|
Name |
Accession |
Description |
Interval |
E-value |
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
1-212 |
6.73e-123 |
|
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: 347.56 E-value: 6.73e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:cd01086 26 VTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGDIVNIDVGVELDGYHGDSARTFIVGE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHA-NDSDLPMEE 159
Cdd:cd01086 106 VSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGGHGIGRKFHEEPQIPNYGrPGTGPKLKP 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1016470462 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTK 212
Cdd:cd01086 186 GMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILTL 238
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
1-216 |
2.82e-108 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 311.17 E-value: 2.82e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:COG0024 34 VTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSVNEVVVHGIPSDRVLKDGDIVNIDVGAILDGYHGDSARTFVVGE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHH-ANDSDLPMEE 159
Cdd:COG0024 114 VSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSVVREFVGHGIGREMHEEPQVPNYgRPGRGPRLKP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1016470462 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKLPHE 216
Cdd:COG0024 194 GMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTEDGPEILTLPDGG 250
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
1-216 |
2.72e-104 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 300.90 E-value: 2.72e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:PRK05716 36 VTTKELDRIAEEYIRDQGAIPAPLGYHGFPKSICTSVNEVVCHGIPSDKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHANDSDLP-MEE 159
Cdd:PRK05716 116 ISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGFSVVREYCGHGIGRKFHEEPQIPHYGAPGDGPvLKE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1016470462 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKLPHE 216
Cdd:PRK05716 196 GMVFTIEPMINAGKREVKTLKDGWTVVTKDGSLSAQYEHTVAVTEDGPEILTLRPEE 252
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
1-213 |
8.24e-85 |
|
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: 251.50 E-value: 8.24e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:TIGR00500 34 VSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISVNEVVIHGIPDKKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHANDSDLP-MEE 159
Cdd:TIGR00500 114 ISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSVVREYCGHGIGRKFHEEPQIPNYGKKFTNVrLKE 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1016470462 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKL 213
Cdd:TIGR00500 194 GMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITDNGPEILTER 247
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
1-203 |
6.81e-51 |
|
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: 163.95 E-value: 6.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 1 MTTEEIDALVHREIISHNAYpsplGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYN-GYHGDTSETFLVG 79
Cdd:pfam00557 25 VTERELAAELEAARLRRGGA----RGPAFPPIVASGPNAAIPHYIPNDRVLKPGDLVLIDVGAEYDgGYCSDITRTFVVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 80 NVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGF-QVCPHFVGHGIGSYFHGHPEIWHhaNDSDLPME 158
Cdd:pfam00557 101 KPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLgEYFPHGLGHGIGLEVHEGPYISR--GGDDRVLE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1016470462 159 EGMAFTIEPIITEgspefkvledawtvvsLDNQRSAQFEHTVLIT 203
Cdd:pfam00557 179 PGMVFTIEPGIYF----------------IPGWGGVRIEDTVLVT 207
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
1-212 |
6.73e-123 |
|
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: 347.56 E-value: 6.73e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:cd01086 26 VTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGDIVNIDVGVELDGYHGDSARTFIVGE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHA-NDSDLPMEE 159
Cdd:cd01086 106 VSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGGHGIGRKFHEEPQIPNYGrPGTGPKLKP 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1016470462 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTK 212
Cdd:cd01086 186 GMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILTL 238
