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Conserved domains on  [gi|18406472|ref|NP_566013|]
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methionine aminopeptidase 2A [Arabidopsis thaliana]

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
 1-441 0e+00

methionine aminopeptidase 2; Provisional


:

Pssm-ID: 240246 [Multi-domain]  Cd Length: 470  Bit Score: 704.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472    1 MAIGNPEVATMGKENTEAESSNGNES-QLSSDLTKSLDLAEVKEDEKDNNQEEEDGLKAEASTkkkkkkskskkkksslQ 79
Cdd:PTZ00053  45 SENQEAENKQNNKKKKKKKKKKKKKNlGEAYDLAYDLPVVWSSAAFQDNSHIRKLGNWPEQEW----------------K 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472   80 QTDPPSIPVLELFPSGDFPQGEIQQYNDDNLWRTTSEEKREMERLQKPIYNSLRQAAEVHRQVRKYMRSILKPGMLMIDL 159
Cdd:PTZ00053 109 QTQPPTIPVSKQFKDGEYPVGEIQEYPGENSSRTSSEEKRELEKLSEEQYQDLRRAAEVHRQVRRYAQSVIKPGVKLIDI 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472  160 CETLENTVRKLISENGLQAGIAFPTGCSLNNVAAHWTPNSGDKTVLQYDDVMKLDFGTHIDGHIVDSAFTVAFNPMFDPL 239
Cdd:PTZ00053 189 CERIESKSRELIEADGLKCGWAFPTGCSLNHCAAHYTPNTGDKTVLTYDDVCKLDFGTHVNGRIIDCAFTVAFNPKYDPL 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472  240 LAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESYEVEINGKVYQVKSIRNLNGHSIGRYQIHAEKSVPNVRGGEQTKME 319
Cdd:PTZ00053 269 LQATKDATNTGIKEAGIDVRLSDIGAAIQEVIESYEVEIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPIVKGGENTRME 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472  320 EGELYAIETFGSTGKGYVREDLECSHYMKNYDVGHVPLRLPRAKQLLATINKNFSTLAFCRRYLDRLGETKYLMALKNLC 399
Cdd:PTZ00053 349 EGELFAIETFASTGRGYVNEDLECSHYMKDPGAEFVPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQDRHLLALKQLV 428

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 18406472  400 DSGIIEPCPPVCDVKGSYISQFEHTILLRPTCKEIISKGDDY 441
Cdd:PTZ00053 429 DAGIVNPYPPLCDVRGSYTSQMEHTILLRPTCKEVLSRGDDY 470
 
Name Accession Description Interval E-value
PTZ00053 PTZ00053
methionine aminopeptidase 2; Provisional
 1-441 0e+00

methionine aminopeptidase 2; Provisional


Pssm-ID: 240246 [Multi-domain]  Cd Length: 470  Bit Score: 704.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472    1 MAIGNPEVATMGKENTEAESSNGNES-QLSSDLTKSLDLAEVKEDEKDNNQEEEDGLKAEASTkkkkkkskskkkksslQ 79
Cdd:PTZ00053  45 SENQEAENKQNNKKKKKKKKKKKKKNlGEAYDLAYDLPVVWSSAAFQDNSHIRKLGNWPEQEW----------------K 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472   80 QTDPPSIPVLELFPSGDFPQGEIQQYNDDNLWRTTSEEKREMERLQKPIYNSLRQAAEVHRQVRKYMRSILKPGMLMIDL 159
Cdd:PTZ00053 109 QTQPPTIPVSKQFKDGEYPVGEIQEYPGENSSRTSSEEKRELEKLSEEQYQDLRRAAEVHRQVRRYAQSVIKPGVKLIDI 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472  160 CETLENTVRKLISENGLQAGIAFPTGCSLNNVAAHWTPNSGDKTVLQYDDVMKLDFGTHIDGHIVDSAFTVAFNPMFDPL 239
Cdd:PTZ00053 189 CERIESKSRELIEADGLKCGWAFPTGCSLNHCAAHYTPNTGDKTVLTYDDVCKLDFGTHVNGRIIDCAFTVAFNPKYDPL 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472  240 LAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESYEVEINGKVYQVKSIRNLNGHSIGRYQIHAEKSVPNVRGGEQTKME 319
Cdd:PTZ00053 269 LQATKDATNTGIKEAGIDVRLSDIGAAIQEVIESYEVEIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPIVKGGENTRME 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472  320 EGELYAIETFGSTGKGYVREDLECSHYMKNYDVGHVPLRLPRAKQLLATINKNFSTLAFCRRYLDRLGETKYLMALKNLC 399
Cdd:PTZ00053 349 EGELFAIETFASTGRGYVNEDLECSHYMKDPGAEFVPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQDRHLLALKQLV 428

