|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
110-455 |
0e+00 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 687.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 110 QECEYPPTQdgrtaAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENG 189
Cdd:PTZ00053 130 EIQEYPGEN-----SSRTSSEEKRELEKLSEEQYQDLRRAAEVHRQVRRYAQSVIKPGVKLIDICERIESKSRELIEADG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 190 LNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAG 269
Cdd:PTZ00053 205 LKCGWAFPTGCSLNHCAAHYTPNTGDKTVLTYDDVCKLDFGTHVNGRIIDCAFTVAFNPKYDPLLQATKDATNTGIKEAG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 270 IDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKG 349
Cdd:PTZ00053 285 IDVRLSDIGAAIQEVIESYEVEIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPIVKGGENTRMEEGELFAIETFASTGRG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 350 VVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKG 429
Cdd:PTZ00053 365 YVNEDLECSHYMKDPGAEFVPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQDRHLLALKQLVDAGIVNPYPPLCDVRG 444
|
330 340
....*....|....*....|....*.
gi 953768343 430 SYTAQFEHTILLRPTCKEVVSRGDDY 455
Cdd:PTZ00053 445 SYTSQMEHTILLRPTCKEVLSRGDDY 470
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
143-451 |
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: 552.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 143 WNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIkenglnAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYD 222
Cdd:cd01088 1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELG------AGPAFPVNLSINECAAHYTPNAGDDTVLKEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 223 DICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESyeveidgktYQVKPI 302
Cdd:cd01088 75 DVVKLDFGAHVDGYIADSAFTVDFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIES---------YGFKPI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 303 RNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDvghVPIRLPRTKHLLNV 382
Cdd:cd01088 146 RNLTGHSIERYRLHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIYMLNRD---KPLRLPRARKLLDV 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 953768343 383 INENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSR 451
Cdd:cd01088 223 IYENFGTLPFARRWLDRLGETKLLMALKNLCKAGIVYPYPVLKEISGGYVAQFEHTIIVREDGKEVTTR 291
|
|
| met_pdase_II |
TIGR00501 |
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ... |
148-451 |
8.21e-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: 331.36 E-value: 8.21e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 148 EAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLikenglNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKI 227
Cdd:TIGR00501 10 EAGKIHSKVRREAADRIVPGVKLLEVAEFVENRIREL------GAEPAFPCNISINECAAHFTPKAGDKTVFKDGDVVKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 228 DFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESyeveidgktYQVKPIRNLNG 307
Cdd:TIGR00501 84 DLGAHVDGYIADTAITVDLGDQYDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIES---------YGVKPISNLTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 308 HSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYmkNFDVGHvPIRLPRTKHLLNVINENF 387
Cdd:TIGR00501 155 HSMAPYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDGVGYVTDGGEVSIY--AFLAER-PVRLDSARNLLKTIDENY 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 953768343 388 GTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSR 451
Cdd:TIGR00501 232 GTLPFARRWLDKLGDEKYLFALNNLIRHGLIYDYPVLNEISGGYVAQWEHTILVEEHGKEVTTK 295
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
146-352 |
2.15e-33 |
|
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: 125.05 E-value: 2.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 146 FREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrKLIKENGLNaGLAFPT--GCSLNNCAAHYTPNagdTTVLQYDD 223
