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Conserved domains on  [gi|2217326789|ref|XP_047299828|]
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methionine aminopeptidase 1D, mitochondrial isoform X3 [Homo sapiens]

Protein Classification

methionyl aminopeptidase( domain architecture ID 10099531)

methionyl aminopeptidase catalyzes the hydrolytic removal of N-terminal methionine residues

CATH:  3.90.230.10
EC:  3.4.11.18
Gene Ontology:  GO:0070006|GO:0046872|GO:0006508
PubMed:  7674922

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MetAP1 cd01086
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 1-212 6.73e-123

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: 347.56  E-value: 6.73e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:cd01086    26 VTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGDIVNIDVGVELDGYHGDSARTFIVGE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHA-NDSDLPMEE 159
Cdd:cd01086   106 VSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGGHGIGRKFHEEPQIPNYGrPGTGPKLKP 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217326789 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTK 212
Cdd:cd01086   186 GMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILTL 238
 
Name Accession Description Interval E-value
MetAP1 cd01086
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 1-212 6.73e-123

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: 347.56  E-value: 6.73e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:cd01086    26 VTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGDIVNIDVGVELDGYHGDSARTFIVGE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHA-NDSDLPMEE 159
Cdd:cd01086   106 VSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGGHGIGRKFHEEPQIPNYGrPGTGPKLKP 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217326789 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTK 212
Cdd:cd01086   186 GMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILTL 238
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
1-216 2.82e-108

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 311.17  E-value: 2.82e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:COG0024    34 VTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSVNEVVVHGIPSDRVLKDGDIVNIDVGAILDGYHGDSARTFVVGE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHH-ANDSDLPMEE 159
Cdd:COG0024   114 VSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSVVREFVGHGIGREMHEEPQVPNYgRPGRGPRLKP 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217326789 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKLPHE 216
Cdd:COG0024   194 GMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTEDGPEILTLPDGG 250
PRK05716 PRK05716
methionine aminopeptidase; Validated
 1-216 2.72e-104

methionine aminopeptidase; Validated


Pssm-ID: 235576 [Multi-domain]  Cd Length: 252  Bit Score: 300.90  E-value: 2.72e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:PRK05716   36 VTTKELDRIAEEYIRDQGAIPAPLGYHGFPKSICTSVNEVVCHGIPSDKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHANDSDLP-MEE 159
Cdd:PRK05716  116 ISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGFSVVREYCGHGIGRKFHEEPQIPHYGAPGDGPvLKE 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217326789 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKLPHE 216
Cdd:PRK05716  196 GMVFTIEPMINAGKREVKTLKDGWTVVTKDGSLSAQYEHTVAVTEDGPEILTLRPEE 252
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
 1-213 8.24e-85

methionine aminopeptidase, type I; Methionine aminopeptidase 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. This model describes type I. The role of this protein in general is to produce the mature form of cytosolic proteins by removing the N-terminal methionine. [Protein fate, Protein modification and repair]


Pssm-ID: 129591 [Multi-domain]  Cd Length: 247  Bit Score: 251.50  E-value: 8.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:TIGR00500  34 VSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISVNEVVIHGIPDKKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGK 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHANDSDLP-MEE 159
Cdd:TIGR00500 114 ISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSVVREYCGHGIGRKFHEEPQIPNYGKKFTNVrLKE 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217326789 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKL 213
Cdd:TIGR00500 194 GMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITDNGPEILTER 247
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 1-203 6.81e-51

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: 163.95  E-value: 6.81e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNAYpsplGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYN-GYHGDTSETFLVG 79
Cdd:pfam00557  25 VTERELAAELEAARLRRGGA----RGPAFPPIVASGPNAAIPHYIPNDRVLKPGDLVLIDVGAEYDgGYCSDITRTFVVG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  80 NVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGF-QVCPHFVGHGIGSYFHGHPEIWHhaNDSDLPME 158
Cdd:pfam00557 101 KPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLgEYFPHGLGHGIGLEVHEGPYISR--GGDDRVLE 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2217326789 159 EGMAFTIEPIITEgspefkvledawtvvsLDNQRSAQFEHTVLIT 203
Cdd:pfam00557 179 PGMVFTIEPGIYF----------------IPGWGGVRIEDTVLVT 207
 
Name Accession Description Interval E-value
MetAP1 cd01086
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 1-212 6.73e-123