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 18406472  400 DSGIIEPCPPVCDVKGSYISQFEHTILLRPTCKEIISKGDDY 441
Cdd:PTZ00053 429 DAGIVNPYPPLCDVRGSYTSQMEHTILLRPTCKEVLSRGDDY 470
MetAP2 cd01088
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 129-437 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: 516.80  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472 129 YNSLRQAAEVHRQVRKYMRSILKPGMLMIDLCETLENTVRKLIsenglqAGIAFPTGCSLNNVAAHWTPNSGDKTVLQYD 208
Cdd:cd01088   1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELG------AGPAFPVNLSINECAAHYTPNAGDDTVLKEG 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472 209 DVMKLDFGTHIDGHIVDSAFTVAFNPMFDPLLAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESyeveingkvYQVKSI 288
Cdd:cd01088  75 DVVKLDFGAHVDGYIADSAFTVDFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIES---------YGFKPI 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472 289 RNLNGHSIGRYQIHAEKSVPNVRGGEQTKMEEGELYAIETFGSTGKGYVREDLECSHYMKNYDvghVPLRLPRAKQLLAT 368
Cdd:cd01088 146 RNLTGHSIERYRLHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIYMLNRD---KPLRLPRARKLLDV 222

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18406472 369 INKNFSTLAFCRRYLDRLGETKYLMALKNLCDSGIIEPCPPVCDVKGSYISQFEHTILLRPTCKEIISK 437
Cdd:cd01088 223 IYENFGTLPFARRWLDRLGETKLLMALKNLCKAGIVYPYPVLKEISGGYVAQFEHTIIVREDGKEVTTR 291
met_pdase_II TIGR00501
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ...
 129-437 6.13e-113

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: 333.68  E-value: 6.13e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472   129 YNSLRQAAEVHRQVRKYMRSILKPGMLMIDLCETLENTVRKLISENglqagiAFPTGCSLNNVAAHWTPNSGDKTVLQYD 208
Cdd:TIGR00501   5 AEKWIEAGKIHSKVRREAADRIVPGVKLLEVAEFVENRIRELGAEP------AFPCNISINECAAHFTPKAGDKTVFKDG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472   209 DVMKLDFGTHIDGHIVDSAFTVAFNPMFDPLLAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESyeveingkvYQVKSI 288
Cdd:TIGR00501  79 DVVKLDLGAHVDGYIADTAITVDLGDQYDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIES---------YGVKPI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472   289 RNLNGHSIGRYQIHAEKSVPNVRGGEQTKMEEGELYAIETFGSTGKGYVREDLECSHYMKnydVGHVPLRLPRAKQLLAT 368
Cdd:TIGR00501 150 SNLTGHSMAPYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDGVGYVTDGGEVSIYAF---LAERPVRLDSARNLLKT 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18406472   369 INKNFSTLAFCRRYLDRLGETKYLMALKNLCDSGIIEPCPPVCDVKGSYISQFEHTILLRPTCKEIISK 437
Cdd:TIGR00501 227 IDENYGTLPFARRWLDKLGDEKYLFALNNLIRHGLIYDYPVLNEISGGYVAQWEHTILVEEHGKEVTTK 295
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 132-341 1.20e-29

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: 114.65  E-value: 1.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472   132 LRQAAEVHRQVRKYMRSILKPGMLMIDLCETLENTVRKlisENGLQaGIAFPT--GCSLNNVAAHWTPNsgdKTVLQYDD 209
Cdd:pfam00557   3 MRKAARIAAAALEAALAAIRPGVTERELAAELEAARLR---RGGAR-GPAFPPivASGPNAAIPHYIPN---DRVLKPGD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472   210 VMKLDFGTHIDGH-IVDSAFTVA---FNPMFDPLLAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESYEVEingkvyqv 285
Cdd:pfam00557  76 LVLIDVGAEYDGGyCSDITRTFVvgkPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLG-------- 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18406472   286 KSIRNLNGHSIGRyQIHAEKSVPnvRGGEQTKMEEGELYAIET--FGSTGKGYVR-EDL 341
Cdd:pfam00557 148 EYFPHGLGHGIGL-EVHEGPYIS--RGGDDRVLEPGMVFTIEPgiYFIPGWGGVRiEDT 203
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
132-340 7.63e-26

