|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
58-421 |
0e+00 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 572.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 58 IELLFPDGKYPEGAWMDYhQDFNLQRTTDEEsrylKRDLERA--EHWNDVRKGAEIHRRVRRAIKDRIVPGMKLMDIADM 135
Cdd:PTZ00053 117 VSKQFKDGEYPVGEIQEY-PGENSSRTSSEE----KRELEKLseEQYQDLRRAAEVHRQVRRYAQSVIKPGVKLIDICER 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 136 IENTTRKYTGAENLLAmedpksqGIGFPTGLSLNHCAAHFTPNAGDKTVLKYEDVMKVDYGVQVNGNIIDSAFTVSFDPQ 215
Cdd:PTZ00053 192 IESKSRELIEADGLKC-------GWAFPTGCSLNHCAAHYTPNTGDKTVLTYDDVCKLDFGTHVNGRIIDCAFTVAFNPK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 216 YDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESYEVEINGETYQVKPCRNLCGHSIAPYRIHGGKSVPIVKNGDT 295
Cdd:PTZ00053 265 YDPLLQATKDATNTGIKEAGIDVRLSDIGAAIQEVIESYEVEIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPIVKGGEN 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 296 TKMEEGEHFAIETFGSTGRGYVTAGGEVSHYARSAEDHQVMPTLDSAKNLLKTIDRNFGTLPFCRRYLDRLGQEKYLFAL 375
Cdd:PTZ00053 345 TRMEEGELFAIETFASTGRGYVNEDLECSHYMKDPGAEFVPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQDRHLLAL 424
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 330443401 376 NNLVRHGLVQDYPPLNDIPGSYTAQFEHTILLHAHKKEVVSKGDDY 421
Cdd:PTZ00053 425 KQLVDAGIVNPYPPLCDVRGSYTSQMEHTILLRPTCKEVLSRGDDY 470
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
102-417 |
5.47e-171 |
|
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: 480.21 E-value: 5.47e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 102 WNDVRKGAEIHRRVRRAIKDRIVPGMKLMDIADMIENTTRKYTGaenllamedpksqGIGFPTGLSLNHCAAHFTPNAGD 181
Cdd:cd01088 1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELGA-------------GPAFPVNLSINECAAHYTPNAGD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 182 KTVLKYEDVMKVDYGVQVNGNIIDSAFTVSFDPQYDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESyeveinge 261
Cdd:cd01088 68 DTVLKEGDVVKLDFGAHVDGYIADSAFTVDFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIES-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 262 tYQVKPCRNLCGHSIAPYRIHGGKSVPIVKNGDTTKMEEGEHFAIETFGSTGRGYVTAGGEVSHYARSAEdhqVMPTLDS 341
Cdd:cd01088 140 -YGFKPIRNLTGHSIERYRLHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIYMLNRD---KPLRLPR 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330443401 342 AKNLLKTIDRNFGTLPFCRRYLDRLGQEKYLFALNNLVRHGLVQDYPPLNDIPGSYTAQFEHTILLHAHKKEVVSK 417
Cdd:cd01088 216 ARKLLDVIYENFGTLPFARRWLDRLGETKLLMALKNLCKAGIVYPYPVLKEISGGYVAQFEHTIIVREDGKEVTTR 291
|
|
| met_pdase_II |
TIGR00501 |
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ... |
95-417 |
3.07e-170 |
|
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: 478.51 E-value: 3.07e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 95 DLERAEHWndVRKGaEIHRRVRRAIKDRIVPGMKLMDIADMIENTTRKYtGAEnllamedPksqgiGFPTGLSLNHCAAH 174
Cdd:TIGR00501 1 DIERAEKW--IEAG-KIHSKVRREAADRIVPGVKLLEVAEFVENRIREL-GAE-------P-----AFPCNISINECAAH 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 175 FTPNAGDKTVLKYEDVMKVDYGVQVNGNIIDSAFTVSFDPQYDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESy 254
Cdd:TIGR00501 65 FTPKAGDKTVFKDGDVVKLDLGAHVDGYIADTAITVDLGDQYDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIES- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 255 eveingetYQVKPCRNLCGHSIAPYRIHGGKSVPIVKNGDTTKMEEGEHFAIETFGSTGRGYVTAGGEVSHYARSAEdHQ 334
Cdd:TIGR00501 144 --------YGVKPISNLTGHSMAPYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDGVGYVTDGGEVSIYAFLAE-RP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 335 VMptLDSAKNLLKTIDRNFGTLPFCRRYLDRLGQEKYLFALNNLVRHGLVQDYPPLNDIPGSYTAQFEHTILLHAHKKEV 414
Cdd:TIGR00501 215 VR--LDSARNLLKTIDENYGTLPFARRWLDKLGDEKYLFALNNLIRHGLIYDYPVLNEISGGYVAQWEHTILVEEHGKEV 292
|
...
