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Conserved domains on  [gi|1824718315|ref|NP_001366191|]
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conserved oligomeric Golgi complex subunit 8 isoform 4 [Homo sapiens]

Protein Classification

Dor1 and Pep_deformylase domain-containing protein( domain architecture ID 10514062)

Dor1 and Pep_deformylase domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Dor1 pfam04124
Dor1-like family; Dor1 is involved in vesicle targeting to the yeast Golgi apparatus and ...
 50-364 4.10e-160

Dor1-like family; Dor1 is involved in vesicle targeting to the yeast Golgi apparatus and complexes with a number of other trafficking proteins, which include Sec34 and Sec35.


:

Pssm-ID: 427729  Cd Length: 315  Bit Score: 461.89  E-value: 4.10e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718315  50 LRELSGSGLERLRREPERLAEERAQLLQQTRDLAFANYKTFIRGAECTERIHRLFGDVEASLGRLLDRLPSFQQSCRNFV 129
Cdd:pfam04124   1 LRDLSTKPLEELEKEPELLAEEAAEILAQIQDLARKNYKTFIDAARATIAIRQLLGDIAKSLEQLVDDIPKLTSSCVRFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718315 130 KEAEEISSNRRMNSLTLNRHTEILEILEIPQLMDTCVRNSYYEEALELAAYVRRLERKYSSIPVIQGIVNEVRQSMQLML 209
Cdd:pfam04124  81 EDAKEISETRRLNNLLLQNHDQLLDLLELPQLMDTCIRTGYYSEALELAAYATRLRSRFPGSPVIQEIAAQVEEAMQTML 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718315 210 SQLIQQLRTNIQLPACLRVIGYLRRMDVFTEAELRVKFLQARDAWLRSILTAIPNDDPYFHITKTIEASRVHLFDIITQY 289
Cdd:pfam04124 161 SQLIQQLRTPLQLPSCLKVVGYLRRMPPFTENELRLKFLQARDAWLESILTALDDDNPEKYLLKTIEVCRVNLFDILTQY 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824718315 290 RAIFSDEDPLLPPAMGEHTVNESAIFHGWVLQKVSQFLQVLETDLYRGIGGHLDSLLGQCMYFGLSFSRVGADFR 364
Cdd:pfam04124 241 RAIFPEDEVVLKNAWGSWNNNGGSILESWVEMKIKRFLEVLREDLYVKLGVSLSSVLGQLMYFALSFGRVGADFR 315
Def super family cl42281
Peptide deformylase [Translation, ribosomal structure and biogenesis];
588-626 3.77e-13

Peptide deformylase [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG0242:

Pssm-ID: 440012  Cd Length: 163  Bit Score: 67.43  E-value: 3.77e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1824718315 588 LDPNGEQVVWQASGWAARIIQHEMDHLQGCLFIDKMDSR 626
Cdd:COG0242   115 LDLDGEPVELEAEGLLARCIQHEIDHLDGILFIDRLSPL 153
 
Name Accession Description Interval E-value
Dor1 pfam04124
Dor1-like family; Dor1 is involved in vesicle targeting to the yeast Golgi apparatus and ...
 50-364 4.10e-160

Dor1-like family; Dor1 is involved in vesicle targeting to the yeast Golgi apparatus and complexes with a number of other trafficking proteins, which include Sec34 and Sec35.


Pssm-ID: 427729  Cd Length: 315  Bit Score: 461.89  E-value: 4.10e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718315  50 LRELSGSGLERLRREPERLAEERAQLLQQTRDLAFANYKTFIRGAECTERIHRLFGDVEASLGRLLDRLPSFQQSCRNFV 129
Cdd:pfam04124   1 LRDLSTKPLEELEKEPELLAEEAAEILAQIQDLARKNYKTFIDAARATIAIRQLLGDIAKSLEQLVDDIPKLTSSCVRFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718315 130 KEAEEISSNRRMNSLTLNRHTEILEILEIPQLMDTCVRNSYYEEALELAAYVRRLERKYSSIPVIQGIVNEVRQSMQLML 209
Cdd:pfam04124  81 EDAKEISETRRLNNLLLQNHDQLLDLLELPQLMDTCIRTGYYSEALELAAYATRLRSRFPGSPVIQEIAAQVEEAMQTML 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718315 210 SQLIQQLRTNIQLPACLRVIGYLRRMDVFTEAELRVKFLQARDAWLRSILTAIPNDDPYFHITKTIEASRVHLFDIITQY 289
Cdd:pfam04124 161 SQLIQQLRTPLQLPSCLKVVGYLRRMPPFTENELRLKFLQARDAWLESILTALDDDNPEKYLLKTIEVCRVNLFDILTQY 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824718315 290 RAIFSDEDPLLPPAMGEHTVNESAIFHGWVLQKVSQFLQVLETDLYRGIGGHLDSLLGQCMYFGLSFSRVGADFR 364
Cdd:pfam04124 241 RAIFPEDEVVLKNAWGSWNNNGGSILESWVEMKIKRFLEVLREDLYVKLGVSLSSVLGQLMYFALSFGRVGADFR 315
Def COG0242
Peptide deformylase [Translation, ribosomal structure and biogenesis];
588-626 3.77e-13

