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Conserved domains on  [gi|953768345|ref|NP_001304112|]
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methionine aminopeptidase 2 isoform 3 [Homo sapiens]

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
 89-455 0e+00

methionine aminopeptidase 2; Provisional


:

Pssm-ID: 240246 [Multi-domain]  Cd Length: 470  Bit Score: 717.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345  89 QTDPPSVPICDLYPNGVFPKGQECEYPPTQdgrtaAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGM 168
Cdd:PTZ00053 109 QTQPPTIPVSKQFKDGEYPVGEIQEYPGEN-----SSRTSSEEKRELEKLSEEQYQDLRRAAEVHRQVRRYAQSVIKPGV 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 169 TMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNP 248
Cdd:PTZ00053 184 KLIDICERIESKSRELIEADGLKCGWAFPTGCSLNHCAAHYTPNTGDKTVLTYDDVCKLDFGTHVNGRIIDCAFTVAFNP 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 249 KYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGE 328
Cdd:PTZ00053 264 KYDPLLQATKDATNTGIKEAGIDVRLSDIGAAIQEVIESYEVEIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPIVKGGE 343

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 329 ATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMA 408
Cdd:PTZ00053 344 NTRMEEGELFAIETFASTGRGYVNEDLECSHYMKDPGAEFVPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQDRHLLA 423

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 953768345 409 LKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY 455
Cdd:PTZ00053 424 LKQLVDAGIVNPYPPLCDVRGSYTSQMEHTILLRPTCKEVLSRGDDY 470
 
Name Accession Description Interval E-value
PTZ00053 PTZ00053
methionine aminopeptidase 2; Provisional
 89-455 0e+00

methionine aminopeptidase 2; Provisional


Pssm-ID: 240246 [Multi-domain]  Cd Length: 470  Bit Score: 717.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345  89 QTDPPSVPICDLYPNGVFPKGQECEYPPTQdgrtaAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGM 168
Cdd:PTZ00053 109 QTQPPTIPVSKQFKDGEYPVGEIQEYPGEN-----SSRTSSEEKRELEKLSEEQYQDLRRAAEVHRQVRRYAQSVIKPGV 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 169 TMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNP 248
Cdd:PTZ00053 184 KLIDICERIESKSRELIEADGLKCGWAFPTGCSLNHCAAHYTPNTGDKTVLTYDDVCKLDFGTHVNGRIIDCAFTVAFNP 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 249 KYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGE 328
Cdd:PTZ00053 264 KYDPLLQATKDATNTGIKEAGIDVRLSDIGAAIQEVIESYEVEIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPIVKGGE 343

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 329 ATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMA 408
Cdd:PTZ00053 344 NTRMEEGELFAIETFASTGRGYVNEDLECSHYMKDPGAEFVPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQDRHLLA 423

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 953768345 409 LKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY 455
Cdd:PTZ00053 424 LKQLVDAGIVNPYPPLCDVRGSYTSQMEHTILLRPTCKEVLSRGDDY 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: 554.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 143 WNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIkenglnAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYD 222
Cdd:cd01088    1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELG------AGPAFPVNLSINECAAHYTPNAGDDTVLKEG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 223 DICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESyeveidgktYQVKPI 302
Cdd:cd01088   75 DVVKLDFGAHVDGYIADSAFTVDFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIES---------YGFKPI 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 303 RNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDvghVPIRLPRTKHLLNV 382
Cdd:cd01088  146 RNLTGHSIERYRLHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIYMLNRD---KPLRLPRARKLLDV 222

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 953768345 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 4.18e-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: 332.13  E-value: 4.18e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345  148 EAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLikenglNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKI 227
Cdd:TIGR00501  10 EAGKIHSKVRREAADRIVPGVKLLEVAEFVENRIREL------GAEPAFPCNISINECAAHFTPKAGDKTVFKDGDVVKL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345  228 DFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESyeveidgktYQVKPIRNLNG 307
Cdd:TIGR00501  84 DLGAHVDGYIADTAITVDLGDQYDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIES---------YGVKPISNLTG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345  308 HSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYmkNFDVGHvPIRLPRTKHLLNVINENF 387
Cdd:TIGR00501 155 HSMAPYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDGVGYVTDGGEVSIY--AFLAER-PVRLDSARNLLKTIDENY 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 953768345  388 GTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSR 451
Cdd:TIGR00501 232 GTLPFARRWLDKLGDEKYLFALNNLIRHGLIYDYPVLNEISGGYVAQWEHTILVEEHGKEVTTK 295
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 146-352 6.52e-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: 126.20  E-value: 6.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345  146 FREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrKLIKENGLNaGLAFPT--GCSLNNCAAHYTPNagdTTVLQYDD 223
Cdd:pfam00557   3 MRKAARIAAAALEAALAAIRPGVTERELAAELEA---ARLRRGGAR-GPAFPPivASGPNAAIPHYIPN---DRVLKPGD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345  224 ICKIDFGTHISGR-IIDCAFTV---TFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEidgktyqv 299
Cdd:pfam00557  76 LVLIDVGAEYDGGyCSDITRTFvvgKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLG-------- 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 953768345  300 KPIRNLNGHSIGqYRIHAGKTVPivKGGEATRMEEGEVYAIET--FGSTGKGVVH 352
Cdd:pfam00557 148 EYFPHGLGHGIG-LEVHEGPYIS--RGGDDRVLEPGMVFTIEPgiYFIPGWGGVR 199
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
149-354 1.28e-17