gi 330443401 415 VSK 417
Cdd:TIGR00501 293 TTK 295
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
106-307 |
6.94e-28 |
|
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: 109.25 E-value: 6.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 106 RKGAEIHRRVRRAIKDRIVPGMKLMDIADMIENTTRKYTGAEnllamedpksqGIGFPT--GLSLNHCAAHFTPNagdKT 183
Cdd:pfam00557 4 RKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGAR-----------GPAFPPivASGPNAAIPHYIPN---DR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 184 VLKYEDVMKVDYGVQVNGN-IIDSAFTV---SFDPQYDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESYEVEin 259
Cdd:pfam00557 70 VLKPGDLVLIDVGAEYDGGyCSDITRTFvvgKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLG-- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 330443401 260 getyqvKPCRNLCGHSIApYRIHGGKSVPivKNGDTTKMEEGEHFAIE 307
Cdd:pfam00557 148 ------EYFPHGLGHGIG-LEVHEGPYIS--RGGDDRVLEPGMVFTIE 186
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
106-317 |
1.45e-21 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 93.15 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 106 RKGAEIHRRVRRAIKDRIVPGMKLMDIADMIENTTRKYtGAEnllamedPKSQGI-GFP--TGLSLNHCAAHFTPnagDK 182
Cdd:COG0024 13 REAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDH-GAI-------PAFLGYyGFPksICTSVNEVVVHGIP---SD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 183 TVLKYEDVMKVDYGVQVNGNIIDSAFTV---SFDPQYDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESyeveiN 259
Cdd:COG0024 82 RVLKDGDIVNIDVGAILDGYHGDSARTFvvgEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAES-----N 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330443401 260 GetYQVkpCRNLCGHSIapyrihgGKSV---PIV----KNGDTTKMEEGEHFAIETFGSTGRGYV 317
Cdd:COG0024 157 G--YSV--VREFVGHGI-------GREMheePQVpnygRPGRGPRLKPGMVLAIEPMINAGTPEV 210
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
58-421 |
0e+00 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 572.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 58 IELLFPDGKYPEGAWMDYhQDFNLQRTTDEEsrylKRDLERA--EHWNDVRKGAEIHRRVRRAIKDRIVPGMKLMDIADM 135
Cdd:PTZ00053 117 VSKQFKDGEYPVGEIQEY-PGENSSRTSSEE----KRELEKLseEQYQDLRRAAEVHRQVRRYAQSVIKPGVKLIDICER 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 136 IENTTRKYTGAENLLAmedpksqGIGFPTGLSLNHCAAHFTPNAGDKTVLKYEDVMKVDYGVQVNGNIIDSAFTVSFDPQ 215
Cdd:PTZ00053 192 IESKSRELIEADGLKC-------GWAFPTGCSLNHCAAHYTPNTGDKTVLTYDDVCKLDFGTHVNGRIIDCAFTVAFNPK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 216 YDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESYEVEINGETYQVKPCRNLCGHSIAPYRIHGGKSVPIVKNGDT 295
Cdd:PTZ00053 265 YDPLLQATKDATNTGIKEAGIDVRLSDIGAAIQEVIESYEVEIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPIVKGGEN 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 296 TKMEEGEHFAIETFGSTGRGYVTAGGEVSHYARSAEDHQVMPTLDSAKNLLKTIDRNFGTLPFCRRYLDRLGQEKYLFAL 375
Cdd:PTZ00053 345 TRMEEGELFAIETFASTGRGYVNEDLECSHYMKDPGAEFVPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQDRHLLAL 424
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 330443401 376 NNLVRHGLVQDYPPLNDIPGSYTAQFEHTILLHAHKKEVVSKGDDY 421
Cdd:PTZ00053 425 KQLVDAGIVNPYPPLCDVRGSYTSQMEHTILLRPTCKEVLSRGDDY 470
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
102-417 |
5.47e-171 |
|
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: 480.21 E-value: 5.47e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 102 WNDVRKGAEIHRRVRRAIKDRIVPGMKLMDIADMIENTTRKYTGaenllamedpksqGIGFPTGLSLNHCAAHFTPNAGD 181
