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Conserved domains on  [gi|16129496|ref|NP_416055|]
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PF02464 family protein YdeJ [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

CinA family protein( domain architecture ID 10012062)

CinA family protein similar to Escherichia coli protein YdeJ that does not have nicotinamide-nucleotide (NMN) amidohydrolase activity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK03657 PRK03657
2-oxo-tetronate isomerase;
6-162 2.12e-98

2-oxo-tetronate isomerase;


:

Pssm-ID: 235149  Cd Length: 170  Bit Score: 281.01  E-value: 2.12e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129496    6 DKIVQLVDTDTIENLTSALSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDQAKMKILSVSQQSLER 85
Cdd:PRK03657   1 DKIVQLADADTIENLTKALSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDEAKMKILSVSQQSLER 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129496   86 YSAVSEKVAAEMATGAIERADADVSIAITGYGGPEGGEDGTPAGTVWFAWHIKGQNYTAVMHFAGDCETVLALAVRF 162
Cdd:PRK03657  81 YSAVSEAVVAEMATGAIERADADISIAISGYGGPEGGEDGTPAGTVWFAWNIKGQTYTARMHFAGDCETVLAKAVRF 157
 
Name Accession Description Interval E-value
PRK03657 PRK03657
2-oxo-tetronate isomerase;
6-162 2.12e-98

2-oxo-tetronate isomerase;


Pssm-ID: 235149  Cd Length: 170  Bit Score: 281.01  E-value: 2.12e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129496    6 DKIVQLVDTDTIENLTSALSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDQAKMKILSVSQQSLER 85
Cdd:PRK03657   1 DKIVQLADADTIENLTKALSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDEAKMKILSVSQQSLER 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129496   86 YSAVSEKVAAEMATGAIERADADVSIAITGYGGPEGGEDGTPAGTVWFAWHIKGQNYTAVMHFAGDCETVLALAVRF 162
Cdd:PRK03657  81 YSAVSEAVVAEMATGAIERADADISIAISGYGGPEGGEDGTPAGTVWFAWNIKGQTYTARMHFAGDCETVLAKAVRF 157
PncC_domain TIGR00199
amidohydrolase, PncC family; CinA is a DNA damage- or competence-inducible protein that is ...
24-162 2.80e-72

amidohydrolase, PncC family; CinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species. Several bacterial species have a protein consisting largely of the C-terminal domain of CinA but lacking the N-terminal domain, including nicotinamide mononucleotide (NMN) deamidase (3.5.1.42) proteins PncC in Shewanella oneidensis and ygaD in E. coli. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129303 [Multi-domain]  Cd Length: 146  Bit Score: 214.19  E-value: 2.80e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129496    24 LSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDQAKMKILSVSQQSLERYSAVSEKVAAEMATGAIE 103
Cdd:TIGR00199   1 LSERLKALGLTVATAESCTGGLLAHALTDISGASKYFGGGVVCYTNQVKINLLGVSQETLARFGAVSEECAAEMALGVKE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129496   104 RADADVSIAITGYGGPEGGEDGTPAGTVWFAWHI-KGQNYTAVMHFAGDCETVLALAVRF 162
Cdd:TIGR00199  81 RFGADVGIAISGIAGPDGGEEEKPGGTVWFIWIIaKGQAYTAEMHFAGDRETIRALAVRY 140
PncC COG1546
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; ...
17-162 9.72e-55

Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; Nicotinamide mononucleotide (NMN) deamidase PncC is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 441155  Cd Length: 154  Bit Score: 169.84  E-value: 9.72e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129496  17 IENLTSALSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDQAKMKILSVSQQSLERYSAVSEKVAAE 96
Cdd:COG1546   1 LESLAEVVGELLRERGLTLATAESCTGGLIAAALTDVPGSSAVFDGGFVTYSNEAKEELLGVPAETLEKHGAVSEEVARE 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129496  97 MATGAIERADADVSIAITGYGGPEGGEDGTPAGTVWFAWHIKGQNYTAVMHFAGDCETVLALAVRF 162
Cdd:COG1546  81 MAEGARRLSGADIAVAVTGIAGPGGGTPGKPVGTVYIALAGPGGVVVRRLHFGGDREAVREQAVRA 146
CinA pfam02464
Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, ...
17-162 1.71e-50

Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, and is thought to be specifically required at some stage in the process of transformation. This Pfam family consists of putative competence-damaged proteins from the cin operon. Some members of this family have nicotinamide mononucleotide (NMN) deamidase activity.