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
1-216 |
2.82e-108 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 311.17 E-value: 2.82e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:COG0024 34 VTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSVNEVVVHGIPSDRVLKDGDIVNIDVGAILDGYHGDSARTFVVGE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHH-ANDSDLPMEE 159
Cdd:COG0024 114 VSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSVVREFVGHGIGREMHEEPQVPNYgRPGRGPRLKP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1016470462 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKLPHE 216
Cdd:COG0024 194 GMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTEDGPEILTLPDGG 250
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
1-216 |
2.72e-104 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 300.90 E-value: 2.72e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:PRK05716 36 VTTKELDRIAEEYIRDQGAIPAPLGYHGFPKSICTSVNEVVCHGIPSDKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHANDSDLP-MEE 159
Cdd:PRK05716 116 ISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGFSVVREYCGHGIGRKFHEEPQIPHYGAPGDGPvLKE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1016470462 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKLPHE 216
Cdd:PRK05716 196 GMVFTIEPMINAGKREVKTLKDGWTVVTKDGSLSAQYEHTVAVTEDGPEILTLRPEE 252
|
|
| PRK12896 |
PRK12896 |
methionine aminopeptidase; Reviewed |
1-211 |
3.97e-93 |
|
methionine aminopeptidase; Reviewed
Pssm-ID: 237252 [Multi-domain] Cd Length: 255 Bit Score: 272.87 E-value: 3.97e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:PRK12896 41 MTTKELDRIAEKRLEEHGAIPSPEGYYGFPGSTCISVNEEVAHGIPGPRVIKDGDLVNIDVSAYLDGYHGDTGITFAVGP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHP-EIWHHANDSD-LPME 158
Cdd:PRK12896 121 VSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAIEDFAKKNGYSVVRDLTGHGVGRSLHEEPsVILTYTDPLPnRLLR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1016470462 159 EGMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILT 211
Cdd:PRK12896 201 PGMTLAVEPFLNLGAKDAETLDDGWTVVTPDKSLSAQFEHTVVVTRDGPEILT 253
|
|
| PLN03158 |
PLN03158 |
methionine aminopeptidase; Provisional |
1-214 |
9.64e-89 |
|
methionine aminopeptidase; Provisional
Pssm-ID: 215607 [Multi-domain] Cd Length: 396 Bit Score: 266.70 E-value: 9.64e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:PLN03158 168 VTTDEIDRVVHEATIAAGGYPSPLNYHFFPKSCCTSVNEVICHGIPDARKLEDGDIVNVDVTVYYKGCHGDLNETFFVGN 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHA-NDSDLPMEE 159
Cdd:PLN03158 248 VDEASRQLVKCTYECLEKAIAIVKPGVRYREVGEVINRHATMSGLSVVKSYCGHGIGELFHCAPNIPHYArNKAVGVMKA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1016470462 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILT-KLP 214
Cdd:PLN03158 328 GQVFTIEPMINAGVWRDRMWPDGWTAVTADGKRSAQFEHTLLVTETGVEVLTaRLP 383
|
|
| met_pdase_I |
TIGR00500 |
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ... |
1-213 |
8.24e-85 |
|
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: 251.50 E-value: 8.24e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:TIGR00500 34 VSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISVNEVVIHGIPDKKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHANDSDLP-MEE 159
Cdd:TIGR00500 114 ISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSVVREYCGHGIGRKFHEEPQIPNYGKKFTNVrLKE 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1016470462 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKL 213
Cdd:TIGR00500 194 GMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITDNGPEILTER 247
|
|
| PRK12318 |
PRK12318 |
methionyl aminopeptidase; |
2-213 |
1.37e-72 |
|
methionyl aminopeptidase;
Pssm-ID: 183434 [Multi-domain] Cd Length: 291 Bit Score: 222.00 E-value: 1.37e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 2 TTEEIDALVHREIISHNAYPSPLGYGG--FPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVG 79
Cdd:PRK12318 75 TTNELDELSRELHKEYNAIPAPLNYGSppFPKTICTSLNEVICHGIPNDIPLKNGDIMNIDVSCIVDGYYGDCSRMVMIG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 80 NVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHANDSDLPMEE 159
Cdd:PRK12318 155 EVSEIKKKVCQASLECLNAAIAILKPGIPLYEIGEVIENCADKYGFSVVDQFVGHGVGIKFHENPYVPHHRNSSKIPLAP 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1016470462 160 GMAFTIEPIITEGSPE-FKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKL 213
