|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
1-254 |
1.26e-170 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 470.77 E-value: 1.26e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 1 MAISIKTSEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNeQKAISACLGYHGYPKSVCISVNEVVCHG 80
Cdd:PRK05716 1 MAITIKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKELDRIAEEYIRD-QGAIPAPLGYHGFPKSICTSVNEVVCHG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 81 IPDDgKLLKDGDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAE 160
Cdd:PRK05716 80 IPSD-KVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 161 GFSVVREYCGHGIGRGFHEEPQVLHYDSPETNVVLKPGMTFTIEPMVNAGKKEIRSMKDGWTVKTKDRSLSAQYEHTIVV 240
Cdd:PRK05716 159 GFSVVREYCGHGIGRKFHEEPQIPHYGAPGDGPVLKEGMVFTIEPMINAGKREVKTLKDGWTVVTKDGSLSAQYEHTVAV 238
|
250
....*....|....
gi 488978444 241 TDNGCEILTLRKDD 254
Cdd:PRK05716 239 TEDGPEILTLRPEE 252
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
3-254 |
1.34e-163 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 452.92 E-value: 1.34e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 3 ISIKTSEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVnEQKAISACLGYHGYPKSVCISVNEVVCHGIP 82
Cdd:COG0024 1 IEIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIR-DHGAIPAFLGYYGFPKSICTSVNEVVVHGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 83 DDgKLLKDGDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAEGF 162
Cdd:COG0024 80 SD-RVLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 163 SVVREYCGHGIGRGFHEEPQVLHYDSPETNVVLKPGMTFTIEPMVNAGKKEIRSMKDGWTVKTKDRSLSAQYEHTIVVTD 242
Cdd:COG0024 159 SVVREFVGHGIGREMHEEPQVPNYGRPGRGPRLKPGMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTE 238
|
250
....*....|..
gi 488978444 243 NGCEILTLRKDD 254
Cdd:COG0024 239 DGPEILTLPDGG 250
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
3-251 |
1.35e-143 |
|
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: 402.50 E-value: 1.35e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 3 ISIKTSEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQkAISACLGYHGYPKSVCISVNEVVCHGIP 82
Cdd:TIGR00500 1 ISLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHG-AKPAFLGYYGFPGSVCISVNEVVIHGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 83 DDgKLLKDGDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAEGF 162
Cdd:TIGR00500 80 DK-KVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 163 SVVREYCGHGIGRGFHEEPQVLHYDSPETNVVLKPGMTFTIEPMVNAGKKEIRSMKDGWTVKTKDRSLSAQYEHTIVVTD 242
Cdd:TIGR00500 159 SVVREYCGHGIGRKFHEEPQIPNYGKKFTNVRLKEGMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITD 238
|
....*....
gi 488978444 243 NGCEILTLR 251
Cdd:TIGR00500 239 NGPEILTER 247
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
11-250 |
4.88e-140 |
|
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: 393.01 E-value: 4.88e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 11 IEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVnEQKAISACLGYHGYPKSVCISVNEVVCHGIPDDgKLLKD 90
Cdd:cd01086 1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIE-EHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDD-RVLKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 91 GDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAEGFSVVREYCG 170
Cdd:cd01086 79 GDIVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 171 HGIGRGFHEEPQVLHYDSPETNVVLKPGMTFTIEPMVNAGKKEIRSMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTL 250
Cdd:cd01086 159 HGIGRKFHEEPQIPNYGRPGTGPKLKPGMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILTL 238
