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Conserved domains on  [gi|1277948730|gb|PIV46452|]
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type II methionyl aminopeptidase [Candidatus Huberarchaeum crystalense]

Protein Classification

M24 family metallopeptidase( domain architecture ID 320)

M24 family metallopeptidase cleaves amido-, imido-, or amidino-containing bonds, exhibiting a fairly narrow substrate specificity compared to other metallo-aminopeptidases, possibly playing roles in regulation of biological processes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
APP_MetAP super family cl00279
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
 6-297 2.87e-101

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.


The actual alignment was detected with superfamily member cd01088:

Pssm-ID: 469704 [Multi-domain]  Cd Length: 291  Bit Score: 298.39  E-value: 2.87e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   6 IEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSKTGergGLAFPVSVCVNEIAAHKTPSIQNPYLFKKGDVV 85
Cdd:cd01088     1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELGA---GPAFPVNLSINECAAHYTPNAGDDTVLKEGDVV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  86 KIDLGVHINGYIADTATTFDFG-DNKNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGFMPITNLAGHQIKPYN 164
Cdd:cd01088    78 KLDFGAHVDGYIADSAFTVDFDpKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIESYGFKPIRNLTGHSIERYR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730 165 IHAGVSVPNCETNNQAKFQKGEAYAIEPFATTGCGLVVSSAGGGIMkVLKPEAKPRLETSRTILKYVIDNFGLFEFSKRn 244
Cdd:cd01088   158 LHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIY-MLNRDKPLRLPRARKLLDVIYENFGTLPFARR- 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1277948730 245 ILKKY--PNAQLFIESLKKDGVLYEYPGLKEKTNAVVSQFEDTILVLGDGKIIIT 297
Cdd:cd01088   236 WLDRLgeTKLLMALKNLCKAGIVYPYPVLKEISGGYVAQFEHTIIVREDGKEVTT 290
 
Name Accession Description Interval E-value
MetAP2 cd01088
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 6-297 2.87e-101

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: 298.39  E-value: 2.87e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   6 IEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSKTGergGLAFPVSVCVNEIAAHKTPSIQNPYLFKKGDVV 85
Cdd:cd01088     1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELGA---GPAFPVNLSINECAAHYTPNAGDDTVLKEGDVV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  86 KIDLGVHINGYIADTATTFDFG-DNKNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGFMPITNLAGHQIKPYN 164
Cdd:cd01088    78 KLDFGAHVDGYIADSAFTVDFDpKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIESYGFKPIRNLTGHSIERYR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730 165 IHAGVSVPNCETNNQAKFQKGEAYAIEPFATTGCGLVVSSAGGGIMkVLKPEAKPRLETSRTILKYVIDNFGLFEFSKRn 244
Cdd:cd01088   158 LHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIY-MLNRDKPLRLPRARKLLDVIYENFGTLPFARR- 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1277948730 245 ILKKY--PNAQLFIESLKKDGVLYEYPGLKEKTNAVVSQFEDTILVLGDGKIIIT 297
Cdd:cd01088   236 WLDRLgeTKLLMALKNLCKAGIVYPYPVLKEISGGYVAQFEHTIIVREDGKEVTT 290
met_pdase_II TIGR00501
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ...
 2-297 6.71e-83

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: 251.63  E-value: 6.71e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   2 ESEEIEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSKTGERgglAFPVSVCVNEIAAHKTPSIQNPYLFKK 81
Cdd:TIGR00501   1 DIERAEKWIEAGKIHSKVRREAADRIVPGVKLLEVAEFVENRIRELGAEP---AFPCNISINECAAHFTPKAGDKTVFKD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  82 GDVVKIDLGVHINGYIADTATTFDFGDN-KNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGFMPITNLAGHQI 160
Cdd:TIGR00501  78 GDVVKLDLGAHVDGYIADTAITVDLGDQyDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIESYGVKPISNLTGHSM 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730 161 KPYNIHAGVSVPNCETNNQAKFQKGEAYAIEPFATTGCGLVVSSAGGGIMKVLKPeaKP-RLETSRTILKYVIDNFGLFE 239
Cdd:TIGR00501 158 APYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDGVGYVTDGGEVSIYAFLAE--RPvRLDSARNLLKTIDENYGTLP 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730 240 FSKRnILKKYPNAQLF--IESLKKDGVLYEYPGLKEKTNAVVSQFEDTILVLGDGKIIIT 297
Cdd:TIGR00501 236 FARR-WLDKLGDEKYLfaLNNLIRHGLIYDYPVLNEISGGYVAQWEHTILVEEHGKEVTT 294
PTZ00053 PTZ00053
methionine aminopeptidase 2; Provisional
 4-288 2.35e-52

