|
Name |
Accession |
Description |
Interval |
E-value |
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
6-257 |
1.60e-162 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 450.23 E-value: 1.60e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 6 VSIKSEQDIEKLRISGRLAAQVLQMIGEHVKPGVTTEYLDDLCHDYIVNtLKVIPANVGYHGYTKTTCISPNEVVCHGIP 85
Cdd:COG0024 1 IEIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRD-HGAIPAFLGYYGFPKSICTSVNEVVVHGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 86 SSKtILKDGDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGF 165
Cdd:COG0024 80 SDR-VLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 166 SIVREYCGHGIGQVYHEQPSVLHYGQPGQGLVLKKGMVFTIEPMVNAGKARVKELKDGWTVVTTDKSLSAQWEHMVAVTD 245
Cdd:COG0024 159 SVVREFVGHGIGREMHEEPQVPNYGRPGRGPRLKPGMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTE 238
|
250
....*....|..
gi 491118278 246 TGFEVLSPWPEG 257
Cdd:COG0024 239 DGPEILTLPDGG 250
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
6-257 |
1.79e-152 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 424.93 E-value: 1.79e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 6 VSIKSEQDIEKLRISGRLAAQVLQMIGEHVKPGVTTEYLDDLCHDYIVNtLKVIPANVGYHGYTKTTCISPNEVVCHGIP 85
Cdd:PRK05716 3 ITIKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKELDRIAEEYIRD-QGAIPAPLGYHGFPKSICTSVNEVVCHGIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 86 SSKtILKDGDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGF 165
Cdd:PRK05716 82 SDK-VLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 166 SIVREYCGHGIGQVYHEQPSVLHYGQPGQGLVLKKGMVFTIEPMVNAGKARVKELKDGWTVVTTDKSLSAQWEHMVAVTD 245
Cdd:PRK05716 161 SVVREYCGHGIGRKFHEEPQIPHYGAPGDGPVLKEGMVFTIEPMINAGKREVKTLKDGWTVVTKDGSLSAQYEHTVAVTE 240
|
250
....*....|..
gi 491118278 246 TGFEVLSPWPEG 257
Cdd:PRK05716 241 DGPEILTLRPEE 252
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
14-252 |
4.44e-136 |
|
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: 383.00 E-value: 4.44e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 14 IEKLRISGRLAAQVLQMIGEHVKPGVTTEYLDDLCHDYIVNtLKVIPANVGYHGYTKTTCISPNEVVCHGIPSsKTILKD 93
Cdd:cd01086 1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEE-HGAYPAPLGYYGFPKSICTSVNEVVCHGIPD-DRVLKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 94 GDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGFSIVREYCG 173
Cdd:cd01086 79 GDIVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491118278 174 HGIGQVYHEQPSVLHYGQPGQGLVLKKGMVFTIEPMVNAGKARVKELKDGWTVVTTDKSLSAQWEHMVAVTDTGFEVLS 252
Cdd:cd01086 159 HGIGRKFHEEPQIPNYGRPGTGPKLKPGMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILT 237
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
6-252 |
1.29e-114 |
|
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: 328.92 E-value: 1.29e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 6 VSIKSEQDIEKLRISGRLAAQVLQMIGEHVKPGVTTEYLDDLCHDYIVNTlKVIPANVGYHGYTKTTCISPNEVVCHGIP 85
Cdd:TIGR00500 1 ISLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKH-GAKPAFLGYYGFPGSVCISVNEVVIHGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 86 SsKTILKDGDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGF 165
Cdd:TIGR00500 80 D-KKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 166 SIVREYCGHGIGQVYHEQPSVLHYGQPGQGLVLKKGMVFTIEPMVNAGKARVKELKDGWTVVTTDKSLSAQWEHMVAVTD 245
Cdd:TIGR00500 159 SVVREYCGHGIGRKFHEEPQIPNYGKKFTNVRLKEGMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITD 238
|
....*..