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
12-242 |
9.00e-59 |
|
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: 185.52 E-value: 9.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 12 EKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQKAisaclGYHGYPKSVCISVNEVVCHGIPDDGKLlKDG 91
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGA-----RGPAFPPIVASGPNAAIPHYIPNDRVL-KPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 92 DIVNIDVTVIKDD-FHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAEGFS-VVREYC 169
Cdd:pfam00557 75 DLVLIDVGAEYDGgYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGeYFPHGL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488978444 170 GHGIGRGFHEEPQVLHYDSpetNVVLKPGMTFTIEPMVNagkkeirsMKDGWTvktkdrslSAQYEHTIVVTD 242
Cdd:pfam00557 155 GHGIGLEVHEGPYISRGGD---DRVLEPGMVFTIEPGIY--------FIPGWG--------GVRIEDTVLVTE 208
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
1-254 |
1.26e-170 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 470.77 E-value: 1.26e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 1 MAISIKTSEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNeQKAISACLGYHGYPKSVCISVNEVVCHG 80
Cdd:PRK05716 1 MAITIKTPEEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKELDRIAEEYIRD-QGAIPAPLGYHGFPKSICTSVNEVVCHG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 81 IPDDgKLLKDGDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAE 160
Cdd:PRK05716 80 IPSD-KVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 161 GFSVVREYCGHGIGRGFHEEPQVLHYDSPETNVVLKPGMTFTIEPMVNAGKKEIRSMKDGWTVKTKDRSLSAQYEHTIVV 240
Cdd:PRK05716 159 GFSVVREYCGHGIGRKFHEEPQIPHYGAPGDGPVLKEGMVFTIEPMINAGKREVKTLKDGWTVVTKDGSLSAQYEHTVAV 238
|
250
....*....|....
gi 488978444 241 TDNGCEILTLRKDD 254
Cdd:PRK05716 239 TEDGPEILTLRPEE 252
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
3-254 |
1.34e-163 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 452.92 E-value: 1.34e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 3 ISIKTSEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVnEQKAISACLGYHGYPKSVCISVNEVVCHGIP 82
Cdd:COG0024 1 IEIKTPEEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIR-DHGAIPAFLGYYGFPKSICTSVNEVVVHGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 83 DDgKLLKDGDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAEGF 162
Cdd:COG0024 80 SD-RVLKDGDIVNIDVGAILDGYHGDSARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 163 SVVREYCGHGIGRGFHEEPQVLHYDSPETNVVLKPGMTFTIEPMVNAGKKEIRSMKDGWTVKTKDRSLSAQYEHTIVVTD 242
Cdd:COG0024 159 SVVREFVGHGIGREMHEEPQVPNYGRPGRGPRLKPGMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTE 238
|
250
....*....|..
gi 488978444 243 NGCEILTLRKDD 254
Cdd:COG0024 239 DGPEILTLPDGG 250
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
3-251 |
1.35e-143 |
|
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: 402.50 E-value: 1.35e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 3 ISIKTSEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQkAISACLGYHGYPKSVCISVNEVVCHGIP 82
Cdd:TIGR00500 1 ISLKSPDEIEKIRKAGRLAAEVLEELEREVKPGVSTKELDRIAKDFIEKHG-AKPAFLGYYGFPGSVCISVNEVVIHGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 83 DDgKLLKDGDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAEGF 162
Cdd:TIGR00500 80 DK-KVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 163 SVVREYCGHGIGRGFHEEPQVLHYDSPETNVVLKPGMTFTIEPMVNAGKKEIRSMKDGWTVKTKDRSLSAQYEHTIVVTD 242
Cdd:TIGR00500 159 SVVREYCGHGIGRKFHEEPQIPNYGKKFTNVRLKEGMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITD 238
|
....*....
