NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1102963142|ref|WP_071610598|]
View 

BPL-N domain-containing protein [Glaesserella parasuis]

Protein Classification

COG4285 family protein( domain architecture ID 10790659)

COG4285 family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COG4285 COG4285
Uncharacterized conserved protein, conains N-terminal glutamine amidotransferase (GATase1) ...
 2-217 3.30e-75

Uncharacterized conserved protein, conains N-terminal glutamine amidotransferase (GATase1)-like domain [General function prediction only];


:

Pssm-ID: 443426 [Multi-domain]  Cd Length: 221  Bit Score: 227.62  E-value: 3.30e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102963142   2 VKPVCIYVDDGVSDVGVASLQLAIAT-NLGLPTKTITAQHIIDNELEHCQMLIMPGGADLPYCAKLNGKGNQHIRQFVQC 80
Cdd:COG4285     8 RPRVLVYRGPGASDDCVEALVRALKQlNLGFKVRYVTAEDITAGTLANADLLIQPGGGDLPYYKALGGEGNAAIREFVEN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102963142  81 GGFYLGICAGAYYATKTIEFT-GDGYQIFENRElaLFNGKAVGSLpdltNQYYYDGTAASKTFATLTFqNNTQLSFYYHG 159
Cdd:COG4285    88 GGGYLGICAGAYLASKYVGFGlGTDARVVGNRE--FFPGVAVGPL----GRPGADVSLTESTAVLVRW-RGDTLTIYYQG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1102963142 160 GPMF-LSEAEDAETVVACYSANRPAIVCGSYGKGKFLLSGVHFELQPEiYEQYIIRDTL 217
Cdd:COG4285   161 GPYFePAPDGPGYTVLATYADGSPAIVSGTYGKGRVVLSGPHPEATPG-LEEMIPAGVL 218
 
Name Accession Description Interval E-value
COG4285 COG4285
Uncharacterized conserved protein, conains N-terminal glutamine amidotransferase (GATase1) ...
 2-217 3.30e-75

Uncharacterized conserved protein, conains N-terminal glutamine amidotransferase (GATase1)-like domain [General function prediction only];


Pssm-ID: 443426 [Multi-domain]  Cd Length: 221  Bit Score: 227.62  E-value: 3.30e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102963142   2 VKPVCIYVDDGVSDVGVASLQLAIAT-NLGLPTKTITAQHIIDNELEHCQMLIMPGGADLPYCAKLNGKGNQHIRQFVQC 80
Cdd:COG4285     8 RPRVLVYRGPGASDDCVEALVRALKQlNLGFKVRYVTAEDITAGTLANADLLIQPGGGDLPYYKALGGEGNAAIREFVEN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102963142  81 GGFYLGICAGAYYATKTIEFT-GDGYQIFENRElaLFNGKAVGSLpdltNQYYYDGTAASKTFATLTFqNNTQLSFYYHG 159
Cdd:COG4285    88 GGGYLGICAGAYLASKYVGFGlGTDARVVGNRE--FFPGVAVGPL----GRPGADVSLTESTAVLVRW-RGDTLTIYYQG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1102963142 160 GPMF-LSEAEDAETVVACYSANRPAIVCGSYGKGKFLLSGVHFELQPEiYEQYIIRDTL 217
Cdd:COG4285   161 GPYFePAPDGPGYTVLATYADGSPAIVSGTYGKGRVVLSGPHPEATPG-LEEMIPAGVL 218
BPL_N pfam09825
Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is ...
 34-202 1.18e-38

Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is found to the N terminus of the biotin protein ligase (BPL) catalytic domain. This domain is essential in BPL activity.


