|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
106-477 |
0e+00 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 718.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 106 RGPRVQTDPPSVPICDLYPNGVFPKGQECEYPPTQdgrtaAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSW 185
Cdd:PTZ00053 104 EQEWKQTQPPTIPVSKQFKDGEYPVGEIQEYPGEN-----SSRTSSEEKRELEKLSEEQYQDLRRAAEVHRQVRRYAQSV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 186 IKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFT 265
Cdd:PTZ00053 179 IKPGVKLIDICERIESKSRELIEADGLKCGWAFPTGCSLNHCAAHYTPNTGDKTVLTYDDVCKLDFGTHVNGRIIDCAFT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 266 VTFNPKYDILLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGPYRIHAGKTVPI 345
Cdd:PTZ00053 259 VAFNPKYDPLLQATKDATNTGIKEAGIDVRLSDIGAAIQEVIESYEVEIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPI 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 346 VKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGES 425
Cdd:PTZ00053 339 VKGGENTRMEEGELFAIETFASTGRGYVNEDLECSHYMKDPGAEFVPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQD 418
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958791266 426 KYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY 477
Cdd:PTZ00053 419 RHLLALKQLVDAGIVNPYPPLCDVRGSYTSQMEHTILLRPTCKEVLSRGDDY 470
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
165-473 |
0e+00 |
|
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: 554.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 165 WNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIkenglnAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYD 244
Cdd:cd01088 1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELG------AGPAFPVNLSINECAAHYTPNAGDDTVLKEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 245 DICKIDFGTHISGRIIDCAFTVTFNPKYDILLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESyeveidgktYQVKPI 324
Cdd:cd01088 75 DVVKLDFGAHVDGYIADSAFTVDFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIES---------YGFKPI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 325 RNLNGHSIGPYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDvghVPIRLPRTKHLLNV 404
Cdd:cd01088 146 RNLTGHSIERYRLHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIYMLNRD---KPLRLPRARKLLDV 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791266 405 INENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSR 473
Cdd:cd01088 223 IYENFGTLPFARRWLDRLGETKLLMALKNLCKAGIVYPYPVLKEISGGYVAQFEHTIIVREDGKEVTTR 291
|
|
| met_pdase_II |
TIGR00501 |
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ... |
170-473 |
3.85e-113 |
|
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: 335.60 E-value: 3.85e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 170 EAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLikenglNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKI 249
Cdd:TIGR00501 10 EAGKIHSKVRREAADRIVPGVKLLEVAEFVENRIREL------GAEPAFPCNISINECAAHFTPKAGDKTVFKDGDVVKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 250 DFGTHISGRIIDCAFTVTFNPKYDILLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESyeveidgktYQVKPIRNLNG 329
Cdd:TIGR00501 84 DLGAHVDGYIADTAITVDLGDQYDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIES---------YGVKPISNLTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 330 HSIGPYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYmkNFDVGHvPIRLPRTKHLLNVINENF 409
Cdd:TIGR00501 155 HSMAPYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDGVGYVTDGGEVSIY--AFLAER-PVRLDSARNLLKTIDENY 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958791266 410 GTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSR 473
Cdd:TIGR00501 232 GTLPFARRWLDKLGDEKYLFALNNLIRHGLIYDYPVLNEISGGYVAQWEHTILVEEHGKEVTTK 295