gi 491118278 246 TGFEVLS 252
Cdd:TIGR00500 239 NGPEILT 245
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
15-245 |
7.31e-58 |
|
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: 183.21 E-value: 7.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 15 EKLRISGRLAAQVLQMIGEHVKPGVTTEYLDDLCHDYIVNTLkvipaNVGYHGYTKTTCISPNEVVCHGIPSsKTILKDG 94
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRG-----GARGPAFPPIVASGPNAAIPHYIPN-DRVLKPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 95 DIINIDV-AVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGFS-IVREYC 172
Cdd:pfam00557 75 DLVLIDVgAEYDGGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGeYFPHGL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491118278 173 GHGIGQVYHEQPSVlhyGQPGQGLVLKKGMVFTIEPMVNAgkarvkelKDGWTvvttdkslSAQWEHMVAVTD 245
Cdd:pfam00557 155 GHGIGLEVHEGPYI---SRGGDDRVLEPGMVFTIEPGIYF--------IPGWG--------GVRIEDTVLVTE 208
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
6-257 |
1.60e-162 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 450.23 E-value: 1.60e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 6 VSIKSEQDIEKLRISGRLAAQVLQMIGEHVKPGVTTEYLDDLCHDYIVNtLKVIPANVGYHGYTKTTCISPNEVVCHGIP 85
Cdd:COG0024 1 IEIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRD-HGAIPAFLGYYGFPKSICTSVNEVVVHGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 86 SSKtILKDGDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGF 165
Cdd:COG0024 80 SDR-VLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 166 SIVREYCGHGIGQVYHEQPSVLHYGQPGQGLVLKKGMVFTIEPMVNAGKARVKELKDGWTVVTTDKSLSAQWEHMVAVTD 245
Cdd:COG0024 159 SVVREFVGHGIGREMHEEPQVPNYGRPGRGPRLKPGMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTE 238
|
250
....*....|..
gi 491118278 246 TGFEVLSPWPEG 257
Cdd:COG0024 239 DGPEILTLPDGG 250
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
6-257 |
1.79e-152 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 424.93 E-value: 1.79e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 6 VSIKSEQDIEKLRISGRLAAQVLQMIGEHVKPGVTTEYLDDLCHDYIVNtLKVIPANVGYHGYTKTTCISPNEVVCHGIP 85
Cdd:PRK05716 3 ITIKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKELDRIAEEYIRD-QGAIPAPLGYHGFPKSICTSVNEVVCHGIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 86 SSKtILKDGDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGF 165
Cdd:PRK05716 82 SDK-VLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 166 SIVREYCGHGIGQVYHEQPSVLHYGQPGQGLVLKKGMVFTIEPMVNAGKARVKELKDGWTVVTTDKSLSAQWEHMVAVTD 245
Cdd:PRK05716 161 SVVREYCGHGIGRKFHEEPQIPHYGAPGDGPVLKEGMVFTIEPMINAGKREVKTLKDGWTVVTKDGSLSAQYEHTVAVTE 240
|
250
....*....|..
gi 491118278 246 TGFEVLSPWPEG 257
Cdd:PRK05716 241 DGPEILTLRPEE 252
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
14-252 |
4.44e-136 |
|
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: 383.00 E-value: 4.44e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 14 IEKLRISGRLAAQVLQMIGEHVKPGVTTEYLDDLCHDYIVNtLKVIPANVGYHGYTKTTCISPNEVVCHGIPSsKTILKD 93
Cdd:cd01086 1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEE-HGAYPAPLGYYGFPKSICTSVNEVVCHGIPD-DRVLKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 94 GDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGFSIVREYCG 173
Cdd:cd01086 79 GDIVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491118278 174 HGIGQVYHEQPSVLHYGQPGQGLVLKKGMVFTIEPMVNAGKARVKELKDGWTVVTTDKSLSAQWEHMVAVTDTGFEVLS 252
Cdd:cd01086 159 HGIGRKFHEEPQIPNYGRPGTGPKLKPGMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILT 237
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
6-252 |
1.29e-114 |
|
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: 328.92 E-value: 1.29e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 6 VSIKSEQDIEKLRISGRLAAQVLQMIGEHVKPGVTTEYLDDLCHDYIVNTlKVIPANVGYHGYTKTTCISPNEVVCHGIP 85
Cdd:TIGR00500 1 ISLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKH-GAKPAFLGYYGFPGSVCISVNEVVIHGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 86 SsKTILKDGDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGF 165
Cdd:TIGR00500 80 D-KKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 166 SIVREYCGHGIGQVYHEQPSVLHYGQPGQGLVLKKGMVFTIEPMVNAGKARVKELKDGWTVVTTDKSLSAQWEHMVAVTD 245
Cdd:TIGR00500 159 SVVREYCGHGIGRKFHEEPQIPNYGKKFTNVRLKEGMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITD 238
|
....*..