gi 488978444 243 NGCEILTLR 251
Cdd:TIGR00500 239 NGPEILTER 247
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
11-250 |
4.88e-140 |
|
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: 393.01 E-value: 4.88e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 11 IEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVnEQKAISACLGYHGYPKSVCISVNEVVCHGIPDDgKLLKD 90
Cdd:cd01086 1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIE-EHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDD-RVLKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 91 GDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAEGFSVVREYCG 170
Cdd:cd01086 79 GDIVNIDVGVELDGYHGDSARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 171 HGIGRGFHEEPQVLHYDSPETNVVLKPGMTFTIEPMVNAGKKEIRSMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTL 250
Cdd:cd01086 159 HGIGRKFHEEPQIPNYGRPGTGPKLKPGMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILTL 238
|
|
| PRK12896 |
PRK12896 |
methionine aminopeptidase; Reviewed |
3-251 |
1.22e-126 |
|
methionine aminopeptidase; Reviewed
Pssm-ID: 237252 [Multi-domain] Cd Length: 255 Bit Score: 359.92 E-value: 1.22e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 3 ISIKTSEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVnEQKAISACLGYHGYPKSVCISVNEVVCHGIP 82
Cdd:PRK12896 8 MEIKSPRELEKMRKIGRIVATALKEMGKAVEPGMTTKELDRIAEKRLE-EHGAIPSPEGYYGFPGSTCISVNEEVAHGIP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 83 DDgKLLKDGDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAEGF 162
Cdd:PRK12896 87 GP-RVIKDGDLVNIDVSAYLDGYHGDTGITFAVGPVSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAIEDFAKKNGY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 163 SVVREYCGHGIGRGFHEEPQV-LHYDSPETNVVLKPGMTFTIEPMVNAGKKEIRSMKDGWTVKTKDRSLSAQYEHTIVVT 241
Cdd:PRK12896 166 SVVRDLTGHGVGRSLHEEPSViLTYTDPLPNRLLRPGMTLAVEPFLNLGAKDAETLDDGWTVVTPDKSLSAQFEHTVVVT 245
|
250
....*....|
gi 488978444 242 DNGCEILTLR 251
Cdd:PRK12896 246 RDGPEILTDR 255
|
|
| PLN03158 |
PLN03158 |
methionine aminopeptidase; Provisional |
3-251 |
2.52e-89 |
|
methionine aminopeptidase; Provisional
Pssm-ID: 215607 [Multi-domain] Cd Length: 396 Bit Score: 270.17 E-value: 2.52e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 3 ISIKTSEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVnEQKAISACLGYHGYPKSVCISVNEVVCHGIP 82
Cdd:PLN03158 135 VEIKTPEQIQRMRETCRIAREVLDAAARAIKPGVTTDEIDRVVHEATI-AAGGYPSPLNYHFFPKSCCTSVNEVICHGIP 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 83 DDGKLlKDGDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAEGF 162
Cdd:PLN03158 214 DARKL-EDGDIVNVDVTVYYKGCHGDLNETFFVGNVDEASRQLVKCTYECLEKAIAIVKPGVRYREVGEVINRHATMSGL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 163 SVVREYCGHGIGRGFHEEPQVLHYDSPETNVVLKPGMTFTIEPMVNAGKKEIRSMKDGWTVKTKDRSLSAQYEHTIVVTD 242
Cdd:PLN03158 293 SVVKSYCGHGIGELFHCAPNIPHYARNKAVGVMKAGQVFTIEPMINAGVWRDRMWPDGWTAVTADGKRSAQFEHTLLVTE 372
|
....*....
gi 488978444 243 NGCEILTLR 251
Cdd:PLN03158 373 TGVEVLTAR 381
|
|
| PRK12318 |
PRK12318 |
methionyl aminopeptidase; |
3-253 |
4.57e-81 |
|
methionyl aminopeptidase;
Pssm-ID: 183434 [Multi-domain] Cd Length: 291 Bit Score: 245.50 E-value: 4.57e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 3 ISIKTSEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDyIVNEQKAISACLGYHG--YPKSVCISVNEVVCHG 80
Cdd:PRK12318 41 IIIKTPEQIEKIRKACQVTARILDALCEAAKEGVTTNELDELSRE-LHKEYNAIPAPLNYGSppFPKTICTSLNEVICHG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 81 IPDDGKLlKDGDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAE 160
Cdd:PRK12318 120 IPNDIPL-KNGDIMNIDVSCIVDGYYGDCSRMVMIGEVSEIKKKVCQASLECLNAAIAILKPGIPLYEIGEVIENCADKY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 161 GFSVVREYCGHGIGRGFHEEPQVLHYDSpETNVVLKPGMTFTIEPMVNAGKKE-IRSMKDGWTVKTKDRSLSAQYEHTIV 239
Cdd:PRK12318 199 GFSVVDQFVGHGVGIKFHENPYVPHHRN-SSKIPLAPGMIFTIEPMINVGKKEgVIDPINHWEARTCDNQPSAQWEHTIL 277
|
250
....*....|....