Cdd:pfam00557 3 MRKAARIAAAALEAALAAIRPGVTERELAAELEA---ARLRRGGAR-GPAFPPivASGPNAAIPHYIPN---DRVLKPGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 224 ICKIDFGTHISGR-IIDCAFTV---TFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEidgktyqv 299
Cdd:pfam00557 76 LVLIDVGAEYDGGyCSDITRTFvvgKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLG-------- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 953768343 300 KPIRNLNGHSIGqYRIHAGKTVPivKGGEATRMEEGEVYAIET--FGSTGKGVVH 352
Cdd:pfam00557 148 EYFPHGLGHGIG-LEVHEGPYIS--RGGDDRVLEPGMVFTIEPgiYFIPGWGGVR 199
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
149-354 |
1.89e-17 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 81.59 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 149 AAEAHRQVRKYVmswiKPGMTMIEicekLEDCSRKLIKENG-----LNAGlAFP--TGCSLNNCAAHYTPNAgdtTVLQY 221
Cdd:COG0024 19 VAEVLDELAEAV----KPGVTTLE----LDRIAEEFIRDHGaipafLGYY-GFPksICTSVNEVVVHGIPSD---RVLKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 222 DDICKIDFGTHISGRIIDCAFTV---TFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEveidgktYQ 298
Cdd:COG0024 87 GDIVNIDVGAILDGYHGDSARTFvvgEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNG-------YS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 953768343 299 VkpIRNLNGHSIGQyRIHAGktvPIV----KGGEATRMEEGEVYAIETFGSTGK-GVVHDD 354
Cdd:COG0024 160 V--VREFVGHGIGR-EMHEE---PQVpnygRPGRGPRLKPGMVLAIEPMINAGTpEVKVLD 214
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00053 |
PTZ00053 |
methionine aminopeptidase 2; Provisional |
110-455 |
0e+00 |
|
methionine aminopeptidase 2; Provisional
Pssm-ID: 240246 [Multi-domain] Cd Length: 470 Bit Score: 687.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 110 QECEYPPTQdgrtaAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENG 189
Cdd:PTZ00053 130 EIQEYPGEN-----SSRTSSEEKRELEKLSEEQYQDLRRAAEVHRQVRRYAQSVIKPGVKLIDICERIESKSRELIEADG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 190 LNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAG 269
Cdd:PTZ00053 205 LKCGWAFPTGCSLNHCAAHYTPNTGDKTVLTYDDVCKLDFGTHVNGRIIDCAFTVAFNPKYDPLLQATKDATNTGIKEAG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 270 IDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKG 349
Cdd:PTZ00053 285 IDVRLSDIGAAIQEVIESYEVEIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPIVKGGENTRMEEGELFAIETFASTGRG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 350 VVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKG 429
Cdd:PTZ00053 365 YVNEDLECSHYMKDPGAEFVPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQDRHLLALKQLVDAGIVNPYPPLCDVRG 444
|
330 340
....*....|....*....|....*.
gi 953768343 430 SYTAQFEHTILLRPTCKEVVSRGDDY 455
Cdd:PTZ00053 445 SYTSQMEHTILLRPTCKEVLSRGDDY 470
|
|
| MetAP2 |
cd01088 |
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
143-451 |
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: 552.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 143 WNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIkenglnAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYD 222
Cdd:cd01088 1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELG------AGPAFPVNLSINECAAHYTPNAGDDTVLKEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 223 DICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESyeveidgktYQVKPI 302
Cdd:cd01088 75 DVVKLDFGAHVDGYIADSAFTVDFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIES---------YGFKPI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 303 RNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDvghVPIRLPRTKHLLNV 382
Cdd:cd01088 146 RNLTGHSIERYRLHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIYMLNRD---KPLRLPRARKLLDV 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 953768343 383 INENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSR 451
Cdd:cd01088 223 IYENFGTLPFARRWLDRLGETKLLMALKNLCKAGIVYPYPVLKEISGGYVAQFEHTIIVREDGKEVTTR 291
|
|
| met_pdase_II |
TIGR00501 |
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ... |