gi 491118278 246 TGFEVLS 252
Cdd:TIGR00500 239 NGPEILT 245
|
|
| PRK12896 |
PRK12896 |
methionine aminopeptidase; Reviewed |
6-251 |
3.12e-113 |
|
methionine aminopeptidase; Reviewed
Pssm-ID: 237252 [Multi-domain] Cd Length: 255 Bit Score: 325.64 E-value: 3.12e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 6 VSIKSEQDIEKLRISGRLAAQVLQMIGEHVKPGVTTEYLDDLCHDYIVNtLKVIPANVGYHGYTKTTCISPNEVVCHGIP 85
Cdd:PRK12896 8 MEIKSPRELEKMRKIGRIVATALKEMGKAVEPGMTTKELDRIAEKRLEE-HGAIPSPEGYYGFPGSTCISVNEEVAHGIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 86 SSKtILKDGDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGF 165
Cdd:PRK12896 87 GPR-VIKDGDLVNIDVSAYLDGYHGDTGITFAVGPVSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAIEDFAKKNGY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 166 SIVREYCGHGIGQVYHEQPSV-LHYGQPGQGLVLKKGMVFTIEPMVNAGKARVKELKDGWTVVTTDKSLSAQWEHMVAVT 244
Cdd:PRK12896 166 SVVRDLTGHGVGRSLHEEPSViLTYTDPLPNRLLRPGMTLAVEPFLNLGAKDAETLDDGWTVVTPDKSLSAQFEHTVVVT 245
|
....*..
gi 491118278 245 DTGFEVL 251
Cdd:PRK12896 246 RDGPEIL 252
|
|
| PLN03158 |
PLN03158 |
methionine aminopeptidase; Provisional |
6-252 |
4.91e-80 |
|
methionine aminopeptidase; Provisional
Pssm-ID: 215607 [Multi-domain] Cd Length: 396 Bit Score: 246.29 E-value: 4.91e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 6 VSIKSEQDIEKLRISGRLAAQVLQMIGEHVKPGVTTEYLDDLCHDYIVnTLKVIPANVGYHGYTKTTCISPNEVVCHGIP 85
Cdd:PLN03158 135 VEIKTPEQIQRMRETCRIAREVLDAAARAIKPGVTTDEIDRVVHEATI-AAGGYPSPLNYHFFPKSCCTSVNEVICHGIP 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 86 SSKTiLKDGDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGF 165
Cdd:PLN03158 214 DARK-LEDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEASRQLVKCTYECLEKAIAIVKPGVRYREVGEVINRHATMSGL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 166 SIVREYCGHGIGQVYHEQPSVLHYGQPGQGLVLKKGMVFTIEPMVNAGKARVKELKDGWTVVTTDKSLSAQWEHMVAVTD 245
Cdd:PLN03158 293 SVVKSYCGHGIGELFHCAPNIPHYARNKAVGVMKAGQVFTIEPMINAGVWRDRMWPDGWTAVTADGKRSAQFEHTLLVTE 372
|
....*..
gi 491118278 246 TGFEVLS 252
Cdd:PLN03158 373 TGVEVLT 379
|
|
| PRK12318 |
PRK12318 |
methionyl aminopeptidase; |
8-254 |
2.56e-79 |
|
methionyl aminopeptidase;
Pssm-ID: 183434 [Multi-domain] Cd Length: 291 Bit Score: 240.88 E-value: 2.56e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 8 IKSEQDIEKLRISGRLAAQVLQMIGEHVKPGVTTEYLDDLCHDyIVNTLKVIPA--NVGYHGYTKTTCISPNEVVCHGIP 85
Cdd:PRK12318 43 IKTPEQIEKIRKACQVTARILDALCEAAKEGVTTNELDELSRE-LHKEYNAIPAplNYGSPPFPKTICTSLNEVICHGIP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 86 SSkTILKDGDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGF 165
Cdd:PRK12318 122 ND-IPLKNGDIMNIDVSCIVDGYYGDCSRMVMIGEVSEIKKKVCQASLECLNAAIAILKPGIPLYEIGEVIENCADKYGF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 166 SIVREYCGHGIGQVYHEQPSVLHYgQPGQGLVLKKGMVFTIEPMVNAGKAR-VKELKDGWTVVTTDKSLSAQWEHMVAVT 244
Cdd:PRK12318 201 SVVDQFVGHGVGIKFHENPYVPHH-RNSSKIPLAPGMIFTIEPMINVGKKEgVIDPINHWEARTCDNQPSAQWEHTILIT 279
|
250
....*....|
gi 491118278 245 DTGFEVLSPW 254
Cdd:PRK12318 280 ETGYEILTLL 289
|
|
| PRK12897 |
PRK12897 |
type I methionyl aminopeptidase; |
6-252 |
6.80e-62 |
|
type I methionyl aminopeptidase;
Pssm-ID: 171806 Cd Length: 248 Bit Score: 195.25 E-value: 6.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 6 VSIKSEQDIEKLRISGRLAAQVLQMIGEHVKPGVTTEYLDDLCHDYIvNTLKVIPANVGYHGYTKTTCISPNEVVCHGIP 85
Cdd:PRK12897 2 ITIKTKNEIDLMHESGKLLASCHREIAKIMKPGITTKEINTFVEAYL-EKHGATSEQKGYNGYPYAICASVNDEMCHAFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 86 SSkTILKDGDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGF 165
Cdd:PRK12897 81 AD-VPLTEGDIVTIDMVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNRVGDIGYAIESYVANEGF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 166 SIVREYCGHGIGQVYHEQPSVLHYGQPGQGLVLKKGMVFTIEPMVNAGKARVKELKDGWTVVTTDKSLSAQWEHMVAVTD 245
Cdd:PRK12897 160 SVARDFTGHGIGKEIHEEPAIFHFGKQGQGPELQEGMVITIEPIVNVGMRYSKVDLNGWTARTMDGKLSAQYEHTIAITK 239
|
....*..