gi 488978444 240 VTDNGCEILTLRKD 253
Cdd:PRK12318 278 ITETGYEILTLLDK 291
|
|
| PRK12897 |
PRK12897 |
type I methionyl aminopeptidase; |
3-249 |
4.34e-61 |
|
type I methionyl aminopeptidase;
Pssm-ID: 171806 Cd Length: 248 Bit Score: 192.94 E-value: 4.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 3 ISIKTSEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIvNEQKAISACLGYHGYPKSVCISVNEVVCHGIP 82
Cdd:PRK12897 2 ITIKTKNEIDLMHESGKLLASCHREIAKIMKPGITTKEINTFVEAYL-EKHGATSEQKGYNGYPYAICASVNDEMCHAFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 83 DDGKLlKDGDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAEGF 162
Cdd:PRK12897 81 ADVPL-TEGDIVTIDMVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNRVGDIGYAIESYVANEGF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 163 SVVREYCGHGIGRGFHEEPQVLHYDSPETNVVLKPGMTFTIEPMVNAGKKEIRSMKDGWTVKTKDRSLSAQYEHTIVVTD 242
Cdd:PRK12897 160 SVARDFTGHGIGKEIHEEPAIFHFGKQGQGPELQEGMVITIEPIVNVGMRYSKVDLNGWTARTMDGKLSAQYEHTIAITK 239
|
....*..
gi 488978444 243 NGCEILT 249
Cdd:PRK12897 240 DGPIILT 246
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
12-242 |
9.00e-59 |
|
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: 185.52 E-value: 9.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 12 EKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQKAisaclGYHGYPKSVCISVNEVVCHGIPDDGKLlKDG 91
Cdd:pfam00557 1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGA-----RGPAFPPIVASGPNAAIPHYIPNDRVL-KPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 92 DIVNIDVTVIKDD-FHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAEGFS-VVREYC 169
Cdd:pfam00557 75 DLVLIDVGAEYDGgYCSDITRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGeYFPHGL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488978444 170 GHGIGRGFHEEPQVLHYDSpetNVVLKPGMTFTIEPMVNagkkeirsMKDGWTvktkdrslSAQYEHTIVVTD 242
Cdd:pfam00557 155 GHGIGLEVHEGPYISRGGD---DRVLEPGMVFTIEPGIY--------FIPGWG--------GVRIEDTVLVTE 208
|
|
| PRK07281 |
PRK07281 |
methionyl aminopeptidase; |
3-249 |
2.25e-45 |
|
methionyl aminopeptidase;
Pssm-ID: 180918 Cd Length: 286 Bit Score: 153.85 E-value: 2.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 3 ISIKTSEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELD----RICNdyivnEQKAISACLGYHG----YPKSVCISVN 74
Cdd:PRK07281 2 ITLKSAREIEAMDRAGDFLASIHIGLRDLIKPGVDMWEVEeyvrRRCK-----EENVLPLQIGVDGammdYPYATCCGLN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 75 EVVCHGIPDDgKLLKDGDIVNID-----------VTVIKDDFH----------------GDTSKMFIVGKPTILGERLCR 127
Cdd:PRK07281 77 DEVAHAFPRH-YILKEGDLLKVDmvlsepldksiVDVSKLNFDnveqmkkytesyrgglADSCWAYAVGTPSDEVKNLMD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 128 ITQESLYLALRMVKPGINLRTIGAAIQKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSPETNVVLKPGMTFTIEPMV 207
Cdd:PRK07281 156 VTKEAMYRGIEQAVVGNRIGDIGAAIQEYAESRGYGVVRDLVGHGVGPTMHEEPMVPNYGTAGRGLRLREGMVLTIEPMI 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 488978444 208 NAGKKEIRS-MKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILT 249
Cdd:PRK07281 236 NTGTWEIDTdMKTGWAHKTLDGGLSCQYEHQFVITKDGPVILT 278
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
11-245 |
4.05e-44 |
|