Pssm-ID: 460565  Cd Length: 155  Bit Score: 159.24  E-value: 1.71e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129496    17 IENLTSALSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDQAKMKILSVSQQSLERYSAVSEKVAAE 96
Cdd:pfam02464   1 LESLAEEVGKLLKARGLTLATAESCTGGLLAAALTSVPGASDVFLGGVVTYSNEAKRELLGVPPETLEEHGAVSEEVARE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129496    97 MATGAIERADADVSIAITGYGGPEGGEDGTPAGTVWFAWHIKGQNYTAVMHFAGDCETVLALAVRF 162
Cdd:pfam02464  81 MAEGARKRLGADIGVAITGIAGPSGGTEGKPVGTVYIAIAGPGGTVTRRLNFGGDREAIREQAVVA 146
 
Name Accession Description Interval E-value
PRK03657 PRK03657
2-oxo-tetronate isomerase;
6-162 2.12e-98

2-oxo-tetronate isomerase;


Pssm-ID: 235149  Cd Length: 170  Bit Score: 281.01  E-value: 2.12e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129496    6 DKIVQLVDTDTIENLTSALSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDQAKMKILSVSQQSLER 85
Cdd:PRK03657   1 DKIVQLADADTIENLTKALSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDEAKMKILSVSQQSLER 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129496   86 YSAVSEKVAAEMATGAIERADADVSIAITGYGGPEGGEDGTPAGTVWFAWHIKGQNYTAVMHFAGDCETVLALAVRF 162
Cdd:PRK03657  81 YSAVSEAVVAEMATGAIERADADISIAISGYGGPEGGEDGTPAGTVWFAWNIKGQTYTARMHFAGDCETVLAKAVRF 157
PncC_domain TIGR00199
amidohydrolase, PncC family; CinA is a DNA damage- or competence-inducible protein that is ...
24-162 2.80e-72

amidohydrolase, PncC family; CinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species. Several bacterial species have a protein consisting largely of the C-terminal domain of CinA but lacking the N-terminal domain, including nicotinamide mononucleotide (NMN) deamidase (3.5.1.42) proteins PncC in Shewanella oneidensis and ygaD in E. coli. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129303 [Multi-domain]  Cd Length: 146  Bit Score: 214.19  E-value: 2.80e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129496    24 LSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDQAKMKILSVSQQSLERYSAVSEKVAAEMATGAIE 103
Cdd:TIGR00199   1 LSERLKALGLTVATAESCTGGLLAHALTDISGASKYFGGGVVCYTNQVKINLLGVSQETLARFGAVSEECAAEMALGVKE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129496   104 RADADVSIAITGYGGPEGGEDGTPAGTVWFAWHI-KGQNYTAVMHFAGDCETVLALAVRF 162
Cdd:TIGR00199  81 RFGADVGIAISGIAGPDGGEEEKPGGTVWFIWIIaKGQAYTAEMHFAGDRETIRALAVRY 140
PncC COG1546
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; ...
17-162 9.72e-55

Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; Nicotinamide mononucleotide (NMN) deamidase PncC is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 441155  Cd Length: 154  Bit Score: 169.84  E-value: 9.72e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129496  17 IENLTSALSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDQAKMKILSVSQQSLERYSAVSEKVAAE 96
Cdd:COG1546   1 LESLAEVVGELLRERGLTLATAESCTGGLIAAALTDVPGSSAVFDGGFVTYSNEAKEELLGVPAETLEKHGAVSEEVARE 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129496  97 MATGAIERADADVSIAITGYGGPEGGEDGTPAGTVWFAWHIKGQNYTAVMHFAGDCETVLALAVRF 162
Cdd:COG1546  81 MAEGARRLSGADIAVAVTGIAGPGGGTPGKPVGTVYIALAGPGGVVVRRLHFGGDREAVREQAVRA 146
CinA pfam02464
Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, ...
17-162 1.71e-50

Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, and is thought to be specifically required at some stage in the process of transformation. This Pfam family consists of putative competence-damaged proteins from the cin operon. Some members of this family have nicotinamide mononucleotide (NMN) deamidase activity.