gi 491118278 246 TGFEVLS 252
Cdd:PRK12897 240 DGPIILT 246
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
15-245 |
7.31e-58 |
|
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: 183.21 E-value: 7.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 15 EKLRISGRLAAQVLQMIGEHVKPGVTTEYLDDLCHDYIVNTLkvipaNVGYHGYTKTTCISPNEVVCHGIPSsKTILKDG 94
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRG-----GARGPAFPPIVASGPNAAIPHYIPN-DRVLKPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 95 DIINIDV-AVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGFS-IVREYC 172
Cdd:pfam00557 75 DLVLIDVgAEYDGGYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGeYFPHGL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491118278 173 GHGIGQVYHEQPSVlhyGQPGQGLVLKKGMVFTIEPMVNAgkarvkelKDGWTvvttdkslSAQWEHMVAVTD 245
Cdd:pfam00557 155 GHGIGLEVHEGPYI---SRGGDDRVLEPGMVFTIEPGIYF--------IPGWG--------GVRIEDTVLVTE 208
|
|
| PRK07281 |
PRK07281 |
methionyl aminopeptidase; |
6-258 |
2.68e-48 |
|
methionyl aminopeptidase;
Pssm-ID: 180918 Cd Length: 286 Bit Score: 161.55 E-value: 2.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 6 VSIKSEQDIEKLRISGRLAAQVLQMIGEHVKPGV----TTEYLDDLCHDYivntlKVIPANVGYHG----YTKTTCISPN 77
Cdd:PRK07281 2 ITLKSAREIEAMDRAGDFLASIHIGLRDLIKPGVdmweVEEYVRRRCKEE-----NVLPLQIGVDGammdYPYATCCGLN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 78 EVVCHGIPSSKtILKDGDIINID---------------------VAVIKD------GFYGDTSRMYYVGQVKPEAKKLVD 130
Cdd:PRK07281 77 DEVAHAFPRHY-ILKEGDLLKVDmvlsepldksivdvsklnfdnVEQMKKytesyrGGLADSCWAYAVGTPSDEVKNLMD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 131 TTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGFSIVREYCGHGIGQVYHEQPSVLHYGQPGQGLVLKKGMVFTIEPMV 210
Cdd:PRK07281 156 VTKEAMYRGIEQAVVGNRIGDIGAAIQEYAESRGYGVVRDLVGHGVGPTMHEEPMVPNYGTAGRGLRLREGMVLTIEPMI 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 491118278 211 NAGKARV-KELKDGWTVVTTDKSLSAQWEHMVAVTDTGFEVL-SPWPEGT 258
Cdd:PRK07281 236 NTGTWEIdTDMKTGWAHKTLDGGLSCQYEHQFVITKDGPVILtSQGEERT 285
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
14-247 |
4.26e-40 |
|
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: 137.97 E-value: 4.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 14 IEKLRISGRLAAQVLQMIGEHVKPGVTTEYLDDLCHDYIVNtlkvipanvGYHGYTKTTCISPNEV--VCHGIPSSKTIl 91
Cdd:cd01066 1 IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRA---------AGGYPAGPTIVGSGARtaLPHYRPDDRRL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 92 KDGDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGFSIVR-E 170
Cdd:cd01066 71 QEGDLVLVDLGGVYDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLGPNFgH 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491118278 171 YCGHGIGQVYHEQPsvlhYGQPGQGLVLKKGMVFTIEPMVNAGKARvkelkdgwtvvttdkslSAQWEHMVAVTDTG 247
Cdd:cd01066 151 RTGHGIGLEIHEPP----VLKAGDDTVLEPGMVFAVEPGLYLPGGG-----------------GVRIEDTVLVTEDG 206
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
1-255 |
3.30e-37 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 133.02 E-value: 3.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 1 MRAlkvsIKSEQDIEKLRISGRLAAQVLQMIGEHVKPGVTtEY--------------LDDLCHDYIVNTlkvipanvGYH 66