Cdd:cd01088 1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELGA-------------GPAFPVNLSINECAAHYTPNAGD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 182 KTVLKYEDVMKVDYGVQVNGNIIDSAFTVSFDPQYDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESyeveinge 261
Cdd:cd01088 68 DTVLKEGDVVKLDFGAHVDGYIADSAFTVDFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIES-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 262 tYQVKPCRNLCGHSIAPYRIHGGKSVPIVKNGDTTKMEEGEHFAIETFGSTGRGYVTAGGEVSHYARSAEdhqVMPTLDS 341
Cdd:cd01088 140 -YGFKPIRNLTGHSIERYRLHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIYMLNRD---KPLRLPR 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330443401 342 AKNLLKTIDRNFGTLPFCRRYLDRLGQEKYLFALNNLVRHGLVQDYPPLNDIPGSYTAQFEHTILLHAHKKEVVSK 417
Cdd:cd01088 216 ARKLLDVIYENFGTLPFARRWLDRLGETKLLMALKNLCKAGIVYPYPVLKEISGGYVAQFEHTIIVREDGKEVTTR 291
|
|
| met_pdase_II |
TIGR00501 |
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ... |
95-417 |
3.07e-170 |
|
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: 478.51 E-value: 3.07e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 95 DLERAEHWndVRKGaEIHRRVRRAIKDRIVPGMKLMDIADMIENTTRKYtGAEnllamedPksqgiGFPTGLSLNHCAAH 174
Cdd:TIGR00501 1 DIERAEKW--IEAG-KIHSKVRREAADRIVPGVKLLEVAEFVENRIREL-GAE-------P-----AFPCNISINECAAH 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 175 FTPNAGDKTVLKYEDVMKVDYGVQVNGNIIDSAFTVSFDPQYDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESy 254
Cdd:TIGR00501 65 FTPKAGDKTVFKDGDVVKLDLGAHVDGYIADTAITVDLGDQYDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIES- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 255 eveingetYQVKPCRNLCGHSIAPYRIHGGKSVPIVKNGDTTKMEEGEHFAIETFGSTGRGYVTAGGEVSHYARSAEdHQ 334
Cdd:TIGR00501 144 --------YGVKPISNLTGHSMAPYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDGVGYVTDGGEVSIYAFLAE-RP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 335 VMptLDSAKNLLKTIDRNFGTLPFCRRYLDRLGQEKYLFALNNLVRHGLVQDYPPLNDIPGSYTAQFEHTILLHAHKKEV 414
Cdd:TIGR00501 215 VR--LDSARNLLKTIDENYGTLPFARRWLDKLGDEKYLFALNNLIRHGLIYDYPVLNEISGGYVAQWEHTILVEEHGKEV 292
|
...
gi 330443401 415 VSK 417
Cdd:TIGR00501 293 TTK 295
|
|
| crvDNA_42K |
TIGR00495 |
42K curved DNA binding protein; Proteins identified by this model have been identified in a ... |
84-407 |
3.86e-35 |
|
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: 133.86 E-value: 3.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 84 TTDEESRYLKRDLERAEHWNDVRKGAEIHRRVRRAIKDRIVPGMKLMDIA----DMIENTTRK-YTGAENLlamedpkSQ 158
Cdd:TIGR00495 2 SGKDEQQEQAYSLSNPEVVTKYKMAGEIANNVLKSVVEACSPGAKVVDICekgdAFIMEETAKiFKKEKEM-------EK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 159 GIGFPTGLSLNHCAAHFTPNAGDKT-VLKYEDVMKVDYGVQVNGNIIDSAFTVSFDPQYDNLL----AAVKDATYTGIKE 233
Cdd:TIGR00495 75 GIAFPTCISVNNCVGHFSPLKSDQDyILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEEPVtgrkADVIAAAHLAAEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 234 AGIDVRL----TDIGEAIQEVMESYEVeingetyqvKPCRNLCGHSIAPYRIHGGKSVPIV------KNGDTTKMEEGEH 303
Cdd:TIGR00495 155 ALRLVKPgntnTQVTEAINKVAHSYGC---------TPVEGMLSHQLKQHVIDGEKVIISNpsdsqkKDHDTAEFEENEV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 304 FAIETFGSTGRGYVTAGGEVSHYARSAEDHQVMPTLDSAKNLLKTIDRNFGTLPFCRRYLDrlGQEKYLFALNNLVRHGL 383
Cdd:TIGR00495 226 YAVDILVSTGEGKAKDADQRTTIYKRDPSKTYGLKMKASRAFFSEIERRFDAMPFTLRNFE--DEKRARMGLVECVKHEL 303
|
330 340
....*....|....*....|....