methionine aminopeptidase 2; Provisional


Pssm-ID: 240246 [Multi-domain]  Cd Length: 470  Bit Score: 177.98  E-value: 2.35e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   4 EEIEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEE---FILSKTGERGGLAFPVSVCVNEIAAHKTPSIQNPYLFK 80
Cdd:PTZ00053  156 EQYQDLRRAAEVHRQVRRYAQSVIKPGVKLIDICERIESksrELIEADGLKCGWAFPTGCSLNHCAAHYTPNTGDKTVLT 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  81 KGDVVKIDLGVHINGYIADTATTFDFGDN-KNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTM-------KGRGF--M 150
Cdd:PTZ00053  236 YDDVCKLDFGTHVNGRIIDCAFTVAFNPKyDPLLQATKDATNTGIKEAGIDVRLSDIGAAIQEVIesyeveiKGKTYpiK 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730 151 PITNLAGHQIKPYNIHAGVSVPNCETNNQAKFQKGEAYAIEPFATTGCGLVVSSAG-GGIMKVLKPEAKP-RLETSRTIL 228
Cdd:PTZ00053  316 SIRNLNGHSIGPYIIHGGKSVPIVKGGENTRMEEGELFAIETFASTGRGYVNEDLEcSHYMKDPGAEFVPlRLPKAKQLL 395

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277948730 229 KYVIDNFGLFEFSKRNILK-KYPNAQLFIESLKKDGVLYEYPGLKEKTNAVVSQFEDTILV 288
Cdd:PTZ00053  396 KHINTNFGTLAFCRRWLDRlGQDRHLLALKQLVDAGIVNPYPPLCDVRGSYTSQMEHTILL 456
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
4-197 1.63e-34

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 125.50  E-value: 1.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   4 EEIEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSK------TGERGglaFPVSVC--VNEIAAHKTPSiqn 75
Cdd:COG0024     7 EEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHgaipafLGYYG---FPKSICtsVNEVVVHGIPS--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  76 PYLFKKGDVVKIDLGVHINGYIADTATTFDFGD----NKNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGFMP 151
Cdd:COG0024    81 DRVLKDGDIVNIDVGAILDGYHGDSARTFVVGEvspeARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1277948730 152 ITNLAGHQIKPyNIHAGVSVPNCETNNQ-AKFQKGEAYAIEPFATTG 197
Cdd:COG0024   161 VREFVGHGIGR-EMHEEPQVPNYGRPGRgPRLKPGMVLAIEPMINAG 206
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 7-192 2.13e-28

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: 108.48  E-value: 2.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   7 EKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSKTGERgGLAFPVSVC--VNEIAAHKTPsiqNPYLFKKGDV 84
Cdd:pfam00557   1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGAR-GPAFPPIVAsgPNAAIPHYIP---NDRVLKPGDL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  85 VKIDLGVHIN-GYIADTATTFDFGDN----KNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGFMP-ITNLAGH 158
Cdd:pfam00557  77 VLIDVGAEYDgGYCSDITRTFVVGKPspeqRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGEyFPHGLGH 156

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1277948730 159 QIKpYNIHAGVSVPNceTNNQAKFQKGEAYAIEP 192
Cdd:pfam00557 157 GIG-LEVHEGPYISR--GGDDRVLEPGMVFTIEP 187
 