Cdd:COG0006 70 LRA----IKSPEEIELMRKAARIADAAHEAALAALRPGVT-ERevaaeleaamrrrgAEGPSFDTIVAS--------GEN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 67 GytkttcispneVVCHGIPSSKTIlKDGDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPG 146
Cdd:COG0006 137 A-----------AIPHYTPTDRPL-KPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYEAVLEAQEAAIAALKPG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 147 ATLGDIGYAIQSVAHREGFsivREY----CGHGIGQVYHEQPSVlhygQPGQGLVLKKGMVFTIEPMV---NAGKARVke 219
Cdd:COG0006 205 VTGGEVDAAARDVLAEAGY---GEYfphgTGHGVGLDVHEGPQI----SPGNDRPLEPGMVFTIEPGIyipGIGGVRI-- 275
|
250 260 270
....*....|....*....|....*....|....*.
gi 491118278 220 lkdgwtvvttdkslsaqwEHMVAVTDTGFEVLSPWP 255
Cdd:COG0006 276 ------------------EDTVLVTEDGAEVLTRLP 293
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
14-208 |
9.93e-31 |
|
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: 113.37 E-value: 9.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 14 IEKLRISGRLAAQVLQMIGEHVKPGVTtEYlddlchdYIVNTLKVIPANVGYHGYTKTTCIS--PNEVVCHGIPSSKtIL 91
Cdd:cd01092 1 IELLRKAARIADKAFEELLEFIKPGMT-ER-------EVAAELEYFMRKLGAEGPSFDTIVAsgPNSALPHGVPSDR-KI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 92 KDGDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGFSivrEY 171
Cdd:cd01092 72 EEGDLVLIDFGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGYG---EY 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491118278 172 ----CGHGIGQVYHEQPSVlhygQPGQGLVLKKGMVFTIEP 208
Cdd:cd01092 149 fihrTGHGVGLEVHEAPYI----SPGSDDVLEEGMVFTIEP 185
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
14-219 |
3.22e-25 |
|
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and peptidase M. Catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Pssm-ID: 238521 [Multi-domain] Cd Length: 291 Bit Score: 101.17 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 14 IEKLRISGRLAAQVLQMIGEHVKPGVTteyLDDLChDYIVNTLKVIPANVGYhgytkTTCISPNEVVCHGIPSS--KTIL 91
Cdd:cd01088 1 LEKYREAGEIHRQVRKYAQSLIKPGMT---LLEIA-EFVENRIRELGAGPAF-----PVNLSINECAAHYTPNAgdDTVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 92 KDGDIINIDVAVIKDGFYGDTSrmyYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGFSIVREY 171
Cdd:cd01088 72 KEGDVVKLDFGAHVDGYIADSA---FTVDFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIESYGFKPIRNL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491118278 172 CGHGIGQvY--HEQPSVLHYGQPGQGlVLKKGMVFTIEPMVNAGKARVKE 219
Cdd:cd01088 149 TGHSIER-YrlHAGKSIPNVKGGEGT-RLEEGDVYAIEPFATTGKGYVHD 196
|
|
| met_pdase_II |
TIGR00501 |
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ... |
14-219 |
1.13e-22 |
|
methionine aminopeptidase, type II; Methionine aminopeptidase (map) 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. The role of this protein in general is to produce the mature amino end of cytosolic proteins by removing the N-terminal methionine. This model describes type II, among which the eukaryotic members typically have an N-terminal extension not present in archaeal members. It can act cotranslationally. The enzyme from rat has been shown to associate with translation initiation factor 2 (IF-2) and may have a role in translational regulation. [Protein fate, Protein modification and repair]
