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Conserved domains on  [gi|1906445069|ref|WP_189211962|]
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type I methionyl aminopeptidase [Actinokineospora fastidiosa]

Protein Classification

type I methionyl aminopeptidase( domain architecture ID 10000257)

type I methionyl aminopeptidase (M24A family metallopeptidase) catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides

CATH:  3.90.230.10
EC:  3.4.11.18
Gene Ontology:  GO:0070006|GO:0046914|GO:0006508|GO:0004239
MEROPS:  M24
PubMed:  7674922

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
33-254 1.41e-111

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 320.80  E-value: 1.41e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  33 VGTTLLELDDVARGVLAAHGAGSSFLGYRPqfaptpFPAVLCTSLNDAIVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDA 112
Cdd:COG0024    32 PGVTTLELDRIAEEFIRDHGAIPAFLGYYG------FPKSICTSVNEVVVHGIPSDRVLKDGDIVNIDVGAILDGYHGDS 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 113 AMSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAGYGIPPDFGGHGIGRAMHESPSVPNEGDP 192
Cdd:COG0024   106 ARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSVVREFVGHGIGREMHEEPQVPNYGRP 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906445069 193 GRGMRLREGLVLAIEPMVHKGGRDpYYVDDDGWTLRTRDGSRAAHSEHTVAITADGPVILTA 254
Cdd:COG0024   186 GRGPRLKPGMVLAIEPMINAGTPE-VKVLDDGWTVVTKDGSLSAQFEHTVAVTEDGPEILTL 246
 
Name Accession Description Interval E-value
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
33-254 1.41e-111

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 320.80  E-value: 1.41e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  33 VGTTLLELDDVARGVLAAHGAGSSFLGYRPqfaptpFPAVLCTSLNDAIVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDA 112
Cdd:COG0024    32 PGVTTLELDRIAEEFIRDHGAIPAFLGYYG------FPKSICTSVNEVVVHGIPSDRVLKDGDIVNIDVGAILDGYHGDS 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 113 AMSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAGYGIPPDFGGHGIGRAMHESPSVPNEGDP 192
Cdd:COG0024   106 ARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSVVREFVGHGIGREMHEEPQVPNYGRP 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906445069 193 GRGMRLREGLVLAIEPMVHKGGRDpYYVDDDGWTLRTRDGSRAAHSEHTVAITADGPVILTA 254
Cdd:COG0024   186 GRGPRLKPGMVLAIEPMINAGTPE-VKVLDDGWTVVTKDGSLSAQFEHTVAVTEDGPEILTL 246
MetAP1 cd01086
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 33-253 3.43e-99

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: 289.01  E-value: 3.43e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  33 VGTTLLELDDVARGVLAAHGAGSSFLGYRPqfaptpFPAVLCTSLNDAIVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDA 112
Cdd:cd01086    24 PGVTTKELDQIAHEFIEEHGAYPAPLGYYG------FPKSICTSVNEVVCHGIPDDRVLKDGDIVNIDVGVELDGYHGDS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 113 AMSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAGYGIPPDFGGHGIGRAMHESPSVPNEGDP 192
Cdd:cd01086    98 ARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGGHGIGRKFHEEPQIPNYGRP 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906445069 193 GRGMRLREGLVLAIEPMVHKGGRDpYYVDDDGWTLRTRDGSRAAHSEHTVAITADGPVILT 253
Cdd:cd01086   178 GTGPKLKPGMVFTIEPMINLGTYE-VVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILT 237
PRK05716 PRK05716
methionine aminopeptidase; Validated
 34-253 2.87e-94