Name Accession Description Interval E-value
MetAP2 cd01088
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 6-297 2.87e-101

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: 298.39  E-value: 2.87e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   6 IEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSKTGergGLAFPVSVCVNEIAAHKTPSIQNPYLFKKGDVV 85
Cdd:cd01088     1 LEKYREAGEIHRQVRKYAQSLIKPGMTLLEIAEFVENRIRELGA---GPAFPVNLSINECAAHYTPNAGDDTVLKEGDVV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  86 KIDLGVHINGYIADTATTFDFG-DNKNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGFMPITNLAGHQIKPYN 164
Cdd:cd01088    78 KLDFGAHVDGYIADSAFTVDFDpKYDDLLEAAKEALNAAIKEAGPDVRLGEIGEAIEEVIESYGFKPIRNLTGHSIERYR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730 165 IHAGVSVPNCETNNQAKFQKGEAYAIEPFATTGCGLVVSSAGGGIMkVLKPEAKPRLETSRTILKYVIDNFGLFEFSKRn 244
Cdd:cd01088   158 LHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIY-MLNRDKPLRLPRARKLLDVIYENFGTLPFARR- 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1277948730 245 ILKKY--PNAQLFIESLKKDGVLYEYPGLKEKTNAVVSQFEDTILVLGDGKIIIT 297
Cdd:cd01088   236 WLDRLgeTKLLMALKNLCKAGIVYPYPVLKEISGGYVAQFEHTIIVREDGKEVTT 290
met_pdase_II TIGR00501
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ...
 2-297 6.71e-83

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: 251.63  E-value: 6.71e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   2 ESEEIEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSKTGERgglAFPVSVCVNEIAAHKTPSIQNPYLFKK 81
Cdd:TIGR00501   1 DIERAEKWIEAGKIHSKVRREAADRIVPGVKLLEVAEFVENRIRELGAEP---AFPCNISINECAAHFTPKAGDKTVFKD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  82 GDVVKIDLGVHINGYIADTATTFDFGDN-KNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGFMPITNLAGHQI 160
Cdd:TIGR00501  78 GDVVKLDLGAHVDGYIADTAITVDLGDQyDNLVKAAKDALYTAIKEIRAGVRVGEIGKAIQEVIESYGVKPISNLTGHSM 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730 161 KPYNIHAGVSVPNCETNNQAKFQKGEAYAIEPFATTGCGLVVSSAGGGIMKVLKPeaKP-RLETSRTILKYVIDNFGLFE 239
Cdd:TIGR00501 158 APYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDGVGYVTDGGEVSIYAFLAE--RPvRLDSARNLLKTIDENYGTLP 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730 240 FSKRnILKKYPNAQLF--IESLKKDGVLYEYPGLKEKTNAVVSQFEDTILVLGDGKIIIT 297
Cdd:TIGR00501 236 FARR-WLDKLGDEKYLfaLNNLIRHGLIYDYPVLNEISGGYVAQWEHTILVEEHGKEVTT 294
PTZ00053 PTZ00053
methionine aminopeptidase 2; Provisional
 4-288 2.35e-52

methionine aminopeptidase 2; Provisional


Pssm-ID: 240246 [Multi-domain]  Cd Length: 470  Bit Score: 177.98  E-value: 2.35e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   4 EEIEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEE---FILSKTGERGGLAFPVSVCVNEIAAHKTPSIQNPYLFK 80
Cdd:PTZ00053  156 EQYQDLRRAAEVHRQVRRYAQSVIKPGVKLIDICERIESksrELIEADGLKCGWAFPTGCSLNHCAAHYTPNTGDKTVLT 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  81 KGDVVKIDLGVHINGYIADTATTFDFGDN-KNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTM-------KGRGF--M 150
Cdd:PTZ00053  236 YDDVCKLDFGTHVNGRIIDCAFTVAFNPKyDPLLQATKDATNTGIKEAGIDVRLSDIGAAIQEVIesyeveiKGKTYpiK 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730 151 PITNLAGHQIKPYNIHAGVSVPNCETNNQAKFQKGEAYAIEPFATTGCGLVVSSAG-GGIMKVLKPEAKP-RLETSRTIL 228
Cdd:PTZ00053  316 SIRNLNGHSIGPYIIHGGKSVPIVKGGENTRMEEGELFAIETFASTGRGYVNEDLEcSHYMKDPGAEFVPlRLPKAKQLL 395