Pssm-ID: 129592 Cd Length: 295 Bit Score: 94.08 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 14 IEKLRISGRLAAQVLQMIGEHVKPGVTteyLDDLChDYIVNTLKVIPANVGYhgytkTTCISPNEVVCHGIP--SSKTIL 91
Cdd:TIGR00501 5 AEKWIEAGKIHSKVRREAADRIVPGVK---LLEVA-EFVENRIRELGAEPAF-----PCNISINECAAHFTPkaGDKTVF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 92 KDGDIINIDVAVIKDGFYGDTSRMYYVGqvkPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREGFSIVREY 171
Cdd:TIGR00501 76 KDGDVVKLDLGAHVDGYIADTAITVDLG---DQYDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIESYGVKPISNL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491118278 172 CGHGIGQ-VYHEQPSVLHYGQpGQGLVLKKGMVFTIEPMVNAGKARVKE 219
Cdd:TIGR00501 153 TGHSMAPyRLHGGKSIPNVKE-RDTTKLEEGDVVAIEPFATDGVGYVTD 200
|
|
| crvDNA_42K |
TIGR00495 |
42K curved DNA binding protein; Proteins identified by this model have been identified in a ... |
7-232 |
1.07e-13 |
|
42K curved DNA binding protein; Proteins identified by this model have been identified in a number of species as a nuclear (but not nucleolar) protein with a cell cycle dependence. Various names given to members of this family have included cell cycle protein p38-2G4, DNA-binding protein GBP16, and proliferation-associated protein 1. This protein is closely related to methionine aminopeptidase, a cobolt-binding protein. [Unknown function, General]
Pssm-ID: 273105 Cd Length: 390 Bit Score: 69.92 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 7 SIKSEQDIEKLRISGRLAAQVLQMIGEHVKPGVTT----EYLDDLCHDYIVNTLKviPANVGYHGYTKTTCISPNEVVCH 82
Cdd:TIGR00495 13 SLSNPEVVTKYKMAGEIANNVLKSVVEACSPGAKVvdicEKGDAFIMEETAKIFK--KEKEMEKGIAFPTCISVNNCVGH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 83 GIP---SSKTILKDGDIINIDVAVIKDGFYGDTSRMYYVG-----QVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGY 154
Cdd:TIGR00495 91 FSPlksDQDYILKEGDVVKIDLGCHIDGFIALVAHTFVVGvaqeePVTGRKADVIAAAHLAAEAALRLVKPGNTNTQVTE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 155 AIQSVAHREGFSIVREYCGHGIGQ-VYHEQPSVLHYGQPGQGLVLKK-----GMVFTIEPMVNAGKARVKELKDGWTVVT 228
Cdd:TIGR00495 171 AINKVAHSYGCTPVEGMLSHQLKQhVIDGEKVIISNPSDSQKKDHDTaefeeNEVYAVDILVSTGEGKAKDADQRTTIYK 250
|
....
gi 491118278 229 TDKS 232
Cdd:TIGR00495 251 RDPS 254
|
|
| PA2G4-like |
cd01089 |
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ... |
14-253 |
3.89e-13 |
|
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family members have been implicated in cell cycle control.
Pssm-ID: 238522 Cd Length: 228 Bit Score: 66.97 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 14 IEKLRISGRLAAQVLQMIGEHVKPGVTT----EYLDDLCHDYIVNTLKviPANVGYHGYTKTTCISPNEVVCHGIP---S 86
Cdd:cd01089 1 VTKYKTAGQIANKVLKQVISLCVPGAKVvdlcEKGDKLILEELGKVYK--KEKKLEKGIAFPTCISVNNCVCHFSPlksD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 87 SKTILKDGDIINIDVAVIKDGFYGDTSRMYYVGQVKPE-----AKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAH 161
Cdd:cd01089 79 ATYTLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAETpvtgkKADVIAAAHYALEAALRLLRPGNQNSDITEAIQKVIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 162 regfsivrEYCGHGIGQVYHEQpsvlhygqpgqglvLKKGMVFTiepmvnAGKARVKELKDG-----WTVVTT-DKSLSA 235
Cdd:cd01089 159 --------DYGCTPVEGVLSHQ--------------LKRVVSSG------EGKAKLVECVKHgllfpYPVLYEkEGEVVA 210
|
250
....*....|....*...