methionine aminopeptidase; Validated


Pssm-ID: 235576 [Multi-domain]  Cd Length: 252  Bit Score: 277.02  E-value: 2.87e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  34 GTTLLELDDVARGVLAAHGAGSSFLGYRPqfaptpFPAVLCTSLNDAIVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDAA 113
Cdd:PRK05716   35 GVTTKELDRIAEEYIRDQGAIPAPLGYHG------FPKSICTSVNEVVCHGIPSDKVLKEGDIVNIDVTVIKDGYHGDTS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 114 MSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAGYGIPPDFGGHGIGRAMHESPSVPNEGDPG 193
Cdd:PRK05716  109 RTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGFSVVREYCGHGIGRKFHEEPQIPHYGAPG 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 194 RGMRLREGLVLAIEPMVHKGGRDPyYVDDDGWTLRTRDGSRAAHSEHTVAITADGPVILT 253
Cdd:PRK05716  189 DGPVLKEGMVFTIEPMINAGKREV-KTLKDGWTVVTKDGSLSAQYEHTVAVTEDGPEILT 247
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
 34-254 4.76e-80

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: 241.10  E-value: 4.76e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  34 GTTLLELDDVARGVLAAHGAGSSFLGYRPqfaptpFPAVLCTSLNDAIVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDAA 113
Cdd:TIGR00500  33 GVSTKELDRIAKDFIEKHGAKPAFLGYYG------FPGSVCISVNEVVIHGIPDKKVLKDGDIVNIDVGVIYDGYHGDTA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 114 MSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAGYGIPPDFGGHGIGRAMHESPSVPNEGDPG 193
Cdd:TIGR00500 107 KTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSVVREYCGHGIGRKFHEEPQIPNYGKKF 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906445069 194 RGMRLREGLVLAIEPMVHKGGRDPyYVDDDGWTLRTRDGSRAAHSEHTVAITADGPVILTA 254
Cdd:TIGR00500 187 TNVRLKEGMVFTIEPMVNTGTEEI-TTAADGWTVKTKDGSLSAQFEHTIVITDNGPEILTE 246
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 34-246 1.58e-35

Metallopeptidase family M24; This family contains metallopeptidases. It also contains non-peptidase homologs such as the N terminal domain of Spt16 which is a histone H3-H4 binding module.


Pssm-ID: 459852 [Multi-domain]  Cd Length: 208  Bit Score: 125.82  E-value: 1.58e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  34 GTTLLELDDVARGVLAAHGAGSSFlgyrpqfaptPFPAVLCTSLNDAIVHGIPDRTRLSDGDLLSIDFGAHVD-GWHGDA 112
Cdd:pfam00557  24 GVTERELAAELEAARLRRGGARGP----------AFPPIVASGPNAAIPHYIPNDRVLKPGDLVLIDVGAEYDgGYCSDI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 113 AMSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAGYGIP-PDFGGHGIGRAMHESPSVPNegd 191
Cdd:pfam00557  94 TRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGEYfPHGLGHGIGLEVHEGPYISR--- 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1906445069 192 PGRGMRLREGLVLAIEPMVhkggrdpYYVDDDGwtlrtrdgsrAAHSEHTVAITA 246
Cdd:pfam00557 171 GGDDRVLEPGMVFTIEPGI-------YFIPGWG----------GVRIEDTVLVTE 208
 
Name Accession Description Interval E-value
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
33-254 1.41e-111

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 320.80  E-value: 1.41e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  33 VGTTLLELDDVARGVLAAHGAGSSFLGYRPqfaptpFPAVLCTSLNDAIVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDA 112
Cdd:COG0024    32 PGVTTLELDRIAEEFIRDHGAIPAFLGYYG------FPKSICTSVNEVVVHGIPSDRVLKDGDIVNIDVGAILDGYHGDS 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 113 AMSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAGYGIPPDFGGHGIGRAMHESPSVPNEGDP 192
Cdd:COG0024   106 ARTFVVGEVSPEARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSVVREFVGHGIGREMHEEPQVPNYGRP 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906445069 193 GRGMRLREGLVLAIEPMVHKGGRDpYYVDDDGWTLRTRDGSRAAHSEHTVAITADGPVILTA 254
Cdd:COG0024   186 GRGPRLKPGMVLAIEPMINAGTPE-VKVLDDGWTVVTKDGSLSAQFEHTVAVTEDGPEILTL 246
MetAP1 cd01086
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 33-253 3.43e-99