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: 347.56  E-value: 6.73e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:cd01086    26 VTTKELDQIAHEFIEEHGAYPAPLGYYGFPKSICTSVNEVVCHGIPDDRVLKDGDIVNIDVGVELDGYHGDSARTFIVGE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHA-NDSDLPMEE 159
Cdd:cd01086   106 VSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGGHGIGRKFHEEPQIPNYGrPGTGPKLKP 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217326789 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTK 212
Cdd:cd01086   186 GMVFTIEPMINLGTYEVVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILTL 238
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
1-216 2.82e-108

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 311.17  E-value: 2.82e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:COG0024    34 VTTLELDRIAEEFIRDHGAIPAFLGYYGFPKSICTSVNEVVVHGIPSDRVLKDGDIVNIDVGAILDGYHGDSARTFVVGE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHH-ANDSDLPMEE 159
Cdd:COG0024   114 VSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSVVREFVGHGIGREMHEEPQVPNYgRPGRGPRLKP 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217326789 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKLPHE 216
Cdd:COG0024   194 GMVLAIEPMINAGTPEVKVLDDGWTVVTKDGSLSAQFEHTVAVTEDGPEILTLPDGG 250
PRK05716 PRK05716
methionine aminopeptidase; Validated
 1-216 2.72e-104

methionine aminopeptidase; Validated


Pssm-ID: 235576 [Multi-domain]  Cd Length: 252  Bit Score: 300.90  E-value: 2.72e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:PRK05716   36 VTTKELDRIAEEYIRDQGAIPAPLGYHGFPKSICTSVNEVVCHGIPSDKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHANDSDLP-MEE 159
Cdd:PRK05716  116 ISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGFSVVREYCGHGIGRKFHEEPQIPHYGAPGDGPvLKE 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217326789 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKLPHE 216
Cdd:PRK05716  196 GMVFTIEPMINAGKREVKTLKDGWTVVTKDGSLSAQYEHTVAVTEDGPEILTLRPEE 252
PRK12896 PRK12896
methionine aminopeptidase; Reviewed
 1-211 3.97e-93

methionine aminopeptidase; Reviewed


Pssm-ID: 237252 [Multi-domain]  Cd Length: 255  Bit Score: 272.87  E-value: 3.97e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:PRK12896   41 MTTKELDRIAEKRLEEHGAIPSPEGYYGFPGSTCISVNEEVAHGIPGPRVIKDGDLVNIDVSAYLDGYHGDTGITFAVGP 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHP-EIWHHANDSD-LPME 158
Cdd:PRK12896  121 VSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAIEDFAKKNGYSVVRDLTGHGVGRSLHEEPsVILTYTDPLPnRLLR 200

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217326789 159 EGMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILT 211
Cdd:PRK12896  201 PGMTLAVEPFLNLGAKDAETLDDGWTVVTPDKSLSAQFEHTVVVTRDGPEILT 253
PLN03158 PLN03158
methionine aminopeptidase; Provisional
 1-214 9.64e-89

methionine aminopeptidase; Provisional


Pssm-ID: 215607 [Multi-domain]  Cd Length: 396  Bit Score: 266.70  E-value: 9.64e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:PLN03158  168 VTTDEIDRVVHEATIAAGGYPSPLNYHFFPKSCCTSVNEVICHGIPDARKLEDGDIVNVDVTVYYKGCHGDLNETFFVGN 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHA-NDSDLPMEE 159
Cdd:PLN03158  248 VDEASRQLVKCTYECLEKAIAIVKPGVRYREVGEVINRHATMSGLSVVKSYCGHGIGELFHCAPNIPHYArNKAVGVMKA 327

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217326789 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILT-KLP 214
Cdd:PLN03158  328 GQVFTIEPMINAGVWRDRMWPDGWTAVTADGKRSAQFEHTLLVTETGVEVLTaRLP 383
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
 1-213 8.24e-85

methionine aminopeptidase, type I; Methionine aminopeptidase 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. This model describes type I. The role of this protein in general is to produce the mature form of cytosolic proteins by removing the N-terminal methionine. [Protein fate, Protein modification and repair]


Pssm-ID: 129591 [Multi-domain]  Cd Length: 247  Bit Score: 251.50  E-value: 8.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:TIGR00500  34 VSTKELDRIAKDFIEKHGAKPAFLGYYGFPGSVCISVNEVVIHGIPDKKVLKDGDIVNIDVGVIYDGYHGDTAKTFLVGK 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHANDSDLP-MEE 159
Cdd:TIGR00500 114 ISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSVVREYCGHGIGRKFHEEPQIPNYGKKFTNVrLKE 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217326789 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKL 213
Cdd:TIGR00500 194 GMVFTIEPMVNTGTEEITTAADGWTVKTKDGSLSAQFEHTIVITDNGPEILTER 247
PRK12318 PRK12318
methionyl aminopeptidase;
2-213 1.37e-72

methionyl aminopeptidase;


