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Conserved domains on  [gi|515085788|ref|WP_016715434|]
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MULTISPECIES: CinA family protein [Pseudomonas]

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]; ...
4-157 1.81e-71

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: 211.83  E-value: 1.81e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515085788   4 ITTLATRLGKHLRRLSAQVTTAESCTGGGIAEAITRVPGSSAWFEAGYVTYSNAQKTRQLGVPEVLFGQVGAVSQEVVEA 83
Cdd:COG1546    1 LESLAEVVGELLRERGLTLATAESCTGGLIAAALTDVPGSSAVFDGGFVTYSNEAKEELLGVPAETLEKHGAVSEEVARE 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515085788  84 MVRGAQAASGARFAVAVSGVAGPDGGSPAKPVGTVWLAWGDGSRVFSERRQFDGDREAVRRQTVIAALDGLLQL 157
Cdd:COG1546   81 MAEGARRLSGADIAVAVTGIAGPGGGTPGKPVGTVYIALAGPGGVVVRRLHFGGDREAVREQAVRAALDLLREL 154
 
Name Accession Description Interval E-value
PncC COG1546
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; ...
4-157 1.81e-71

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: 211.83  E-value: 1.81e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515085788   4 ITTLATRLGKHLRRLSAQVTTAESCTGGGIAEAITRVPGSSAWFEAGYVTYSNAQKTRQLGVPEVLFGQVGAVSQEVVEA 83
Cdd:COG1546    1 LESLAEVVGELLRERGLTLATAESCTGGLIAAALTDVPGSSAVFDGGFVTYSNEAKEELLGVPAETLEKHGAVSEEVARE 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515085788  84 MVRGAQAASGARFAVAVSGVAGPDGGSPAKPVGTVWLAWGDGSRVFSERRQFDGDREAVRRQTVIAALDGLLQL 157
Cdd:COG1546   81 MAEGARRLSGADIAVAVTGIAGPGGGTPGKPVGTVYIALAGPGGVVVRRLHFGGDREAVREQAVRAALDLLREL 154
PRK03661 PRK03661
nicotinamide-nucleotide amidase;
4-156 1.48e-61

nicotinamide-nucleotide amidase;


Pssm-ID: 179627  Cd Length: 164  Bit Score: 187.15  E-value: 1.48e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515085788   4 ITTLATRLGKHLRRLSAQVTTAESCTGGGIAEAITRVPGSSAWFEAGYVTYSNAQKTRQLGVPEVLFGQVGAVSQEVVEA 83
Cdd:PRK03661   6 LMQLSEQVGQALKARGATVTTAESCTGGWVAKVITDIAGSSAWFERGFVTYSNEAKAQMIGVREETLAQHGAVSEPVVVE 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515085788  84 MVRGAQAASGARFAVAVSGVAGPDGGSPAKPVGTVWLAWGDGS-RVFSERRQFDGDREAVRRQTVIAALDGLLQ 156
Cdd:PRK03661  86 MAIGALKAARADYAVSISGIAGPDGGSEEKPVGTVWFGFASASgEGITRRECFSGDRDAVRRQATAYALQTLWQ 159
CinA pfam02464
Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, ...
4-157 3.08e-60

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: 183.50  E-value: 3.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515085788    4 ITTLATRLGKHLRRLSAQVTTAESCTGGGIAEAITRVPGSSAWFEAGYVTYSNAQKTRQLGVPEVLFGQVGAVSQEVVEA 83
Cdd:pfam02464   1 LESLAEEVGKLLKARGLTLATAESCTGGLLAAALTSVPGASDVFLGGVVTYSNEAKRELLGVPPETLEEHGAVSEEVARE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515085788   84 MVRGAQAASGARFAVAVSGVAGPDGGSPAKPVGTVWLAWGDGSRVFSERRQFDGDREAVRRQTVIAALDGLLQL 157
Cdd:pfam02464  81 MAEGARKRLGADIGVAITGIAGPSGGTEGKPVGTVYIAIAGPGGTVTRRLNFGGDREAIREQAVVAALELLRRL 154
PncC_domain TIGR00199
amidohydrolase, PncC family; CinA is a DNA damage- or competence-inducible protein that is ...
11-155 2.36e-44