gi 330443401 384 VQDYPPLNDIPGSYTAQFEHTILL 407
Cdd:TIGR00495 304 LQPYPVLYEKEGEFVAQFKFTVLL 327
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
106-307 |
6.94e-28 |
|
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: 109.25 E-value: 6.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 106 RKGAEIHRRVRRAIKDRIVPGMKLMDIADMIENTTRKYTGAEnllamedpksqGIGFPT--GLSLNHCAAHFTPNagdKT 183
Cdd:pfam00557 4 RKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGAR-----------GPAFPPivASGPNAAIPHYIPN---DR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 184 VLKYEDVMKVDYGVQVNGN-IIDSAFTV---SFDPQYDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESYEVEin 259
Cdd:pfam00557 70 VLKPGDLVLIDVGAEYDGGyCSDITRTFvvgKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLG-- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 330443401 260 getyqvKPCRNLCGHSIApYRIHGGKSVPivKNGDTTKMEEGEHFAIE 307
Cdd:pfam00557 148 ------EYFPHGLGHGIG-LEVHEGPYIS--RGGDDRVLEPGMVFTIE 186
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
106-318 |
7.89e-26 |
|
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: 104.50 E-value: 7.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 106 RKGAEIHRRVRRAIKDRIVPGMKLMDIADMIENTTRKYtgaenlLAMEDPKSQGiGFP--TGLSLNHCAAHFTPnagDKT 183
Cdd:cd01086 5 REAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEH------GAYPAPLGYY-GFPksICTSVNEVVCHGIP---DDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 184 VLKYEDVMKVDYGVQVNGNIIDSAFTV---SFDPQYDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESYeveing 260
Cdd:cd01086 75 VLKDGDIVNIDVGVELDGYHGDSARTFivgEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKN------ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 330443401 261 eTYQVkpCRNLCGHSIAPYrIHGGKSVPIV-KNGDTTKMEEGEHFAIETFGSTGRGYVT 318
Cdd:cd01086 149 -GYSV--VREFGGHGIGRK-FHEEPQIPNYgRPGTGPKLKPGMVFTIEPMINLGTYEVV 203
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
106-317 |
1.45e-21 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 93.15 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 106 RKGAEIHRRVRRAIKDRIVPGMKLMDIADMIENTTRKYtGAEnllamedPKSQGI-GFP--TGLSLNHCAAHFTPnagDK 182
Cdd:COG0024 13 REAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDH-GAI-------PAFLGYyGFPksICTSVNEVVVHGIP---SD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 183 TVLKYEDVMKVDYGVQVNGNIIDSAFTV---SFDPQYDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESyeveiN 259
Cdd:COG0024 82 RVLKDGDIVNIDVGAILDGYHGDSARTFvvgEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAES-----N 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330443401 260 GetYQVkpCRNLCGHSIapyrihgGKSV---PIV----KNGDTTKMEEGEHFAIETFGSTGRGYV 317
Cdd:COG0024 157 G--YSV--VREFVGHGI-------GREMheePQVpnygRPGRGPRLKPGMVLAIEPMINAGTPEV 210
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
106-318 |