148-451 |
8.21e-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: 331.36 E-value: 8.21e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 148 EAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLikenglNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKI 227
Cdd:TIGR00501 10 EAGKIHSKVRREAADRIVPGVKLLEVAEFVENRIREL------GAEPAFPCNISINECAAHFTPKAGDKTVFKDGDVVKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 228 DFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESyeveidgktYQVKPIRNLNG 307
Cdd:TIGR00501 84 DLGAHVDGYIADTAITVDLGDQYDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIES---------YGVKPISNLTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 308 HSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYmkNFDVGHvPIRLPRTKHLLNVINENF 387
Cdd:TIGR00501 155 HSMAPYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDGVGYVTDGGEVSIY--AFLAER-PVRLDSARNLLKTIDENY 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 953768343 388 GTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSR 451
Cdd:TIGR00501 232 GTLPFARRWLDKLGDEKYLFALNNLIRHGLIYDYPVLNEISGGYVAQWEHTILVEEHGKEVTTK 295
|
|
| crvDNA_42K |
TIGR00495 |
42K curved DNA binding protein; Proteins identified by this model have been identified in a ... |
133-443 |
2.34e-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: 135.02 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 133 KALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEK-----LEDCSRKLIKENGLNAGLAFPTGCSLNNCAA 207
Cdd:TIGR00495 10 QAYSLSNPEVVTKYKMAGEIANNVLKSVVEACSPGAKVVDICEKgdafiMEETAKIFKKEKEMEKGIAFPTCISVNNCVG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 208 HYTPNAGDTT-VLQYDDICKIDFGTHISGRIIDCAFT-VTFNPKYDTLLKAVKDATNTGIKCAGIDVRLC-------DVG 278
Cdd:TIGR00495 90 HFSPLKSDQDyILKEGDVVKIDLGCHIDGFIALVAHTfVVGVAQEEPVTGRKADVIAAAHLAAEAALRLVkpgntntQVT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 279 EAIQEVMESYEveidgktyqVKPIRNLNGHSIGQYRIHAGKTVPIV------KGGEATRMEEGEVYAIETFGSTGKGVVH 352
Cdd:TIGR00495 170 EAINKVAHSYG---------CTPVEGMLSHQLKQHVIDGEKVIISNpsdsqkKDHDTAEFEENEVYAVDILVSTGEGKAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 353 D-DMECSHYMKNFDVGHVpIRLPRTKHLLNVINENFGTLAFCRRWLDrlGESKYLMALKNLCDLGIVDPYPPLCDIKGSY 431
Cdd:TIGR00495 241 DaDQRTTIYKRDPSKTYG-LKMKASRAFFSEIERRFDAMPFTLRNFE--DEKRARMGLVECVKHELLQPYPVLYEKEGEF 317
|
330
....*....|..
gi 953768343 432 TAQFEHTILLRP 443
Cdd:TIGR00495 318 VAQFKFTVLLMP 329
|
|
| Peptidase_M24 |
pfam00557 |
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ... |
146-352 |
2.15e-33 |
|
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: 125.05 E-value: 2.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 146 FREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrKLIKENGLNaGLAFPT--GCSLNNCAAHYTPNagdTTVLQYDD 223
Cdd:pfam00557 3 MRKAARIAAAALEAALAAIRPGVTERELAAELEA---ARLRRGGAR-GPAFPPivASGPNAAIPHYIPN---DRVLKPGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 224 ICKIDFGTHISGR-IIDCAFTV---TFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEidgktyqv 299
Cdd:pfam00557 76 LVLIDVGAEYDGGyCSDITRTFvvgKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLG-------- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 953768343 300 KPIRNLNGHSIGqYRIHAGKTVPivKGGEATRMEEGEVYAIET--FGSTGKGVVH 352
Cdd:pfam00557 148 EYFPHGLGHGIG-LEVHEGPYIS--RGGDDRVLEPGMVFTIEPgiYFIPGWGGVR 199
|
|
| APP_MetAP |
cd01066 |
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ... |
146-355 |
7.95e-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: 107.15 E-value: 7.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 146 FREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIkenglnAGLAFPTGCSLNN--CAAHYTPnagDTTVLQYDD 223
Cdd:cd01066 4 LRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAG------GYPAGPTIVGSGArtALPHYRP---DDRRLQEGD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 224 ICKIDFGTHISGRIIDCAFTVTFNPKYD---TLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEidgktyqvK 300
