDEVRAHLEEN-----GVEIRPYDDIYEDLAALAAG-KKVLLDPSRTSYALYSALPAGAKVVEAPSPITLMK 152
|
....*..
gi 1958806523 304 AVKNSKE 310
Cdd:pfam16189 153 AVKNETE 159
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
282-531 |
3.79e-59 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 200.05 E-value: 3.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 282 VYDVIPKEKLVTETYSPVMLIKAVKNSKEQALLKASHVRDAVAVIQYLVWLEKNVPKGTVdefsgAEHIDQLRRNENFSs 361
Cdd:COG0006 50 FVDELEAERELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRPGVTEREV-----AAELEAAMRRRGAE- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 362 GPSFETISASGLNAALAHYSPTkelHRKLSLDEMYLVDSGGQYWDGTTDITRTVHWGTPTAFQKEAYTRVLMGNIDLSRL 441
Cdd:COG0006 124 GPSFDTIVASGENAAIPHYTPT---DRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYEAVLEAQEAAIAA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 442 VfPAATSGRVVEAFARRALWEVGL--NYGHGTGHGIGnfLCVHEWPVGFQYNNMAMAKGMFTSIEPGYYQDGEFGIRLED 519
Cdd:COG0006 201 L-KPGVTGGEVDAAARDVLAEAGYgeYFPHGTGHGVG--LDVHEGPQISPGNDRPLEPGMVFTIEPGIYIPGIGGVRIED 277
|
250
....*....|....*.
gi 1958806523 520 VALVVEAK----TKYP 531
Cdd:COG0006 278 TVLVTEDGaevlTRLP 293
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
312-525 |
2.68e-49 |
|
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: 170.50 E-value: 2.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 312 ALLKASHVRDAVAVIQYLVWLEKNVpkgtvDEFSGAEHIDQLRRNENFSSGPSFETISASGLNAALAHYSPTKelhRKLS 391
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAIRPGV-----TERELAAELEAARLRRGGARGPAFPPIVASGPNAAIPHYIPND---RVLK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 392 LDEMYLVDSGGQYWDG-TTDITRTVHWGTPTAFQKEAYTRVLMGNIDLSRLVFPAATSGRVVEAfARRALWEVGL--NYG 468
Cdd:pfam00557 73 PGDLVLIDVGAEYDGGyCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAA-AREVLEEAGLgeYFP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958806523 469 HGTGHGIGnfLCVHEWP-VGFQYNNMAMAKGMFTSIEPGYYQ-DGEFGIRLEDVALVVE 525
Cdd:pfam00557 152 HGLGHGIG--LEVHEGPyISRGGDDRVLEPGMVFTIEPGIYFiPGWGGVRIEDTVLVTE 208
|
|
| Peptidase_M24_C |
pfam16188 |
C-terminal region of peptidase_M24; This is a short region at the C-terminus of a number of ... |
533-597 |
1.16e-22 |
|
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: 91.32 E-value: 1.16e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806523 533 TYLTFELVSFVPYDRNLIDVSLLSPEQLQYLNRYYQTIRENIGPELQRRQllEEFAWLERHTEPL 597
Cdd:pfam16188 1 PFLGFETLTLVPIDRKLIDVSLLTEEEIEWLNAYHARVREKLSPLLEEEE--DALEWLKRATRPI 63
|
|
| Creatinase_N |
pfam01321 |
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ... |
2-126 |
1.15e-16 |
|
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: 76.57 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 2 RLAALRQQMEKSNLSAYIIPDtdahmseyigkhDERRAWISGFTGSAGTA-VVTKKKAAVWTD-SRYWTQAeRQMDCNWE 79