Peptide deformylase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440012  Cd Length: 163  Bit Score: 67.43  E-value: 3.77e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1824718315 588 LDPNGEQVVWQASGWAARIIQHEMDHLQGCLFIDKMDSR 626
Cdd:COG0242   115 LDLDGEPVELEAEGLLARCIQHEIDHLDGILFIDRLSPL 153
Pep_deformylase pfam01327
Polypeptide deformylase;
588-626 7.85e-13

Polypeptide deformylase;


Pssm-ID: 426202  Cd Length: 153  Bit Score: 66.45  E-value: 7.85e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1824718315 588 LDPNGEQVVWQASGWAARIIQHEMDHLQGCLFIDKMDSR 626
Cdd:pfam01327 113 LDLNGKEIELEAEGFLARVLQHEIDHLNGILFIDRLSPL 151
def PRK00150
peptide deformylase; Reviewed
 588-626 3.42e-12

peptide deformylase; Reviewed


Pssm-ID: 234668  Cd Length: 165  Bit Score: 64.76  E-value: 3.42e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1824718315 588 LDPNGEQVVWQASGWAARIIQHEMDHLQGCLFIDKMDSR 626
Cdd:PRK00150  114 LDRDGKPFELEADGLLARCIQHEIDHLNGVLFIDRLSPL 152
Pep_deformylase cd00487
Polypeptide or peptide deformylase; a family of metalloenzymes that catalyzes the removal of ...
 588-619 1.39e-11

Polypeptide or peptide deformylase; a family of metalloenzymes that catalyzes the removal of the N-terminal formyl group in a growing polypeptide chain following translation initiation during protein synthesis in prokaryotes. These enzymes utilize Fe(II) as the catalytic metal ion, which can be replaced with a nickel or cobalt ion with no loss of activity. There are two types of peptide deformylases, types I and II, which differ in structure only in the outer surface of the domain. Because these enzymes are essential only in prokaryotes (although eukaryotic gene sequences have been found), they are a target for a new class of antibacterial agents.


Pssm-ID: 238271  Cd Length: 141  Bit Score: 62.50  E-value: 1.39e-11
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1824718315 588 LDPNGEQVVWQASGWAARIIQHEMDHLQGCLF 619
Cdd:cd00487   110 LDEDGNPIELEAEGFLARCIQHEIDHLNGILF 141
pept_deformyl TIGR00079
peptide deformylase; Peptide deformylase (EC 3.5.1.88), also called polypeptide deformylase, ...
 588-635 9.19e-06

peptide deformylase; Peptide deformylase (EC 3.5.1.88), also called polypeptide deformylase, is a metalloenzyme that uses water to release formate from the N-terminal formyl-L-methionine of bacterial and chloroplast peptides. This enzyme should not be confused with formylmethionine deformylase (EC 3.5.1.31) which is active on free N-formyl methionine and has been reported from rat intestine. [Protein fate, Protein modification and repair]


Pssm-ID: 272895  Cd Length: 161  Bit Score: 46.22  E-value: 9.19e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1824718315 588 LDPNGEQVVWQASGWAARIIQHEMDHLQGCLFIDKMD--SRTFTNVYWMK 635
Cdd:TIGR00079 112 DDRFGKPIILEADGLLAICIQHEIDHLNGVFFVDYISplNPKKLKKEMKE 161
 
Name Accession Description Interval E-value
Dor1 pfam04124
Dor1-like family; Dor1 is involved in vesicle targeting to the yeast Golgi apparatus and ...
 50-364 4.10e-160

Dor1-like family; Dor1 is involved in vesicle targeting to the yeast Golgi apparatus and complexes with a number of other trafficking proteins, which include Sec34 and Sec35.


Pssm-ID: 427729  Cd Length: 315  Bit Score: 461.89  E-value: 4.10e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718315  50 LRELSGSGLERLRREPERLAEERAQLLQQTRDLAFANYKTFIRGAECTERIHRLFGDVEASLGRLLDRLPSFQQSCRNFV 129
Cdd:pfam04124   1 LRDLSTKPLEELEKEPELLAEEAAEILAQIQDLARKNYKTFIDAARATIAIRQLLGDIAKSLEQLVDDIPKLTSSCVRFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718315 130 KEAEEISSNRRMNSLTLNRHTEILEILEIPQLMDTCVRNSYYEEALELAAYVRRLERKYSSIPVIQGIVNEVRQSMQLML 209
Cdd:pfam04124  81 EDAKEISETRRLNNLLLQNHDQLLDLLELPQLMDTCIRTGYYSEALELAAYATRLRSRFPGSPVIQEIAAQVEEAMQTML 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824718315 210 SQLIQQLRTNIQLPACLRVIGYLRRMDVFTEAELRVKFLQARDAWLRSILTAIPNDDPYFHITKTIEASRVHLFDIITQY 289
Cdd:pfam04124 161 SQLIQQLRTPLQLPSCLKVVGYLRRMPPFTENELRLKFLQARDAWLESILTALDDDNPEKYLLKTIEVCRVNLFDILTQY 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824718315 290 RAIFSDEDPLLPPAMGEHTVNESAIFHGWVLQKVSQFLQVLETDLYRGIGGHLDSLLGQCMYFGLSFSRVGADFR 364
Cdd:pfam04124 241 RAIFPEDEVVLKNAWGSWNNNGGSILESWVEMKIKRFLEVLREDLYVKLGVSLSSVLGQLMYFALSFGRVGADFR 315
Def COG0242
Peptide deformylase [Translation, ribosomal structure and biogenesis];
588-626 3.77e-13

