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Conserved domains on  [gi|17570097|ref|NP_510627|]
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Putative uncharacterized protein T27A8.3 [Caenorhabditis elegans]

Protein Classification

methionine aminopeptidase family protein( domain architecture ID 1003285)

methionine aminopeptidase family protein may cotranslationally remove the N-terminal methionine from nascent proteins; similar to fungal methionine aminopeptidase 2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00053 super family cl36503
methionine aminopeptidase 2; Provisional
 29-150 6.05e-57

methionine aminopeptidase 2; Provisional


The actual alignment was detected with superfamily member PTZ00053:

Pssm-ID: 240246 [Multi-domain]  Cd Length: 470  Bit Score: 185.69  E-value: 6.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570097   29 EFHGNSNEVKPIGSLNGQSIAQCRIHTGKTVPIVKGGEQARMEENEIYAIETFGSTGKGYFHDDMETSHYMKNFElaDEK 108
Cdd:PTZ00053 306 EIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPIVKGGENTRMEEGELFAIETFASTGRGYVNEDLECSHYMKDPG--AEF 383

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 17570097  109 IPLRLQKSKGLLKLIDKNFATLAFCRCWIDRLEETKYLMALK 150
Cdd:PTZ00053 384 VPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQDRHLLALK 425
 
Name Accession Description Interval E-value
PTZ00053 PTZ00053
methionine aminopeptidase 2; Provisional
 29-150 6.05e-57

methionine aminopeptidase 2; Provisional


Pssm-ID: 240246 [Multi-domain]  Cd Length: 470  Bit Score: 185.69  E-value: 6.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570097   29 EFHGNSNEVKPIGSLNGQSIAQCRIHTGKTVPIVKGGEQARMEENEIYAIETFGSTGKGYFHDDMETSHYMKNFElaDEK 108
Cdd:PTZ00053 306 EIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPIVKGGENTRMEEGELFAIETFASTGRGYVNEDLECSHYMKDPG--AEF 383

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 17570097  109 IPLRLQKSKGLLKLIDKNFATLAFCRCWIDRLEETKYLMALK 150
Cdd:PTZ00053 384 VPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQDRHLLALK 425
MetAP2 cd01088
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 37-151 2.55e-52

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: 168.58  E-value: 2.55e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570097  37 VKPIGSLNGQSIAQCRIHTGKTVPIVKGGEQARMEENEIYAIETFGSTGKGYFHDDMETSHYMKNFELadekiPLRLQKS 116
Cdd:cd01088 142 FKPIRNLTGHSIERYRLHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIYMLNRDK-----PLRLPRA 216

                        90       100       110
                ....*....|....*....|....*....|....*
gi 17570097 117 KGLLKLIDKNFATLAFCRCWIDRLEETKYLMALKD 151
Cdd:cd01088 217 RKLLDVIYENFGTLPFARRWLDRLGETKLLMALKN 251
met_pdase_II TIGR00501
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ...
 34-149 1.08e-29

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: 110.26  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570097    34 SNEVKPIGSLNGQSIAQCRIHTGKTVPIVKGGEQARMEENEIYAIETFGSTGKGYFHDDMETSHYmknfELADEKiPLRL 113
Cdd:TIGR00501 143 SYGVKPISNLTGHSMAPYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDGVGYVTDGGEVSIY----AFLAER-PVRL 217

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 17570097   114 QKSKGLLKLIDKNFATLAFCRCWIDRLEETKYLMAL 149
Cdd:TIGR00501 218 DSARNLLKTIDENYGTLPFARRWLDKLGDEKYLFAL 253
 
Name Accession Description Interval E-value
PTZ00053 PTZ00053
methionine aminopeptidase 2; Provisional
 29-150 6.05e-57

methionine aminopeptidase 2; Provisional


Pssm-ID: 240246 [Multi-domain]  Cd Length: 470  Bit Score: 185.69  E-value: 6.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570097   29 EFHGNSNEVKPIGSLNGQSIAQCRIHTGKTVPIVKGGEQARMEENEIYAIETFGSTGKGYFHDDMETSHYMKNFElaDEK 108
Cdd:PTZ00053 306 EIKGKTYPIKSIRNLNGHSIGPYIIHGGKSVPIVKGGENTRMEEGELFAIETFASTGRGYVNEDLECSHYMKDPG--AEF 383

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 17570097  109 IPLRLQKSKGLLKLIDKNFATLAFCRCWIDRLEETKYLMALK 150
Cdd:PTZ00053 384 VPLRLPKAKQLLKHINTNFGTLAFCRRWLDRLGQDRHLLALK 425
MetAP2 cd01088
Methionine Aminopeptidase 2. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and ...
 37-151 2.55e-52

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: 168.58  E-value: 2.55e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570097  37 VKPIGSLNGQSIAQCRIHTGKTVPIVKGGEQARMEENEIYAIETFGSTGKGYFHDDMETSHYMKNFELadekiPLRLQKS 116
Cdd:cd01088 142 FKPIRNLTGHSIERYRLHAGKSIPNVKGGEGTRLEEGDVYAIEPFATTGKGYVHDGPECSIYMLNRDK-----PLRLPRA 216

                        90       100       110
                ....*....|....*....|....*....|....*
gi 17570097 117 KGLLKLIDKNFATLAFCRCWIDRLEETKYLMALKD 151
Cdd:cd01088 217 RKLLDVIYENFGTLPFARRWLDRLGETKLLMALKN 251
met_pdase_II TIGR00501
methionine aminopeptidase, type II; Methionine aminopeptidase (map) is a cobalt-binding enzyme. ...
 34-149 1.08e-29

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: 110.26  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17570097    34 SNEVKPIGSLNGQSIAQCRIHTGKTVPIVKGGEQARMEENEIYAIETFGSTGKGYFHDDMETSHYmknfELADEKiPLRL 113
Cdd:TIGR00501 143 SYGVKPISNLTGHSMAPYRLHGGKSIPNVKERDTTKLEEGDVVAIEPFATDGVGYVTDGGEVSIY----AFLAER-PVRL 217

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 17570097   114 QKSKGLLKLIDKNFATLAFCRCWIDRLEETKYLMAL 149
Cdd:TIGR00501 218 DSARNLLKTIDENYGTLPFARRWLDKLGDEKYLFAL 253
crvDNA_42K TIGR00495
42K curved DNA binding protein; Proteins identified by this model have been identified in a ...
 66-132 1.15e-03

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: 38.72  E-value: 1.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17570097    66 EQARMEENEIYAIETFGSTGKGYFHD-DMETSHYMKNfelADEKIPLRLQKSKGLLKLIDKNFATLAF 132
Cdd:TIGR00495 216 DTAEFEENEVYAVDILVSTGEGKAKDaDQRTTIYKRD---PSKTYGLKMKASRAFFSEIERRFDAMPF 280
 
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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