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
168-374 |
5.21e-34 |
|
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: 126.97 E-value: 5.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 168 FREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrKLIKENGLNaGLAFPT--GCSLNNCAAHYTPNagdTTVLQYDD 245
Cdd:pfam00557 3 MRKAARIAAAALEAALAAIRPGVTERELAAELEA---ARLRRGGAR-GPAFPPivASGPNAAIPHYIPN---DRVLKPGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 246 ICKIDFGTHISGR-IIDCAFTV---TFNPKYDILLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEidgktyqv 321
Cdd:pfam00557 76 LVLIDVGAEYDGGyCSDITRTFvvgKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLG-------- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958791266 322 KPIRNLNGHSIGpYRIHAGKTVPivKGGEATRMEEGEVYAIET--FGSTGKGVVH 374
Cdd:pfam00557 148 EYFPHGLGHGIG-LEVHEGPYIS--RGGDDRVLEPGMVFTIEPgiYFIPGWGGVR 199
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
171-376 |
9.91e-17 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 79.66 E-value: 9.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 171 AAEAHRQVRKYVmswiKPGMTMIEicekLEDCSRKLIKENG-----LNAGlAFP--TGCSLNNCAAHYTPNAgdtTVLQY 243
Cdd:COG0024 19 VAEVLDELAEAV----KPGVTTLE----LDRIAEEFIRDHGaipafLGYY-GFPksICTSVNEVVVHGIPSD---RVLKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 244 DDICKIDFGTHISGRIIDCAFTV---TFNPKYDILLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEveidgktYQ 320
Cdd:COG0024 87 GDIVNIDVGAILDGYHGDSARTFvvgEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNG-------YS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958791266 321 VkpIRNLNGHSIGPyRIHAGktvPIV----KGGEATRMEEGEVYAIETFGSTGK-GVVHDD 376
Cdd:COG0024 160 V--VREFVGHGIGR-EMHEE---PQVpnygRPGRGPRLKPGMVLAIEPMINAGTpEVKVLD 214
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
106-477 |
0e+00 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 718.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 106 RGPRVQTDPPSVPICDLYPNGVFPKGQECEYPPTQdgrtaAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSW 185
Cdd:PTZ00053 104 EQEWKQTQPPTIPVSKQFKDGEYPVGEIQEYPGEN-----SSRTSSEEKRELEKLSEEQYQDLRRAAEVHRQVRRYAQSV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 186 IKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFT 265
Cdd:PTZ00053 179 IKPGVKLIDICERIESKSRELIEADGLKCGWAFPTGCSLNHCAAHYTPNTGDKTVLTYDDVCKLDFGTHVNGRIIDCAFT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 266 VTFNPKYDILLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGPYRIHAGKTVPI 345
Cdd:PTZ00053 259 VAFNPKYDPLLQATKDATNTGIKEAGIDVRLSDIGAAIQEVIESYEVEIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPI 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 346 VKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGES 425
Cdd:PTZ00053 339 VKGGENTRMEEGELFAIETFASTGRGYVNEDLECSHYMKDPGAEFVPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQD 418
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1958791266 426 KYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY 477
Cdd:PTZ00053 419 RHLLALKQLVDAGIVNPYPPLCDVRGSYTSQMEHTILLRPTCKEVLSRGDDY 470
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
165-473 |
0e+00 |
|
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: 554.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 165 WNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIkenglnAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYD 244
Cdd:cd01088 1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELG------AGPAFPVNLSINECAAHYTPNAGDDTVLKEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 245 DICKIDFGTHISGRIIDCAFTVTFNPKYDILLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESyeveidgktYQVKPI 324
Cdd:cd01088 75 DVVKLDFGAHVDGYIADSAFTVDFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIES---------YGFKPI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 325 RNLNGHSIGPYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDvghVPIRLPRTKHLLNV 404
Cdd:cd01088 146 RNLTGHSIERYRLHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIYMLNRD---KPLRLPRARKLLDV 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791266 405 INENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSR 473
Cdd:cd01088 223 IYENFGTLPFARRWLDRLGETKLLMALKNLCKAGIVYPYPVLKEISGGYVAQFEHTIIVREDGKEVTTR 291
|
|
| met_pdase_II |
TIGR00501 |
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ... |
170-473 |
3.85e-113 |
|
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: 335.60 E-value: 3.85e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 170 EAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLikenglNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKI 249
Cdd:TIGR00501 10 EAGKIHSKVRREAADRIVPGVKLLEVAEFVENRIREL------GAEPAFPCNISINECAAHFTPKAGDKTVFKDGDVVKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 250 DFGTHISGRIIDCAFTVTFNPKYDILLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESyeveidgktYQVKPIRNLNG 329
Cdd:TIGR00501 84 DLGAHVDGYIADTAITVDLGDQYDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIES---------YGVKPISNLTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 330 HSIGPYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYmkNFDVGHvPIRLPRTKHLLNVINENF 409
Cdd:TIGR00501 155 HSMAPYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDGVGYVTDGGEVSIY--AFLAER-PVRLDSARNLLKTIDENY 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958791266 410 GTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSR 473
Cdd:TIGR00501 232 GTLPFARRWLDKLGDEKYLFALNNLIRHGLIYDYPVLNEISGGYVAQWEHTILVEEHGKEVTTK 295
|
|
| crvDNA_42K |
TIGR00495 |
42K curved DNA binding protein; Proteins identified by this model have been identified in a ... |
155-465 |
4.12e-34 |
|
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: 131.93 E-value: 4.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 155 KALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEK-----LEDCSRKLIKENGLNAGLAFPTGCSLNNCAA 229
Cdd:TIGR00495 10 QAYSLSNPEVVTKYKMAGEIANNVLKSVVEACSPGAKVVDICEKgdafiMEETAKIFKKEKEMEKGIAFPTCISVNNCVG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 230 HYTPNAGDTT-VLQYDDICKIDFGTHISGRIIDCAFT-VTFNPKYDILLKAVKDATNTGIKCAGIDVRLC-------DVG 300
Cdd:TIGR00495 90 HFSPLKSDQDyILKEGDVVKIDLGCHIDGFIALVAHTfVVGVAQEEPVTGRKADVIAAAHLAAEAALRLVkpgntntQVT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 301 EAIQEVMESYEveidgktyqVKPIRNLNGHSIGPYRIHAGKTVPIV------KGGEATRMEEGEVYAIETFGSTGKGVVH 374
Cdd:TIGR00495 170 EAINKVAHSYG---------CTPVEGMLSHQLKQHVIDGEKVIISNpsdsqkKDHDTAEFEENEVYAVDILVSTGEGKAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 375 D-DMECSHYMKNFDVGHVpIRLPRTKHLLNVINENFGTLAFCRRWLDrlGESKYLMALKNLCDLGIVDPYPPLCDIKGSY 453
Cdd:TIGR00495 241 DaDQRTTIYKRDPSKTYG-LKMKASRAFFSEIERRFDAMPFTLRNFE--DEKRARMGLVECVKHELLQPYPVLYEKEGEF 317
|
330
....*....|..
gi 1958791266 454 TAQFEHTILLRP 465
Cdd:TIGR00495 318 VAQFKFTVLLMP 329
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
168-374 |
5.21e-34 |
|
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: 126.97 E-value: 5.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 168 FREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrKLIKENGLNaGLAFPT--GCSLNNCAAHYTPNagdTTVLQYDD 245
Cdd:pfam00557 3 MRKAARIAAAALEAALAAIRPGVTERELAAELEA---ARLRRGGAR-GPAFPPivASGPNAAIPHYIPN---DRVLKPGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 246 ICKIDFGTHISGR-IIDCAFTV---TFNPKYDILLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEidgktyqv 321