Cdd:PRK12318 235 GMIFTIEPMINVGKKEgVIDPINHWEARTCDNQPSAQWEHTILITETGYEILTLL 289
|
|
| PRK12897 |
PRK12897 |
type I methionyl aminopeptidase; |
1-213 |
5.24e-51 |
|
type I methionyl aminopeptidase;
Pssm-ID: 171806 Cd Length: 248 Bit Score: 165.59 E-value: 5.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:PRK12897 35 ITTKEINTFVEAYLEKHGATSEQKGYNGYPYAICASVNDEMCHAFPADVPLTEGDIVTIDMVVNLNGGLSDSAWTYRVGK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHANDSDLP-MEE 159
Cdd:PRK12897 115 VSDEAEKLLLVAENALYKGIDQAVIGNRVGDIGYAIESYVANEGFSVARDFTGHGIGKEIHEEPAIFHFGKQGQGPeLQE 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1016470462 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKL 213
Cdd:PRK12897 195 GMVITIEPIVNVGMRYSKVDLNGWTARTMDGKLSAQYEHTIAITKDGPIILTKL 248
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
1-203 |
6.81e-51 |
|
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: 163.95 E-value: 6.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 1 MTTEEIDALVHREIISHNAYpsplGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYN-GYHGDTSETFLVG 79
Cdd:pfam00557 25 VTERELAAELEAARLRRGGA----RGPAFPPIVASGPNAAIPHYIPNDRVLKPGDLVLIDVGAEYDgGYCSDITRTFVVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 80 NVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGF-QVCPHFVGHGIGSYFHGHPEIWHhaNDSDLPME 158
Cdd:pfam00557 101 KPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLgEYFPHGLGHGIGLEVHEGPYISR--GGDDRVLE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1016470462 159 EGMAFTIEPIITEgspefkvledawtvvsLDNQRSAQFEHTVLIT 203
Cdd:pfam00557 179 PGMVFTIEPGIYF----------------IPGWGGVRIEDTVLVT 207
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
1-207 |
1.21e-36 |
|
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as metallopeptidase family M24. This family of enzymes is able to cleave amido-, imido- and amidino-containing bonds. Members exibit relatively narrow substrate specificity compared to other metallo-aminopeptidases, suggesting they play roles in regulation of biological processes rather than general protein degradation.
Pssm-ID: 238514 [Multi-domain] Cd Length: 207 Bit Score: 127.18 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 1 MTTEEIDALVHREIISHNAYPSPlgyggfpkSVCTSVNNV--LCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLV 78
Cdd:cd01066 26 VTEAEVAAAIEQALRAAGGYPAG--------PTIVGSGARtaLPHYRPDDRRLQEGDLVLVDLGGVYDGYHADLTRTFVI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 79 GNVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGF-QVCPHFVGHGIGSYFHGHPEIwhhANDSDLPM 157
Cdd:cd01066 98 GEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLgPNFGHRTGHGIGLEIHEPPVL---KAGDDTVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1016470462 158 EEGMAFTIEPIItegspefkvledawtvvSLDNQRSAQFEHTVLITSRGA 207
Cdd:cd01066 175 EPGMVFAVEPGL-----------------YLPGGGGVRIEDTVLVTEDGP 207
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
1-216 |
1.59e-33 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 121.85 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 1 MTTEEIDALVHREIISHNAYpsplgYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:COG0006 104 VTEREVAAELEAAMRRRGAE-----GPSFDTIVASGENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVC-PHFVGHGIGSYFHGHPEIwhhANDSDLPMEE 159
Cdd:COG0006 179 PSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAGYGEYfPHGTGHGVGLDVHEGPQI---SPGNDRPLEP 255
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1016470462 160 GMAFTIEPIITegspefkvLEDAWTVvsldnqRSaqfEHTVLITSRGAQILTKLPHE 216
Cdd:COG0006 256 GMVFTIEPGIY--------IPGIGGV------RI---EDTVLVTEDGAEVLTRLPRE 295
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
1-169 |
4.88e-26 |
|
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: 99.89 E-value: 4.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 1 MTTEEIDALVHREIISHNAY-PSplgyggFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVG 79
Cdd:cd01092 26 MTEREVAAELEYFMRKLGAEgPS------FDTIVASGPNSALPHGVPSDRKIEEGDLVLIDFGAIYDGYCSDITRTVAVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 80 NVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGF-QVCPHFVGHGIGSYFHGHPEIwhhANDSDLPME 158
Cdd:cd01092 100 EPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGYgEYFIHRTGHGVGLEVHEAPYI---SPGSDDVLE 176
|
170
....*....|.