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277948730 229 KYVIDNFGLFEFSKRNILK-KYPNAQLFIESLKKDGVLYEYPGLKEKTNAVVSQFEDTILV 288
Cdd:PTZ00053  396 KHINTNFGTLAFCRRWLDRlGQDRHLLALKQLVDAGIVNPYPPLCDVRGSYTSQMEHTILL 456
crvDNA_42K TIGR00495
42K curved DNA binding protein; Proteins identified by this model have been identified in a ...
 2-299 1.54e-37

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: 136.94  E-value: 1.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   2 ESEEIEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSKTGE--------RGGLAFPVSVCVNEIAAHKTPSI 73
Cdd:TIGR00495  16 NPEVVTKYKMAGEIANNVLKSVVEACSPGAKVVDICEKGDAFIMEETAKifkkekemEKGIAFPTCISVNNCVGHFSPLK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  74 QNP-YLFKKGDVVKIDLGVHINGYIADTATTFDFGDNKNLLQTNK---------LALKKAIEAIKKDKPLGDLGKIVEQT 143
Cdd:TIGR00495  96 SDQdYILKEGDVVKIDLGCHIDGFIALVAHTFVVGVAQEEPVTGRkadviaaahLAAEAALRLVKPGNTNTQVTEAINKV 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730 144 MKGRGFMPITNLAGHQIKPYNIHAG---VSVPNCE---TNNQAKFQKGEAYAIEPFATTGCGLVVSSAGGGIM--KVLKP 215
Cdd:TIGR00495 176 AHSYGCTPVEGMLSHQLKQHVIDGEkviISNPSDSqkkDHDTAEFEENEVYAVDILVSTGEGKAKDADQRTTIykRDPSK 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730 216 EAKPRLETSRTILKYVIDNFGLFEFSKRNIlKKYPNAQLFIESLKKDGVLYEYPGLKEKTNAVVSQFEDTILVLGDGKII 295
Cdd:TIGR00495 256 TYGLKMKASRAFFSEIERRFDAMPFTLRNF-EDEKRARMGLVECVKHELLQPYPVLYEKEGEFVAQFKFTVLLMPNGPMR 334


                  ....
gi 1277948730 296 ITTS 299
Cdd:TIGR00495 335 ITSG 338
MetAP1 cd01086
Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 6-197 9.08e-35

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: 126.07  E-value: 9.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   6 IEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSKtGER----GGLAFPVSVC--VNEIAAHKTPSiqnPYLF 79
Cdd:cd01086     1 IEGMREAGRIVAEVLDELAKAIKPGVTTKELDQIAHEFIEEH-GAYpaplGYYGFPKSICtsVNEVVCHGIPD---DRVL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  80 KKGDVVKIDLGVHINGYIADTATTFDFGDN----KNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGFMPITNL 155
Cdd:cd01086    77 KDGDIVNIDVGVELDGYHGDSARTFIVGEVseeaKKLVEVTEEALYKGIEAVKPGNRIGDIGHAIEKYAEKNGYSVVREF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1277948730 156 AGHQIKPYnIHAGVSVPNCETNNQ-AKFQKGEAYAIEPFATTG 197
Cdd:cd01086   157 GGHGIGRK-FHEEPQIPNYGRPGTgPKLKPGMVFTIEPMINLG 198
Map COG0024
Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];
4-197 1.63e-34