Pssm-ID: 183434 [Multi-domain]  Cd Length: 291  Bit Score: 222.00  E-value: 1.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   2 TTEEIDALVHREIISHNAYPSPLGYGG--FPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVG 79
Cdd:PRK12318   75 TTNELDELSRELHKEYNAIPAPLNYGSppFPKTICTSLNEVICHGIPNDIPLKNGDIMNIDVSCIVDGYYGDCSRMVMIG 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  80 NVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHANDSDLPMEE 159
Cdd:PRK12318  155 EVSEIKKKVCQASLECLNAAIAILKPGIPLYEIGEVIENCADKYGFSVVDQFVGHGVGIKFHENPYVPHHRNSSKIPLAP 234

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217326789 160 GMAFTIEPIITEGSPE-FKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKL 213
Cdd:PRK12318  235 GMIFTIEPMINVGKKEgVIDPINHWEARTCDNQPSAQWEHTILITETGYEILTLL 289
PRK12897 PRK12897
type I methionyl aminopeptidase;
1-213 5.24e-51

type I methionyl aminopeptidase;


Pssm-ID: 171806  Cd Length: 248  Bit Score: 165.59  E-value: 5.24e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:PRK12897   35 ITTKEINTFVEAYLEKHGATSEQKGYNGYPYAICASVNDEMCHAFPADVPLTEGDIVTIDMVVNLNGGLSDSAWTYRVGK 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHANDSDLP-MEE 159
Cdd:PRK12897  115 VSDEAEKLLLVAENALYKGIDQAVIGNRVGDIGYAIESYVANEGFSVARDFTGHGIGKEIHEEPAIFHFGKQGQGPeLQE 194

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217326789 160 GMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLITSRGAQILTKL 213
Cdd:PRK12897  195 GMVITIEPIVNVGMRYSKVDLNGWTARTMDGKLSAQYEHTIAITKDGPIILTKL 248
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 1-203 6.81e-51

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: 163.95  E-value: 6.81e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNAYpsplGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYN-GYHGDTSETFLVG 79
Cdd:pfam00557  25 VTERELAAELEAARLRRGGA----RGPAFPPIVASGPNAAIPHYIPNDRVLKPGDLVLIDVGAEYDgGYCSDITRTFVVG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  80 NVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGF-QVCPHFVGHGIGSYFHGHPEIWHhaNDSDLPME 158
Cdd:pfam00557 101 KPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLgEYFPHGLGHGIGLEVHEGPYISR--GGDDRVLE 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2217326789 159 EGMAFTIEPIITEgspefkvledawtvvsLDNQRSAQFEHTVLIT 203
Cdd:pfam00557 179 PGMVFTIEPGIYF----------------IPGWGGVRIEDTVLVT 207
APP_MetAP cd01066
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
 1-207 1.21e-36

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: 127.18  E-value: 1.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNAYPSPlgyggfpkSVCTSVNNV--LCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLV 78
Cdd:cd01066    26 VTEAEVAAAIEQALRAAGGYPAG--------PTIVGSGARtaLPHYRPDDRRLQEGDLVLVDLGGVYDGYHADLTRTFVI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  79 GNVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGF-QVCPHFVGHGIGSYFHGHPEIwhhANDSDLPM 157
Cdd:cd01066    98 GEPSDEQRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLgPNFGHRTGHGIGLEIHEPPVL---KAGDDTVL 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217326789 158 EEGMAFTIEPIItegspefkvledawtvvSLDNQRSAQFEHTVLITSRGA 207
Cdd:cd01066   175 EPGMVFAVEPGL-----------------YLPGGGGVRIEDTVLVTEDGP 207
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
1-216 1.59e-33

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


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 121.85  E-value: 1.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNAYpsplgYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGN 80
Cdd:COG0006   104 VTEREVAAELEAAMRRRGAE-----GPSFDTIVASGENAAIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGE 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  81 VDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVC-PHFVGHGIGSYFHGHPEIwhhANDSDLPMEE 159
Cdd:COG0006   179 PSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAEAGYGEYfPHGTGHGVGLDVHEGPQI---SPGNDRPLEP 255

