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Conserved domains on  [gi|15598814|ref|NP_252308|]
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hypothetical protein PA3618 [Pseudomonas aeruginosa PAO1]

Protein Classification

CinA family protein( domain architecture ID 10003960)

competence/damage-inducible CinA family protein containing only the C-terminal CinA domain, similar to Pseudomonas putida nicotinamide-nucleotide (NMN) amidohydrolase PncC

PubMed:  7538190|21953451

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PncC COG1546
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; ...
8-161 6.94e-73

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: 215.68  E-value: 6.94e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598814   8 LTALAARLGESLRYLGEQVSTAESCTGGGIAEAITRIPGSSGWFEAGYVTYSNRQKTLQLEVPESLFPAVGAVSREVVEA 87
Cdd:COG1546   1 LESLAEVVGELLRERGLTLATAESCTGGLIAAALTDVPGSSAVFDGGFVTYSNEAKEELLGVPAETLEKHGAVSEEVARE 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598814  88 MVRGAQRHSGARFAVAVSGVAGPDGGSPEKPVGTVWLAWADGERLVSERCQFNGDRDAVRRQTVATALTGLLRM 161
Cdd:COG1546  81 MAEGARRLSGADIAVAVTGIAGPGGGTPGKPVGTVYIALAGPGGVVVRRLHFGGDREAVREQAVRAALDLLREL 154
 
Name Accession Description Interval E-value
PncC COG1546
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; ...
8-161 6.94e-73

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: 215.68  E-value: 6.94e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598814   8 LTALAARLGESLRYLGEQVSTAESCTGGGIAEAITRIPGSSGWFEAGYVTYSNRQKTLQLEVPESLFPAVGAVSREVVEA 87
Cdd:COG1546   1 LESLAEVVGELLRERGLTLATAESCTGGLIAAALTDVPGSSAVFDGGFVTYSNEAKEELLGVPAETLEKHGAVSEEVARE 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598814  88 MVRGAQRHSGARFAVAVSGVAGPDGGSPEKPVGTVWLAWADGERLVSERCQFNGDRDAVRRQTVATALTGLLRM 161
Cdd:COG1546  81 MAEGARRLSGADIAVAVTGIAGPGGGTPGKPVGTVYIALAGPGGVVVRRLHFGGDREAVREQAVRAALDLLREL 154
PRK03661 PRK03661
nicotinamide-nucleotide amidase;
1-159 1.26e-62

nicotinamide-nucleotide amidase;


Pssm-ID: 179627  Cd Length: 164  Bit Score: 190.23  E-value: 1.26e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598814    1 MTlmESDLTALAARLGESLRYLGEQVSTAESCTGGGIAEAITRIPGSSGWFEAGYVTYSNRQKTLQLEVPESLFPAVGAV 80
Cdd:PRK03661   1 MT--DSELMQLSEQVGQALKARGATVTTAESCTGGWVAKVITDIAGSSAWFERGFVTYSNEAKAQMIGVREETLAQHGAV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598814   81 SREVVEAMVRGAQRHSGARFAVAVSGVAGPDGGSPEKPVGTVWLAWADGE-RLVSERCQFNGDRDAVRRQTVATALTGLL 159
Cdd:PRK03661  79 SEPVVVEMAIGALKAARADYAVSISGIAGPDGGSEEKPVGTVWFGFASASgEGITRRECFSGDRDAVRRQATAYALQTLW 158
CinA pfam02464
Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, ...
8-161 1.96e-62

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: 189.28  E-value: 1.96e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598814     8 LTALAARLGESLRYLGEQVSTAESCTGGGIAEAITRIPGSSGWFEAGYVTYSNRQKTLQLEVPESLFPAVGAVSREVVEA 87
Cdd:pfam02464   1 LESLAEEVGKLLKARGLTLATAESCTGGLLAAALTSVPGASDVFLGGVVTYSNEAKRELLGVPPETLEEHGAVSEEVARE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598814    88 MVRGAQRHSGARFAVAVSGVAGPDGGSPEKPVGTVWLAWADGERLVSERCQFNGDRDAVRRQTVATALTGLLRM 161
Cdd:pfam02464  81 MAEGARKRLGADIGVAITGIAGPSGGTEGKPVGTVYIAIAGPGGTVTRRLNFGGDREAIREQAVVAALELLRRL 154
PncC_domain TIGR00199
amidohydrolase, PncC family; CinA is a DNA damage- or competence-inducible protein that is ...
15-159 1.17e-46