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: 289.01  E-value: 3.43e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  33 VGTTLLELDDVARGVLAAHGAGSSFLGYRPqfaptpFPAVLCTSLNDAIVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDA 112
Cdd:cd01086    24 PGVTTKELDQIAHEFIEEHGAYPAPLGYYG------FPKSICTSVNEVVCHGIPDDRVLKDGDIVNIDVGVELDGYHGDS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 113 AMSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAGYGIPPDFGGHGIGRAMHESPSVPNEGDP 192
Cdd:cd01086    98 ARTFIVGEVSEEAKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREFGGHGIGRKFHEEPQIPNYGRP 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906445069 193 GRGMRLREGLVLAIEPMVHKGGRDpYYVDDDGWTLRTRDGSRAAHSEHTVAITADGPVILT 253
Cdd:cd01086   178 GTGPKLKPGMVFTIEPMINLGTYE-VVTLPDGWTVVTKDGSLSAQFEHTVLITEDGPEILT 237
PRK05716 PRK05716
methionine aminopeptidase; Validated
 34-253 2.87e-94

methionine aminopeptidase; Validated


Pssm-ID: 235576 [Multi-domain]  Cd Length: 252  Bit Score: 277.02  E-value: 2.87e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  34 GTTLLELDDVARGVLAAHGAGSSFLGYRPqfaptpFPAVLCTSLNDAIVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDAA 113
Cdd:PRK05716   35 GVTTKELDRIAEEYIRDQGAIPAPLGYHG------FPKSICTSVNEVVCHGIPSDKVLKEGDIVNIDVTVIKDGYHGDTS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 114 MSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAGYGIPPDFGGHGIGRAMHESPSVPNEGDPG 193
Cdd:PRK05716  109 RTFGVGEISPEDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGFSVVREYCGHGIGRKFHEEPQIPHYGAPG 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 194 RGMRLREGLVLAIEPMVHKGGRDPyYVDDDGWTLRTRDGSRAAHSEHTVAITADGPVILT 253
Cdd:PRK05716  189 DGPVLKEGMVFTIEPMINAGKREV-KTLKDGWTVVTKDGSLSAQYEHTVAVTEDGPEILT 247
met_pdase_I TIGR00500
methionine aminopeptidase, type I; Methionine aminopeptidase is a cobalt-binding enzyme. ...
 34-254 4.76e-80

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: 241.10  E-value: 4.76e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  34 GTTLLELDDVARGVLAAHGAGSSFLGYRPqfaptpFPAVLCTSLNDAIVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDAA 113
Cdd:TIGR00500  33 GVSTKELDRIAKDFIEKHGAKPAFLGYYG------FPGSVCISVNEVVIHGIPDKKVLKDGDIVNIDVGVIYDGYHGDTA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 114 MSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAGYGIPPDFGGHGIGRAMHESPSVPNEGDPG 193
Cdd:TIGR00500 107 KTFLVGKISPEAEKLLECTEESLYKAIEEAKPGNRIGEIGAAIQKYAEAKGFSVVREYCGHGIGRKFHEEPQIPNYGKKF 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906445069 194 RGMRLREGLVLAIEPMVHKGGRDPyYVDDDGWTLRTRDGSRAAHSEHTVAITADGPVILTA 254
Cdd:TIGR00500 187 TNVRLKEGMVFTIEPMVNTGTEEI-TTAADGWTVKTKDGSLSAQFEHTIVITDNGPEILTE 246
PRK12896 PRK12896
methionine aminopeptidase; Reviewed
 34-253 4.20e-73

methionine aminopeptidase; Reviewed


Pssm-ID: 237252 [Multi-domain]  Cd Length: 255  Bit Score: 223.56  E-value: 4.20e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  34 GTTLLELDDVARGVLAAHGAGSSFLGYRPqfaptpFPAVLCTSLNDAIVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDAA 113
Cdd:PRK12896   40 GMTTKELDRIAEKRLEEHGAIPSPEGYYG------FPGSTCISVNEEVAHGIPGPRVIKDGDLVNIDVSAYLDGYHGDTG 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 114 MSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAGYGIPPDFGGHGIGRAMHESPSVPNE-GDP 192
Cdd:PRK12896  114 ITFAVGPVSEEAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAIEDFAKKNGYSVVRDLTGHGVGRSLHEEPSVILTyTDP 193