Cdd:cd01066 75 LVLVDLGGVYDGYHADLTRTFVIGEPSDeqrELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLG--------P 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 953768343 301 PIRNLNGHSIGQYRIHAgktvPIVKGGEATRMEEGEVYAIETF--GSTGKGVVHDDM 355
Cdd:cd01066 147 NFGHRTGHGIGLEIHEP----PVLKAGDDTVLEPGMVFAVEPGlyLPGGGGVRIEDT 199
|
|
| MetAP1 |
cd01086 |
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ... |
147-354 |
2.44e-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: 95.25 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 147 REAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrkLIKENG-----LNAGlAFP-TGC-SLNNCAAHYTPnagDTTVL 219
Cdd:cd01086 5 REAGRIVAEVLDELAKAIKPGVTTKELDQIAHE----FIEEHGaypapLGYY-GFPkSICtSVNEVVCHGIP---DDRVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 220 QYDDICKIDFGTHISGRIIDCAFTV---TFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYeveidgkT 296
Cdd:cd01086 77 KDGDIVNIDVGVELDGYHGDSARTFivgEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKN-------G 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 953768343 297 YQVkpIRNLNGHSIGQYrIHAGKTVPIV-KGGEATRMEEGEVYAIETFGSTGKG--VVHDD 354
Cdd:cd01086 150 YSV--VREFGGHGIGRK-FHEEPQIPNYgRPGTGPKLKPGMVFTIEPMINLGTYevVTLPD 207
|
|
| Map |
COG0024 |
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis]; |
149-354 |
1.89e-17 |
|
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439795 [Multi-domain] Cd Length: 250 Bit Score: 81.59 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 149 AAEAHRQVRKYVmswiKPGMTMIEicekLEDCSRKLIKENG-----LNAGlAFP--TGCSLNNCAAHYTPNAgdtTVLQY 221
Cdd:COG0024 19 VAEVLDELAEAV----KPGVTTLE----LDRIAEEFIRDHGaipafLGYY-GFPksICTSVNEVVVHGIPSD---RVLKD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 222 DDICKIDFGTHISGRIIDCAFTV---TFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEveidgktYQ 298
Cdd:COG0024 87 GDIVNIDVGAILDGYHGDSARTFvvgEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNG-------YS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 953768343 299 VkpIRNLNGHSIGQyRIHAGktvPIV----KGGEATRMEEGEVYAIETFGSTGK-GVVHDD 354
Cdd:COG0024 160 V--VREFVGHGIGR-EMHEE---PQVpnygRPGRGPRLKPGMVLAIEPMINAGTpEVKVLD 214
|
|
| PA2G4-like |
cd01089 |
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ... |
144-300 |
1.40e-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: 78.53 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 144 NDFREAAEAHRQVRKYVMSWIKPGMTMIEICEK-----LEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTV 218
Cdd:cd01089 2 TKYKTAGQIANKVLKQVISLCVPGAKVVDLCEKgdkliLEELGKVYKKEKKLEKGIAFPTCISVNNCVCHFSPLKSDATY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 219 -LQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDT--------LLKAVKDATNTG---IKCAGIDVrlcDVGEAIQEVME 286
Cdd:cd01089 82 tLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAETpvtgkkadVIAAAHYALEAAlrlLRPGNQNS---DITEAIQKVIV 158
|
170
....*....|....*.
gi 953768343 287 SYEV-EIDGKT-YQVK 300
Cdd:cd01089 159 DYGCtPVEGVLsHQLK 174
|
|
| PRK12896 |
PRK12896 |
methionine aminopeptidase; Reviewed |
116-347 |
3.70e-14 |
|
methionine aminopeptidase; Reviewed
Pssm-ID: 237252 [Multi-domain] Cd Length: 255 Bit Score: 72.18 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 116 PTQDGRTAaWRTTSEEKKALDQASeeiwndfREAAeahrQVRKYVMSWIKPGMTMIEicekLEDCSRKLIKENGLNAG-- 193
Cdd:PRK12896 1 PAQEGRGM-EIKSPRELEKMRKIG-------RIVA----TALKEMGKAVEPGMTTKE----LDRIAEKRLEEHGAIPSpe 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 194 --LAFPTGC--SLNNCAAHYTPnagDTTVLQYDDICKIDFGTHISGRIIDCAFTV---TFNPKYDTLLKAVKDATNTGIK 266
Cdd:PRK12896 65 gyYGFPGSTciSVNEEVAHGIP---GPRVIKDGDLVNIDVSAYLDGYHGDTGITFavgPVSEEAEKLCRVAEEALWAGIK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 267 CAGIDVRLCDVGEAIQEvmesyEVEIDGktYQVkpIRNLNGHSIGQyRIHAGKTVPIVKG--GEATRMEEGEVYAIETFG 344
Cdd:PRK12896 142 QVKAGRPLNDIGRAIED-----FAKKNG--YSV--VRDLTGHGVGR-SLHEEPSVILTYTdpLPNRLLRPGMTLAVEPFL 211
|
...
