|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
107-478 |
0e+00 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 717.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 107 RGPKVQTDPPSVPICDLYPNGVFPKGQECEYPPTQdgrtaAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSW 186
Cdd:PTZ00053 104 EQEWKQTQPPTIPVSKQFKDGEYPVGEIQEYPGEN-----SSRTSSEEKRELEKLSEEQYQDLRRAAEVHRQVRRYAQSV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 187 IKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFT 266
Cdd:PTZ00053 179 IKPGVKLIDICERIESKSRELIEADGLKCGWAFPTGCSLNHCAAHYTPNTGDKTVLTYDDVCKLDFGTHVNGRIIDCAFT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 267 VTFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGPYRIHAGKTVPI 346
Cdd:PTZ00053 259 VAFNPKYDPLLQATKDATNTGIKEAGIDVRLSDIGAAIQEVIESYEVEIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPI 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 347 VKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGES 426
Cdd:PTZ00053 339 VKGGENTRMEEGELFAIETFASTGRGYVNEDLECSHYMKDPGAEFVPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQD 418
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907076168 427 KYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY 478
Cdd:PTZ00053 419 RHLLALKQLVDAGIVNPYPPLCDVRGSYTSQMEHTILLRPTCKEVLSRGDDY 470
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
166-474 |
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: 551.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 166 WNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIkenglnAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYD 245
Cdd:cd01088 1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELG------AGPAFPVNLSINECAAHYTPNAGDDTVLKEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 246 DICKIDFGTHISGRIIDCAFTVTFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESyeveidgktYQVKPI 325
Cdd:cd01088 75 DVVKLDFGAHVDGYIADSAFTVDFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIES---------YGFKPI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 326 RNLNGHSIGPYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDvghVPIRLPRTKHLLNV 405
Cdd:cd01088 146 RNLTGHSIERYRLHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIYMLNRD---KPLRLPRARKLLDV 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907076168 406 INENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSR 474
Cdd:cd01088 223 IYENFGTLPFARRWLDRLGETKLLMALKNLCKAGIVYPYPVLKEISGGYVAQFEHTIIVREDGKEVTTR 291
|
|
| met_pdase_II |
TIGR00501 |
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ... |
171-474 |
4.52e-112 |
|
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: 332.91 E-value: 4.52e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 171 EAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLikenglNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKI 250
Cdd:TIGR00501 10 EAGKIHSKVRREAADRIVPGVKLLEVAEFVENRIREL------GAEPAFPCNISINECAAHFTPKAGDKTVFKDGDVVKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 251 DFGTHISGRIIDCAFTVTFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESyeveidgktYQVKPIRNLNG 330
Cdd:TIGR00501 84 DLGAHVDGYIADTAITVDLGDQYDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIES---------YGVKPISNLTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 331 HSIGPYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYmkNFDVGHvPIRLPRTKHLLNVINENF 410
Cdd:TIGR00501 155 HSMAPYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDGVGYVTDGGEVSIY--AFLAER-PVRLDSARNLLKTIDENY 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907076168 411 GTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSR 474
Cdd:TIGR00501 232 GTLPFARRWLDKLGDEKYLFALNNLIRHGLIYDYPVLNEISGGYVAQWEHTILVEEHGKEVTTK 295