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217326789 160 GMAFTIEPIITegspefkvLEDAWTVvsldnqRSaqfEHTVLITSRGAQILTKLPHE 216
Cdd:COG0006   256 GMVFTIEPGIY--------IPGIGGV------RI---EDTVLVTEDGAEVLTRLPRE 295
APP-like cd01092
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
 1-169 4.88e-26

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: 99.89  E-value: 4.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNAY-PSplgyggFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVG 79
Cdd:cd01092    26 MTEREVAAELEYFMRKLGAEgPS------FDTIVASGPNSALPHGVPSDRKIEEGDLVLIDFGAIYDGYCSDITRTVAVG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  80 NVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGF-QVCPHFVGHGIGSYFHGHPEIwhhANDSDLPME 158
Cdd:cd01092   100 EPSDELKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGYgEYFIHRTGHGVGLEVHEAPYI---SPGSDDVLE 176

                         170
                  ....*....|.
gi 2217326789 159 EGMAFTIEPII 169
Cdd:cd01092   177 EGMVFTIEPGI 187
PRK07281 PRK07281
methionyl aminopeptidase;
5-211 1.50e-25

methionyl aminopeptidase;


Pssm-ID: 180918  Cd Length: 286  Bit Score: 100.31  E-value: 1.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   5 EIDALVHREIISHNAYPSPLGYGG----FPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDV------------------- 61
Cdd:PRK07281   39 EVEEYVRRRCKEENVLPLQIGVDGammdYPYATCCGLNDEVAHAFPRHYILKEGDLLKVDMvlsepldksivdvsklnfd 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  62 --------TVYYNGYHGDTSETFLVGNVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVG 133
Cdd:PRK07281  119 nveqmkkyTESYRGGLADSCWAYAVGTPSDEVKNLMDVTKEAMYRGIEQAVVGNRIGDIGAAIQEYAESRGYGVVRDLVG 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789 134 HGIGSYFHGHPEIWHHANDS-DLPMEEGMAFTIEPIITEGSPEFKV-LEDAWTVVSLDNQRSAQFEHTVLITSRGAQILT 211
Cdd:PRK07281  199 HGVGPTMHEEPMVPNYGTAGrGLRLREGMVLTIEPMINTGTWEIDTdMKTGWAHKTLDGGLSCQYEHQFVITKDGPVILT 278
met_pdase_II TIGR00501
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ...
 5-212 1.72e-19

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: 84.45  E-value: 1.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   5 EIDALVHREIISHNAYPsplgygGFPKSVctSVNNVLCHGIP---DSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNV 81
Cdd:TIGR00501  34 EVAEFVENRIRELGAEP------AFPCNI--SINECAAHFTPkagDKTVFKDGDVVKLDLGAHVDGYIADTAITVDLGDQ 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  82 decGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSY-FHGHPEIWHHANDSDLPMEEG 160
Cdd:TIGR00501 106 ---YDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIESYGVKPISNLTGHSMAPYrLHGGKSIPNVKERDTTKLEEG 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789 161 MAFTIEPIITEG---------------------------------SPEFKVL----------EDAWTVVSLD-------- 189
Cdd:TIGR00501 183 DVVAIEPFATDGvgyvtdggevsiyaflaerpvrldsarnllktiDENYGTLpfarrwldklGDEKYLFALNnlirhgli 262

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2217326789 190 ------NQRS----AQFEHTVLITSRGAQILTK 212
Cdd:TIGR00501 263 ydypvlNEISggyvAQWEHTILVEEHGKEVTTK 295
MetAP2 cd01088
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 28-172 5.61e-15

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: 71.90  E-value: 5.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  28 GFPKSVctSVNNVLCHGIP---DSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVdecGKKLVEVARRCRDEAIAACR 104
Cdd:cd01088    47 AFPVNL--SINECAAHYTPnagDDTVLKEGDVVKLDFGAHVDGYIADSAFTVDFDPK---YDDLLEAAKEALNAAIKEAG 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217326789 105 AGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSY-FHGHPEIWHHANDSDLPMEEGMAFTIEPIITEG 172
Cdd:cd01088   122 PDVRLGEIGEAIEEVIESYGFKPIRNLTGHSIERYrLHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTG 190
Prolidase cd01087
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ...
 5-212 8.65e-12