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 105.09  E-value: 7.63e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472 132 LRQAAEVHRQVRKYMRSILKPGM--LMID-LCEtlentvrKLISENGlqaGIA-------FP--TGCSLNNVAAHWTPns 199
Cdd:COG0024  12 MREAGRIVAEVLDELAEAVKPGVttLELDrIAE-------EFIRDHG---AIPaflgyygFPksICTSVNEVVVHGIP-- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472 200 gDKTVLQYDDVMKLDFGTHIDGHIVDSAFTVA---FNPMFDPLLAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESyev 276
Cdd:COG0024  80 -SDRVLKDGDIVNIDVGAILDGYHGDSARTFVvgeVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAES--- 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18406472 277 eiNGkvYQVksIRNLNGHSIGRyQIHAEKSVPNV-RGGEQTKMEEGELYAIETFGSTGKGYVRED 340
Cdd:COG0024 156 --NG--YSV--VREFVGHGIGR-EMHEEPQVPNYgRPGRGPRLKPGMVLAIEPMINAGTPEVKVL 213
 
Name Accession Description Interval E-value
PTZ00053 PTZ00053
methionine aminopeptidase 2; Provisional
 1-441 0e+00

methionine aminopeptidase 2; Provisional


Pssm-ID: 240246 [Multi-domain]  Cd Length: 470  Bit Score: 704.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472    1 MAIGNPEVATMGKENTEAESSNGNES-QLSSDLTKSLDLAEVKEDEKDNNQEEEDGLKAEASTkkkkkkskskkkksslQ 79
Cdd:PTZ00053  45 SENQEAENKQNNKKKKKKKKKKKKKNlGEAYDLAYDLPVVWSSAAFQDNSHIRKLGNWPEQEW----------------K 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472   80 QTDPPSIPVLELFPSGDFPQGEIQQYNDDNLWRTTSEEKREMERLQKPIYNSLRQAAEVHRQVRKYMRSILKPGMLMIDL 159
Cdd:PTZ00053 109 QTQPPTIPVSKQFKDGEYPVGEIQEYPGENSSRTSSEEKRELEKLSEEQYQDLRRAAEVHRQVRRYAQSVIKPGVKLIDI 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472  160 CETLENTVRKLISENGLQAGIAFPTGCSLNNVAAHWTPNSGDKTVLQYDDVMKLDFGTHIDGHIVDSAFTVAFNPMFDPL 239
Cdd:PTZ00053 189 CERIESKSRELIEADGLKCGWAFPTGCSLNHCAAHYTPNTGDKTVLTYDDVCKLDFGTHVNGRIIDCAFTVAFNPKYDPL 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472  240 LAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESYEVEINGKVYQVKSIRNLNGHSIGRYQIHAEKSVPNVRGGEQTKME 319
Cdd:PTZ00053 269 LQATKDATNTGIKEAGIDVRLSDIGAAIQEVIESYEVEIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPIVKGGENTRME 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472  320 EGELYAIETFGSTGKGYVREDLECSHYMKNYDVGHVPLRLPRAKQLLATINKNFSTLAFCRRYLDRLGETKYLMALKNLC 399
Cdd:PTZ00053 349 EGELFAIETFASTGRGYVNEDLECSHYMKDPGAEFVPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQDRHLLALKQLV 428

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 18406472  400 DSGIIEPCPPVCDVKGSYISQFEHTILLRPTCKEIISKGDDY 441
Cdd:PTZ00053 429 DAGIVNPYPPLCDVRGSYTSQMEHTILLRPTCKEVLSRGDDY 470
MetAP2 cd01088
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 129-437 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: 516.80  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472 129 YNSLRQAAEVHRQVRKYMRSILKPGMLMIDLCETLENTVRKLIsenglqAGIAFPTGCSLNNVAAHWTPNSGDKTVLQYD 208
Cdd:cd01088   1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELG------AGPAFPVNLSINECAAHYTPNAGDDTVLKEG 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472 209 DVMKLDFGTHIDGHIVDSAFTVAFNPMFDPLLAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESyeveingkvYQVKSI 288
Cdd:cd01088  75 DVVKLDFGAHVDGYIADSAFTVDFDPKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIES---------YGFKPI 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472 289 RNLNGHSIGRYQIHAEKSVPNVRGGEQTKMEEGELYAIETFGSTGKGYVREDLECSHYMKNYDvghVPLRLPRAKQLLAT 368
Cdd:cd01088 146 RNLTGHSIERYRLHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIYMLNRD---KPLRLPRARKLLDV 222