Cdd:pfam00557 76 LVLIDVGAEYDGGyCSDITRTFvvgKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLG-------- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958791266 322 KPIRNLNGHSIGpYRIHAGKTVPivKGGEATRMEEGEVYAIET--FGSTGKGVVH 374
Cdd:pfam00557 148 EYFPHGLGHGIG-LEVHEGPYIS--RGGDDRVLEPGMVFTIEPgiYFIPGWGGVR 199
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
168-377 |
5.77e-28 |
|
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: 110.24 E-value: 5.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 168 FREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIkenglnAGLAFPTGCSLNN--CAAHYTPnagDTTVLQYDD 245
Cdd:cd01066 4 LRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAG------GYPAGPTIVGSGArtALPHYRP---DDRRLQEGD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 246 ICKIDFGTHISGRIIDCAFTVTFNPKYD---ILLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEidgktyqvK 322
Cdd:cd01066 75 LVLVDLGGVYDGYHADLTRTFVIGEPSDeqrELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLG--------P 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958791266 323 PIRNLNGHSIGpYRIHAGktvPIVKGGEATRMEEGEVYAIETF--GSTGKGVVHDDM 377
Cdd:cd01066 147 NFGHRTGHGIG-LEIHEP---PVLKAGDDTVLEPGMVFAVEPGlyLPGGGGVRIEDT 199
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
169-376 |
7.20e-22 |
|
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: 94.10 E-value: 7.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 169 REAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrkLIKENG-----LNAGlAFP-TGC-SLNNCAAHYTPnagDTTVL 241
Cdd:cd01086 5 REAGRIVAEVLDELAKAIKPGVTTKELDQIAHE----FIEEHGaypapLGYY-GFPkSICtSVNEVVCHGIP---DDRVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 242 QYDDICKIDFGTHISGRIIDCAFTV---TFNPKYDILLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYeveidgkT 318
Cdd:cd01086 77 KDGDIVNIDVGVELDGYHGDSARTFivgEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKN-------G 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958791266 319 YQVkpIRNLNGHSIGPYrIHAGKTVPIV-KGGEATRMEEGEVYAIETFGSTGKG--VVHDD 376
Cdd:cd01086 150 YSV--VREFGGHGIGRK-FHEEPQIPNYgRPGTGPKLKPGMVFTIEPMINLGTYevVTLPD 207
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
171-376 |
9.91e-17 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 79.66 E-value: 9.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 171 AAEAHRQVRKYVmswiKPGMTMIEicekLEDCSRKLIKENG-----LNAGlAFP--TGCSLNNCAAHYTPNAgdtTVLQY 243
Cdd:COG0024 19 VAEVLDELAEAV----KPGVTTLE----LDRIAEEFIRDHGaipafLGYY-GFPksICTSVNEVVVHGIPSD---RVLKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 244 DDICKIDFGTHISGRIIDCAFTV---TFNPKYDILLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEveidgktYQ 320
Cdd:COG0024 87 GDIVNIDVGAILDGYHGDSARTFvvgEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNG-------YS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958791266 321 VkpIRNLNGHSIGPyRIHAGktvPIV----KGGEATRMEEGEVYAIETFGSTGK-GVVHDD 376
Cdd:COG0024 160 V--VREFVGHGIGR-EMHEE---PQVpnygRPGRGPRLKPGMVLAIEPMINAGTpEVKVLD 214
|
|
| PA2G4-like |
cd01089 |
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ... |
166-322 |
6.49e-16 |
|
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: 76.99 E-value: 6.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 166 NDFREAAEAHRQVRKYVMSWIKPGMTMIEICEK-----LEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTV 240
Cdd:cd01089 2 TKYKTAGQIANKVLKQVISLCVPGAKVVDLCEKgdkliLEELGKVYKKEKKLEKGIAFPTCISVNNCVCHFSPLKSDATY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 241 -LQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDI--------LLKAVKDATNTG---IKCAGIDVrlcDVGEAIQEVME 308
Cdd:cd01089 82 tLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAETpvtgkkadVIAAAHYALEAAlrlLRPGNQNS---DITEAIQKVIV 158
|
170
....*....|....*.