Peptide deformylase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440012  Cd Length: 163  Bit Score: 67.43  E-value: 3.77e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1824718315 588 LDPNGEQVVWQASGWAARIIQHEMDHLQGCLFIDKMDSR 626
Cdd:COG0242   115 LDLDGEPVELEAEGLLARCIQHEIDHLDGILFIDRLSPL 153
Pep_deformylase pfam01327
Polypeptide deformylase;
588-626 7.85e-13

Polypeptide deformylase;


Pssm-ID: 426202  Cd Length: 153  Bit Score: 66.45  E-value: 7.85e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1824718315 588 LDPNGEQVVWQASGWAARIIQHEMDHLQGCLFIDKMDSR 626
Cdd:pfam01327 113 LDLNGKEIELEAEGFLARVLQHEIDHLNGILFIDRLSPL 151
def PRK00150
peptide deformylase; Reviewed
 588-626 3.42e-12

peptide deformylase; Reviewed


Pssm-ID: 234668  Cd Length: 165  Bit Score: 64.76  E-value: 3.42e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1824718315 588 LDPNGEQVVWQASGWAARIIQHEMDHLQGCLFIDKMDSR 626
Cdd:PRK00150  114 LDRDGKPFELEADGLLARCIQHEIDHLNGVLFIDRLSPL 152
Pep_deformylase cd00487
Polypeptide or peptide deformylase; a family of metalloenzymes that catalyzes the removal of ...
 588-619 1.39e-11

Polypeptide or peptide deformylase; a family of metalloenzymes that catalyzes the removal of the N-terminal formyl group in a growing polypeptide chain following translation initiation during protein synthesis in prokaryotes. These enzymes utilize Fe(II) as the catalytic metal ion, which can be replaced with a nickel or cobalt ion with no loss of activity. There are two types of peptide deformylases, types I and II, which differ in structure only in the outer surface of the domain. Because these enzymes are essential only in prokaryotes (although eukaryotic gene sequences have been found), they are a target for a new class of antibacterial agents.


Pssm-ID: 238271  Cd Length: 141  Bit Score: 62.50  E-value: 1.39e-11
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1824718315 588 LDPNGEQVVWQASGWAARIIQHEMDHLQGCLF 619
Cdd:cd00487   110 LDEDGNPIELEAEGFLARCIQHEIDHLNGILF 141
PRK12846 PRK12846
peptide deformylase; Reviewed
 588-622 1.58e-07

peptide deformylase; Reviewed


Pssm-ID: 237227  Cd Length: 165  Bit Score: 51.34  E-value: 1.58e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1824718315 588 LDPNGEQVVWQASGWAARIIQHEMDHLQGCLFIDK 622
Cdd:PRK12846  114 QDRDGKPIEIEAEGFLARVLQHEIDHLDGILYTDR 148
pept_deformyl TIGR00079
peptide deformylase; Peptide deformylase (EC 3.5.1.88), also called polypeptide deformylase, ...
 588-635 9.19e-06

peptide deformylase; Peptide deformylase (EC 3.5.1.88), also called polypeptide deformylase, is a metalloenzyme that uses water to release formate from the N-terminal formyl-L-methionine of bacterial and chloroplast peptides. This enzyme should not be confused with formylmethionine deformylase (EC 3.5.1.31) which is active on free N-formyl methionine and has been reported from rat intestine. [Protein fate, Protein modification and repair]


Pssm-ID: 272895  Cd Length: 161  Bit Score: 46.22  E-value: 9.19e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1824718315 588 LDPNGEQVVWQASGWAARIIQHEMDHLQGCLFIDKMD--SRTFTNVYWMK 635
Cdd:TIGR00079 112 DDRFGKPIILEADGLLAICIQHEIDHLNGVFFVDYISplNPKKLKKEMKE 161
PRK09218 PRK09218
peptide deformylase; Validated
 588-618 7.48e-04

peptide deformylase; Validated


Pssm-ID: 181704  Cd Length: 136  Bit Score: 39.91  E-value: 7.48e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1824718315 588 LDPNGEQVVWQASGWAARIIQHEMDHLQGCL 618
Cdd:PRK09218  105 LDRNWREQTQTFTGFTAQIIQHELDHCEGIL 135
 
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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