gi 491118278 236 QWEHMVAVTDTGFEVLSP 253
Cdd:cd01089 211 QFKLTVLLTPNGVTVLTG 228
|
|
| PRK09795 |
PRK09795 |
aminopeptidase; Provisional |
8-256 |
4.25e-11 |
|
aminopeptidase; Provisional
Pssm-ID: 182080 [Multi-domain] Cd Length: 361 Bit Score: 62.26 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 8 IKSEQDIEKLRISGRLAAQVLQMIGEHVKPGVT-------------TEYLDDLCHDYIVNTlkvipanvGYHGytkttci 74
Cdd:PRK09795 127 IKTPEEVEKIRLACGIADRGAEHIRRFIQAGMSereiaaelewfmrQQGAEKASFDTIVAS--------GWRG------- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 75 spneVVCHGIPSSKtILKDGDIINIDVAVIKDGFYGDTSRMYYV-GQVKPEAKKLVDTTY----EAMRAGIHAVKPGATL 149
Cdd:PRK09795 192 ----ALPHGKASDK-IVAAGEFVTLDFGALYQGYCSDMTRTLLVnGEGVSAESHPLFNVYqivlQAQLAAISAIRPGVRC 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 150 GDIGYAIQSVAHREGFSivrEY----CGHGIGQVYHEQPSVlhygQPGQGLVLKKGMVFTIEPMV---NAGKARVkelkd 222
Cdd:PRK09795 267 QQVDDAARRVITEAGYG---DYfghnTGHAIGIEVHEDPRF----SPRDTTTLQPGMLLTVEPGIylpGQGGVRI----- 334
|
250 260 270
....*....|....*....|....*....|....
gi 491118278 223 gwtvvttdkslsaqwEHMVAVTDTGFEVLSPWPE 256
Cdd:PRK09795 335 ---------------EDVVLVTPQGAEVLYAMPK 353
|
|
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
10-219 |
3.19e-10 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 59.73 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 10 SEQDIEKLRISGRLAAQVLQMIGEHVKPGVTteyLDDLCHDYIVNTLKVIPANVGYHGYTKTTCISPNEVVCHGIPSS-- 87
Cdd:PTZ00053 154 SEEQYQDLRRAAEVHRQVRRYAQSVIKPGVK---LIDICERIESKSRELIEADGLKCGWAFPTGCSLNHCAAHYTPNTgd 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 88 KTILKDGDIINIDVAVIKDGFYGDTSrmyYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAhrEGFSI 167
Cdd:PTZ00053 231 KTVLTYDDVCKLDFGTHVNGRIIDCA---FTVAFNPKYDPLLQATKDATNTGIKEAGIDVRLSDIGAAIQEVI--ESYEV 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491118278 168 -----------VREYCGHGIGQvYHeqpsvLHYGQ------PGQGLVLKKGMVFTIEPMVNAGKARVKE 219
Cdd:PTZ00053 306 eikgktypiksIRNLNGHSIGP-YI-----IHGGKsvpivkGGENTRMEEGELFAIETFASTGRGYVNE 368
|
|
| Prolidase |
cd01087 |
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ... |
14-208 |
4.07e-10 |
|
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: 58.35 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 14 IEKLRISGRLAAQVLQMIGEHVKPGVTtEYldDLCHDYIVNTLKVipANVGYHGYTKTTCIspNEVVCHGIPSSKTIlKD 93
Cdd:cd01087 1 IELMRKACDISAEAHRAAMKASRPGMS-EY--ELEAEFEYEFRSR--GARLAYSYIVAAGS--NAAILHYVHNDQPL-KD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 94 GDIINIDVAVIKDGFYGDTSRMYYV-GQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREG--FSIVRE 170
Cdd:cd01087 73 GDLVLIDAGAEYGGYASDITRTFPVnGKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIHLLAHRVLAEGLkeLGILKG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491118278 171 -------------YCGHGIG-----QVyHEQPSVLHYGqpGQGLVLKKGMVFTIEP 208
Cdd:cd01087 153 dvdeivesgayakFFPHGLGhylglDV-HDVGGYLRYL--RRARPLEPGMVITIEP 205
|
|
| PRK10879 |
PRK10879 |
proline aminopeptidase P II; Provisional |
8-208 |
1.33e-07 |
|
proline aminopeptidase P II; Provisional
Pssm-ID: 182804 [Multi-domain] Cd Length: 438 Bit Score: 52.03 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 8 IKSEQDIEKLRISGRLAAQVLQMIGEHVKPGVTTEYLD-DLCHDYIVNTLKvIPANVGYHGYTKTTCI---SPNEvvchg 83
Cdd:PRK10879 173 FKSPEEIAVLRRAGEISALAHTRAMEKCRPGMFEYQLEgEIHHEFNRHGAR-YPSYNTIVGSGENGCIlhyTENE----- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 84 ipsskTILKDGDIINIDVAVIKDGFYGDTSRMYYV-GQVKPEAKKLVDTTYEAMRAGIHAVKPGATL------------- 149
Cdd:PRK10879 247 -----SEMRDGDLVLIDAGCEYKGYAGDITRTFPVnGKFTPAQREIYDIVLESLETSLRLYRPGTSIrevtgevvrimvs 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491118278 150 ---------GDIGYAIQSVAHREGFsivREYCGHGIGQVYHEqpsVLHYGqPGQGLVLKKGMVFTIEP 208
Cdd:PRK10879 322 glvklgilkGDVDQLIAENAHRPFF---MHGLSHWLGLDVHD---VGVYG-QDRSRILEPGMVLTVEP 382
|
|
| Creatinase |
cd01090 |
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea. |
85-210 |
9.43e-07 |
|
Creatine amidinohydrolase. E.C.3.5.3.3. Hydrolyzes creatine to sarcosine and urea.