Methionine aminopeptidase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439795 [Multi-domain]  Cd Length: 250  Bit Score: 125.50  E-value: 1.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   4 EEIEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSK------TGERGglaFPVSVC--VNEIAAHKTPSiqn 75
Cdd:COG0024     7 EEIEKMREAGRIVAEVLDELAEAVKPGVTTLELDRIAEEFIRDHgaipafLGYYG---FPKSICtsVNEVVVHGIPS--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  76 PYLFKKGDVVKIDLGVHINGYIADTATTFDFGD----NKNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGFMP 151
Cdd:COG0024    81 DRVLKDGDIVNIDVGAILDGYHGDSARTFVVGEvspeARRLVEVTEEALYAGIAAAKPGNRLGDIGHAIQSYAESNGYSV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1277948730 152 ITNLAGHQIKPyNIHAGVSVPNCETNNQ-AKFQKGEAYAIEPFATTG 197
Cdd:COG0024   161 VREFVGHGIGR-EMHEEPQVPNYGRPGRgPRLKPGMVLAIEPMINAG 206
PRK05716 PRK05716
methionine aminopeptidase; Validated
 4-207 1.28e-33

methionine aminopeptidase; Validated


Pssm-ID: 235576 [Multi-domain]  Cd Length: 252  Bit Score: 123.32  E-value: 1.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   4 EEIEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSK------TGERGglaFPVSVC--VNEIAAHKTPSiqn 75
Cdd:PRK05716    9 EEIEKMRVAGRLAAEVLDEIEPHVKPGVTTKELDRIAEEYIRDQgaipapLGYHG---FPKSICtsVNEVVCHGIPS--- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  76 PYLFKKGDVVKIDLGVHINGYIADTATTFDFGD----NKNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGFMP 151
Cdd:PRK05716   83 DKVLKEGDIVNIDVTVIKDGYHGDTSRTFGVGEispeDKRLCEVTKEALYLGIAAVKPGARLGDIGHAIQKYAEAEGFSV 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1277948730 152 ITNLAGHQIKPyNIHAGVSVPNCETNNQA-KFQKGEAYAIEPFATTGCGLVVSSAGG 207
Cdd:PRK05716  163 VREYCGHGIGR-KFHEEPQIPHYGAPGDGpVLKEGMVFTIEPMINAGKREVKTLKDG 218
PRK12896 PRK12896
methionine aminopeptidase; Reviewed
 3-197 6.81e-31

methionine aminopeptidase; Reviewed


Pssm-ID: 237252 [Multi-domain]  Cd Length: 255  Bit Score: 116.09  E-value: 6.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   3 SEEIEKYKEAGNIAKEAKNLAAEIVKIGAS--DLD-VAEK-LEEF--ILSKTGERGglaFPVSVC--VNEIAAHKTPSiq 74
Cdd:PRK12896   13 PRELEKMRKIGRIVATALKEMGKAVEPGMTtkELDrIAEKrLEEHgaIPSPEGYYG---FPGSTCisVNEEVAHGIPG-- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  75 nPYLFKKGDVVKIDLGVHINGYIADTATTFDFGD----NKNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGFM 150
Cdd:PRK12896   88 -PRVIKDGDLVNIDVSAYLDGYHGDTGITFAVGPvseeAEKLCRVAEEALWAGIKQVKAGRPLNDIGRAIEDFAKKNGYS 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1277948730 151 PITNLAGHQIKPyNIHAGVSVPNCETNN--QAKFQKGEAYAIEPFATTG 197
Cdd:PRK12896  167 VVRDLTGHGVGR-SLHEEPSVILTYTDPlpNRLLRPGMTLAVEPFLNLG 214
Peptidase_M24 pfam00557
Metallopeptidase family M24; This family contains metallopeptidases. It also contains ...
 7-192 2.13e-28

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: 108.48  E-value: 2.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   7 EKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSKTGERgGLAFPVSVC--VNEIAAHKTPsiqNPYLFKKGDV 84
Cdd:pfam00557   1 ELMRKAARIAAAALEAALAAIRPGVTERELAAELEAARLRRGGAR-GPAFPPIVAsgPNAAIPHYIP---NDRVLKPGDL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  85 VKIDLGVHIN-GYIADTATTFDFGDN----KNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGFMP-ITNLAGH 158
Cdd:pfam00557  77 VLIDVGAEYDgGYCSDITRTFVVGKPspeqRELYEAVLEAQEAAIAAVKPGVTGGDVDAAAREVLEEAGLGEyFPHGLGH 156