gi 1016470462 159 EGMAFTIEPII 169
Cdd:cd01092 177 EGMVFTIEPGI 187
|
|
| PRK07281 |
PRK07281 |
methionyl aminopeptidase; |
5-211 |
1.50e-25 |
|
methionyl aminopeptidase;
Pssm-ID: 180918 Cd Length: 286 Bit Score: 100.31 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 5 EIDALVHREIISHNAYPSPLGYGG----FPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDV------------------- 61
Cdd:PRK07281 39 EVEEYVRRRCKEENVLPLQIGVDGammdYPYATCCGLNDEVAHAFPRHYILKEGDLLKVDMvlsepldksivdvsklnfd 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 62 --------TVYYNGYHGDTSETFLVGNVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVG 133
Cdd:PRK07281 119 nveqmkkyTESYRGGLADSCWAYAVGTPSDEVKNLMDVTKEAMYRGIEQAVVGNRIGDIGAAIQEYAESRGYGVVRDLVG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 134 HGIGSYFHGHPEIWHHANDS-DLPMEEGMAFTIEPIITEGSPEFKV-LEDAWTVVSLDNQRSAQFEHTVLITSRGAQILT 211
Cdd:PRK07281 199 HGVGPTMHEEPMVPNYGTAGrGLRLREGMVLTIEPMINTGTWEIDTdMKTGWAHKTLDGGLSCQYEHQFVITKDGPVILT 278
|
|
| met_pdase_II |
TIGR00501 |
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ... |
5-212 |
1.72e-19 |
|
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: 84.45 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 5 EIDALVHREIISHNAYPsplgygGFPKSVctSVNNVLCHGIP---DSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNV 81
Cdd:TIGR00501 34 EVAEFVENRIRELGAEP------AFPCNI--SINECAAHFTPkagDKTVFKDGDVVKLDLGAHVDGYIADTAITVDLGDQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 82 decGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSY-FHGHPEIWHHANDSDLPMEEG 160
Cdd:TIGR00501 106 ---YDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIESYGVKPISNLTGHSMAPYrLHGGKSIPNVKERDTTKLEEG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 161 MAFTIEPIITEG---------------------------------SPEFKVL----------EDAWTVVSLD-------- 189
Cdd:TIGR00501 183 DVVAIEPFATDGvgyvtdggevsiyaflaerpvrldsarnllktiDENYGTLpfarrwldklGDEKYLFALNnlirhgli 262
|
250 260 270
....*....|....*....|....*....|...
gi 1016470462 190 ------NQRS----AQFEHTVLITSRGAQILTK 212
Cdd:TIGR00501 263 ydypvlNEISggyvAQWEHTILVEEHGKEVTTK 295
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
28-172 |
5.61e-15 |
|
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: 71.90 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 28 GFPKSVctSVNNVLCHGIP---DSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVdecGKKLVEVARRCRDEAIAACR 104
Cdd:cd01088 47 AFPVNL--SINECAAHYTPnagDDTVLKEGDVVKLDFGAHVDGYIADSAFTVDFDPK---YDDLLEAAKEALNAAIKEAG 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1016470462 105 AGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSY-FHGHPEIWHHANDSDLPMEEGMAFTIEPIITEG 172
Cdd:cd01088 122 PDVRLGEIGEAIEEVIESYGFKPIRNLTGHSIERYrLHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTG 190
|
|
| Prolidase |
cd01087 |
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ... |
5-212 |
8.65e-12 |
|
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: 62.21 E-value: 8.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 5 EIDALVHREIISHNAypsPLGYGgfPKSVCTSVNNVLcHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLV-GNVDE 83
Cdd:cd01087 30 ELEAEFEYEFRSRGA---RLAYS--YIVAAGSNAAIL-HYVHNDQPLKDGDLVLIDAGAEYGGYASDITRTFPVnGKFTD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 84 CGKKLVEVARRCRDEAIAACRAGAPFSVIgNTISHITHQNGFQV--------------------CPHFVGHGIGSYFH-- 141
Cdd:cd01087 104 EQRELYEAVLAAQKAAIAACKPGVSYEDI-HLLAHRVLAEGLKElgilkgdvdeivesgayakfFPHGLGHYLGLDVHdv 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016470462 142 GHPeiwHHANDSDLPMEEGMAFTIEP---IItegsPEFKVLEDAWTVVSL---DNqrsaqfehtVLITSRGAQILTK 212
Cdd:cd01087 183 GGY---LRYLRRARPLEPGMVITIEPgiyFI----PDLLDVPEYFRGGGIrieDD---------VLVTEDGPENLTR 243
|
|
| PRK09795 |
PRK09795 |
aminopeptidase; Provisional |
29-216 |
2.24e-08 |
|
aminopeptidase; Provisional
Pssm-ID: 182080 [Multi-domain] Cd Length: 361 Bit Score: 53.40 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 29 FPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDECGKK-----LVEVARRCRDEAIAAC 103
Cdd:PRK09795 181 FDTIVASGWRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVNGEGVSAEShplfnVYQIVLQAQLAAISAI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 104 RAGAPFSVIGNTISHITHQNGF-QVCPHFVGHGIGSYFHGHPEIwhhANDSDLPMEEGMAFTIEPIITegspefkvleda 182
Cdd:PRK09795 261 RPGVRCQQVDDAARRVITEAGYgDYFGHNTGHAIGIEVHEDPRF---SPRDTTTLQPGMLLTVEPGIY------------ 325
|
170 180 190
....*....|....*....|....*....|....