gi 1958791266 309 SYEV-EIDGKT-YQVK 322
Cdd:cd01089 159 DYGCtPVEGVLsHQLK 174
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
169-363 |
3.26e-14 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 72.93 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 169 REAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrkLIKENGLNaGLAFPT--GCSLNNCAAHYTPNagdTTVLQYDDI 246
Cdd:COG0006 83 RKAARIADAAHEAALAALRPGVTEREVAAELEA----AMRRRGAE-GPSFDTivASGENAAIPHYTPT---DRPLKPGDL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 247 CKIDFGTHISGRIIDCAFTV---TFNPKYDILLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMES--YEVEIDGKTyqv 321
Cdd:COG0006 155 VLIDAGAEYDGYTSDITRTVavgEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEagYGEYFPHGT--- 231
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958791266 322 kpirnlnGHSIGpYRIHagkTVPIVKGGEATRMEEGEVYAIE 363
Cdd:COG0006 232 -------GHGVG-LDVH---EGPQISPGNDRPLEPGMVFTIE 262
|
|
| PRK12896 |
PRK12896 |
methionine aminopeptidase; Reviewed |
138-369 |
4.33e-14 |
|
methionine aminopeptidase; Reviewed
Pssm-ID: 237252 [Multi-domain] Cd Length: 255 Bit Score: 72.18 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 138 PTQDGRTAaWRTTSEEKKALDQASeeiwndfREAAeahrQVRKYVMSWIKPGMTMIEicekLEDCSRKLIKENGLNAG-- 215
Cdd:PRK12896 1 PAQEGRGM-EIKSPRELEKMRKIG-------RIVA----TALKEMGKAVEPGMTTKE----LDRIAEKRLEEHGAIPSpe 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 216 --LAFPTGC--SLNNCAAHYTPnagDTTVLQYDDICKIDFGTHISGRIID-CAftvTF-----NPKYDILLKAVKDATNT 285
Cdd:PRK12896 65 gyYGFPGSTciSVNEEVAHGIP---GPRVIKDGDLVNIDVSAYLDGYHGDtGI---TFavgpvSEEAEKLCRVAEEALWA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 286 GIKCAGIDVRLCDVGEAIQEvmesyEVEIDGktYQVkpIRNLNGHSIGPyRIHAGKTVPIVKG--GEATRMEEGEVYAIE 363
Cdd:PRK12896 139 GIKQVKAGRPLNDIGRAIED-----FAKKNG--YSV--VRDLTGHGVGR-SLHEEPSVILTYTdpLPNRLLRPGMTLAVE 208
|
....*.
gi 1958791266 364 TFGSTG 369
Cdd:PRK12896 209 PFLNLG 214
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
171-371 |
8.51e-14 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 70.93 E-value: 8.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 171 AAEAHRQVRKYVmswiKPGMTMIEicekLEDCSRKLIKENG-LNAGLA---FP-TGC-SLNNCAAHYTPNAgdtTVLQYD 244
Cdd:PRK05716 21 AAEVLDEIEPHV----KPGVTTKE----LDRIAEEYIRDQGaIPAPLGyhgFPkSICtSVNEVVCHGIPSD---KVLKEG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 245 DICKIDFGTHISGRIIDCAFTV---TFNPKYDILLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYeveidgkTYQV 321
Cdd:PRK05716 90 DIVNIDVTVIKDGYHGDTSRTFgvgEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAE-------GFSV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958791266 322 kpIRNLNGHSIGPyRIHAGktvPIV----KGGEATRMEEGEVYAIETFGSTGKG 371
Cdd:PRK05716 163 --VREYCGHGIGR-KFHEE---PQIphygAPGDGPVLKEGMVFTIEPMINAGKR 210
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
169-363 |
8.69e-10 |
|
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: 58.29 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 169 REAAEAHRQVRKYVMSWIKPGMTMIEICEKLEdcsrKLIKENGLNaGLAFPTGCSLNNCAA--HYTPnagDTTVLQYDDI 246
Cdd:cd01092 5 RKAARIADKAFEELLEFIKPGMTEREVAAELE----YFMRKLGAE-GPSFDTIVASGPNSAlpHGVP---SDRKIEEGDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791266 247 CKIDFGTHISGRIIDCAFTVTFNPKYDILLK---AVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVeidGKTYqvkp 323
Cdd:cd01092 77 VLIDFGAIYDGYCSDITRTVAVGEPSDELKEiyeIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGY---GEYF---- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958791266 324 IRNLnGHSIGpYRIHAGktvPIVKGGEATRMEEGEVYAIE 363
Cdd:cd01092 150 IHRT-GHGVG-LEVHEA---PYISPGSDDVLEEGMVFTIE 184
|
|
| |