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
169-375 |
4.53e-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: 4.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 169 FREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrKLIKENGLNaGLAFPT--GCSLNNCAAHYTPNagdTTVLQYDD 246
Cdd:pfam00557 3 MRKAARIAAAALEAALAAIRPGVTERELAAELEA---ARLRRGGAR-GPAFPPivASGPNAAIPHYIPN---DRVLKPGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 247 ICKIDFGTHISGR-IIDCAFTV---TFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEidgktyqv 322
Cdd:pfam00557 76 LVLIDVGAEYDGGyCSDITRTFvvgKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLG-------- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907076168 323 KPIRNLNGHSIGpYRIHAGKTVPivKGGEATRMEEGEVYAIET--FGSTGKGVVH 375
Cdd:pfam00557 148 EYFPHGLGHGIG-LEVHEGPYIS--RGGDDRVLEPGMVFTIEPgiYFIPGWGGVR 199
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
172-377 |
3.62e-16 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 78.12 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 172 AAEAHRQVRKYVmswiKPGMTMIEicekLEDCSRKLIKENG-----LNAGlAFP--TGCSLNNCAAHYTPNAgdtTVLQY 244
Cdd:COG0024 19 VAEVLDELAEAV----KPGVTTLE----LDRIAEEFIRDHGaipafLGYY-GFPksICTSVNEVVVHGIPSD---RVLKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 245 DDICKIDFGTHISGRIIDCAFTV---TFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEveidgktYQ 321
Cdd:COG0024 87 GDIVNIDVGAILDGYHGDSARTFvvgEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNG-------YS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907076168 322 VkpIRNLNGHSIGPyRIHAGktvPIV----KGGEATRMEEGEVYAIETFGSTGK-GVVHDD 377
Cdd:COG0024 160 V--VREFVGHGIGR-EMHEE---PQVpnygRPGRGPRLKPGMVLAIEPMINAGTpEVKVLD 214
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
107-478 |
0e+00 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 717.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 107 RGPKVQTDPPSVPICDLYPNGVFPKGQECEYPPTQdgrtaAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSW 186
Cdd:PTZ00053 104 EQEWKQTQPPTIPVSKQFKDGEYPVGEIQEYPGEN-----SSRTSSEEKRELEKLSEEQYQDLRRAAEVHRQVRRYAQSV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 187 IKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFT 266
Cdd:PTZ00053 179 IKPGVKLIDICERIESKSRELIEADGLKCGWAFPTGCSLNHCAAHYTPNTGDKTVLTYDDVCKLDFGTHVNGRIIDCAFT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 267 VTFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGPYRIHAGKTVPI 346
Cdd:PTZ00053 259 VAFNPKYDPLLQATKDATNTGIKEAGIDVRLSDIGAAIQEVIESYEVEIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPI 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 347 VKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGES 426
Cdd:PTZ00053 339 VKGGENTRMEEGELFAIETFASTGRGYVNEDLECSHYMKDPGAEFVPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQD 418
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907076168 427 KYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY 478
Cdd:PTZ00053 419 RHLLALKQLVDAGIVNPYPPLCDVRGSYTSQMEHTILLRPTCKEVLSRGDDY 470
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
166-474 |
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: 551.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 166 WNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIkenglnAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYD 245
Cdd:cd01088 1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELG------AGPAFPVNLSINECAAHYTPNAGDDTVLKEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 246 DICKIDFGTHISGRIIDCAFTVTFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESyeveidgktYQVKPI 325
Cdd:cd01088 75 DVVKLDFGAHVDGYIADSAFTVDFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIES---------YGFKPI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 326 RNLNGHSIGPYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDvghVPIRLPRTKHLLNV 405
Cdd:cd01088 146 RNLTGHSIERYRLHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIYMLNRD---KPLRLPRARKLLDV 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907076168 406 INENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSR 474
Cdd:cd01088 223 IYENFGTLPFARRWLDRLGETKLLMALKNLCKAGIVYPYPVLKEISGGYVAQFEHTIIVREDGKEVTTR 291
|
|
| met_pdase_II |
TIGR00501 |
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ... |
171-474 |
4.52e-112 |
|
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: 332.91 E-value: 4.52e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 171 EAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLikenglNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKI 250
Cdd:TIGR00501 10 EAGKIHSKVRREAADRIVPGVKLLEVAEFVENRIREL------GAEPAFPCNISINECAAHFTPKAGDKTVFKDGDVVKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 251 DFGTHISGRIIDCAFTVTFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESyeveidgktYQVKPIRNLNG 330
Cdd:TIGR00501 84 DLGAHVDGYIADTAITVDLGDQYDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIES---------YGVKPISNLTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 331 HSIGPYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYmkNFDVGHvPIRLPRTKHLLNVINENF 410
Cdd:TIGR00501 155 HSMAPYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDGVGYVTDGGEVSIY--AFLAER-PVRLDSARNLLKTIDENY 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907076168 411 GTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSR 474
Cdd:TIGR00501 232 GTLPFARRWLDKLGDEKYLFALNNLIRHGLIYDYPVLNEISGGYVAQWEHTILVEEHGKEVTTK 295
|
|
| crvDNA_42K |
TIGR00495 |
42K curved DNA binding protein; Proteins identified by this model have been identified in a ... |
156-466 |
3.42e-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: 132.32 E-value: 3.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 156 KALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEK-----LEDCSRKLIKENGLNAGLAFPTGCSLNNCAA 230
Cdd:TIGR00495 10 QAYSLSNPEVVTKYKMAGEIANNVLKSVVEACSPGAKVVDICEKgdafiMEETAKIFKKEKEMEKGIAFPTCISVNNCVG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 231 HYTPNAGDTT-VLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDILLTAVK-DATNTGIKCAGIDVRLC-------DVG 301
Cdd:TIGR00495 90 HFSPLKSDQDyILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEEPVTGRKaDVIAAAHLAAEAALRLVkpgntntQVT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 302 EAIQEVMESYEveidgktyqVKPIRNLNGHSIGPYRIHAGKTVPIV------KGGEATRMEEGEVYAIETFGSTGKGVVH 375
Cdd:TIGR00495 170 EAINKVAHSYG---------CTPVEGMLSHQLKQHVIDGEKVIISNpsdsqkKDHDTAEFEENEVYAVDILVSTGEGKAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 376 D-DMECSHYMKNFDVGHVpIRLPRTKHLLNVINENFGTLAFCRRWLDrlGESKYLMALKNLCDLGIVDPYPPLCDIKGSY 454
Cdd:TIGR00495 241 DaDQRTTIYKRDPSKTYG-LKMKASRAFFSEIERRFDAMPFTLRNFE--DEKRARMGLVECVKHELLQPYPVLYEKEGEF 317
|
330
....*....|..
gi 1907076168 455 TAQFEHTILLRP 466
Cdd:TIGR00495 318 VAQFKFTVLLMP 329
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
169-375 |
4.53e-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: 4.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 169 FREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrKLIKENGLNaGLAFPT--GCSLNNCAAHYTPNagdTTVLQYDD 246
Cdd:pfam00557 3 MRKAARIAAAALEAALAAIRPGVTERELAAELEA---ARLRRGGAR-GPAFPPivASGPNAAIPHYIPN---DRVLKPGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 247 ICKIDFGTHISGR-IIDCAFTV---TFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEidgktyqv 322