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1277948730 159 QIKpYNIHAGVSVPNceTNNQAKFQKGEAYAIEP 192
Cdd:pfam00557 157 GIG-LEVHEGPYISR--GGDDRVLEPGMVFTIEP 187
PA2G4-like cd01089
Related to aminopepdidase M, this family contains proliferation-associated protein 2G4. Family ...
 6-161 2.11e-23

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: 95.48  E-value: 2.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   6 IEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSKTG---------ERGgLAFPVSVCVNEIAAHKTPSI-QN 75
Cdd:cd01089     1 VTKYKTAGQIANKVLKQVISLCVPGAKVVDLCEKGDKLILEELGkvykkekklEKG-IAFPTCISVNNCVCHFSPLKsDA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  76 PYLFKKGDVVKIDLGVHINGYIADTATTFDFGDNK---------NLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKG 146
Cdd:cd01089    80 TYTLKDGDVVKIDLGCHIDGYIAVVAHTIVVGAEAetpvtgkkaDVIAAAHYALEAALRLLRPGNQNSDITEAIQKVIVD 159

                         170
                  ....*....|....*
gi 1277948730 147 RGFMPITNLAGHQIK 161
Cdd:cd01089   160 YGCTPVEGVLSHQLK 174
APP_MetAP cd01066
A family including aminopeptidase P, aminopeptidase M, and prolidase. Also known as ...
 6-210 7.47e-20

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: 85.58  E-value: 7.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   6 IEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSKTGERGGLAFpVSVCVNEIAAHKTPsiqNPYLFKKGDVV 85
Cdd:cd01066     1 IARLRKAAEIAEAAMAAAAEAIRPGVTEAEVAAAIEQALRAAGGYPAGPTI-VGSGARTALPHYRP---DDRRLQEGDLV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  86 KIDLGVHINGYIADTATTFDFGDN----KNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGFMP-ITNLAGHQI 160
Cdd:cd01066    77 LVDLGGVYDGYHADLTRTFVIGEPsdeqRELYEAVREAQEAALAALRPGVTAEEVDAAAREVLEEHGLGPnFGHRTGHGI 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1277948730 161 kPYNIHAGvsvPNCETNNQAKFQKGEAYAIEPFattgcglVVSSAGGGIM 210
Cdd:cd01066   157 -GLEIHEP---PVLKAGDDTVLEPGMVFAVEPG-------LYLPGGGGVR 195
PepP COG0006
Xaa-Pro aminopeptidase [Amino acid transport and metabolism];
4-192 8.80e-18

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


Pssm-ID: 439777 [Multi-domain]  Cd Length: 299  Bit Score: 81.40  E-value: 8.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   4 EEIEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSKTGErgGLAFPVSVCVNEIAA--HKTPSiqnPYLFKK 81
Cdd:COG0006    77 EEIELMRKAARIADAAHEAALAALRPGVTEREVAAELEAAMRRRGAE--GPSFDTIVASGENAAipHYTPT---DRPLKP 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  82 GDVVKIDLGVHINGYIADTATTFDFGDN----KNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMK----GRGFMPIT 153
Cdd:COG0006   152 GDLVLIDAGAEYDGYTSDITRTVAVGEPsdeqREIYEAVLEAQEAAIAALKPGVTGGEVDAAARDVLAeagyGEYFPHGT 231