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906445069 193 GRGMRLREGLVLAIEPMVHKGGRDpYYVDDDGWTLRTRDGSRAAHSEHTVAITADGPVILT 253
Cdd:PRK12896  194 LPNRLLRPGMTLAVEPFLNLGAKD-AETLDDGWTVVTPDKSLSAQFEHTVVVTRDGPEILT 253
PRK12897 PRK12897
type I methionyl aminopeptidase;
1-253 7.11e-49

type I methionyl aminopeptidase;


Pssm-ID: 171806  Cd Length: 248  Bit Score: 161.36  E-value: 7.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069   1 MIELKTPAEISAMRAAGAVVAAALAAVRAAATVGTTLLELDDVARGVLAAHGAGSSFLGYrpqfapTPFPAVLCTSLNDA 80
Cdd:PRK12897    1 MITIKTKNEIDLMHESGKLLASCHREIAKIMKPGITTKEINTFVEAYLEKHGATSEQKGY------NGYPYAICASVNDE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  81 IVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDAAMSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVA 160
Cdd:PRK12897   75 MCHAFPADVPLTEGDIVTIDMVVNLNGGLSDSAWTYRVGKVSDEAEKLLLVAENALYKGIDQAVIGNRVGDIGYAIESYV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 161 REAGYGIPPDFGGHGIGRAMHESPSVPNEGDPGRGMRLREGLVLAIEPMVHKGGRDPyYVDDDGWTLRTRDGSRAAHSEH 240
Cdd:PRK12897  155 ANEGFSVARDFTGHGIGKEIHEEPAIFHFGKQGQGPELQEGMVITIEPIVNVGMRYS-KVDLNGWTARTMDGKLSAQYEH 233

                         250
                  ....*....|...
gi 1906445069 241 TVAITADGPVILT 253
Cdd:PRK12897  234 TIAITKDGPIILT 246
PRK12318 PRK12318
methionyl aminopeptidase;
33-253 1.16e-41

methionyl aminopeptidase;


Pssm-ID: 183434 [Multi-domain]  Cd Length: 291  Bit Score: 144.19  E-value: 1.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  33 VGTTLLELDDVARGVLAAHGAGSSFLGYrpqfAPTPFPAVLCTSLNDAIVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDA 112
Cdd:PRK12318   72 EGVTTNELDELSRELHKEYNAIPAPLNY----GSPPFPKTICTSLNEVICHGIPNDIPLKNGDIMNIDVSCIVDGYYGDC 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 113 AMSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAGYGIPPDFGGHGIGRAMHESPSVPNEGDP 192
Cdd:PRK12318  148 SRMVMIGEVSEIKKKVCQASLECLNAAIAILKPGIPLYEIGEVIENCADKYGFSVVDQFVGHGVGIKFHENPYVPHHRNS 227

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906445069 193 GRgMRLREGLVLAIEPMVHKGGRDPYYVDDDGWTLRTRDGSRAAHSEHTVAITADGPVILT 253
Cdd:PRK12318  228 SK-IPLAPGMIFTIEPMINVGKKEGVIDPINHWEARTCDNQPSAQWEHTILITETGYEILT 287
PRK07281 PRK07281
methionyl aminopeptidase;
68-254 1.54e-40

methionyl aminopeptidase;