gi 953768343 345 STG 347
Cdd:PRK12896 212 NLG 214
|
|
| PepP |
COG0006 |
Xaa-Pro aminopeptidase [Amino acid transport and metabolism]; |
147-341 |
4.24e-14 |
|
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
Pssm-ID: 439777 [Multi-domain] Cd Length: 299 Bit Score: 72.54 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 147 REAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrkLIKENGLNaGLAFPT--GCSLNNCAAHYTPNagdTTVLQYDDI 224
Cdd:COG0006 83 RKAARIADAAHEAALAALRPGVTEREVAAELEA----AMRRRGAE-GPSFDTivASGENAAIPHYTPT---DRPLKPGDL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 225 CKIDFGTHISGRIIDCAFTV---TFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMES--YEVEIDGKTyqv 299
Cdd:COG0006 155 VLIDAGAEYDGYTSDITRTVavgEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEagYGEYFPHGT--- 231
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 953768343 300 kpirnlnGHSIGqYRIHagkTVPIVKGGEATRMEEGEVYAIE 341
Cdd:COG0006 232 -------GHGVG-LDVH---EGPQISPGNDRPLEPGMVFTIE 262
|
|
| PRK05716 |
PRK05716 |
methionine aminopeptidase; Validated |
149-349 |
7.86e-14 |
|
methionine aminopeptidase; Validated
Pssm-ID: 235576 [Multi-domain] Cd Length: 252 Bit Score: 70.93 E-value: 7.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 149 AAEAHRQVRKYVmswiKPGMTMIEicekLEDCSRKLIKENG-LNAGLA---FP-TGC-SLNNCAAHYTPNAgdtTVLQYD 222
Cdd:PRK05716 21 AAEVLDEIEPHV----KPGVTTKE----LDRIAEEYIRDQGaIPAPLGyhgFPkSICtSVNEVVCHGIPSD---KVLKEG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 223 DICKIDFGTHISGRIIDCAFTV---TFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYeveidgkTYQV 299
Cdd:PRK05716 90 DIVNIDVTVIKDGYHGDTSRTFgvgEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAE-------GFSV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 953768343 300 kpIRNLNGHSIGQyRIHAGktvPIV----KGGEATRMEEGEVYAIETFGSTGKG 349
Cdd:PRK05716 163 --VREYCGHGIGR-KFHEE---PQIphygAPGDGPVLKEGMVFTIEPMINAGKR 210
|
|
| APP-like |
cd01092 |
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ... |
147-341 |
5.96e-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: 58.67 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 147 REAAEAHRQVRKYVMSWIKPGMTMIEICEKLEdcsrKLIKENGLNaGLAFPTGCSLNNCAA--HYTPnagDTTVLQYDDI 224
Cdd:cd01092 5 RKAARIADKAFEELLEFIKPGMTEREVAAELE----YFMRKLGAE-GPSFDTIVASGPNSAlpHGVP---SDRKIEEGDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 225 CKIDFGTHISGRIIDCAFTVTFNPKYDTLLK---AVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVeidGKTYqvkp 301
Cdd:cd01092 77 VLIDFGAIYDGYCSDITRTVAVGEPSDELKEiyeIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGY---GEYF---- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 953768343 302 IRNLnGHSIGqYRIHAGktvPIVKGGEATRMEEGEVYAIE 341
Cdd:cd01092 150 IHRT-GHGVG-LEVHEA---PYISPGSDDVLEEGMVFTIE 184
|
|
| Prolidase |
cd01087 |
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ... |
149-285 |
7.33e-03 |
|
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: 37.94 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768343 149 AAEAHRQVrkyvMSWIKPGMTMIEICEKLEDCSRKlikeNGLNAGLAFPTGCSLNNCAAHYTPNAGdttVLQYDDICKID 228
Cdd:cd01087 11 SAEAHRAA----MKASRPGMSEYELEAEFEYEFRS----RGARLAYSYIVAAGSNAAILHYVHNDQ---PLKDGDLVLID 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 953768343 229 FGTHISGRIID--CAFTV--TFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVM 285
Cdd:cd01087 80 AGAEYGGYASDitRTFPVngKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIHLLAHRVL 140
|
|
| |