3.62e-20 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 89.04 E-value: 3.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 106 RKGAEIHRRVRRAIKDRIVPGMKLMDIADMIENTTRKYtGAEnllamedPKSQGI-GFP--TGLSLNHCAAHFTPnagDK 182
Cdd:PRK05716 15 RVAGRLAAEVLDEIEPHVKPGVTTKELDRIAEEYIRDQ-GAI-------PAPLGYhGFPksICTSVNEVVCHGIP---SD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 183 TVLKYEDVMKVDYGVQVNGNIIDSAFTVSF---DPQYDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESyevein 259
Cdd:PRK05716 84 KVLKEGDIVNIDVTVIKDGYHGDTSRTFGVgeiSPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEA------ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 260 gETYQVkpCRNLCGHSIAPyRIHGGKSVP-IVKNGDTTKMEEGEHFAIETFGSTGRGYVT 318
Cdd:PRK05716 158 -EGFSV--VREYCGHGIGR-KFHEEPQIPhYGAPGDGPVLKEGMVFTIEPMINAGKREVK 213
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
105-309 |
1.05e-18 |
|
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: 84.04 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 105 VRKGAEIHRRVRRAIKDRIVPGMKLMDIADMIENTTRKYTGAEnllamedpksqgiGFPTGLSLNH--CAAHFTPNAgdk 182
Cdd:cd01066 4 LRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAGGYP-------------AGPTIVGSGArtALPHYRPDD--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 183 TVLKYEDVMKVDYGVQVNGNIIDSAFTVSFDPQYD---NLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESYEVEin 259
Cdd:cd01066 68 RRLQEGDLVLVDLGGVYDGYHADLTRTFVIGEPSDeqrELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLG-- 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 330443401 260 getyqvKPCRNLCGHSIaPYRIHGGksvPIVKNGDTTKMEEGEHFAIETF 309
Cdd:cd01066 146 ------PNFGHRTGHGI-GLEIHEP---PVLKAGDDTVLEPGMVFAVEPG 185
|
|
| PRK12896 |
PRK12896 |
methionine aminopeptidase; Reviewed |
106-342 |
1.65e-13 |
|
methionine aminopeptidase; Reviewed
Pssm-ID: 237252 [Multi-domain] Cd Length: 255 Bit Score: 69.87 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 106 RKGAEIHRRVRRAIKDRIVPGMKLMDIaDMIentTRKYtgaenllaMED----PKSQGI-GFP--TGLSLNHCAAHFTPn 178
Cdd:PRK12896 20 RKIGRIVATALKEMGKAVEPGMTTKEL-DRI---AEKR--------LEEhgaiPSPEGYyGFPgsTCISVNEEVAHGIP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 179 agDKTVLKYEDVMKVDYGVQVNGNIIDSAFTV---SFDPQYDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEvmesyE 255
Cdd:PRK12896 87 --GPRVIKDGDLVNIDVSAYLDGYHGDTGITFavgPVSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAIED-----F 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 256 VEINGetYQVkpCRNLCGHSIAPyRIHGGKSVPIV--KNGDTTKMEEGEHFAIETFGSTGrgyvtaggevSHYARSAEDH 333
Cdd:PRK12896 160 AKKNG--YSV--VRDLTGHGVGR-SLHEEPSVILTytDPLPNRLLRPGMTLAVEPFLNLG----------AKDAETLDDG 224
|
....*....
gi 330443401 334 QVMPTLDSA 342
Cdd:PRK12896 225 WTVVTPDKS 233
|
|
| PA2G4-like |
cd01089 |
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ... |
106-416 |
1.97e-13 |
|
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family members have been implicated in cell cycle control.