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: 148.37 E-value: 4.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 11 IEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNeqkaisaclGYHGYPKSVCISVNEV--VCHGIPDDGKLl 88
Cdd:cd01066 1 IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRA---------AGGYPAGPTIVGSGARtaLPHYRPDDRRL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 89 KDGDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAEGFSVVR-E 167
Cdd:cd01066 71 QEGDLVLVDLGGVYDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLGPNFgH 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488978444 168 YCGHGIGRGFHEEPqvlhYDSPETNVVLKPGMTFTIEPMVnagkkeirSMKDGWTVKtkdrslsaqYEHTIVVTDNGC 245
Cdd:cd01066 151 RTGHGIGLEIHEPP----VLKAGDDTVLEPGMVFAVEPGL--------YLPGGGGVR---------IEDTVLVTEDGP 207
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
4-249 |
6.94e-36 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 129.55 E-value: 6.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 4 SIKTSEDIEKMRVAGRLAAEVLEMIEPYVKPGVStgELDricndyIVNEQKAISACLGYHGYPKSVCISVNE--VVCHGI 81
Cdd:COG0006 72 AIKSPEEIELMRKAARIADAAHEAALAALRPGVT--ERE------VAAELEAAMRRRGAEGPSFDTIVASGEnaAIPHYT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 82 PDDGKLlKDGDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAEG 161
Cdd:COG0006 144 PTDRPL-KPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 162 FsvvREY----CGHGIGRGFHEEPQVlhydSPETNVVLKPGMTFTIEPMVnagkkeirSMKDGWTVKTkdrslsaqyEHT 237
Cdd:COG0006 223 Y---GEYfphgTGHGVGLDVHEGPQI----SPGNDRPLEPGMVFTIEPGI--------YIPGIGGVRI---------EDT 278
|
250
....*....|..
gi 488978444 238 IVVTDNGCEILT 249
Cdd:COG0006 279 VLVTEDGAEVLT 290
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
11-205 |
3.74e-27 |
|
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: 104.13 E-value: 3.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 11 IEKMRVAGRLAAEVLEMIEPYVKPGVStgELDricndyIVNEQKAISACLGYHGY--PKSVCISVNEVVCHGIPDDgKLL 88
Cdd:cd01092 1 IELLRKAARIADKAFEELLEFIKPGMT--ERE------VAAELEYFMRKLGAEGPsfDTIVASGPNSALPHGVPSD-RKI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 89 KDGDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAEGFSvvrEY 168
Cdd:cd01092 72 EEGDLVLIDFGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGYG---EY 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488978444 169 ----CGHGIGRGFHEEPQVlhydSPETNVVLKPGMTFTIEP 205
Cdd:cd01092 149 fihrTGHGVGLEVHEAPYI----SPGSDDVLEEGMVFTIEP 185
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
11-249 |
7.53e-24 |
|
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: 97.32 E-value: 7.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 11 IEKMRVAGRLAAEVLEMIEPYVKPGVSTGEldrICNdYIVNEQKAISACLGYhgyPksVCISVNEVVCH--GIPDDGKLL 88
Cdd:cd01088 1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLE---IAE-FVENRIRELGAGPAF---P--VNLSINECAAHytPNAGDDTVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 89 KDGDIVNIDVTVIKDDFHGDTSKMFIVGKptiLGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAEGFSVVREY 168
Cdd:cd01088 72 KEGDVVKLDFGAHVDGYIADSAFTVDFDP---KYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIESYGFKPIRNL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 169 CGHGIGR-GFHEEPQVLHYDSPEtNVVLKPGMTFTIEPMVNAGKKEIRSMKDG--------------------------- 220