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: 62.21  E-value: 8.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   5 EIDALVHREIISHNAypsPLGYGgfPKSVCTSVNNVLcHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLV-GNVDE 83
Cdd:cd01087    30 ELEAEFEYEFRSRGA---RLAYS--YIVAAGSNAAIL-HYVHNDQPLKDGDLVLIDAGAEYGGYASDITRTFPVnGKFTD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  84 CGKKLVEVARRCRDEAIAACRAGAPFSVIgNTISHITHQNGFQV--------------------CPHFVGHGIGSYFH-- 141
Cdd:cd01087   104 EQRELYEAVLAAQKAAIAACKPGVSYEDI-HLLAHRVLAEGLKElgilkgdvdeivesgayakfFPHGLGHYLGLDVHdv 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217326789 142 GHPeiwHHANDSDLPMEEGMAFTIEP---IItegsPEFKVLEDAWTVVSL---DNqrsaqfehtVLITSRGAQILTK 212
Cdd:cd01087   183 GGY---LRYLRRARPLEPGMVITIEPgiyFI----PDLLDVPEYFRGGGIrieDD---------VLVTEDGPENLTR 243
PRK09795 PRK09795
aminopeptidase; Provisional
 29-216 2.24e-08

aminopeptidase; Provisional


Pssm-ID: 182080 [Multi-domain]  Cd Length: 361  Bit Score: 53.40  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  29 FPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDECGKK-----LVEVARRCRDEAIAAC 103
Cdd:PRK09795  181 FDTIVASGWRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVNGEGVSAEShplfnVYQIVLQAQLAAISAI 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789 104 RAGAPFSVIGNTISHITHQNGF-QVCPHFVGHGIGSYFHGHPEIwhhANDSDLPMEEGMAFTIEPIITegspefkvleda 182
Cdd:PRK09795  261 RPGVRCQQVDDAARRVITEAGYgDYFGHNTGHAIGIEVHEDPRF---SPRDTTTLQPGMLLTVEPGIY------------ 325

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2217326789 183 wtvvsLDNQRSAQFEHTVLITSRGAQILTKLPHE 216
Cdd:PRK09795  326 -----LPGQGGVRIEDVVLVTPQGAEVLYAMPKT 354
PA2G4-like cd01089
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ...
 29-211 9.63e-08

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: 50.79  E-value: 9.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  29 FPksVCTSVNNVLCHGIP----DSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDECGK--KLVEVARRCRDEAIAA 102
Cdd:cd01089    59 FP--TCISVNNCVCHFSPlksdATYTLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAETPVtgKKADVIAAAHYALEAA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789 103 CRAGAPfsviGNTISHIThQNGFQVCPHFVGHGIGSyfhghpeIWHHAndsdlpMEEGMAFtiepiiTEGSPEFKVLED- 181
Cdd:cd01089   137 LRLLRP----GNQNSDIT-EAIQKVIVDYGCTPVEG-------VLSHQ------LKRVVSS------GEGKAKLVECVKh 192

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2217326789 182 ----AWTVV-SLDNQRSAQFEHTVLITSRGAQILT 211
Cdd:cd01089   193 gllfPYPVLyEKEGEVVAQFKLTVLLTPNGVTVLT 227
PRK15173 PRK15173
peptidase; Provisional
 45-216 1.28e-07

peptidase; Provisional


Pssm-ID: 185095 [Multi-domain]  Cd Length: 323  Bit Score: 50.87  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  45 IPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNG 124
Cdd:PRK15173  164 IPSNTKACSGDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSG 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789 125 FqvcPHF----VGHGIGSY--FHGHPEIWHHANDSdlpMEEGMAFTIEpiitegSPEFKVledawtvvsldNQRSAQFEH 198
Cdd:PRK15173  244 L---PNYnrghLGHGNGVFlgLEESPFVSTHATES---FTSGMVLSLE------TPYYGY-----------NLGSIMIED 300

                         170
                  ....*....|....*...
gi 2217326789 199 TVLITSRGAQILTKLPHE 216
Cdd:PRK15173  301 MILINKEGIEFLSKLPRD 318
PRK14575 PRK14575
putative peptidase; Provisional
 45-216 2.17e-07

putative peptidase; Provisional


Pssm-ID: 173039 [Multi-domain]  Cd Length: 406  Bit Score: 50.47  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  45 IPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNG 124
Cdd:PRK14575  247 IPSNTKACSGDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSG 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789 125 FqvcPHF----VGHGIGSY--FHGHPEIWHHANDSdlpMEEGMAFTIEpiitegSPEFKVledawtvvsldNQRSAQFEH 198
Cdd:PRK14575  327 L---PNYnrghLGHGNGVFlgLEESPFVSTHATES---FTSGMVLSLE------TPYYGY-----------NLGSIMIED 383