Pssm-ID: 238522 Cd Length: 228 Bit Score: 69.28 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 106 RKGAEIHRRVRRAIKDRIVPGMKLMDIAD----MIENTTRK-YTGAENLlamedpkSQGIGFPTGLSLNHCAAHFTPNAG 180
Cdd:cd01089 5 KTAGQIANKVLKQVISLCVPGAKVVDLCEkgdkLILEELGKvYKKEKKL-------EKGIAFPTCISVNNCVCHFSPLKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 181 DKTV-LKYEDVMKVDYGVQVNGNIIDSAFTVsfdpqydnLLAAVKDATYTGikeagidvRLTDIGEAIQEVMEsyevein 259
Cdd:cd01089 78 DATYtLKDGDVVKIDLGCHIDGYIAVVAHTI--------VVGAEAETPVTG--------KKADVIAAAHYALE------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 260 getyqvkpcrnLCGHSIAPyrihGGKSVPIVKNGDTTkmeegehfaIETFGSTGRGYVTaggevSHyarsaEDHQVMPTL 339
Cdd:cd01089 135 -----------AALRLLRP----GNQNSDITEAIQKV---------IVDYGCTPVEGVL-----SH-----QLKRVVSSG 180
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330443401 340 DsaknllktidrnfgtlpfcrryldrlGQEKylfaLNNLVRHGLVQDYPPLNDIPGSYTAQFEHTILLHAHKKEVVS 416
Cdd:cd01089 181 E--------------------------GKAK----LVECVKHGLLFPYPVLYEKEGEVVAQFKLTVLLTPNGVTVLT 227
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
106-307 |
3.08e-08 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 54.83 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 106 RKGAEIHRRVRRAIKDRIVPGMKLMDIADMIENTTRKYtGAEnllamedpksqGIGFPTGLSL--NHCAAHFTPNAgdkT 183
Cdd:COG0006 83 RKAARIADAAHEAALAALRPGVTEREVAAELEAAMRRR-GAE-----------GPSFDTIVASgeNAAIPHYTPTD---R 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 184 VLKYEDVMKVDYGVQVNGNIIDSAFTVSF---DPQYDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESYEVeinG 260
Cdd:COG0006 148 PLKPGDLVLIDAGAEYDGYTSDITRTVAVgepSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAGY---G 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 330443401 261 ETYqvkPCRnlCGHSIApYRIHGGksvPIVKNGDTTKMEEGEHFAIE 307
Cdd:COG0006 225 EYF---PHG--TGHGVG-LDVHEG---PQISPGNDRPLEPGMVFTIE 262
|
|
| PRK07281 |
PRK07281 |
methionyl aminopeptidase; |
109-313 |
5.33e-08 |
|
methionyl aminopeptidase;
Pssm-ID: 180918 Cd Length: 286 Bit Score: 54.08 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 109 AEIHRRVRRAIKdrivPGMKLMDIadmiENTTRKYTGAENLLAME---DPKSQGIGFPTGLSLNHCAAHFTPNagdKTVL 185
Cdd:PRK07281 21 ASIHIGLRDLIK----PGVDMWEV----EEYVRRRCKEENVLPLQigvDGAMMDYPYATCCGLNDEVAHAFPR---HYIL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 186 KYEDVMKVD---------------------------YGVQVNGNIIDS--AFTV-SFDPQYDNLLAAVKDATYTGIKEAG 235
Cdd:PRK07281 90 KEGDLLKVDmvlsepldksivdvsklnfdnveqmkkYTESYRGGLADScwAYAVgTPSDEVKNLMDVTKEAMYRGIEQAV 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330443401 236 IDVRLTDIGEAIQEVMESYeveingeTYQVkpCRNLCGHSIAPyRIHGGKSVPIV-KNGDTTKMEEGEHFAIETFGSTG 313
Cdd:PRK07281 170 VGNRIGDIGAAIQEYAESR-------GYGV--VRDLVGHGVGP-TMHEEPMVPNYgTAGRGLRLREGMVLTIEPMINTG 238
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
106-307 |
2.57e-06 |
|
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: 47.89 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 106 RKGAEIHRRVRRAIKDRIVPGMKLMDIADMIENTTRKYtGAEnllamedpksqGIGFPTGLSLNHCAA--HFTPnagDKT 183
Cdd:cd01092 5 RKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKL-GAE-----------GPSFDTIVASGPNSAlpHGVP---SDR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443401 184 VLKYEDVMKVDYGVQVNGNIIDSAFTVSF---DPQYDNLLAAVKDATYTGIKEAGIDVRLTDIGEAIQEVMESYEVeinG 260
Cdd:cd01092 70 KIEEGDLVLIDFGAIYDGYCSDITRTVAVgepSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGY---G 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 330443401 261 ETYqvkpcrnlcGHSIApyriHG-GKSV---PIVKNGDTTKMEEGEHFAIE 307
Cdd:cd01092 147 EYF---------IHRTG----HGvGLEVheaPYISPGSDDVLEEGMVFTIE 184
|
|
|