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1277948730 154 nlaGHQIkpynihaGVSV---PNCETNNQAKFQKGEAYAIEP 192
Cdd:COG0006   232 ---GHGV-------GLDVhegPQISPGNDRPLEPGMVFTIEP 263
PLN03158 PLN03158
methionine aminopeptidase; Provisional
 4-197 1.07e-15

methionine aminopeptidase; Provisional


Pssm-ID: 215607 [Multi-domain]  Cd Length: 396  Bit Score: 76.80  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   4 EEIEKYKEAGNIAKEAKNLAAEIVKIGASdldvAEKLEEFILSKTGERGGLA-------FPVSVC--VNEIAAHKTPSIQ 74
Cdd:PLN03158  141 EQIQRMRETCRIAREVLDAAARAIKPGVT----TDEIDRVVHEATIAAGGYPsplnyhfFPKSCCtsVNEVICHGIPDAR 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  75 NpylFKKGDVVKIDLGVHINGYIADTATTFDFG----DNKNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGFM 150
Cdd:PLN03158  217 K---LEDGDIVNVDVTVYYKGCHGDLNETFFVGnvdeASRQLVKCTYECLEKAIAIVKPGVRYREVGEVINRHATMSGLS 293

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1277948730 151 PITNLAGHQIKPYnIHAGVSVPNCETNNQAKFQK-GEAYAIEPFATTG 197
Cdd:PLN03158  294 VVKSYCGHGIGEL-FHCAPNIPHYARNKAVGVMKaGQVFTIEPMINAG 340
APP-like cd01092
Similar to Prolidase and Aminopeptidase P. The members of this subfamily presumably catalyse ...
 6-192 3.30e-15

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: 72.93  E-value: 3.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   6 IEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSKTGErgGLAFPVSVCVNEIAA--HKTPSIQnpyLFKKGD 83
Cdd:cd01092     1 IELLRKAARIADKAFEELLEFIKPGMTEREVAAELEYFMRKLGAE--GPSFDTIVASGPNSAlpHGVPSDR---KIEEGD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  84 VVKIDLGVHINGYIADTATTFDFGDN----KNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGFMP-ITNLAGH 158
Cdd:cd01092    76 LVLIDFGAIYDGYCSDITRTVAVGEPsdelKEIYEIVLEAQQAAIKAVKPGVTAKEVDKAARDVIEEAGYGEyFIHRTGH 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1277948730 159 QIkpynihaGVSV---PNCETNNQAKFQKGEAYAIEP 192
Cdd:cd01092   156 GV-------GLEVheaPYISPGSDDVLEEGMVFTIEP 185
PRK12897 PRK12897
type I methionyl aminopeptidase;
5-197 4.77e-12

type I methionyl aminopeptidase;


Pssm-ID: 171806  Cd Length: 248  Bit Score: 64.67  E-value: 4.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   5 EIEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFIL---SKTGERGGLAFPVSVC--VNEIAAHKTPSiqnPYLF 79
Cdd:PRK12897    9 EIDLMHESGKLLASCHREIAKIMKPGITTKEINTFVEAYLEkhgATSEQKGYNGYPYAICasVNDEMCHAFPA---DVPL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  80 KKGDVVKIDLGVHINGYIADTATTFDFGD----NKNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGFMPITNL 155
Cdd:PRK12897   86 TEGDIVTIDMVVNLNGGLSDSAWTYRVGKvsdeAEKLLLVAENALYKGIDQAVIGNRVGDIGYAIESYVANEGFSVARDF 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1277948730 156 AGHQIKPyNIHAGVSVPNCETNNQA-KFQKGEAYAIEPFATTG 197
Cdd:PRK12897  166 TGHGIGK-EIHEEPAIFHFGKQGQGpELQEGMVITIEPIVNVG 207
PRK12318 PRK12318
methionyl aminopeptidase;
4-197 5.36e-11

methionyl aminopeptidase;


Pssm-ID: 183434 [Multi-domain]  Cd Length: 291  Bit Score: 62.14  E-value: 5.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   4 EEIEKYKEAGNIAKEAKNLAAEIVKIGAS--DLD-VAEKL--EEFILSKTGERGGLAFPVSVC--VNEIAAHKTPsiqNP 76
Cdd:PRK12318   47 EQIEKIRKACQVTARILDALCEAAKEGVTtnELDeLSRELhkEYNAIPAPLNYGSPPFPKTICtsLNEVICHGIP---ND 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  77 YLFKKGDVVKIDLGVHINGYIADTATTFDFGD----NKNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGFMPI 152
Cdd:PRK12318  124 IPLKNGDIMNIDVSCIVDGYYGDCSRMVMIGEvseiKKKVCQASLECLNAAIAILKPGIPLYEIGEVIENCADKYGFSVV 203