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: 142.93  E-value: 2.36e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515085788   11 LGKHLRRLSAQVTTAESCTGGGIAEAITRVPGSSAWFEAGYVTYSNAQKTRQLGVPEVLFGQVGAVSQEVVEAMVRGAQA 90
Cdd:TIGR00199   1 LSERLKALGLTVATAESCTGGLLAHALTDISGASKYFGGGVVCYTNQVKINLLGVSQETLARFGAVSEECAAEMALGVKE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515085788   91 ASGARFAVAVSGVAGPDGGSPAKPVGTVWLAW-GDGSRVFSERRQFDGDREAVRRQTVIAALDGLL 155
Cdd:TIGR00199  81 RFGADVGIAISGIAGPDGGEEEKPGGTVWFIWiIAKGQAYTAEMHFAGDRETIRALAVRYALHQLL 146
 
Name Accession Description Interval E-value
PncC COG1546
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; ...
4-157 1.81e-71

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: 211.83  E-value: 1.81e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515085788   4 ITTLATRLGKHLRRLSAQVTTAESCTGGGIAEAITRVPGSSAWFEAGYVTYSNAQKTRQLGVPEVLFGQVGAVSQEVVEA 83
Cdd:COG1546    1 LESLAEVVGELLRERGLTLATAESCTGGLIAAALTDVPGSSAVFDGGFVTYSNEAKEELLGVPAETLEKHGAVSEEVARE 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515085788  84 MVRGAQAASGARFAVAVSGVAGPDGGSPAKPVGTVWLAWGDGSRVFSERRQFDGDREAVRRQTVIAALDGLLQL 157
Cdd:COG1546   81 MAEGARRLSGADIAVAVTGIAGPGGGTPGKPVGTVYIALAGPGGVVVRRLHFGGDREAVREQAVRAALDLLREL 154
PRK03661 PRK03661
nicotinamide-nucleotide amidase;
4-156 1.48e-61

nicotinamide-nucleotide amidase;


Pssm-ID: 179627  Cd Length: 164  Bit Score: 187.15  E-value: 1.48e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515085788   4 ITTLATRLGKHLRRLSAQVTTAESCTGGGIAEAITRVPGSSAWFEAGYVTYSNAQKTRQLGVPEVLFGQVGAVSQEVVEA 83
Cdd:PRK03661   6 LMQLSEQVGQALKARGATVTTAESCTGGWVAKVITDIAGSSAWFERGFVTYSNEAKAQMIGVREETLAQHGAVSEPVVVE 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515085788  84 MVRGAQAASGARFAVAVSGVAGPDGGSPAKPVGTVWLAWGDGS-RVFSERRQFDGDREAVRRQTVIAALDGLLQ 156
Cdd:PRK03661  86 MAIGALKAARADYAVSISGIAGPDGGSEEKPVGTVWFGFASASgEGITRRECFSGDRDAVRRQATAYALQTLWQ 159
CinA pfam02464
Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, ...
4-157 3.08e-60

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: 183.50  E-value: 3.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515085788    4 ITTLATRLGKHLRRLSAQVTTAESCTGGGIAEAITRVPGSSAWFEAGYVTYSNAQKTRQLGVPEVLFGQVGAVSQEVVEA 83
Cdd:pfam02464   1 LESLAEEVGKLLKARGLTLATAESCTGGLLAAALTSVPGASDVFLGGVVTYSNEAKRELLGVPPETLEEHGAVSEEVARE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515085788   84 MVRGAQAASGARFAVAVSGVAGPDGGSPAKPVGTVWLAWGDGSRVFSERRQFDGDREAVRRQTVIAALDGLLQL 157
Cdd:pfam02464  81 MAEGARKRLGADIGVAITGIAGPSGGTEGKPVGTVYIAIAGPGGTVTRRLNFGGDREAIREQAVVAALELLRRL 154
PRK00549 PRK00549
competence damage-inducible protein A; Provisional
5-157 3.47e-47