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 81.98  E-value: 1.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 149 AAEAHRQVRKYVmswiKPGMTMIEicekLEDCSRKLIKENG-----LNAGlAFP--TGCSLNNCAAHYTPNAgdtTVLQY 221
Cdd:COG0024   19 VAEVLDELAEAV----KPGVTTLE----LDRIAEEFIRDHGaipafLGYY-GFPksICTSVNEVVVHGIPSD---RVLKD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 222 DDICKIDFGTHISGRIIDCAFTV---TFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEveidgktYQ 298
Cdd:COG0024   87 GDIVNIDVGAILDGYHGDSARTFvvgEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNG-------YS 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 953768345 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
 89-455 0e+00

methionine aminopeptidase 2; Provisional


Pssm-ID: 240246 [Multi-domain]  Cd Length: 470  Bit Score: 717.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345  89 QTDPPSVPICDLYPNGVFPKGQECEYPPTQdgrtaAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGM 168
Cdd:PTZ00053 109 QTQPPTIPVSKQFKDGEYPVGEIQEYPGEN-----SSRTSSEEKRELEKLSEEQYQDLRRAAEVHRQVRRYAQSVIKPGV 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 169 TMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNP 248
Cdd:PTZ00053 184 KLIDICERIESKSRELIEADGLKCGWAFPTGCSLNHCAAHYTPNTGDKTVLTYDDVCKLDFGTHVNGRIIDCAFTVAFNP 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 249 KYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGE 328
Cdd:PTZ00053 264 KYDPLLQATKDATNTGIKEAGIDVRLSDIGAAIQEVIESYEVEIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPIVKGGE 343

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 329 ATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMA 408
Cdd:PTZ00053 344 NTRMEEGELFAIETFASTGRGYVNEDLECSHYMKDPGAEFVPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQDRHLLA 423

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 953768345 409 LKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY 455
Cdd:PTZ00053 424 LKQLVDAGIVNPYPPLCDVRGSYTSQMEHTILLRPTCKEVLSRGDDY 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: 554.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 143 WNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIkenglnAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYD 222
Cdd:cd01088    1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELG------AGPAFPVNLSINECAAHYTPNAGDDTVLKEG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 223 DICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESyeveidgktYQVKPI 302
Cdd:cd01088   75 DVVKLDFGAHVDGYIADSAFTVDFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIES---------YGFKPI 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 303 RNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDvghVPIRLPRTKHLLNV 382
Cdd:cd01088  146 RNLTGHSIERYRLHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIYMLNRD---KPLRLPRARKLLDV 222

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 953768345 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 4.18e-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: 332.13  E-value: 4.18e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345  148 EAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLikenglNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKI 227
Cdd:TIGR00501  10 EAGKIHSKVRREAADRIVPGVKLLEVAEFVENRIREL------GAEPAFPCNISINECAAHFTPKAGDKTVFKDGDVVKL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345  228 DFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESyeveidgktYQVKPIRNLNG 307
Cdd:TIGR00501  84 DLGAHVDGYIADTAITVDLGDQYDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIES---------YGVKPISNLTG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345  308 HSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYmkNFDVGHvPIRLPRTKHLLNVINENF 387
Cdd:TIGR00501 155 HSMAPYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDGVGYVTDGGEVSIY--AFLAER-PVRLDSARNLLKTIDENY 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 953768345  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 2.80e-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: 2.80e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345  133 KALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEK-----LEDCSRKLIKENGLNAGLAFPTGCSLNNCAA 207
Cdd:TIGR00495  10 QAYSLSNPEVVTKYKMAGEIANNVLKSVVEACSPGAKVVDICEKgdafiMEETAKIFKKEKEMEKGIAFPTCISVNNCVG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345  208 HYTPNAGDTT-VLQYDDICKIDFGTHISGRIIDCAFT-VTFNPKYDTLLKAVKDATNTGIKCAGIDVRLC-------DVG 278
Cdd:TIGR00495  90 HFSPLKSDQDyILKEGDVVKIDLGCHIDGFIALVAHTfVVGVAQEEPVTGRKADVIAAAHLAAEAALRLVkpgntntQVT 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345  279 EAIQEVMESYEveidgktyqVKPIRNLNGHSIGQYRIHAGKTVPIV------KGGEATRMEEGEVYAIETFGSTGKGVVH 352
Cdd:TIGR00495 170 EAINKVAHSYG---------CTPVEGMLSHQLKQHVIDGEKVIISNpsdsqkKDHDTAEFEENEVYAVDILVSTGEGKAK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345  353 D-DMECSHYMKNFDVGHVpIRLPRTKHLLNVINENFGTLAFCRRWLDrlGESKYLMALKNLCDLGIVDPYPPLCDIKGSY 431
Cdd:TIGR00495 241 DaDQRTTIYKRDPSKTYG-LKMKASRAFFSEIERRFDAMPFTLRNFE--DEKRARMGLVECVKHELLQPYPVLYEKEGEF 317