Cdd:cd01088 149 TGHSIERyRLHAGKSIPNVKGGE-GTRLEEGDVYAIEPFATTGKGYVHDGPECsiymlnrdkplrlprarklldviyenf 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488978444 221 --------W--------------------------TVKTKDRSLSAQYEHTIVVTDNGCEILT 249
Cdd:cd01088 228 gtlpfarrWldrlgetkllmalknlckagivypypVLKEISGGYVAQFEHTIIVREDGKEVTT 290
|
|
| met_pdase_II |
TIGR00501 |
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ... |
9-249 |
2.36e-18 |
|
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: 82.53 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 9 EDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQkaisaclGYHGYPKSvcISVNEVVCHGIP--DDGK 86
Cdd:TIGR00501 3 ERAEKWIEAGKIHSKVRREAADRIVPGVKLLEVAEFVENRIRELG-------AEPAFPCN--ISINECAAHFTPkaGDKT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 87 LLKDGDIVNIDVTVIKDDFHGDTSKMFIVGKPTilgERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAEGFSVVR 166
Cdd:TIGR00501 74 VFKDGDVVKLDLGAHVDGYIADTAITVDLGDQY---DNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIESYGVKPIS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 167 EYCGHGIGR-GFHEEPQVLHYDSpETNVVLKPGMTFTIEPMVNAGKKEIRSMKDG------------------------- 220
Cdd:TIGR00501 151 NLTGHSMAPyRLHGGKSIPNVKE-RDTTKLEEGDVVAIEPFATDGVGYVTDGGEVsiyaflaerpvrldsarnllktide 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488978444 221 ----------WTVKTKDR--------------------------SLSAQYEHTIVVTDNGCEILT 249
Cdd:TIGR00501 230 nygtlpfarrWLDKLGDEkylfalnnlirhgliydypvlneisgGYVAQWEHTILVEEHGKEVTT 294
|
|
| PRK09795 |
PRK09795 |
aminopeptidase; Provisional |
5-205 |
5.45e-14 |
|
aminopeptidase; Provisional
Pssm-ID: 182080 [Multi-domain] Cd Length: 361 Bit Score: 70.74 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 5 IKTSEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICnDYIVNEQKAISACL------GYHGypksvcisvneVVC 78
Cdd:PRK09795 127 IKTPEEVEKIRLACGIADRGAEHIRRFIQAGMSEREIAAEL-EWFMRQQGAEKASFdtivasGWRG-----------ALP 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 79 HGIPDDgKLLKDGDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGER-----LCRITQESLYLALRMVKPGINLRTIGAAI 153
Cdd:PRK09795 195 HGKASD-KIVAAGEFVTLDFGALYQGYCSDMTRTLLVNGEGVSAEShplfnVYQIVLQAQLAAISAIRPGVRCQQVDDAA 273
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488978444 154 QKFVEAEGFSvvrEY----CGHGIGRGFHEEPQVlhydSPETNVVLKPGMTFTIEP 205
Cdd:PRK09795 274 RRVITEAGYG---DYfghnTGHAIGIEVHEDPRF----SPRDTTTLQPGMLLTVEP 322
|
|
| PA2G4-like |
cd01089 |
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ... |
11-249 |
8.50e-12 |
|
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: 63.12 E-value: 8.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 11 IEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNE-----------QKAISaclgyhgYPksVCISVNEVVCH 79
Cdd:cd01089 1 VTKYKTAGQIANKVLKQVISLCVPGAKVVDLCEKGDKLILEElgkvykkekklEKGIA-------FP--TCISVNNCVCH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 80 GIP---DDGKLLKDGDIVNIDVTVIKDDFHGDTSKMFIVG---KPTILGE--RLCRITQESLYLALRMVKPGINLRTIGA 151
Cdd:cd01089 72 FSPlksDATYTLKDGDVVKIDLGCHIDGYIAVVAHTIVVGaeaETPVTGKkaDVIAAAHYALEAALRLLRPGNQNSDITE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 152 AIQKFVEAEGFSVVREYCGHgigrgfheepqvlhydspetnvVLKPGMTFTiepmvnAGKKEIRSMKDGWTVK------T 225
Cdd:cd01089 152 AIQKVIVDYGCTPVEGVLSH----------------------QLKRVVSSG------EGKAKLVECVKHGLLFpypvlyE 203
|
250 260
....*....|....*....|....