Cdd:pfam01321 1 RLEKLRKLMEEKGLDAALVTS------------PENLRYLTGFTGSRGLLlLVTADGALLLVDaLEYERAA-AESAPDFD 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958806523 80 LHKEVSISSIVAWILAEVPDGENVGFDPFLFSVGSWENYDQELQDSN 126
Cdd:pfam01321 68 VVPYRDYEALADLLKELGAGGKRVGFEADALTVAFYEALKEALPGAE 114
|
|
| PRK09795 |
PRK09795 |
aminopeptidase; Provisional |
364-525 |
3.30e-16 |
|
aminopeptidase; Provisional
Pssm-ID: 182080 [Multi-domain] Cd Length: 361 Bit Score: 80.75 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 364 SFETISASGLNAALAHyspTKELHRKLSLDEMYLVDSGGQYWDGTTDITRTVhW----GTPTAFQK--EAYTRVLMGNID 437
Cdd:PRK09795 180 SFDTIVASGWRGALPH---GKASDKIVAAGEFVTLDFGALYQGYCSDMTRTL-LvngeGVSAESHPlfNVYQIVLQAQLA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 438 LSRLVFPAaTSGRVVEAFARRALWEVGLN--YGHGTGHGIGnfLCVHEWPVGFQYNNMAMAKGMFTSIEPGYYQDGEFGI 515
Cdd:PRK09795 256 AISAIRPG-VRCQQVDDAARRVITEAGYGdyFGHNTGHAIG--IEVHEDPRFSPRDTTTLQPGMLLTVEPGIYLPGQGGV 332
|
170
....*....|
gi 1958806523 516 RLEDVALVVE 525
Cdd:PRK09795 333 RIEDVVLVTP 342
|
|
| |
|
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 ... |
314-532 |
1.65e-123 |
|
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: 364.19 E-value: 1.65e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 314 LKASHVRDAVAVIQYLVWLEKNVPKG-TVDEFSGAEHIDQLRRNENFSSGPSFETISASGLNAALAHYSPTKELHRKLSL 392
Cdd:cd01085 2 MRAAHIRDGVALVEFLAWLEQEVPKGeTITELSAADKLEEFRRQQKGYVGLSFDTISGFGPNGAIVHYSPTEESNRKISP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 393 DEMYLVDSGGQYWDGTTDITRTVHWGTPTAFQKEAYTRVLMGNIDLSRLVFPAATSGRVVEAFARRALWEVGLNYGHGTG 472
Cdd:cd01085 82 DGLYLIDSGGQYLDGTTDITRTVHLGEPTAEQKRDYTLVLKGHIALARAKFPKGTTGSQLDALARQPLWKAGLDYGHGTG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806523 473 HGIGNFLCVHEWPVG--FQYNNMAMAKGMFTSIEPGYYQDGEFGIRLEDVALVVEAKTKYPG 532
Cdd:cd01085 162 HGVGSFLNVHEGPQSisPAPNNVPLKAGMILSNEPGYYKEGKYGIRIENLVLVVEAETTEFG 223
|
|
| Creatinase_N_2 |
pfam16189 |
Creatinase/Prolidase N-terminal domain; |
144-310 |
4.35e-62 |
|
Creatinase/Prolidase N-terminal domain;
Pssm-ID: 465053 Cd Length: 159 Bit Score: 202.72 E-value: 4.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 144 ERPPVPSQPIYALPKEFTGSTWQEKVSAIRSYMQNHTmaPTGVLLSALDETAWLFNLRSSDIPYNPFFYSYTLLTDSSIR 223
Cdd:pfam16189 1 DRPALPANPVFVLPLKYAGESAAEKLARLREALKEKG--ADALVLSALDEIAWLLNLRGSDVPYNPVFLSYALVTDDEAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 224 LFVNKSRFSLETLQYLNTNctlpmCVQLEDYSQIRDGVKAYASGnVKILIGISYTTYGVYDVIPKEKLVTETYSPVMLIK 303
Cdd:pfam16189 79 LFVDPEKLSDEVRAHLEEN-----GVEIRPYDDIYEDLAALAAG-KKVLLDPSRTSYALYSALPAGAKVVEAPSPITLMK 152
|
....*..