Pssm-ID: 180918  Cd Length: 286  Bit Score: 141.14  E-value: 1.54e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  68 PFPAVLCTSLNDAIVHGIPDRTRLSDGDLLSID--FGAHVD-------------------------GWHGDAAMSFVVGT 120
Cdd:PRK07281   66 DYPYATCCGLNDEVAHAFPRHYILKEGDLLKVDmvLSEPLDksivdvsklnfdnveqmkkytesyrGGLADSCWAYAVGT 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 121 PDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAGYGIPPDFGGHGIGRAMHESPSVPNEGDPGRGMRLRE 200
Cdd:PRK07281  146 PSDEVKNLMDVTKEAMYRGIEQAVVGNRIGDIGAAIQEYAESRGYGVVRDLVGHGVGPTMHEEPMVPNYGTAGRGLRLRE 225

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1906445069 201 GLVLAIEPMVHKGgrdPYYVDDD---GWTLRTRDGSRAAHSEHTVAITADGPVILTA 254
Cdd:PRK07281  226 GMVLTIEPMINTG---TWEIDTDmktGWAHKTLDGGLSCQYEHQFVITKDGPVILTS 279
PLN03158 PLN03158
methionine aminopeptidase; Provisional
 34-254 2.40e-36

methionine aminopeptidase; Provisional


Pssm-ID: 215607 [Multi-domain]  Cd Length: 396  Bit Score: 132.65  E-value: 2.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  34 GTTLLELDDVARGVLAAHGAGSSFLGYRPqfaptpFPAVLCTSLNDAIVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDAA 113
Cdd:PLN03158  167 GVTTDEIDRVVHEATIAAGGYPSPLNYHF------FPKSCCTSVNEVICHGIPDARKLEDGDIVNVDVTVYYKGCHGDLN 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 114 MSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAGYGIPPDFGGHGIGRAMHESPSVPNEGDPG 193
Cdd:PLN03158  241 ETFFVGNVDEASRQLVKCTYECLEKAIAIVKPGVRYREVGEVINRHATMSGLSVVKSYCGHGIGELFHCAPNIPHYARNK 320

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1906445069 194 RGMRLREGLVLAIEPMVHKGG-RDPYYvdDDGWTLRTRDGSRAAHSEHTVAITADGPVILTA 254
Cdd:PLN03158  321 AVGVMKAGQVFTIEPMINAGVwRDRMW--PDGWTAVTADGKRSAQFEHTLLVTETGVEVLTA 380
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 34-246 1.58e-35

Metallopeptidase family M24; This family contains metallopeptidases. It also contains non-peptidase homologs such as the N terminal domain of Spt16 which is a histone H3-H4 binding module.


Pssm-ID: 459852 [Multi-domain]  Cd Length: 208  Bit Score: 125.82  E-value: 1.58e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  34 GTTLLELDDVARGVLAAHGAGSSFlgyrpqfaptPFPAVLCTSLNDAIVHGIPDRTRLSDGDLLSIDFGAHVD-GWHGDA 112
Cdd:pfam00557  24 GVTERELAAELEAARLRRGGARGP----------AFPPIVASGPNAAIPHYIPNDRVLKPGDLVLIDVGAEYDgGYCSDI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 113 AMSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAGYGIP-PDFGGHGIGRAMHESPSVPNegd 191
Cdd:pfam00557  94 TRTFVVGKPSPEQRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGEYfPHGLGHGIGLEVHEGPYISR--- 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1906445069 192 PGRGMRLREGLVLAIEPMVhkggrdpYYVDDDGwtlrtrdgsrAAHSEHTVAITA 246
Cdd:pfam00557 171 GGDDRVLEPGMVFTIEPGI-------YFIPGWG----------GVRIEDTVLVTE 208
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
80-254 7.42e-24

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


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 97.20  E-value: 7.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  80 AIVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDAAMSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVV 159
Cdd:COG0006   138 AIPHYTPTDRPLKPGDLVLIDAGAEYDGYTSDITRTVAVGEPSDEQREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDV 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 160 AREAGYGipPDFG---GHGIGRAMHESPSVpnegDPGRGMRLREGLVLAIEPMvhkggrdpYYVDDDGwtlrtrdGSRaa 236
Cdd:COG0006   218 LAEAGYG--EYFPhgtGHGVGLDVHEGPQI----SPGNDRPLEPGMVFTIEPG--------IYIPGIG-------GVR-- 274

