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Conserved domains on  [gi|1907076168|ref|XP_036011787|]
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methionine aminopeptidase 2 isoform X1 [Mus musculus]

Protein Classification

methionine aminopeptidase 2( domain architecture ID 11487928)

methionine aminopeptidase 2 cotranslationally removes the N-terminal methionine from nascent proteins

Graphical summary

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List of domain hits

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
 
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 4.34e-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: 4.34e-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
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
162-478 3.75e-63

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 223103 [Multi-domain]  Cd Length: 255  Bit Score: 205.52  E-value: 3.75e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 162 SEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrkLIKENG-----LNA-GLAFPTGCSLNNCAAHYTPN 235
Cdd:COG0024     7 TPEEIEKMREAGKIAAKALKEVASLVKPGVTTLELDEIAEE----FIREKGaypafLGYkGFPFPTCISVNEVVAHGIPG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 236 agDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPK----YDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESy 311
Cdd:COG0024    83 --DKKVLKEGDIVKIDVGAHIDGYIGDTAITFVVGEVsdedAKRLLEATKEALYAGIEAVKPGARLGDIGRAIQEYAES- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 312 eveidgktYQVKPIRNLNGHSIGPyRIHAGKTVPIV-KGGEATRMEEGEVYAIETFGSTGKGVVHDDMEcshymknfdvg 390
Cdd:COG0024   160 --------RGFSVVRNLTGHGIGR-ELHEEPSIPNYgKDGTGVRLKEGMVFAIEPMINTGSGEVVEGPS----------- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 391 hvpirlprtkhllnvinenfgtlafcRRWLdrlgeskylmalknlcdlgivdpyppLCDIKGSYTAQFEHTILLRPTCKE 470
Cdd:COG0024   220 --------------------------DRWT--------------------------LVTKDGSLSAQFEHTVIVTEDGCE 247

                  ....*...
gi 1907076168 471 VVSRGDDY 478
Cdd:COG0024   248 ILTLRPEE 255
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
169-375 2.06e-35

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: 425750 [Multi-domain]  Cd Length: 207  Bit Score: 130.82  E-value: 2.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 169 FREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrKLIKENGLNaGLAFPT--GCSLNNCAAHYTPNagdTTVLQYDD 246
Cdd:pfam00557   3 MRKAARIAAAALEAALAAIRPGVTERELAAELEA---ARLRRGGAR-GPAFPPivASGPNAALPHYIPN---DRVLKPGD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 247 ICKIDFGTHISGRIIDCAFTV---TFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEidgktyqvK 323
Cdd:pfam00557  76 LVLIDVGAEYDGYCSDITRTFvvgKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGEVDAAAREVLEEAGLG--------E 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907076168 324 PIRNLNGHSIGpYRIHAGKTVPivKGGEATRMEEGEVYAIET--FGSTGKGVVH 375
Cdd:pfam00557 148 YFPHGLGHGIG-LEVHEGPYIS--RGGDDRVLEPGMVFTIEPgiYFIPGWGGVR 198
 
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 4.34e-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: 4.34e-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
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
162-478 3.75e-63

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 223103 [Multi-domain]  Cd Length: 255  Bit Score: 205.52  E-value: 3.75e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 162 SEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrkLIKENG-----LNA-GLAFPTGCSLNNCAAHYTPN 235
Cdd:COG0024     7 TPEEIEKMREAGKIAAKALKEVASLVKPGVTTLELDEIAEE----FIREKGaypafLGYkGFPFPTCISVNEVVAHGIPG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 236 agDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPK----YDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESy 311
Cdd:COG0024    83 --DKKVLKEGDIVKIDVGAHIDGYIGDTAITFVVGEVsdedAKRLLEATKEALYAGIEAVKPGARLGDIGRAIQEYAES- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 312 eveidgktYQVKPIRNLNGHSIGPyRIHAGKTVPIV-KGGEATRMEEGEVYAIETFGSTGKGVVHDDMEcshymknfdvg 390
Cdd:COG0024   160 --------RGFSVVRNLTGHGIGR-ELHEEPSIPNYgKDGTGVRLKEGMVFAIEPMINTGSGEVVEGPS----------- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 391 hvpirlprtkhllnvinenfgtlafcRRWLdrlgeskylmalknlcdlgivdpyppLCDIKGSYTAQFEHTILLRPTCKE 470
Cdd:COG0024   220 --------------------------DRWT--------------------------LVTKDGSLSAQFEHTVIVTEDGCE 247