                         330
                  ....*....|..
gi 953768345  432 TAQFEHTILLRP 443
Cdd:TIGR00495 318 VAQFKFTVLLMP 329
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 146-352 6.52e-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: 126.20  E-value: 6.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345  146 FREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrKLIKENGLNaGLAFPT--GCSLNNCAAHYTPNagdTTVLQYDD 223
Cdd:pfam00557   3 MRKAARIAAAALEAALAAIRPGVTERELAAELEA---ARLRRGGAR-GPAFPPivASGPNAAIPHYIPN---DRVLKPGD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345  224 ICKIDFGTHISGR-IIDCAFTV---TFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEidgktyqv 299
Cdd:pfam00557  76 LVLIDVGAEYDGGyCSDITRTFvvgKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLG-------- 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 953768345  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 1.64e-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: 109.08  E-value: 1.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 146 FREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIkenglnAGLAFPTGCSLNN--CAAHYTPnagDTTVLQYDD 223
Cdd:cd01066    4 LRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAG------GYPAGPTIVGSGArtALPHYRP---DDRRLQEGD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 224 ICKIDFGTHISGRIIDCAFTVTFNPKYD---TLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEidgktyqvK 300
Cdd:cd01066   75 LVLVDLGGVYDGYHADLTRTFVIGEPSDeqrELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLG--------P 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 953768345 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 2.09e-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: 95.64  E-value: 2.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 147 REAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrkLIKENG-----LNAGlAFP-TGC-SLNNCAAHYTPnagDTTVL 219
Cdd:cd01086    5 REAGRIVAEVLDELAKAIKPGVTTKELDQIAHE----FIEEHGaypapLGYY-GFPkSICtSVNEVVCHGIP---DDRVL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 220 QYDDICKIDFGTHISGRIIDCAFTV---TFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYeveidgkT 296
Cdd:cd01086   77 KDGDIVNIDVGVELDGYHGDSARTFivgEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKN-------G 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 953768345 297 YQVkpIRNLNGHSIGQYrIHAGKTVPIV-KGGEATRMEEGEVYAIETFGSTGKG--VVHDD 354
Cdd:cd01086  150 YSV--VREFGGHGIGRK-FHEEPQIPNYgRPGTGPKLKPGMVFTIEPMINLGTYevVTLPD 207
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
149-354 1.28e-17

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 81.98  E-value: 1.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 149 AAEAHRQVRKYVmswiKPGMTMIEicekLEDCSRKLIKENG-----LNAGlAFP--TGCSLNNCAAHYTPNAgdtTVLQY 221
Cdd:COG0024   19 VAEVLDELAEAV----KPGVTTLE----LDRIAEEFIRDHGaipafLGYY-GFPksICTSVNEVVVHGIPSD---RVLKD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 222 DDICKIDFGTHISGRIIDCAFTV---TFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEveidgktYQ 298
Cdd:COG0024   87 GDIVNIDVGAILDGYHGDSARTFvvgEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNG-------YS 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 953768345 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 1.82e-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: 78.14  E-value: 1.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 144 NDFREAAEAHRQVRKYVMSWIKPGMTMIEICEK-----LEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTV 218
Cdd:cd01089    2 TKYKTAGQIANKVLKQVISLCVPGAKVVDLCEKgdkliLEELGKVYKKEKKLEKGIAFPTCISVNNCVCHFSPLKSDATY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 219 -LQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDT--------LLKAVKDATNTG---IKCAGIDVrlcDVGEAIQEVME 286
Cdd:cd01089   82 tLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAETpvtgkkadVIAAAHYALEAAlrlLRPGNQNS---DITEAIQKVIV 158

                        170
                 ....*....|....*.
gi 953768345 287 SYEV-EIDGKT-YQVK 300
Cdd:cd01089  159 DYGCtPVEGVLsHQLK 174
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
147-341 1.92e-14