                         170
                  ....*....|....*...
gi 1906445069 237 hSEHTVAITADGPVILTA 254
Cdd:COG0006   275 -IEDTVLVTEDGAEVLTR 291
APP_MetAP cd01066
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
 65-249 5.74e-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: 90.21  E-value: 5.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  65 APTPFPAVLCTSLNDAIVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDAAMSFVVGTPDPTDTALVEASERALAAGIAAAV 144
Cdd:cd01066    44 GYPAGPTIVGSGARTALPHYRPDDRRLQEGDLVLVDLGGVYDGYHADLTRTFVIGEPSDEQRELYEAVREAQEAALAALR 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 145 PGNRMGDIAHAIGVVAREAGYGIP-PDFGGHGIGRAMHESPSVPnegdPGRGMRLREGLVLAIEPMVhkggrdpYYVDDD 223
Cdd:cd01066   124 PGVTAEEVDAAAREVLEEHGLGPNfGHRTGHGIGLEIHEPPVLK----AGDDTVLEPGMVFAVEPGL-------YLPGGG 192

                         170       180
                  ....*....|....*....|....*.
gi 1906445069 224 GWTLrtrdgsraahsEHTVAITADGP 249
Cdd:cd01066   193 GVRI-----------EDTVLVTEDGP 207
MetAP2 cd01088
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 69-226 4.15e-20

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: 86.92  E-value: 4.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  69 FPAVLctSLNDAIVHGIP---DRTRLSDGDLLSIDFGAHVDGWHGDAAmsFVVgTPDPTDTALVEASERALAAGIAAAVP 145
Cdd:cd01088    48 FPVNL--SINECAAHYTPnagDDTVLKEGDVVKLDFGAHVDGYIADSA--FTV-DFDPKYDDLLEAAKEALNAAIKEAGP 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 146 GNRMGDIAHAIGVVAREagYGIPP--DFGGHGIGR-AMHESPSVPNEGDPGrGMRLREGLVLAIEPMVHKGGRdpyYVDD 222
Cdd:cd01088   123 DVRLGEIGEAIEEVIES--YGFKPirNLTGHSIERyRLHAGKSIPNVKGGE-GTRLEEGDVYAIEPFATTGKG---YVHD 196


                  ....
gi 1906445069 223 DGWT 226
Cdd:cd01088   197 GPEC 200
APP-like cd01092
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
 69-224 3.08e-17

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: 77.55  E-value: 3.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  69 FPAVLCTSLNDAIVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDAAMSFVVGTPDPTDTALVEASERALAAGIAAAVPGNR 148
Cdd:cd01092    49 FDTIVASGPNSALPHGVPSDRKIEEGDLVLIDFGAIYDGYCSDITRTVAVGEPSDELKEIYEIVLEAQQAAIKAVKPGVT 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 149 MGDIAHAIGVVAREAGYGipPDFG---GHGIGRAMHESPSVPnegdPGRGMRLREGLVLAIEPMVH---KGG-R--DPYY 219
Cdd:cd01092   129 AKEVDKAARDVIEEAGYG--EYFIhrtGHGVGLEVHEAPYIS----PGSDDVLEEGMVFTIEPGIYipgKGGvRieDDVL 202


                  ....*
gi 1906445069 220 VDDDG 224
Cdd:cd01092   203 VTEDG 207
met_pdase_II TIGR00501
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ...
 58-213 2.96e-15