competence damage-inducible protein A; Provisional


Pssm-ID: 234789 [Multi-domain]  Cd Length: 414  Bit Score: 157.64  E-value: 3.47e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515085788   5 TTLATRLGKHLRRLSAQVTTAESCTGGGIAEAITRVPGSSAWFEAGYVTYSNAQKTRQLGVPEVLFGQVGAVSQEVVEAM 84
Cdd:PRK00549 257 DSLEEVVAKLLKEKGLTIATAESCTGGLLAARLTDFPGSSSYFKGGVVTYSNEAKAKLLGVPPETLEEHGAVSEETAEEM 336
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515085788  85 VRGAQAASGARFAVAVSGVAGPDGGSPAKPVGTVWLA-WGDGSRVFSERRQFDGDREAVRRQTVIAALDGLLQL 157
Cdd:PRK00549 337 AEGARKLLGADIGISITGVAGPDGGTEEKPVGTVYIGlATPGGETVVKELILGGSRSDIRERAVTYALDLLRRA 410
PncC_domain TIGR00199
amidohydrolase, PncC family; CinA is a DNA damage- or competence-inducible protein that is ...
11-155 2.36e-44

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: 142.93  E-value: 2.36e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515085788   11 LGKHLRRLSAQVTTAESCTGGGIAEAITRVPGSSAWFEAGYVTYSNAQKTRQLGVPEVLFGQVGAVSQEVVEAMVRGAQA 90
Cdd:TIGR00199   1 LSERLKALGLTVATAESCTGGLLAHALTDISGASKYFGGGVVCYTNQVKINLLGVSQETLARFGAVSEECAAEMALGVKE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515085788   91 ASGARFAVAVSGVAGPDGGSPAKPVGTVWLAW-GDGSRVFSERRQFDGDREAVRRQTVIAALDGLL 155
Cdd:TIGR00199  81 RFGADVGIAISGIAGPDGGEEEKPGGTVWFIWiIAKGQAYTAEMHFAGDRETIRALAVRYALHQLL 146
PRK03657 PRK03657
2-oxo-tetronate isomerase;
2-157 3.60e-29

2-oxo-tetronate isomerase;


Pssm-ID: 235149  Cd Length: 170  Bit Score: 104.97  E-value: 3.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515085788   2 DLITTLATRLGKHLRRLSAQVTTAESCTGGGIAEAITRVPGSSAWFEAGYVTYSNAQKTRQLGVPEVLFGQVGAVSQEVV 81
Cdd:PRK03657  10 DTIENLTKALSQRLIADQLRLTTAESCTGGKLASALCAAEDTPKFYGAGFVTFTDEAKMKILSVSQQSLERYSAVSEAVV 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515085788  82 EAMVRGAQAASGARFAVAVSGVAGPDGGSPAKPVGTVWLAWGDGSRVFSERRQFDGDREAVRRQTVIAALDGLLQL 157
Cdd:PRK03657  90 AEMATGAIERADADISIAISGYGGPEGGEDGTPAGTVWFAWNIKGQTYTARMHFAGDCETVLAKAVRFALAQLLQL 165
cinA_nterm TIGR00200
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ...
5-157 2.54e-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: 2.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515085788    5 TTLATRLGKHLRRLSAQVTTAESCTGGGIAEAITRVPGSSAWFEAGYVTYSNAQKTRQLGVPEVLFGQVGAVSQEVVEAM 84
Cdd:TIGR00200 258 EGLPAQISRELQERGFTLTLAESFTGGLLALQLTDHSGASKLFAGGVPLYANEVKPSQLGVLAETAHWIGAVSANHAAGL 337
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515085788   85 VRGAQAASGARFAVAVSGVAGPDgGSPAKPVGTVWLAWGDGSRVFSERRQFDGDREAVRRQTVIAALDGLLQL 157
Cdd:TIGR00200 338 ALGVSGFEGEDLGIALTGPAGPD-FAERVRFGTVRYGLAIRQEVAMHALNMLGRRLGIRDIAAEHGWIEVVES 409
 
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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