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18406472 369 INKNFSTLAFCRRYLDRLGETKYLMALKNLCDSGIIEPCPPVCDVKGSYISQFEHTILLRPTCKEIISK 437
Cdd:cd01088 223 IYENFGTLPFARRWLDRLGETKLLMALKNLCKAGIVYPYPVLKEISGGYVAQFEHTIIVREDGKEVTTR 291
met_pdase_II TIGR00501
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ...
 129-437 6.13e-113

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: 333.68  E-value: 6.13e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472   129 YNSLRQAAEVHRQVRKYMRSILKPGMLMIDLCETLENTVRKLISENglqagiAFPTGCSLNNVAAHWTPNSGDKTVLQYD 208
Cdd:TIGR00501   5 AEKWIEAGKIHSKVRREAADRIVPGVKLLEVAEFVENRIRELGAEP------AFPCNISINECAAHFTPKAGDKTVFKDG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472   209 DVMKLDFGTHIDGHIVDSAFTVAFNPMFDPLLAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESyeveingkvYQVKSI 288
Cdd:TIGR00501  79 DVVKLDLGAHVDGYIADTAITVDLGDQYDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIES---------YGVKPI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472   289 RNLNGHSIGRYQIHAEKSVPNVRGGEQTKMEEGELYAIETFGSTGKGYVREDLECSHYMKnydVGHVPLRLPRAKQLLAT 368
Cdd:TIGR00501 150 SNLTGHSMAPYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDGVGYVTDGGEVSIYAF---LAERPVRLDSARNLLKT 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18406472   369 INKNFSTLAFCRRYLDRLGETKYLMALKNLCDSGIIEPCPPVCDVKGSYISQFEHTILLRPTCKEIISK 437
Cdd:TIGR00501 227 IDENYGTLPFARRWLDKLGDEKYLFALNNLIRHGLIYDYPVLNEISGGYVAQWEHTILVEEHGKEVTTK 295
crvDNA_42K TIGR00495
42K curved DNA binding protein; Proteins identified by this model have been identified in a ...
 113-438 2.47e-33

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: 129.24  E-value: 2.47e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472   113 TTSEEKRE-MERLQKP-IYNSLRQAAEVHRQVRKYMRSILKPGMLMIDLCE-----TLENTVRKLISENGLQAGIAFPTG 185
Cdd:TIGR00495   2 SGKDEQQEqAYSLSNPeVVTKYKMAGEIANNVLKSVVEACSPGAKVVDICEkgdafIMEETAKIFKKEKEMEKGIAFPTC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472   186 CSLNNVAAHWTPNSGDKT-VLQYDDVMKLDFGTHIDGHIVDSAFT-VAFNPMFDPLLAASRDATYTGIKEAGVDVRLCDV 263
Cdd:TIGR00495  82 ISVNNCVGHFSPLKSDQDyILKEGDVVKIDLGCHIDGFIALVAHTfVVGVAQEEPVTGRKADVIAAAHLAAEAALRLVKP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472   264 GAAVQEVMESYEveingKV---YQVKSIRNLNGHSIGRYQIHAEKSVPNVRGGEQTK------MEEGELYAIETFGSTGK 334
Cdd:TIGR00495 162 GNTNTQVTEAIN-----KVahsYGCTPVEGMLSHQLKQHVIDGEKVIISNPSDSQKKdhdtaeFEENEVYAVDILVSTGE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472   335 GYVRE-DLECSHYMKNYDVGHVpLRLPRAKQLLATINKNFSTLAFCRRYLDrlGETKYLMALKNLCDSGIIEPCPPVCDV 413
Cdd:TIGR00495 237 GKAKDaDQRTTIYKRDPSKTYG-LKMKASRAFFSEIERRFDAMPFTLRNFE--DEKRARMGLVECVKHELLQPYPVLYEK 313

                         330       340
                  ....*....|....*....|....*
gi 18406472   414 KGSYISQFEHTILLRPTCKEIISKG 438
Cdd:TIGR00495 314 EGEFVAQFKFTVLLMPNGPMRITSG 338
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 132-341 1.20e-29