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: 73.67  E-value: 2.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  58 LGYRPQFaptpfPAVLctSLNDAIVHGIP---DRTRLSDGDLLSIDFGAHVDGWHGDAAMSFVVGtpdPTDTALVEASER 134
Cdd:TIGR00501  46 LGAEPAF-----PCNI--SINECAAHFTPkagDKTVFKDGDVVKLDLGAHVDGYIADTAITVDLG---DQYDNLVKAAKD 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 135 ALAAGIAAAVPGNRMGDIAHAIGVVAREAGYGIPPDFGGHGIGR-AMHESPSVPNEGDpGRGMRLREGLVLAIEPMVHKG 213
Cdd:TIGR00501 116 ALYTAIKEIRAGVRVGEIGKAIQEVIESYGVKPISNLTGHSMAPyRLHGGKSIPNVKE-RDTTKLEEGDVVAIEPFATDG 194
PA2G4-like cd01089
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ...
 69-254 1.23e-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: 53.87  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  69 FPAvlCTSLNDAIVHGIP----DRTRLSDGDLLSIDFGAHVDGWHGDAAMSFVVGTPDPTDTA-----LVEASERALAAG 139
Cdd:cd01089    59 FPT--CISVNNCVCHFSPlksdATYTLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAETPVTgkkadVIAAAHYALEAA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 140 IAAAVPGNRMGDIAHAIGVVAreagygipPDFGGHGI-GRAMHESPsvpnegdpgRGMRLREGLVLAIEpMVHKGGRDPY 218
Cdd:cd01089   137 LRLLRPGNQNSDITEAIQKVI--------VDYGCTPVeGVLSHQLK---------RVVSSGEGKAKLVE-CVKHGLLFPY 198

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1906445069 219 YVdddgwtLRTRDGSRAAHSEHTVAITADGPVILTA 254
Cdd:cd01089   199 PV------LYEKEGEVVAQFKLTVLLTPNGVTVLTG 228
PRK15173 PRK15173
peptidase; Provisional
 85-219 3.66e-08

peptidase; Provisional


Pssm-ID: 185095 [Multi-domain]  Cd Length: 323  Bit Score: 53.18  E-value: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  85 IPDRTRLSDGDLLSIDFGAHVDGWHGDAAMSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAG 164
Cdd:PRK15173  164 IPSNTKACSGDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSG 243

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906445069 165 YgipPDFG------GHGIGRAMHESPSVPNEGDPGrgmrLREGLVLAIEpmvhkggrDPYY 219
Cdd:PRK15173  244 L---PNYNrghlghGNGVFLGLEESPFVSTHATES----FTSGMVLSLE--------TPYY 289
PRK14575 PRK14575
putative peptidase; Provisional
 85-219 5.89e-08

putative peptidase; Provisional


Pssm-ID: 173039 [Multi-domain]  Cd Length: 406  Bit Score: 52.79  E-value: 5.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  85 IPDRTRLSDGDLLSIDFGAHVDGWHGDAAMSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAG 164
Cdd:PRK14575  247 IPSNTKACSGDLIKFDCGVDVDGYGADIARTFVVGEPPEITRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSG 326

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906445069 165 YgipPDFG------GHGIGRAMHESPSVPNEGDPGrgmrLREGLVLAIEpmvhkggrDPYY 219
Cdd:PRK14575  327 L---PNYNrghlghGNGVFLGLEESPFVSTHATES----FTSGMVLSLE--------TPYY 372
PRK09795 PRK09795
aminopeptidase; Provisional
 67-222 2.30e-06

aminopeptidase; Provisional


Pssm-ID: 182080 [Multi-domain]  Cd Length: 361  Bit Score: 48.01  E-value: 2.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  67 TPFPAVLCTSLNDAIVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDAAMSFVV-GTPDPTDT----ALVEASERALAAGIA 141
Cdd:PRK09795  179 ASFDTIVASGWRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVnGEGVSAEShplfNVYQIVLQAQLAAIS 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 142 AAVPGNRMGDIAHAIGVVAREAGYGipPDFG---GHGIGRAMHESPSVpnegDPGRGMRLREGLVLAIEPMVHKGGRDPY 218
Cdd:PRK09795  259 AIRPGVRCQQVDDAARRVITEAGYG--DYFGhntGHAIGIEVHEDPRF----SPRDTTTLQPGMLLTVEPGIYLPGQGGV 332