Pssm-ID: 238523 [Multi-domain] Cd Length: 228 Bit Score: 48.69 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 85 PSSKTILKDGDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHREG 164
Cdd:cd01090 71 PVTNRKVQRGDILSLNCFPMIAGYYTALERTLFLDEVSDAHLKIWEANVAVHERGLELIKPGARCKDIAAELNEMYREHD 150
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 491118278 165 FSIVREY-CGHGIGQVYHeqpsvlHYGQPGqGL--------VLKKGMVFTIEPMV 210
Cdd:cd01090 151 LLRYRTFgYGHSFGVLSH------YYGREA-GLelredidtVLEPGMVVSMEPMI 198
|
|
| PRK14576 |
PRK14576 |
putative endopeptidase; Provisional |
8-252 |
3.39e-05 |
|
putative endopeptidase; Provisional
Pssm-ID: 173040 [Multi-domain] Cd Length: 405 Bit Score: 44.62 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 8 IKSEQDIEKLRISGRLAAQVLQMIGEHVKPGVTTEYLddlchdyiVNTLKVIPANVGYHGYTKTTCISPNEVVCHGIPSS 87
Cdd:PRK14576 177 IKSPWEIEHLRKSAEITEYGIASAAKKIRVGCTAAEL--------TAAFKAAVMSFPETNFSRFNLISVGDNFSPKIIAD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 88 KTILKDGDIINIDVAVIKDGFYGDTSRMYYVGqvkpEAKKLVDTTYEAMRAG----IHAVKPGATLGDIGYAIQSVAHRE 163
Cdd:PRK14576 249 TTPAKVGDLIKFDCGIDVAGYGADLARTFVLG----EPDKLTQQIYDTIRTGhehmLSMVAPGVKLKAVFDSTMAVIKTS 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 164 GFS-IVREYCGHGIGQVY--HEQPSVLHYGQPgqglVLKKGMVFTIE-PMVNAGKArvkelkdgwtvvttdkslSAQWEH 239
Cdd:PRK14576 325 GLPhYNRGHLGHGDGVFLglEEVPFVSTQATE----TFCPGMVLSLEtPYYGIGVG------------------SIMLED 382
|
250
....*....|...
gi 491118278 240 MVAVTDTGFEVLS 252
Cdd:PRK14576 383 MILITDSGFEFLS 395
|
|
| PRK15173 |
PRK15173 |
peptidase; Provisional |
84-207 |
1.60e-04 |
|
peptidase; Provisional
Pssm-ID: 185095 [Multi-domain] Cd Length: 323 Bit Score: 42.40 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 84 IPSSkTILKDGDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHRE 163
Cdd:PRK15173 164 IPSN-TKACSGDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKS 242
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 491118278 164 GF-SIVREYCGHGIGQV--YHEQPSVLHYGQPGqglvLKKGMVFTIE 207
Cdd:PRK15173 243 GLpNYNRGHLGHGNGVFlgLEESPFVSTHATES----FTSGMVLSLE 285
|
|
| PRK14575 |
PRK14575 |
putative peptidase; Provisional |
84-207 |
2.30e-04 |
|
putative peptidase; Provisional
Pssm-ID: 173039 [Multi-domain] Cd Length: 406 Bit Score: 42.00 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491118278 84 IPSSkTILKDGDIINIDVAVIKDGFYGDTSRMYYVGQVKPEAKKLVDTTYEAMRAGIHAVKPGATLGDIGYAIQSVAHRE 163
Cdd:PRK14575 247 IPSN-TKACSGDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKS 325
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 491118278 164 GF-SIVREYCGHGIGQV--YHEQPSVLHYGQPGqglvLKKGMVFTIE 207
Cdd:PRK14575 326 GLpNYNRGHLGHGNGVFlgLEESPFVSTHATES----FTSGMVLSLE 368
|
|
| |