                  ....*...
gi 1907076168 471 VVSRGDDY 478
Cdd:COG0024   248 ILTLRPEE 255
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
169-375 2.06e-35

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: 425750 [Multi-domain]  Cd Length: 207  Bit Score: 130.82  E-value: 2.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 169 FREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrKLIKENGLNaGLAFPT--GCSLNNCAAHYTPNagdTTVLQYDD 246
Cdd:pfam00557   3 MRKAARIAAAALEAALAAIRPGVTERELAAELEA---ARLRRGGAR-GPAFPPivASGPNAALPHYIPN---DRVLKPGD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 247 ICKIDFGTHISGRIIDCAFTV---TFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEidgktyqvK 323
Cdd:pfam00557  76 LVLIDVGAEYDGYCSDITRTFvvgKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGEVDAAAREVLEEAGLG--------E 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907076168 324 PIRNLNGHSIGpYRIHAGKTVPivKGGEATRMEEGEVYAIET--FGSTGKGVVH 375
Cdd:pfam00557 148 YFPHGLGHGIG-LEVHEGPYIS--RGGDDRVLEPGMVFTIEPgiYFIPGWGGVR 198
crvDNA_42K TIGR00495
42K curved DNA binding protein; Proteins identified by this model have been identified in a ...
156-466 3.28e-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: 3.28e-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
APP_MetAP cd01066
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
169-378 4.76e-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: 4.76e-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 6.76e-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: 6.76e-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
PA2G4-like cd01089
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ...
167-323 7.70e-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: 7.70e-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
PRK12896 PRK12896
methionine aminopeptidase; Reviewed
139-370 1.51e-13

methionine aminopeptidase; Reviewed


Pssm-ID: 237252 [Multi-domain]  Cd Length: 255  Bit Score: 70.25  E-value: 1.51e-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 3.20e-13

methionine aminopeptidase; Validated


Pssm-ID: 235576 [Multi-domain]  Cd Length: 252  Bit Score: 69.39  E-value: 3.20e-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
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
170-365 2.89e-10

Xaa-Pro aminopeptidase [Amino acid transport and metabolism];


Pssm-ID: 223085 [Multi-domain]  Cd Length: 384  Bit Score: 61.67  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 170 REAAEAHRQVRKYVMSWIKPGMTMIEICEKLEdcsRKLIKENGlnAGLAFPTGCSL--NNCAAHYTPNAgdtTVLQYDDI 247
Cdd:COG0006   164 RKAAEIADAALEAALEAIRPGMTEAEIAAELE---YALRKGGA--EGPSFDTIVASgeNAALPHYTPSD---RKLRDGDL 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907076168 248 CKIDFGTHISGRIIDCAFTVTFNP-------KYDILLTAVK---DATNTGIKCAGIDvrlcdvgEAIQEVMESYEVEIDg 317
Cdd:COG0006   236 VLIDLGGVYNGYCSDITRTFPIGKpsdeqreIYEAVLEAQEaaiAAIRPGVTGGEVD-------AAARQVLEKAGYGLY- 307
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907076168 318 ktyqvkpIRNLNGHSIG-PYRIHAGKTvpIVKGGEATRMEEGEVYAIET 365
Cdd:COG0006   308 -------FLHGTGHGVGfVLDVHEHPQ--YLSPGSDTTLEPGMVFSIEP 347
APP-like cd01092
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
170-364 1.95e-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: 1.95e-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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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