                  ....
gi 1906445069 219 YVDD 222
Cdd:PRK09795  333 RIED 336
PTZ00053 PTZ00053
methionine aminopeptidase 2; Provisional
 76-207 7.31e-06

methionine aminopeptidase 2; Provisional


Pssm-ID: 240246 [Multi-domain]  Cd Length: 470  Bit Score: 46.63  E-value: 7.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  76 SLNDAIVHGIP---DRTRLSDGDLLSIDFGAHVDGWHGDAAmsFVV-----------GTPDPTDTALVEASeralaagia 141
Cdd:PTZ00053  216 SLNHCAAHYTPntgDKTVLTYDDVCKLDFGTHVNGRIIDCA--FTVafnpkydpllqATKDATNTGIKEAG--------- 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 142 aavPGNRMGDIAHAIgvvaREA-----------GYGIPP--DFGGHGIGR-AMHESPSVPNEGdPGRGMRLREGLVLAIE 207
Cdd:PTZ00053  285 ---IDVRLSDIGAAI----QEViesyeveikgkTYPIKSirNLNGHSIGPyIIHGGKSVPIVK-GGENTRMEEGELFAIE 356
crvDNA_42K TIGR00495
42K curved DNA binding protein; Proteins identified by this model have been identified in a ...
 69-169 1.58e-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: 45.26  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  69 FPAvlCTSLNDAIVH-----GIPDRTrLSDGDLLSIDFGAHVDGWHGDAAMSFVVGTPDPTDTA-----LVEASERALAA 138
Cdd:TIGR00495  78 FPT--CISVNNCVGHfsplkSDQDYI-LKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEEPVTgrkadVIAAAHLAAEA 154

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1906445069 139 GIAAAVPGNRMGDIAHAIGVVAreAGYGIPP 169
Cdd:TIGR00495 155 ALRLVKPGNTNTQVTEAINKVA--HSYGCTP 183
PRK14576 PRK14576
putative endopeptidase; Provisional
 85-219 2.18e-04

putative endopeptidase; Provisional


Pssm-ID: 173040 [Multi-domain]  Cd Length: 405  Bit Score: 41.92  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  85 IPDRTRLSDGDLLSIDFGAHVDGWHGDAAMSFVVGTPDPTDTALVEASERALAAGIAAAVPGNRMGDIAHAIGVVAREAg 164
Cdd:PRK14576  246 IADTTPAKVGDLIKFDCGIDVAGYGADLARTFVLGEPDKLTQQIYDTIRTGHEHMLSMVAPGVKLKAVFDSTMAVIKTS- 324

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 165 yGIPPDFGGH-----GIGRAMHESPSVPNEGDPgrgmRLREGLVLAIEpmvhkggrDPYY 219
Cdd:PRK14576  325 -GLPHYNRGHlghgdGVFLGLEEVPFVSTQATE----TFCPGMVLSLE--------TPYY 371
Prolidase cd01087
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ...
 70-254 6.37e-04

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: 39.86  E-value: 6.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069  70 PAVLCTSlNDAIVHGIPDRTRLSDGDLLSIDFGAHVDGWHGDAAMSFVV-GTPDPTDTALVEASERALAAGIAAAVPGNR 148
Cdd:cd01087    50 YIVAAGS-NAAILHYVHNDQPLKDGDLVLIDAGAEYGGYASDITRTFPVnGKFTDEQRELYEAVLAAQKAAIAACKPGVS 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906445069 149 MGDI---AHAI----------------GVVAREAGYGIPPDFGGHGIGRAMHESPSVPNEGDPGRgmRLREGLVLAIEPM 209
Cdd:cd01087   129 YEDIhllAHRVlaeglkelgilkgdvdEIVESGAYAKFFPHGLGHYLGLDVHDVGGYLRYLRRAR--PLEPGMVITIEPG 206

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1906445069 210 VhkggrdpYYVDDDGWTLRTRD--GSRAahsEHTVAITADGPVILTA 254
Cdd:cd01087   207 I-------YFIPDLLDVPEYFRggGIRI---EDDVLVTEDGPENLTR 243
 
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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