gi 488978444 226 KDRSLSAQYEHTIVVTDNGCEILT 249
Cdd:cd01089 204 KEGEVVAQFKLTVLLTPNGVTVLT 227
|
|
| crvDNA_42K |
TIGR00495 |
42K curved DNA binding protein; Proteins identified by this model have been identified in a ... |
2-234 |
1.35e-09 |
|
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: 57.98 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 2 AISIKTSEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQKAISACLG--YHGYPKSVCISVNEVVCH 79
Cdd:TIGR00495 11 AYSLSNPEVVTKYKMAGEIANNVLKSVVEACSPGAKVVDICEKGDAFIMEETAKIFKKEKemEKGIAFPTCISVNNCVGH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 80 GIP---DDGKLLKDGDIVNIDVTVIKDDFHGDTSKMFIVGKPT---ILGERLCRITQESLYL--ALRMVKPGINLRTIGA 151
Cdd:TIGR00495 91 FSPlksDQDYILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQeepVTGRKADVIAAAHLAAeaALRLVKPGNTNTQVTE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 152 AIQKFVEAEGFSVVREYCGHGIGRGFHE-EPQVLHYDSPETN-----VVLKPGMTFTIEPMVNAGKKEIRSMKDGWTVKT 225
Cdd:TIGR00495 171 AINKVAHSYGCTPVEGMLSHQLKQHVIDgEKVIISNPSDSQKkdhdtAEFEENEVYAVDILVSTGEGKAKDADQRTTIYK 250
|
....*....
gi 488978444 226 KDrsLSAQY 234
Cdd:TIGR00495 251 RD--PSKTY 257
|
|
| PRK10879 |
PRK10879 |
proline aminopeptidase P II; Provisional |
5-261 |
2.08e-08 |
|
proline aminopeptidase P II; Provisional
Pssm-ID: 182804 [Multi-domain] Cd Length: 438 Bit Score: 54.35 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 5 IKTSEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELD-RICNDYivNEQKAisaclGYHGYPKSVCISVNEVVCHGIPD 83
Cdd:PRK10879 173 FKSPEEIAVLRRAGEISALAHTRAMEKCRPGMFEYQLEgEIHHEF--NRHGA-----RYPSYNTIVGSGENGCILHYTEN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 84 DGKLlKDGDIVNIDVTVIKDDFHGDTSKMFIV-GKPTILGERLCRITQESLYLALRMVKPGINLRTI-GAAIQKFVE--- 158
Cdd:PRK10879 246 ESEM-RDGDLVLIDAGCEYKGYAGDITRTFPVnGKFTPAQREIYDIVLESLETSLRLYRPGTSIREVtGEVVRIMVSglv 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 159 -------------AEgfSVVREYCGHGI----GRGFHEepqVLHYDsPETNVVLKPGMTFTIEPMVnagkkEIRSMKDgw 221
Cdd:PRK10879 325 klgilkgdvdqliAE--NAHRPFFMHGLshwlGLDVHD---VGVYG-QDRSRILEPGMVLTVEPGL-----YIAPDAD-- 391
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 488978444 222 tVKTKDRSLSAQYEHTIVVTDNGCEILT---LRKDDTIPAIIS 261
Cdd:PRK10879 392 -VPEQYRGIGIRIEDDIVITETGNENLTasvVKKPDEIEALMA 433
|
|
| Prolidase |
cd01087 |
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ... |
11-249 |
1.17e-07 |
|
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: 51.42 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 11 IEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRicndYIVNEQKAISACLGYHgypkSVCIS-VNEVVCHGIPDDgKLLK 89
Cdd:cd01087 1 IELMRKACDISAEAHRAAMKASRPGMSEYELEA----EFEYEFRSRGARLAYS----YIVAAgSNAAILHYVHND-QPLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 90 DGDIVNIDVTVIKDDFHGDTSKMFIV-GKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQK------------- 155
Cdd:cd01087 72 DGDLVLIDAGAEYGGYASDITRTFPVnGKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIHLLAHRvlaeglkelgilk 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 156 --FVEAEGFSVVREYCGHGIGRGF----HEEPQVLHYDSpeTNVVLKPGMTFTIEP--MVNAGKKEIRSMKDGWTVKTKD 227
Cdd:cd01087 152 gdVDEIVESGAYAKFFPHGLGHYLgldvHDVGGYLRYLR--RARPLEPGMVITIEPgiYFIPDLLDVPEYFRGGGIRIED 229
|
250 260
....*....|....*....|..