Cdd:pfam00557 76 LVLIDVGAEYDGGyCSDITRTFvvgKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLG-------- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907076168 323 KPIRNLNGHSIGpYRIHAGKTVPivKGGEATRMEEGEVYAIET--FGSTGKGVVH 375
Cdd:pfam00557 148 EYFPHGLGHGIG-LEVHEGPYIS--RGGDDRVLEPGMVFTIEPgiYFIPGWGGVR 199
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
169-378 |
4.97e-27 |
|
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: 107.92 E-value: 4.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 169 FREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIkenglnAGLAFPTGCSLNN--CAAHYTPnagDTTVLQYDD 246
Cdd:cd01066 4 LRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAG------GYPAGPTIVGSGArtALPHYRP---DDRRLQEGD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 247 ICKIDFGTHISGRIIDCAFTVTFNPKYD---ILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEidgktyqvK 323
Cdd:cd01066 75 LVLVDLGGVYDGYHADLTRTFVIGEPSDeqrELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLG--------P 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907076168 324 PIRNLNGHSIGpYRIHAGktvPIVKGGEATRMEEGEVYAIETF--GSTGKGVVHDDM 378
Cdd:cd01066 147 NFGHRTGHGIG-LEIHEP---PVLKAGDDTVLEPGMVFAVEPGlyLPGGGGVRIEDT 199
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
170-377 |
7.05e-21 |
|
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: 91.40 E-value: 7.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 170 REAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrkLIKENG-----LNAGlAFP-TGC-SLNNCAAHYTPnagDTTVL 242
Cdd:cd01086 5 REAGRIVAEVLDELAKAIKPGVTTKELDQIAHE----FIEEHGaypapLGYY-GFPkSICtSVNEVVCHGIP---DDRVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 243 QYDDICKIDFGTHISGRIIDCAFTV---TFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYeveidgkT 319
Cdd:cd01086 77 KDGDIVNIDVGVELDGYHGDSARTFivgEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKN-------G 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907076168 320 YQVkpIRNLNGHSIGPYrIHAGKTVPIV-KGGEATRMEEGEVYAIETFGSTGKG--VVHDD 377
Cdd:cd01086 150 YSV--VREFGGHGIGRK-FHEEPQIPNYgRPGTGPKLKPGMVFTIEPMINLGTYevVTLPD 207
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
172-377 |
3.62e-16 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 78.12 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 172 AAEAHRQVRKYVmswiKPGMTMIEicekLEDCSRKLIKENG-----LNAGlAFP--TGCSLNNCAAHYTPNAgdtTVLQY 244
Cdd:COG0024 19 VAEVLDELAEAV----KPGVTTLE----LDRIAEEFIRDHGaipafLGYY-GFPksICTSVNEVVVHGIPSD---RVLKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 245 DDICKIDFGTHISGRIIDCAFTV---TFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEveidgktYQ 321
Cdd:COG0024 87 GDIVNIDVGAILDGYHGDSARTFvvgEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNG-------YS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907076168 322 VkpIRNLNGHSIGPyRIHAGktvPIV----KGGEATRMEEGEVYAIETFGSTGK-GVVHDD 377
Cdd:COG0024 160 V--VREFVGHGIGR-EMHEE---PQVpnygRPGRGPRLKPGMVLAIEPMINAGTpEVKVLD 214
|
|
| PA2G4-like |
cd01089 |
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ... |
167-323 |
8.03e-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: 76.60 E-value: 8.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 167 NDFREAAEAHRQVRKYVMSWIKPGMTMIEICEK-----LEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTV 241
Cdd:cd01089 2 TKYKTAGQIANKVLKQVISLCVPGAKVVDLCEKgdkliLEELGKVYKKEKKLEKGIAFPTCISVNNCVCHFSPLKSDATY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 242 -LQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDILLTAVK-DATNTGIKCAGIDVRLC-------DVGEAIQEVMESYE 312
Cdd:cd01089 82 tLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAETPVTGKKaDVIAAAHYALEAALRLLrpgnqnsDITEAIQKVIVDYG 161
|
170
....*....|...