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: 149.09  E-value: 1.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598814    15 LGESLRYLGEQVSTAESCTGGGIAEAITRIPGSSGWFEAGYVTYSNRQKTLQLEVPESLFPAVGAVSREVVEAMVRGAQR 94
Cdd:TIGR00199   1 LSERLKALGLTVATAESCTGGLLAHALTDISGASKYFGGGVVCYTNQVKINLLGVSQETLARFGAVSEECAAEMALGVKE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598814    95 HSGARFAVAVSGVAGPDGGSPEKPVGTVWLAWAD--GERLVsERCQFNGDRDAVRRQTVATALTGLL 159
Cdd:TIGR00199  81 RFGADVGIAISGIAGPDGGEEEKPGGTVWFIWIIakGQAYT-AEMHFAGDRETIRALAVRYALHQLL 146
 
Name Accession Description Interval E-value
PncC COG1546
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; ...
8-161 6.94e-73

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: 215.68  E-value: 6.94e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598814   8 LTALAARLGESLRYLGEQVSTAESCTGGGIAEAITRIPGSSGWFEAGYVTYSNRQKTLQLEVPESLFPAVGAVSREVVEA 87
Cdd:COG1546   1 LESLAEVVGELLRERGLTLATAESCTGGLIAAALTDVPGSSAVFDGGFVTYSNEAKEELLGVPAETLEKHGAVSEEVARE 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598814  88 MVRGAQRHSGARFAVAVSGVAGPDGGSPEKPVGTVWLAWADGERLVSERCQFNGDRDAVRRQTVATALTGLLRM 161
Cdd:COG1546  81 MAEGARRLSGADIAVAVTGIAGPGGGTPGKPVGTVYIALAGPGGVVVRRLHFGGDREAVREQAVRAALDLLREL 154
PRK03661 PRK03661
nicotinamide-nucleotide amidase;
1-159 1.26e-62

nicotinamide-nucleotide amidase;


Pssm-ID: 179627  Cd Length: 164  Bit Score: 190.23  E-value: 1.26e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598814    1 MTlmESDLTALAARLGESLRYLGEQVSTAESCTGGGIAEAITRIPGSSGWFEAGYVTYSNRQKTLQLEVPESLFPAVGAV 80
Cdd:PRK03661   1 MT--DSELMQLSEQVGQALKARGATVTTAESCTGGWVAKVITDIAGSSAWFERGFVTYSNEAKAQMIGVREETLAQHGAV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598814   81 SREVVEAMVRGAQRHSGARFAVAVSGVAGPDGGSPEKPVGTVWLAWADGE-RLVSERCQFNGDRDAVRRQTVATALTGLL 159
Cdd:PRK03661  79 SEPVVVEMAIGALKAARADYAVSISGIAGPDGGSEEKPVGTVWFGFASASgEGITRRECFSGDRDAVRRQATAYALQTLW 158
CinA pfam02464
Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, ...
8-161 1.96e-62

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: 189.28  E-value: 1.96e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598814     8 LTALAARLGESLRYLGEQVSTAESCTGGGIAEAITRIPGSSGWFEAGYVTYSNRQKTLQLEVPESLFPAVGAVSREVVEA 87
Cdd:pfam02464   1 LESLAEEVGKLLKARGLTLATAESCTGGLLAAALTSVPGASDVFLGGVVTYSNEAKRELLGVPPETLEEHGAVSEEVARE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598814    88 MVRGAQRHSGARFAVAVSGVAGPDGGSPEKPVGTVWLAWADGERLVSERCQFNGDRDAVRRQTVATALTGLLRM 161
Cdd:pfam02464  81 MAEGARKRLGADIGVAITGIAGPSGGTEGKPVGTVYIAIAGPGGTVTRRLNFGGDREAIREQAVVAALELLRRL 154
PRK00549 PRK00549
competence damage-inducible protein A; Provisional
11-161 1.55e-47