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: 114.65  E-value: 1.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472   132 LRQAAEVHRQVRKYMRSILKPGMLMIDLCETLENTVRKlisENGLQaGIAFPT--GCSLNNVAAHWTPNsgdKTVLQYDD 209
Cdd:pfam00557   3 MRKAARIAAAALEAALAAIRPGVTERELAAELEAARLR---RGGAR-GPAFPPivASGPNAAIPHYIPN---DRVLKPGD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472   210 VMKLDFGTHIDGH-IVDSAFTVA---FNPMFDPLLAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESYEVEingkvyqv 285
Cdd:pfam00557  76 LVLIDVGAEYDGGyCSDITRTFVvgkPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLG-------- 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18406472   286 KSIRNLNGHSIGRyQIHAEKSVPnvRGGEQTKMEEGELYAIET--FGSTGKGYVR-EDL 341
Cdd:pfam00557 148 EYFPHGLGHGIGL-EVHEGPYIS--RGGDDRVLEPGMVFTIEPgiYFIPGWGGVRiEDT 203
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
132-340 7.63e-26

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 105.09  E-value: 7.63e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472 132 LRQAAEVHRQVRKYMRSILKPGM--LMID-LCEtlentvrKLISENGlqaGIA-------FP--TGCSLNNVAAHWTPns 199
Cdd:COG0024  12 MREAGRIVAEVLDELAEAVKPGVttLELDrIAE-------EFIRDHG---AIPaflgyygFPksICTSVNEVVVHGIP-- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472 200 gDKTVLQYDDVMKLDFGTHIDGHIVDSAFTVA---FNPMFDPLLAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESyev 276
Cdd:COG0024  80 -SDRVLKDGDIVNIDVGAILDGYHGDSARTFVvgeVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAES--- 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18406472 277 eiNGkvYQVksIRNLNGHSIGRyQIHAEKSVPNV-RGGEQTKMEEGELYAIETFGSTGKGYVRED 340
Cdd:COG0024 156 --NG--YSV--VREFVGHGIGR-EMHEEPQVPNYgRPGRGPRLKPGMVLAIEPMINAGTPEVKVL 213
PRK12896 PRK12896
methionine aminopeptidase; Reviewed
 117-339 4.86e-24

methionine aminopeptidase; Reviewed


Pssm-ID: 237252 [Multi-domain]  Cd Length: 255  Bit Score: 100.30  E-value: 4.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472  117 EKREMERLQKPIYNSLRQAAEVHRQVRKYMRSILKPGMLMIDlcetLENTVRKLISENGLQAGI----AFPTGC--SLNN 190
Cdd:PRK12896   4 EGRGMEIKSPRELEKMRKIGRIVATALKEMGKAVEPGMTTKE----LDRIAEKRLEEHGAIPSPegyyGFPGSTciSVNE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472  191 VAAHWTPNSgdkTVLQYDDVMKLDFGTHIDGHIVDSAFTVAF---NPMFDPLLAASRDATYTGIKEAGVDVRLCDVGAAV 267
Cdd:PRK12896  80 EVAHGIPGP---RVIKDGDLVNIDVSAYLDGYHGDTGITFAVgpvSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAI 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18406472  268 QEvmesyEVEINGkvYQVksIRNLNGHSIGRyQIHAEKSVPNVRG--GEQTKMEEGELYAIETFGSTGKGYVRE 339
Cdd:PRK12896 157 ED-----FAKKNG--YSV--VRDLTGHGVGR-SLHEEPSVILTYTdpLPNRLLRPGMTLAVEPFLNLGAKDAET 220
APP_MetAP cd01066
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
 132-340 1.13e-22