gi 488978444 228 rslsaqyehTIVVTDNGCEILT 249
Cdd:cd01087 230 ---------DVLVTEDGPENLT 242
|
|
| PRK15173 |
PRK15173 |
peptidase; Provisional |
81-204 |
1.34e-05 |
|
peptidase; Provisional
Pssm-ID: 185095 [Multi-domain] Cd Length: 323 Bit Score: 45.48 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 81 IPDDGKLLKdGDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAE 160
Cdd:PRK15173 164 IPSNTKACS-GDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKS 242
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 488978444 161 GF-SVVREYCGHGIG--RGFHEEPQVlhydSPETNVVLKPGMTFTIE 204
Cdd:PRK15173 243 GLpNYNRGHLGHGNGvfLGLEESPFV----STHATESFTSGMVLSLE 285
|
|
| PRK14575 |
PRK14575 |
putative peptidase; Provisional |
81-204 |
1.99e-05 |
|
putative peptidase; Provisional
Pssm-ID: 173039 [Multi-domain] Cd Length: 406 Bit Score: 45.08 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 81 IPDDGKLLKdGDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIGAAIQKFVEAE 160
Cdd:PRK14575 247 IPSNTKACS-GDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKS 325
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 488978444 161 GF-SVVREYCGHGIG--RGFHEEPQVlhydSPETNVVLKPGMTFTIE 204
Cdd:PRK14575 326 GLpNYNRGHLGHGNGvfLGLEESPFV----STHATESFTSGMVLSLE 368
|
|
| PRK14576 |
PRK14576 |
putative endopeptidase; Provisional |
71-249 |
8.99e-05 |
|
putative endopeptidase; Provisional
Pssm-ID: 173040 [Multi-domain] Cd Length: 405 Bit Score: 43.08 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 71 ISVNEVVCHGIPDDGKLLKDGDIVNIDVTVIKDDFHGDTSKMFIVGKPTILGERLCRITQESLYLALRMVKPGINLRTIG 150
Cdd:PRK14576 235 ISVGDNFSPKIIADTTPAKVGDLIKFDCGIDVAGYGADLARTFVLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVF 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978444 151 AAIQKFVEAEGFS-VVREYCGHGIG--RGFHEEPQVlhydSPETNVVLKPGMTFTIE-PMVNAGKKEIrsmkdgwtvktk 226
Cdd:PRK14576 315 DSTMAVIKTSGLPhYNRGHLGHGDGvfLGLEEVPFV----STQATETFCPGMVLSLEtPYYGIGVGSI------------ 378
|
170 180
....*....|....*....|...
gi 488978444 227 drslsaQYEHTIVVTDNGCEILT 249
Cdd:PRK14576 379 ------MLEDMILITDSGFEFLS 395
|
|
| APP |
cd01085 |
X-Prolyl Aminopeptidase 2. E.C. 3.4.11.9. Also known as X-Pro aminopeptidase, proline ... |
170-205 |
3.97e-04 |
|
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: 40.62 E-value: 3.97e-04
10 20 30
....*....|....*....|....*....|....*...
gi 488978444 170 GHGIGR--GFHEEPQVLHydSPETNVVLKPGMTFTIEP 205
Cdd:cd01085 161 GHGVGSflNVHEGPQSIS--PAPNNVPLKAGMILSNEP 196
|
|
| |