gi 1016470462 183 wtvvsLDNQRSAQFEHTVLITSRGAQILTKLPHE 216
Cdd:PRK09795 326 -----LPGQGGVRIEDVVLVTPQGAEVLYAMPKT 354
|
|
| PA2G4-like |
cd01089 |
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ... |
29-211 |
9.63e-08 |
|
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: 50.79 E-value: 9.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 29 FPksVCTSVNNVLCHGIP----DSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDECGK--KLVEVARRCRDEAIAA 102
Cdd:cd01089 59 FP--TCISVNNCVCHFSPlksdATYTLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAETPVtgKKADVIAAAHYALEAA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 103 CRAGAPfsviGNTISHIThQNGFQVCPHFVGHGIGSyfhghpeIWHHAndsdlpMEEGMAFtiepiiTEGSPEFKVLED- 181
Cdd:cd01089 137 LRLLRP----GNQNSDIT-EAIQKVIVDYGCTPVEG-------VLSHQ------LKRVVSS------GEGKAKLVECVKh 192
|
170 180 190
....*....|....*....|....*....|....*
gi 1016470462 182 ----AWTVV-SLDNQRSAQFEHTVLITSRGAQILT 211
Cdd:cd01089 193 gllfPYPVLyEKEGEVVAQFKLTVLLTPNGVTVLT 227
|
|
| PRK15173 |
PRK15173 |
peptidase; Provisional |
45-216 |
1.28e-07 |
|
peptidase; Provisional
Pssm-ID: 185095 [Multi-domain] Cd Length: 323 Bit Score: 50.87 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 45 IPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNG 124
Cdd:PRK15173 164 IPSNTKACSGDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSG 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 125 FqvcPHF----VGHGIGSY--FHGHPEIWHHANDSdlpMEEGMAFTIEpiitegSPEFKVledawtvvsldNQRSAQFEH 198
Cdd:PRK15173 244 L---PNYnrghLGHGNGVFlgLEESPFVSTHATES---FTSGMVLSLE------TPYYGY-----------NLGSIMIED 300
|
170
....*....|....*...
gi 1016470462 199 TVLITSRGAQILTKLPHE 216
Cdd:PRK15173 301 MILINKEGIEFLSKLPRD 318
|
|
| PRK14575 |
PRK14575 |
putative peptidase; Provisional |
45-216 |
2.17e-07 |
|
putative peptidase; Provisional
Pssm-ID: 173039 [Multi-domain] Cd Length: 406 Bit Score: 50.47 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 45 IPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNG 124
Cdd:PRK14575 247 IPSNTKACSGDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 125 FqvcPHF----VGHGIGSY--FHGHPEIWHHANDSdlpMEEGMAFTIEpiitegSPEFKVledawtvvsldNQRSAQFEH 198
Cdd:PRK14575 327 L---PNYnrghLGHGNGVFlgLEESPFVSTHATES---FTSGMVLSLE------TPYYGY-----------NLGSIMIED 383
|
170
....*....|....*...