gi 1907076168 313 V-EIDGKT-YQVK 323
Cdd:cd01089 162 CtPVEGVLsHQLK 174
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
170-364 |
2.06e-14 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 73.70 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 170 REAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrkLIKENGLNaGLAFPT--GCSLNNCAAHYTPNagdTTVLQYDDI 247
Cdd:COG0006 83 RKAARIADAAHEAALAALRPGVTEREVAAELEA----AMRRRGAE-GPSFDTivASGENAAIPHYTPT---DRPLKPGDL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 248 CKIDFGTHISGRIIDCAFTV---TFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMES--YEVEIDGKTyqv 322
Cdd:COG0006 155 VLIDAGAEYDGYTSDITRTVavgEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEagYGEYFPHGT--- 231
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907076168 323 kpirnlnGHSIGpYRIHagkTVPIVKGGEATRMEEGEVYAIE 364
Cdd:COG0006 232 -------GHGVG-LDVH---EGPQISPGNDRPLEPGMVFTIE 262
|
|
| PRK12896 |
PRK12896 |
methionine aminopeptidase; Reviewed |
139-370 |
1.57e-13 |
|
methionine aminopeptidase; Reviewed
Pssm-ID: 237252 [Multi-domain] Cd Length: 255 Bit Score: 70.25 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 139 PTQDGRTAaWRTTSEEKKALDQASeeiwndfREAAeahrQVRKYVMSWIKPGMTMIEicekLEDCSRKLIKENGLNAG-- 216
Cdd:PRK12896 1 PAQEGRGM-EIKSPRELEKMRKIG-------RIVA----TALKEMGKAVEPGMTTKE----LDRIAEKRLEEHGAIPSpe 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 217 --LAFPTGC--SLNNCAAHYTPnagDTTVLQYDDICKIDFGTHISGRIID-CAftvTF-----NPKYDILLTAVKDATNT 286
Cdd:PRK12896 65 gyYGFPGSTciSVNEEVAHGIP---GPRVIKDGDLVNIDVSAYLDGYHGDtGI---TFavgpvSEEAEKLCRVAEEALWA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 287 GIKCAGIDVRLCDVGEAIQEvmesyEVEIDGktYQVkpIRNLNGHSIGPyRIHAGKTVPIVKG--GEATRMEEGEVYAIE 364
Cdd:PRK12896 139 GIKQVKAGRPLNDIGRAIED-----FAKKNG--YSV--VRDLTGHGVGR-SLHEEPSVILTYTdpLPNRLLRPGMTLAVE 208
|
....*.
gi 1907076168 365 TFGSTG 370
Cdd:PRK12896 209 PFLNLG 214
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
172-372 |
3.33e-13 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 69.39 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 172 AAEAHRQVRKYVmswiKPGMTMIEicekLEDCSRKLIKENG-LNAGLA---FP-TGC-SLNNCAAHYTPNAgdtTVLQYD 245
Cdd:PRK05716 21 AAEVLDEIEPHV----KPGVTTKE----LDRIAEEYIRDQGaIPAPLGyhgFPkSICtSVNEVVCHGIPSD---KVLKEG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 246 DICKIDFGTHISGRIIDCAFTV---TFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYeveidgkTYQV 322
Cdd:PRK05716 90 DIVNIDVTVIKDGYHGDTSRTFgvgEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAE-------GFSV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907076168 323 kpIRNLNGHSIGPyRIHAGktvPIV----KGGEATRMEEGEVYAIETFGSTGKG 372
Cdd:PRK05716 163 --VREYCGHGIGR-KFHEE---PQIphygAPGDGPVLKEGMVFTIEPMINAGKR 210
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
170-364 |
2.03e-09 |
|
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: 57.52 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 170 REAAEAHRQVRKYVMSWIKPGMTMIEICEKLEdcsrKLIKENGLNaGLAFPTGCSLNNCAA--HYTPnagDTTVLQYDDI 247
Cdd:cd01092 5 RKAARIADKAFEELLEFIKPGMTEREVAAELE----YFMRKLGAE-GPSFDTIVASGPNSAlpHGVP---SDRKIEEGDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 248 CKIDFGTHISGRIIDCAFTVTFNPKYDILLT---AVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVeidGKTYqvkp 324
Cdd:cd01092 77 VLIDFGAIYDGYCSDITRTVAVGEPSDELKEiyeIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGY---GEYF---- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907076168 325 IRNLnGHSIGpYRIHAGktvPIVKGGEATRMEEGEVYAIE 364
Cdd:cd01092 150 IHRT-GHGVG-LEVHEA---PYISPGSDDVLEEGMVFTIE 184
|
|
| |