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1277948730 153 TNLAGHQIKpYNIHAGVSVPNCETNNQAKFQKGEAYAIEPFATTG 197
Cdd:PRK12318  204 DQFVGHGVG-IKFHENPYVPHHRNSSKIPLAPGMIFTIEPMINVG 247
Prolidase cd01087
Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline ...
 6-166 9.35e-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: 9.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   6 IEKYKEAGNIAKEAKNLAAEIVKIGASDLDvaekLEEFILSKTGERGG---LAFPVSVCVNEIAAHKTpsiQNPYLFKKG 82
Cdd:cd01087     1 IELMRKACDISAEAHRAAMKASRPGMSEYE----LEAEFEYEFRSRGArlaYSYIVAAGSNAAILHYV---HNDQPLKDG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  83 DVVKIDLGVHINGYIADTATTFDF-----GDNKNLLQTNKLALKKAIEAIKKDKPLGDL----GKIVEQTMKGRGFM--- 150
Cdd:cd01087    74 DLVLIDAGAEYGGYASDITRTFPVngkftDEQRELYEAVLAAQKAAIAACKPGVSYEDIhllaHRVLAEGLKELGILkgd 153

                         170
                  ....*....|....*.
gi 1277948730 151 PITNLAGHQIKPYNIH 166
Cdd:cd01087   154 VDEIVESGAYAKFFPH 169
PRK15173 PRK15173
peptidase; Provisional
 5-191 1.78e-03

peptidase; Provisional


Pssm-ID: 185095 [Multi-domain]  Cd Length: 323  Bit Score: 39.32  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   5 EIEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSKTGERGGLAFPVSVCVnEIAAHKTPSIQNPYlfkKGDV 84
Cdd:PRK15173  100 EIKRLRKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSKSETHFSRFHLISVGA-DFSPKLIPSNTKAC---SGDL 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  85 VKIDLGVHINGYIADTATTFDFGD----NKNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGfMPITNlAGHQI 160
Cdd:PRK15173  176 IKFDCGVDVDGYGADIARTFVVGEppeiTRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSG-LPNYN-RGHLG 253

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1277948730 161 KPYNIHAGV-SVPNCETNNQAKFQKGEAYAIE 191
Cdd:PRK15173  254 HGNGVFLGLeESPFVSTHATESFTSGMVLSLE 285
PRK14575 PRK14575
putative peptidase; Provisional
 5-191 2.83e-03

putative peptidase; Provisional


Pssm-ID: 173039 [Multi-domain]  Cd Length: 406  Bit Score: 38.92  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730   5 EIEKYKEAGNIAKEAKNLAAEIVKIGASDLDVAEKLEEFILSKTGERGGLAFPVSVCVnEIAAHKTPSIQNPYlfkKGDV 84
Cdd:PRK14575  183 EIKRLRKSAEITEYGITEASKLIRVGCTSAELTAAYKAAVMSKSETHFSRFHLISVGA-DFSPKLIPSNTKAC---SGDL 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277948730  85 VKIDLGVHINGYIADTATTFDFGD----NKNLLQTNKLALKKAIEAIKKDKPLGDLGKIVEQTMKGRGfMPITNlAGHQI 160
Cdd:PRK14575  259 IKFDCGVDVDGYGADIARTFVVGEppeiTRKIYQTIRTGHEHMLSMVAPGVKMKDVFDSTMEVIKKSG-LPNYN-RGHLG 336

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1277948730 161 KPYNIHAGV-SVPNCETNNQAKFQKGEAYAIE 191
Cdd:PRK14575  337 HGNGVFLGLeESPFVSTHATESFTSGMVLSLE 368
 
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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