gi 1016470462 199 TVLITSRGAQILTKLPHE 216
Cdd:PRK14575 384 MILINKEGIEFLSKLPRD 401
|
|
| PRK14576 |
PRK14576 |
putative endopeptidase; Provisional |
45-213 |
1.87e-05 |
|
putative endopeptidase; Provisional
Pssm-ID: 173040 [Multi-domain] Cd Length: 405 Bit Score: 44.62 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 45 IPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNG 124
Cdd:PRK14576 246 IADTTPAKVGDLIKFDCGIDVAGYGADLARTFVLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVFDSTMAVIKTSG 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 125 FqvcPHF----VGHGIGSY--FHGHPEIWHHANDSDLPmeeGMAFTIEpiitegSPEFKVledawtvvsldNQRSAQFEH 198
Cdd:PRK14576 326 L---PHYnrghLGHGDGVFlgLEEVPFVSTQATETFCP---GMVLSLE------TPYYGI-----------GVGSIMLED 382
|
170
....*....|....*
gi 1016470462 199 TVLITSRGAQILTKL 213
Cdd:PRK14576 383 MILITDSGFEFLSKL 397
|
|
| crvDNA_42K |
TIGR00495 |
42K curved DNA binding protein; Proteins identified by this model have been identified in a ... |
29-185 |
2.30e-05 |
|
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: 44.49 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 29 FPksVCTSVNNVLCHGIP----DSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDE---CGKK--LVEVARRCRDEA 99
Cdd:TIGR00495 78 FP--TCISVNNCVGHFSPlksdQDYILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEepvTGRKadVIAAAHLAAEAA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 100 IAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSY-FHGHPEIWHHANDSD------LPMEEGMAFTIEPIITEG 172
Cdd:TIGR00495 156 LRLVKPGNTNTQVTEAINKVAHSYGCTPVEGMLSHQLKQHvIDGEKVIISNPSDSQkkdhdtAEFEENEVYAVDILVSTG 235
|
170
....*....|...
gi 1016470462 173 SPEFKVLEDAWTV 185
Cdd:TIGR00495 236 EGKAKDADQRTTI 248
|
|
| PRK10879 |
PRK10879 |
proline aminopeptidase P II; Provisional |
1-167 |
1.61e-04 |
|
proline aminopeptidase P II; Provisional
Pssm-ID: 182804 [Multi-domain] Cd Length: 438 Bit Score: 42.02 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 1 MTTEEIDALVHREIISHNA-YPSplgyggFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLV- 78
Cdd:PRK10879 204 MFEYQLEGEIHHEFNRHGArYPS------YNTIVGSGENGCILHYTENESEMRDGDLVLIDAGCEYKGYAGDITRTFPVn 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 79 GNVDECGKKLVEVARRCRDEAIAACRAGAPFSVI-------------------GNTISHITHQNGFQVCPHFVGHGIGSY 139
Cdd:PRK10879 278 GKFTPAQREIYDIVLESLETSLRLYRPGTSIREVtgevvrimvsglvklgilkGDVDQLIAENAHRPFFMHGLSHWLGLD 357
|
170 180
....*....|....*....|....*...
gi 1016470462 140 FHghpEIWHHANDSDLPMEEGMAFTIEP 167
Cdd:PRK10879 358 VH---DVGVYGQDRSRILEPGMVLTVEP 382
|
|
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
28-166 |
3.33e-04 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 40.85 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016470462 28 GFPKSVctSVNNVLCHGIP---DSRPLQDGDIINIDVTVYYNGYHGDTSET--FlvgnvDECGKKLVEVARRCRDEAIAA 102
Cdd:PTZ00053 210 AFPTGC--SLNHCAAHYTPntgDKTVLTYDDVCKLDFGTHVNGRIIDCAFTvaF-----NPKYDPLLQATKDATNTGIKE 282
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016470462 103 CRAGAPFSVIGNTI-----SHITHQNGfQVCP-----HFVGHGIGSY-FHGH---PEIwhHANDSDLpMEEGMAFTIE 166
Cdd:PTZ00053 283 AGIDVRLSDIGAAIqevieSYEVEIKG-KTYPiksirNLNGHSIGPYiIHGGksvPIV--KGGENTR-MEEGELFAIE 356
|
|
|