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


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 73.70  E-value: 1.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 147 REAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDcsrkLIKENGLNaGLAFPT--GCSLNNCAAHYTPNagdTTVLQYDDI 224
Cdd:COG0006   83 RKAARIADAAHEAALAALRPGVTEREVAAELEA----AMRRRGAE-GPSFDTivASGENAAIPHYTPT---DRPLKPGDL 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 225 CKIDFGTHISGRIIDCAFTV---TFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMES--YEVEIDGKTyqv 299
Cdd:COG0006  155 VLIDAGAEYDGYTSDITRTVavgEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEagYGEYFPHGT--- 231

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 953768345 300 kpirnlnGHSIGqYRIHagkTVPIVKGGEATRMEEGEVYAIE 341
Cdd:COG0006  232 -------GHGVG-LDVH---EGPQISPGNDRPLEPGMVFTIE 262
PRK12896 PRK12896
methionine aminopeptidase; Reviewed
 116-347 2.25e-14

methionine aminopeptidase; Reviewed


Pssm-ID: 237252 [Multi-domain]  Cd Length: 255  Bit Score: 72.56  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 116 PTQDGRTAaWRTTSEEKKALDQASeeiwndfREAAeahrQVRKYVMSWIKPGMTMIEicekLEDCSRKLIKENGLNAG-- 193
Cdd:PRK12896   1 PAQEGRGM-EIKSPRELEKMRKIG-------RIVA----TALKEMGKAVEPGMTTKE----LDRIAEKRLEEHGAIPSpe 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 194 --LAFPTGC--SLNNCAAHYTPnagDTTVLQYDDICKIDFGTHISGRIID-CAftvTF-----NPKYDTLLKAVKDATNT 263
Cdd:PRK12896  65 gyYGFPGSTciSVNEEVAHGIP---GPRVIKDGDLVNIDVSAYLDGYHGDtGI---TFavgpvSEEAEKLCRVAEEALWA 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 264 GIKCAGIDVRLCDVGEAIQEvmesyEVEIDGktYQVkpIRNLNGHSIGQyRIHAGKTVPIVKG--GEATRMEEGEVYAIE 341
Cdd:PRK12896 139 GIKQVKAGRPLNDIGRAIED-----FAKKNG--YSV--VRDLTGHGVGR-SLHEEPSVILTYTdpLPNRLLRPGMTLAVE 208


                 ....*.
gi 953768345 342 TFGSTG 347
Cdd:PRK12896 209 PFLNLG 214
PRK05716 PRK05716
methionine aminopeptidase; Validated
 149-349 6.57e-14

methionine aminopeptidase; Validated


Pssm-ID: 235576 [Multi-domain]  Cd Length: 252  Bit Score: 71.32  E-value: 6.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 149 AAEAHRQVRKYVmswiKPGMTMIEicekLEDCSRKLIKENG-LNAGLA---FP-TGC-SLNNCAAHYTPNAgdtTVLQYD 222
Cdd:PRK05716  21 AAEVLDEIEPHV----KPGVTTKE----LDRIAEEYIRDQGaIPAPLGyhgFPkSICtSVNEVVCHGIPSD---KVLKEG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 223 DICKIDFGTHISGRIIDCAFTV---TFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYeveidgkTYQV 299
Cdd:PRK05716  90 DIVNIDVTVIKDGYHGDTSRTFgvgEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAE-------GFSV 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 953768345 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 3.58e-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: 59.45  E-value: 3.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 147 REAAEAHRQVRKYVMSWIKPGMTMIEICEKLEdcsrKLIKENGLNaGLAFPTGCSLNNCAA--HYTPnagDTTVLQYDDI 224
Cdd:cd01092    5 RKAARIADKAFEELLEFIKPGMTEREVAAELE----YFMRKLGAE-GPSFDTIVASGPNSAlpHGVP---SDRKIEEGDL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 225 CKIDFGTHISGRIIDCAFTVTFNPKYDTLLK---AVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVeidGKTYqvkp 301
Cdd:cd01092   77 VLIDFGAIYDGYCSDITRTVAVGEPSDELKEiyeIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGY---GEYF---- 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 953768345 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 5.75e-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: 38.32  E-value: 5.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 953768345 149 AAEAHRQVrkyvMSWIKPGMTMIEICEKLEDCSRKlikeNGLNAGLAFPTGCSLNNCAAHYTPNAGdttVLQYDDICKID 228
Cdd:cd01087   11 SAEAHRAA----MKASRPGMSEYELEAEFEYEFRS----RGARLAYSYIVAAGSNAAILHYVHNDQ---PLKDGDLVLID 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 953768345 229 FGTHISGRIID--CAFTV--TFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVM 285
Cdd:cd01087   80 AGAEYGGYASDitRTFPVngKFTDEQRELYEAVLAAQKAAIAACKPGVSYEDIHLLAHRVL 140
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
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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