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: 95.21  E-value: 1.13e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472 132 LRQAAEVHRQVRKYMRSILKPGMLMIDLCETLENTVRKLIsenglqAGIAFPTGCSLNNVAA--HWTPNSgdkTVLQYDD 209
Cdd:cd01066   4 LRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAG------GYPAGPTIVGSGARTAlpHYRPDD---RRLQEGD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472 210 VMKLDFGTHIDGHIVDSAFTVAFNPMFDP---LLAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESYEVEINgkvyqvk 286
Cdd:cd01066  75 LVLVDLGGVYDGYHADLTRTFVIGEPSDEqreLYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLGPN------- 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18406472 287 sIRNLNGHSIGrYQIHAEksvPNVRGGEQTKMEEGELYAIETF--GSTGKGYVRED 340
Cdd:cd01066 148 -FGHRTGHGIG-LEIHEP---PVLKAGDDTVLEPGMVFAVEPGlyLPGGGGVRIED 198
PRK05716 PRK05716
methionine aminopeptidase; Validated
 132-340 3.73e-21

methionine aminopeptidase; Validated


Pssm-ID: 235576 [Multi-domain]  Cd Length: 252  Bit Score: 92.12  E-value: 3.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472  132 LRQAAEVHRQVRKYMRSILKPGM--LMID-LCEtlentvrKLISENGlqaGIAFPTG--------C-SLNNVAAHWTPns 199
Cdd:PRK05716  14 MRVAGRLAAEVLDEIEPHVKPGVttKELDrIAE-------EYIRDQG---AIPAPLGyhgfpksiCtSVNEVVCHGIP-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472  200 gDKTVLQYDDVMKLDFGTHIDGHIVDSAFTVAF---NPMFDPLLAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESyev 276
Cdd:PRK05716  82 -SDKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVgeiSPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEA--- 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18406472  277 eiNGkvYQVksIRNLNGHSIGRyQIHAEKSVPN-VRGGEQTKMEEGELYAIETFGSTGKGYVRED 340
Cdd:PRK05716 158 --EG--FSV--VREYCGHGIGR-KFHEEPQIPHyGAPGDGPVLKEGMVFTIEPMINAGKREVKTL 215
PA2G4-like cd01089
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ...
 130-230 1.25e-15

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: 75.83  E-value: 1.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472 130 NSLRQAAEVHRQVRKYMRSILKPGMLMIDLCETLENTVRKLI-----SENGLQAGIAFPTGCSLNNVAAHWTPNSGDKTV 204
Cdd:cd01089   2 TKYKTAGQIANKVLKQVISLCVPGAKVVDLCEKGDKLILEELgkvykKEKKLEKGIAFPTCISVNNCVCHFSPLKSDATY 81

                        90       100
                ....*....|....*....|....*..
gi 18406472 205 -LQYDDVMKLDFGTHIDGHIVDSAFTV 230
Cdd:cd01089  82 tLKDGDVVKIDLGCHIDGYIAVVAHTI 108
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
132-341 5.49e-11

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


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 63.30  E-value: 5.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472 132 LRQAAEVHRQVRKYMRSILKPGMLMIDLCETLENTVRKLISEnglqaGIAFPTGCSLNNVAA--HWTPNSgdkTVLQYDD 209
Cdd:COG0006  82 MRKAARIADAAHEAALAALRPGVTEREVAAELEAAMRRRGAE-----GPSFDTIVASGENAAipHYTPTD---RPLKPGD 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472 210 VMKLDFGTHIDGHIVDSAFTVAFNPmFDP----LLAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESYEVeingKVYQV 285
Cdd:COG0006 154 LVLIDAGAEYDGYTSDITRTVAVGE-PSDeqreIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAGY----GEYFP 228

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18406472 286 KSIrnlnGHSIGrYQIHaekSVPNVRGGEQTKMEEGELYAIE-TFGSTGKGYVR-EDL 341
Cdd:COG0006 229 HGT----GHGVG-LDVH---EGPQISPGNDRPLEPGMVFTIEpGIYIPGIGGVRiEDT 278
APP-like cd01092
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
 132-327 4.68e-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: 59.06  E-value: 4.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472 132 LRQAAEVHRQVRKYMRSILKPGMLMIDLCETLENTVRKLISEnglqaGIAFPTGCSLNNVAA--HWTPnsgDKTVLQYDD 209
Cdd:cd01092   4 LRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKLGAE-----GPSFDTIVASGPNSAlpHGVP---SDRKIEEGD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406472 210 VMKLDFGTHIDGHIVDSAFTVAF---NPMFDPLLAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESYEVeinGKvYQVK 286
Cdd:cd01092  76 LVLIDFGAIYDGYCSDITRTVAVgepSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGY---GE-YFIH 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18406472 287 SIrnlnGHSIGRyQIHAEksvPNVRGGEQTKMEEGELYAIE 327
Cdd:cd01092 152 RT----GHGVGL-EVHEA---PYISPGSDDVLEEGMVFTIE 184
 
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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