Pssm-ID: 460565  Cd Length: 155  Bit Score: 159.24  E-value: 1.71e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129496    17 IENLTSALSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDQAKMKILSVSQQSLERYSAVSEKVAAE 96
Cdd:pfam02464   1 LESLAEEVGKLLKARGLTLATAESCTGGLLAAALTSVPGASDVFLGGVVTYSNEAKRELLGVPPETLEEHGAVSEEVARE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16129496    97 MATGAIERADADVSIAITGYGGPEGGEDGTPAGTVWFAWHIKGQNYTAVMHFAGDCETVLALAVRF 162
Cdd:pfam02464  81 MAEGARKRLGADIGVAITGIAGPSGGTEGKPVGTVYIAIAGPGGTVTRRLNFGGDREAIREQAVVA 146
PRK03661 PRK03661
nicotinamide-nucleotide amidase;
20-162 6.65e-41

nicotinamide-nucleotide amidase;


Pssm-ID: 179627  Cd Length: 164  Bit Score: 135.14  E-value: 6.65e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129496   20 LTSALSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDQAKMKILSVSQQSLERYSAVSEKVAAEMAT 99
Cdd:PRK03661   9 LSEQVGQALKARGATVTTAESCTGGWVAKVITDIAGSSAWFERGFVTYSNEAKAQMIGVREETLAQHGAVSEPVVVEMAI 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129496  100 GAIERADADVSIAITGYGGPEGGEDGTPAGTVWFAWHIK-GQNYTAVMHFAGDCETVLALAVRF 162
Cdd:PRK03661  89 GALKAARADYAVSISGIAGPDGGSEEKPVGTVWFGFASAsGEGITRRECFSGDRDAVRRQATAY 152
PRK00549 PRK00549
competence damage-inducible protein A; Provisional
12-160 1.86e-34

competence damage-inducible protein A; Provisional


Pssm-ID: 234789 [Multi-domain]  Cd Length: 414  Bit Score: 124.90  E-value: 1.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129496   12 VDTDTIENLTSALsqrLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDQAKMKILSVSQQSLERYSAVSE 91
Cdd:PRK00549 254 YDEDSLEEVVAKL---LKEKGLTIATAESCTGGLLAARLTDFPGSSSYFKGGVVTYSNEAKAKLLGVPPETLEEHGAVSE 330
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129496   92 KVAAEMATGAIERADADVSIAITGYGGPEGGEDGTPAGTVWFAWHIKGQN-YTAVMHFAGDCETVLALAV 160
Cdd:PRK00549 331 ETAEEMAEGARKLLGADIGISITGVAGPDGGTEEKPVGTVYIGLATPGGEtVVKELILGGSRSDIRERAV 400
cinA_nterm TIGR00200
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ...
18-151 3.52e-20

competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 161761 [Multi-domain]  Cd Length: 413  Bit Score: 86.11  E-value: 3.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129496    18 ENLTSALSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDQAKMKILSVSQQSLERYSAVSEKVAAEM 97
Cdd:TIGR00200 258 EGLPAQISRELQERGFTLTLAESFTGGLLALQLTDHSGASKLFAGGVPLYANEVKPSQLGVLAETAHWIGAVSANHAAGL 337
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 16129496    98 ATGAIERADADVSIAITGYGGPeGGEDGTPAGTVWFAWHIKGQNYTAVMHFAGD 151
Cdd:TIGR00200 338 ALGVSGFEGEDLGIALTGPAGP-DFAERVRFGTVRYGLAIRQEVAMHALNMLGR 390
 
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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