gi 1958806523 304 AVKNSKE 310
Cdd:pfam16189 153 AVKNETE 159
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
282-531 |
3.79e-59 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 200.05 E-value: 3.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 282 VYDVIPKEKLVTETYSPVMLIKAVKNSKEQALLKASHVRDAVAVIQYLVWLEKNVPKGTVdefsgAEHIDQLRRNENFSs 361
Cdd:COG0006 50 FVDELEAERELVDASDLLEELRAIKSPEEIELMRKAARIADAAHEAALAALRPGVTEREV-----AAELEAAMRRRGAE- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 362 GPSFETISASGLNAALAHYSPTkelHRKLSLDEMYLVDSGGQYWDGTTDITRTVHWGTPTAFQKEAYTRVLMGNIDLSRL 441
Cdd:COG0006 124 GPSFDTIVASGENAAIPHYTPT---DRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYEAVLEAQEAAIAA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 442 VfPAATSGRVVEAFARRALWEVGL--NYGHGTGHGIGnfLCVHEWPVGFQYNNMAMAKGMFTSIEPGYYQDGEFGIRLED 519
Cdd:COG0006 201 L-KPGVTGGEVDAAARDVLAEAGYgeYFPHGTGHGVG--LDVHEGPQISPGNDRPLEPGMVFTIEPGIYIPGIGGVRIED 277
|
250
....*....|....*.
gi 1958806523 520 VALVVEAK----TKYP 531
Cdd:COG0006 278 TVLVTEDGaevlTRLP 293
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
312-525 |
2.68e-49 |
|
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: 170.50 E-value: 2.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 312 ALLKASHVRDAVAVIQYLVWLEKNVpkgtvDEFSGAEHIDQLRRNENFSSGPSFETISASGLNAALAHYSPTKelhRKLS 391
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAIRPGV-----TERELAAELEAARLRRGGARGPAFPPIVASGPNAAIPHYIPND---RVLK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 392 LDEMYLVDSGGQYWDG-TTDITRTVHWGTPTAFQKEAYTRVLMGNIDLSRLVFPAATSGRVVEAfARRALWEVGL--NYG 468
Cdd:pfam00557 73 PGDLVLIDVGAEYDGGyCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAA-AREVLEEAGLgeYFP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958806523 469 HGTGHGIGnfLCVHEWP-VGFQYNNMAMAKGMFTSIEPGYYQ-DGEFGIRLEDVALVVE 525
Cdd:pfam00557 152 HGLGHGIG--LEVHEGPyISRGGDDRVLEPGMVFTIEPGIYFiPGWGGVRIEDTVLVTE 208
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
361-525 |
9.84e-36 |
|
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: 133.40 E-value: 9.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 361 SGPSFETISASGLNAALAHYSPTKelhRKLSLDEMYLVDSGGqYWDG-TTDITRTVHWGTPTAFQKEAYTRVLMGN---I 436
Cdd:cd01092 45 EGPSFDTIVASGPNSALPHGVPSD---RKIEEGDLVLIDFGA-IYDGyCSDITRTVAVGEPSDELKEIYEIVLEAQqaaI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 437 DLSRlvfPAATsGRVVEAFARRALWEVGL--NYGHGTGHGIGnfLCVHEWPVGFQYNNMAMAKGMFTSIEPGYYQDGEFG 514
Cdd:cd01092 121 KAVK---PGVT-AKEVDKAARDVIEEAGYgeYFIHRTGHGVG--LEVHEAPYISPGSDDVLEEGMVFTIEPGIYIPGKGG 194
|
170
....*....|.
gi 1958806523 515 IRLEDVALVVE 525
Cdd:cd01092 195 VRIEDDVLVTE 205
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
361-528 |
2.51e-30 |
|
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: 118.33 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 361 SGPSFETISASGLNAALAHYSPTkelHRKLSLDEMYLVDSGGQYWDGTTDITRTVHWGTPTAFQKEAYTRVLMGNIDLSR 440
Cdd:cd01066 44 GYPAGPTIVGSGARTALPHYRPD---DRRLQEGDLVLVDLGGVYDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 441 LVFPAATsGRVVEAFARRAL--WEVGLNYGHGTGHGIGnfLCVHEWPVGFQYNNMAMAKGMFTSIEPGYYQDGEFGIRLE 518
Cdd:cd01066 121 ALRPGVT-AEEVDAAAREVLeeHGLGPNFGHRTGHGIG--LEIHEPPVLKAGDDTVLEPGMVFAVEPGLYLPGGGGVRIE 197
|
170
....*....|
gi 1958806523 519 DVALVVEAKT 528
Cdd:cd01066 198 DTVLVTEDGP 207
|
|
| Peptidase_M24_C |
pfam16188 |
C-terminal region of peptidase_M24; This is a short region at the C-terminus of a number of ... |
533-597 |
1.16e-22 |
|
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: 91.32 E-value: 1.16e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806523 533 TYLTFELVSFVPYDRNLIDVSLLSPEQLQYLNRYYQTIRENIGPELQRRQllEEFAWLERHTEPL 597
Cdd:pfam16188 1 PFLGFETLTLVPIDRKLIDVSLLTEEEIEWLNAYHARVREKLSPLLEEEE--DALEWLKRATRPI 63
|
|
| Creatinase_N |
pfam01321 |
Creatinase/Prolidase N-terminal domain; This family includes the N-terminal non-catalytic ... |
2-126 |
1.15e-16 |
|
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: 76.57 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 2 RLAALRQQMEKSNLSAYIIPDtdahmseyigkhDERRAWISGFTGSAGTA-VVTKKKAAVWTD-SRYWTQAeRQMDCNWE 79
Cdd:pfam01321 1 RLEKLRKLMEEKGLDAALVTS------------PENLRYLTGFTGSRGLLlLVTADGALLLVDaLEYERAA-AESAPDFD 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958806523 80 LHKEVSISSIVAWILAEVPDGENVGFDPFLFSVGSWENYDQELQDSN 126
Cdd:pfam01321 68 VVPYRDYEALADLLKELGAGGKRVGFEADALTVAFYEALKEALPGAE 114
|
|
| PRK09795 |
PRK09795 |
aminopeptidase; Provisional |
364-525 |
3.30e-16 |
|
aminopeptidase; Provisional
Pssm-ID: 182080 [Multi-domain] Cd Length: 361 Bit Score: 80.75 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 364 SFETISASGLNAALAHyspTKELHRKLSLDEMYLVDSGGQYWDGTTDITRTVhW----GTPTAFQK--EAYTRVLMGNID 437
Cdd:PRK09795 180 SFDTIVASGWRGALPH---GKASDKIVAAGEFVTLDFGALYQGYCSDMTRTL-LvngeGVSAESHPlfNVYQIVLQAQLA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 438 LSRLVFPAaTSGRVVEAFARRALWEVGLN--YGHGTGHGIGnfLCVHEWPVGFQYNNMAMAKGMFTSIEPGYYQDGEFGI 515
Cdd:PRK09795 256 AISAIRPG-VRCQQVDDAARRVITEAGYGdyFGHNTGHAIG--IEVHEDPRFSPRDTTTLQPGMLLTVEPGIYLPGQGGV 332
|
170
....*....|
gi 1958806523 516 RLEDVALVVE 525
Cdd:PRK09795 333 RIEDVVLVTP 342
|
|
| Prolidase |
cd01087 |
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ... |
363-525 |
2.61e-15 |
|
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: 75.69 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 363 PSFETISASGLNAALAHYSptkELHRKLSLDEMYLVDSGGQYWDGTTDITRTvhW---GTPTAFQKEAYTRVLMGNIDLS 439
Cdd:cd01087 46 LAYSYIVAAGSNAAILHYV---HNDQPLKDGDLVLIDAGAEYGGYASDITRT--FpvnGKFTDEQRELYEAVLAAQKAAI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 440 RLVFPAATSGRVVEAFARRA---LWEVGLNYG----------------HGTGHGIGnfLCVHEWPVGFQYNNMAM--AKG 498
Cdd:cd01087 121 AACKPGVSYEDIHLLAHRVLaegLKELGILKGdvdeivesgayakffpHGLGHYLG--LDVHDVGGYLRYLRRARplEPG 198
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958806523 499 MFTSIEPGYYQDGEF----------GIRLEDVALVVE 525