competence damage-inducible protein A; Provisional


Pssm-ID: 234789 [Multi-domain]  Cd Length: 414  Bit Score: 159.18  E-value: 1.55e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598814   11 LAARLGESLRYLGEQVSTAESCTGGGIAEAITRIPGSSGWFEAGYVTYSNRQKTLQLEVPESLFPAVGAVSREVVEAMVR 90
Cdd:PRK00549 259 LEEVVAKLLKEKGLTIATAESCTGGLLAARLTDFPGSSSYFKGGVVTYSNEAKAKLLGVPPETLEEHGAVSEETAEEMAE 338
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598814   91 GAQRHSGARFAVAVSGVAGPDGGSPEKPVGTVWLAWAD-GERLVSERCQFNGDRDAVRRQTVATALTGLLRM 161
Cdd:PRK00549 339 GARKLLGADIGISITGVAGPDGGTEEKPVGTVYIGLATpGGETVVKELILGGSRSDIRERAVTYALDLLRRA 410
PncC_domain TIGR00199
amidohydrolase, PncC family; CinA is a DNA damage- or competence-inducible protein that is ...
15-159 1.17e-46

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: 149.09  E-value: 1.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598814    15 LGESLRYLGEQVSTAESCTGGGIAEAITRIPGSSGWFEAGYVTYSNRQKTLQLEVPESLFPAVGAVSREVVEAMVRGAQR 94
Cdd:TIGR00199   1 LSERLKALGLTVATAESCTGGLLAHALTDISGASKYFGGGVVCYTNQVKINLLGVSQETLARFGAVSEECAAEMALGVKE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598814    95 HSGARFAVAVSGVAGPDGGSPEKPVGTVWLAWAD--GERLVsERCQFNGDRDAVRRQTVATALTGLL 159
Cdd:TIGR00199  81 RFGADVGIAISGIAGPDGGEEEKPGGTVWFIWIIakGQAYT-AEMHFAGDRETIRALAVRYALHQLL 146
PRK03657 PRK03657
2-oxo-tetronate isomerase;
10-159 4.43e-27

2-oxo-tetronate isomerase;


Pssm-ID: 235149  Cd Length: 170  Bit Score: 99.97  E-value: 4.43e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598814   10 ALAARLGESLRYLGEQVSTAESCTGGGIAEAITRIPGSSGWFEAGYVTYSNRQKTLQLEVPESLFPAVGAVSREVVEAMV 89
Cdd:PRK03657  14 NLTKALSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDEAKMKILSVSQQSLERYSAVSEAVVAEMA 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598814   90 RGAQRHSGARFAVAVSGVAGPDGGSPEKPVGTVWLAWADGERLVSERCQFNGDRDAVRRQTVATALTGLL 159
Cdd:PRK03657  94 TGAIERADADISIAISGYGGPEGGEDGTPAGTVWFAWNIKGQTYTARMHFAGDCETVLAKAVRFALAQLL 163
cinA_nterm TIGR00200
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ...
7-160 2.79e-22

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: 91.89  E-value: 2.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598814     7 DLTALAARLGESLRYLGEQVSTAESCTGGGIAEAITRIPGSSGWFEAGYVTYSNRQKTLQLEVPESLFPAVGAVSREVVE 86
Cdd:TIGR00200 256 DTEGLPAQISRELQERGFTLTLAESFTGGLLALQLTDHSGASKLFAGGVPLYANEVKPSQLGVLAETAHWIGAVSANHAA 335
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598814    87 AMVRGAQRHSGARFAVAVSGVAGPDgGSPEKPVGTVWLAWADGERLVSERCQFNGDRDAVRRQTVATALTGLLR 160
Cdd:TIGR00200 336 GLALGVSGFEGEDLGIALTGPAGPD-FAERVRFGTVRYGLAIRQEVAMHALNMLGRRLGIRDIAAEHGWIEVVE 408
 
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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