Pssm-ID: 462915  Cd Length: 277  Bit Score: 135.73  E-value: 1.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102963142  34 KTITAQhIIDNE--LEHCQMLIMPGGADLPYCAKLNGKGNQHIRQFVQCGGFYLGICAGAYYATKTIEF-TGD-GYQIFE 109
Cdd:pfam09825  34 IPVSAK-VLLKEpwTSKCALLVFPGGADLPYCRELNGEGNRRIKQFVRRGGAYLGFCAGGYYGSARCEFeVGDpKLEVVG 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102963142 110 NRELALFNGKAVGslpdltnqyyydgtAASKTF----------ATLTFQNNTQLSF---YYHGGPMFLseaeDAET---- 172
Cdd:pfam09825 113 PRELAFFPGTCRG--------------PAFPGFvynseagaraAKLKVNTSPVPDEfksYYNGGGVFV----DADKyanv 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1102963142 173 -VVACYS---------ANRPAIVCGSYGKGKFLLSGVHFE 202
Cdd:pfam09825 175 eVLARYTedldvdggdGGPAAVVYCKVGKGKALLTGPHPE 214
GATase1_ScBLP_like cd03144
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 5-94 5.22e-22

Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Saccharomyces cerevisiae biotin-apoprotein ligase (ScBLP); Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Saccharomyces cerevisiae biotin-apoprotein ligase (ScBLP). Biotin-apoprotein ligase modifies proteins by covalently attaching biotin. ScBLP is known to biotinylate acety-CoA carboxylase and pyruvate carboxylase. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, the Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in a typical GATase1 domain is conserved.


Pssm-ID: 153238  Cd Length: 114  Bit Score: 87.69  E-value: 5.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102963142   5 VCIYVDDGVSDVGVASLQLAIAtnLGLPTKTITAQHIIDNELEH-CQMLIMPGGADLPYCAKLNGKGNQHIRQFVQCGGF 83
Cdd:cd03144     2 VLVYNGPGASPGSLKHLAELLR--LYLAVSTVTADELAVGPWESkTALLVVPGGADLPYCRALNGKGNRRIRNFVRNGGN 79

                          90
                  ....*....|.
gi 1102963142  84 YLGICAGAYYA 94
Cdd:cd03144    80 YLGICAGAYLA 90
PRK06278 PRK06278
cobyrinic acid a,c-diamide synthase; Validated
 31-90 6.06e-04

cobyrinic acid a,c-diamide synthase; Validated


Pssm-ID: 180505 [Multi-domain]  Cd Length: 476  Bit Score: 40.79  E-value: 6.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102963142  31 LPTKTITAQHIidNELEHCQMLIMPGGAdLPYCAKLNGKGNQHIRQFvqcGGFYLGICAG 90
Cdd:PRK06278   21 LPTKIIDENNI--KEIKDLDGLIIPGGS-LVESGSLTDELKKEILNF---DGYIIGICSG 74
 
Name Accession Description Interval E-value
COG4285 COG4285
Uncharacterized conserved protein, conains N-terminal glutamine amidotransferase (GATase1) ...
 2-217 3.30e-75

Uncharacterized conserved protein, conains N-terminal glutamine amidotransferase (GATase1)-like domain [General function prediction only];


Pssm-ID: 443426 [Multi-domain]  Cd Length: 221  Bit Score: 227.62  E-value: 3.30e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102963142   2 VKPVCIYVDDGVSDVGVASLQLAIAT-NLGLPTKTITAQHIIDNELEHCQMLIMPGGADLPYCAKLNGKGNQHIRQFVQC 80
Cdd:COG4285     8 RPRVLVYRGPGASDDCVEALVRALKQlNLGFKVRYVTAEDITAGTLANADLLIQPGGGDLPYYKALGGEGNAAIREFVEN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102963142  81 GGFYLGICAGAYYATKTIEFT-GDGYQIFENRElaLFNGKAVGSLpdltNQYYYDGTAASKTFATLTFqNNTQLSFYYHG 159
Cdd:COG4285    88 GGGYLGICAGAYLASKYVGFGlGTDARVVGNRE--FFPGVAVGPL----GRPGADVSLTESTAVLVRW-RGDTLTIYYQG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1102963142 160 GPMF-LSEAEDAETVVACYSANRPAIVCGSYGKGKFLLSGVHFELQPEiYEQYIIRDTL 217
Cdd:COG4285   161 GPYFePAPDGPGYTVLATYADGSPAIVSGTYGKGRVVLSGPHPEATPG-LEEMIPAGVL 218
BPL_N pfam09825
Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is ...
 34-202 1.18e-38

Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is found to the N terminus of the biotin protein ligase (BPL) catalytic domain. This domain is essential in BPL activity.