Cdd:cd01087 199 MVITIEPGIYFIPDLldvpeyfrggGIRIEDDVLVTE 235
|
|
| PRK10879 |
PRK10879 |
proline aminopeptidase P II; Provisional |
363-526 |
7.15e-08 |
|
proline aminopeptidase P II; Provisional
Pssm-ID: 182804 [Multi-domain] Cd Length: 438 Bit Score: 55.12 E-value: 7.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 363 PSFETISASGLNAALAHYSptkELHRKLSLDEMYLVDSGGQYWDGTTDITRT--VHwGTPTAFQKEAYTRVLmGNIDLSR 440
Cdd:PRK10879 225 PSYNTIVGSGENGCILHYT---ENESEMRDGDLVLIDAGCEYKGYAGDITRTfpVN-GKFTPAQREIYDIVL-ESLETSL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 441 LVFPAATSGRVVEAFARR----ALWEVGLNYG----------------HGTGHGIGnfLCVHEwpVGF--QYNNMAMAKG 498
Cdd:PRK10879 300 RLYRPGTSIREVTGEVVRimvsGLVKLGILKGdvdqliaenahrpffmHGLSHWLG--LDVHD--VGVygQDRSRILEPG 375
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958806523 499 MFTSIEPGYY--QDGE-------FGIRLEDVALVVEA 526
Cdd:PRK10879 376 MVLTVEPGLYiaPDADvpeqyrgIGIRIEDDIVITET 412
|
|
| PRK15173 |
PRK15173 |
peptidase; Provisional |
410-537 |
4.40e-05 |
|
peptidase; Provisional
Pssm-ID: 185095 [Multi-domain] Cd Length: 323 Bit Score: 45.86 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 410 DITRTVHWGTPTAFQKEAYTRVLMGNIDLSRLVFPAATSGRVVEAfARRALWEVGL-NYGHG-TGHGIGNFLCVHEWPVG 487
Cdd:PRK15173 190 DIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDS-TMEVIKKSGLpNYNRGhLGHGNGVFLGLEESPFV 268
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1958806523 488 FQYNNMAMAKGMFTSIEPGYYQDGEFGIRLEDVALV----VEAKTKYPGTYLTF 537
Cdd:PRK15173 269 STHATESFTSGMVLSLETPYYGYNLGSIMIEDMILInkegIEFLSKLPRDLVSF 322
|
|
| PRK14575 |
PRK14575 |
putative peptidase; Provisional |
410-537 |
6.59e-05 |
|
putative peptidase; Provisional
Pssm-ID: 173039 [Multi-domain] Cd Length: 406 Bit Score: 45.85 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 410 DITRTVHWGTPTAFQKEAYTRVLMGNIDLSRLVFPAATSGRVVEAfARRALWEVGL-NYGHG-TGHGIGNFLCVHEWPVG 487
Cdd:PRK14575 273 DIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDS-TMEVIKKSGLpNYNRGhLGHGNGVFLGLEESPFV 351
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1958806523 488 FQYNNMAMAKGMFTSIEPGYYQDGEFGIRLEDVALV----VEAKTKYPGTYLTF 537
Cdd:PRK14575 352 STHATESFTSGMVLSLETPYYGYNLGSIMIEDMILInkegIEFLSKLPRDLVSF 405
|
|
| PRK14576 |
PRK14576 |
putative endopeptidase; Provisional |
410-530 |
2.06e-03 |
|
putative endopeptidase; Provisional
Pssm-ID: 173040 [Multi-domain] Cd Length: 405 Bit Score: 40.77 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806523 410 DITRTVHWGTPTAFQKEAYTRVLMGNIDLSRLVFPAATSGRVVEAfARRALWEVGL---NYGHgTGHGIGNFLCVHEWPV 486
Cdd:PRK14576 272 DLARTFVLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVFDS-TMAVIKTSGLphyNRGH-LGHGDGVFLGLEEVPF 349
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1958806523 487 GFQYNNMAMAKGMFTSIEPGYYQDGEFGIRLEDVALVVEAKTKY 530
Cdd:PRK14576 350 VSTQATETFCPGMVLSLETPYYGIGVGSIMLEDMILITDSGFEF 393
|
|
| HemE |
COG0407 |
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ... |
415-475 |
4.24e-03 |
|
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440176 [Multi-domain] Cd Length: 336 Bit Score: 39.82 E-value: 4.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806523 415 VHWGTPTAFQKEAY--TRVLMGNIDLSRLVFPAatSGRVVEAFARRALWEVGLNYGH--GTGHGI 475
Cdd:COG0407 254 VDWRVDLAEAKERLgdKVALQGNLDPALLLLNG--TPEEVEAEVKRILDAGGGGPGHifNLGHGI 316
|
|
| |