                         170
                  ....*....|....*...
gi 2217326789 199 TVLITSRGAQILTKLPHE 216
Cdd:PRK14575  384 MILINKEGIEFLSKLPRD 401
PRK14576 PRK14576
putative endopeptidase; Provisional
 45-213 1.87e-05

putative endopeptidase; Provisional


Pssm-ID: 173040 [Multi-domain]  Cd Length: 405  Bit Score: 44.62  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  45 IPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNG 124
Cdd:PRK14576  246 IADTTPAKVGDLIKFDCGIDVAGYGADLARTFVLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVFDSTMAVIKTSG 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789 125 FqvcPHF----VGHGIGSY--FHGHPEIWHHANDSDLPmeeGMAFTIEpiitegSPEFKVledawtvvsldNQRSAQFEH 198
Cdd:PRK14576  326 L---PHYnrghLGHGDGVFlgLEEVPFVSTQATETFCP---GMVLSLE------TPYYGI-----------GVGSIMLED 382

                         170
                  ....*....|....*
gi 2217326789 199 TVLITSRGAQILTKL 213
Cdd:PRK14576  383 MILITDSGFEFLSKL 397
crvDNA_42K TIGR00495
42K curved DNA binding protein; Proteins identified by this model have been identified in a ...
 29-185 2.30e-05

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: 44.49  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  29 FPksVCTSVNNVLCHGIP----DSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDE---CGKK--LVEVARRCRDEA 99
Cdd:TIGR00495  78 FP--TCISVNNCVGHFSPlksdQDYILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEepvTGRKadVIAAAHLAAEAA 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789 100 IAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSY-FHGHPEIWHHANDSD------LPMEEGMAFTIEPIITEG 172
Cdd:TIGR00495 156 LRLVKPGNTNTQVTEAINKVAHSYGCTPVEGMLSHQLKQHvIDGEKVIISNPSDSQkkdhdtAEFEENEVYAVDILVSTG 235

                         170
                  ....*....|...
gi 2217326789 173 SPEFKVLEDAWTV 185
Cdd:TIGR00495 236 EGKAKDADQRTTI 248
PRK10879 PRK10879
proline aminopeptidase P II; Provisional
 1-167 1.61e-04

proline aminopeptidase P II; Provisional


Pssm-ID: 182804 [Multi-domain]  Cd Length: 438  Bit Score: 42.02  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789   1 MTTEEIDALVHREIISHNA-YPSplgyggFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLV- 78
Cdd:PRK10879  204 MFEYQLEGEIHHEFNRHGArYPS------YNTIVGSGENGCILHYTENESEMRDGDLVLIDAGCEYKGYAGDITRTFPVn 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  79 GNVDECGKKLVEVARRCRDEAIAACRAGAPFSVI-------------------GNTISHITHQNGFQVCPHFVGHGIGSY 139
Cdd:PRK10879  278 GKFTPAQREIYDIVLESLETSLRLYRPGTSIREVtgevvrimvsglvklgilkGDVDQLIAENAHRPFFMHGLSHWLGLD 357

                         170       180
                  ....*....|....*....|....*...
gi 2217326789 140 FHghpEIWHHANDSDLPMEEGMAFTIEP 167
Cdd:PRK10879  358 VH---DVGVYGQDRSRILEPGMVLTVEP 382
PTZ00053 PTZ00053
methionine aminopeptidase 2; Provisional
 28-166 3.33e-04

methionine aminopeptidase 2; Provisional


Pssm-ID: 240246 [Multi-domain]  Cd Length: 470  Bit Score: 40.85  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217326789  28 GFPKSVctSVNNVLCHGIP---DSRPLQDGDIINIDVTVYYNGYHGDTSET--FlvgnvDECGKKLVEVARRCRDEAIAA 102
Cdd:PTZ00053  210 AFPTGC--SLNHCAAHYTPntgDKTVLTYDDVCKLDFGTHVNGRIIDCAFTvaF-----NPKYDPLLQATKDATNTGIKE 282

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217326789 103 CRAGAPFSVIGNTI-----SHITHQNGfQVCP-----HFVGHGIGSY-FHGH---PEIwhHANDSDLpMEEGMAFTIE 166
Cdd:PTZ00053  283 AGIDVRLSDIGAAIqevieSYEVEIKG-KTYPiksirNLNGHSIGPYiIHGGksvPIV--KGGENTR-MEEGELFAIE 356
 
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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