Pssm-ID: 462915  Cd Length: 277  Bit Score: 135.73  E-value: 1.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102963142  34 KTITAQhIIDNE--LEHCQMLIMPGGADLPYCAKLNGKGNQHIRQFVQCGGFYLGICAGAYYATKTIEF-TGD-GYQIFE 109
Cdd:pfam09825  34 IPVSAK-VLLKEpwTSKCALLVFPGGADLPYCRELNGEGNRRIKQFVRRGGAYLGFCAGGYYGSARCEFeVGDpKLEVVG 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102963142 110 NRELALFNGKAVGslpdltnqyyydgtAASKTF----------ATLTFQNNTQLSF---YYHGGPMFLseaeDAET---- 172
Cdd:pfam09825 113 PRELAFFPGTCRG--------------PAFPGFvynseagaraAKLKVNTSPVPDEfksYYNGGGVFV----DADKyanv 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1102963142 173 -VVACYS---------ANRPAIVCGSYGKGKFLLSGVHFE 202
Cdd:pfam09825 175 eVLARYTedldvdggdGGPAAVVYCKVGKGKALLTGPHPE 214
GATase1_ScBLP_like cd03144
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 5-94 5.22e-22

Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Saccharomyces cerevisiae biotin-apoprotein ligase (ScBLP); Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Saccharomyces cerevisiae biotin-apoprotein ligase (ScBLP). Biotin-apoprotein ligase modifies proteins by covalently attaching biotin. ScBLP is known to biotinylate acety-CoA carboxylase and pyruvate carboxylase. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, the Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in a typical GATase1 domain is conserved.


Pssm-ID: 153238  Cd Length: 114  Bit Score: 87.69  E-value: 5.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102963142   5 VCIYVDDGVSDVGVASLQLAIAtnLGLPTKTITAQHIIDNELEH-CQMLIMPGGADLPYCAKLNGKGNQHIRQFVQCGGF 83
Cdd:cd03144     2 VLVYNGPGASPGSLKHLAELLR--LYLAVSTVTADELAVGPWESkTALLVVPGGADLPYCRALNGKGNRRIRNFVRNGGN 79

                          90
                  ....*....|.
gi 1102963142  84 YLGICAGAYYA 94
Cdd:cd03144    80 YLGICAGAYLA 90
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 5-93 2.79e-06

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 44.50  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102963142   5 VCIYVDDGVSDVGVASLqLAIATNLGLPTKTITA---QHIIDNELEHCQMLIMPGGADLPYCAKLNGKGNQHIRQFVQCG 81
Cdd:cd03128     1 VAVLLFGGSEELELASP-LDALREAGAEVDVVSPdggPVESDVDLDDYDGLILPGGPGTPDDLAWDEALLALLREAAAAG 79

                          90
                  ....*....|..
gi 1102963142  82 GFYLGICAGAYY 93
Cdd:cd03128    80 KPVLGICLGAQL 91
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 5-110 3.07e-06

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 44.90  E-value: 3.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102963142   5 VCIYVDDGVSDVGVASLqLAIATNLGLPTKTITA---QHIIDNELEHCQMLIMPGGADLPYCAKLNGKGNQHIRQFVQCG 81
Cdd:cd01653     1 VAVLLFPGFEELELASP-LDALREAGAEVDVVSPdggPVESDVDLDDYDGLILPGGPGTPDDLARDEALLALLREAAAAG 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1102963142  82 GFYLGICAGAYYATKTIEF-------TGDGYQIFEN 110
Cdd:cd01653    80 KPILGICLGAQLLVLGVQFhpeaidgAEAGARLLVN 115
PRK06278 PRK06278
cobyrinic acid a,c-diamide synthase; Validated
 31-90 6.06e-04

cobyrinic acid a,c-diamide synthase; Validated


Pssm-ID: 180505 [Multi-domain]  Cd Length: 476  Bit Score: 40.79  E-value: 6.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1102963142  31 LPTKTITAQHIidNELEHCQMLIMPGGAdLPYCAKLNGKGNQHIRQFvqcGGFYLGICAG 90
Cdd:PRK06278   21 LPTKIIDENNI--KEIKDLDGLIIPGGS-LVESGSLTDELKKEILNF---DGYIIGICSG 74
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH