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Conserved domains on  [gi|499243514|ref|WP_010941054|]
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DNA repair protein RadC [Geobacter sulfurreducens]

Protein Classification

JAB domain-containing protein( domain architecture ID 11477685)

JAB or Mpr1p, Pad1p N-terminal (MPN) domain-containing protein contains the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, which is involved in zinc ion coordination; a function as a nuclease has been suggested

Gene Ontology:  GO:0046872|GO:0008237|GO:0006508

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK00024 PRK00024
DNA repair protein RadC;
5-229 1.77e-119

DNA repair protein RadC;


:

Pssm-ID: 178801 [Multi-domain]  Cd Length: 224  Bit Score: 338.97  E-value: 1.77e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514   5 IKAWPEDERPREKLLRRGAPVLSDAELLALIIRTGdsVTGRSAIDLGRALLQECGDLRTLAGATVSELCAVKGMGTAKAT 84
Cdd:PRK00024   3 IKDWPEEERPRERLLKYGAAALSDAELLAILLRTG--TKGKSVLDLARELLQRFGSLRGLLDASLEELQSIKGIGPAKAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514  85 SIKAALEMASRINSERLMIcSERFTSPEQVYNHYHYAFRDRRKEYFMALLLDGKNRIMREIQVSEGSLNQSIVHPREVFN 164
Cdd:PRK00024  81 QLKAALELARRILAERLRE-REVLLSPEDVADYLMAELRDEEQEHFVVLFLDTKNRVIADEELFIGTLNSSIVHPREIVK 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499243514 165 PAVRESAAAVILVHNHPTGDPAPSREDLEITRRLREAGDIMGIRVLDHIIIGDGRFTSFVSAGLL 229
Cdd:PRK00024 160 RALKLNAAALILAHNHPSGDPEPSQADILITKRLKEAGELLGIRLLDHIIIGDGEYVSFAERGLL 224
 
Name Accession Description Interval E-value
PRK00024 PRK00024
DNA repair protein RadC;
5-229 1.77e-119

DNA repair protein RadC;


Pssm-ID: 178801 [Multi-domain]  Cd Length: 224  Bit Score: 338.97  E-value: 1.77e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514   5 IKAWPEDERPREKLLRRGAPVLSDAELLALIIRTGdsVTGRSAIDLGRALLQECGDLRTLAGATVSELCAVKGMGTAKAT 84
Cdd:PRK00024   3 IKDWPEEERPRERLLKYGAAALSDAELLAILLRTG--TKGKSVLDLARELLQRFGSLRGLLDASLEELQSIKGIGPAKAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514  85 SIKAALEMASRINSERLMIcSERFTSPEQVYNHYHYAFRDRRKEYFMALLLDGKNRIMREIQVSEGSLNQSIVHPREVFN 164
Cdd:PRK00024  81 QLKAALELARRILAERLRE-REVLLSPEDVADYLMAELRDEEQEHFVVLFLDTKNRVIADEELFIGTLNSSIVHPREIVK 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499243514 165 PAVRESAAAVILVHNHPTGDPAPSREDLEITRRLREAGDIMGIRVLDHIIIGDGRFTSFVSAGLL 229
Cdd:PRK00024 160 RALKLNAAALILAHNHPSGDPEPSQADILITKRLKEAGELLGIRLLDHIIIGDGEYVSFAERGLL 224
RadC COG2003
DNA repair protein RadC, contains a helix-hairpin-helix DNA-binding motif [Replication, ...
 4-229 1.20e-113

DNA repair protein RadC, contains a helix-hairpin-helix DNA-binding motif [Replication, recombination and repair];


Pssm-ID: 441606 [Multi-domain]  Cd Length: 224  Bit Score: 324.32  E-value: 1.20e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514   4 GIKAWPEDERPREKLLRRGAPVLSDAELLALIIRTGdsVTGRSAIDLGRALLQECGDLRTLAGATVSELCAVKGMGTAKA 83
Cdd:COG2003    2 KIKDLPHRERPRERLLAKGAAALSDAELLAILLRTG--TPGKDAVELAKELLARFGSLRGLLRASVEELRKIKGIGEAKA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514  84 TSIKAALEMASRINSERLMIcSERFTSPEQVYNHYHYAFRDRRKEYFMALLLDGKNRIMREIQVSEGSLNQSIVHPREVF 163
Cdd:COG2003   80 AQLKAALELGRRLLREELEE-RPVISSPEDVADYLRARLAHLPREVFRVLFLDTKNRLIADEELSIGTLNHTPVYPREVF 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499243514 164 NPAVRESAAAVILVHNHPTGDPAPSREDLEITRRLREAGDIMGIRVLDHIIIGDGRFTSFVSAGLL 229
Cdd:COG2003  159 KRALRLNAAAIILAHNHPSGDPEPSRADIELTRRLKEAGELLGIRLLDHIIIGDGGYVSFAEEGLL 224
radc TIGR00608
DNA repair protein radc; The genes in this family for which the functions are known have an as ...
 13-229 1.28e-74

DNA repair protein radc; The genes in this family for which the functions are known have an as yet porrly defined role in determining sensitivity to DNA damaging agents such as UV irradiation. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273171 [Multi-domain]  Cd Length: 218  Bit Score: 225.01  E-value: 1.28e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514   13 RPREKLLRRGAPVLSDAELLALIIRTGdSVTGRSAIDLGRALLQECGD---LRTLAGATVSELCAVKGMGTAKATSIKAA 89
Cdd:TIGR00608   1 MPREKLLKFGAEALSDYELLAIILRTG-TPKGLDVLSLSKRLLDVFGRqdsLGHLLSAPPEELSSVPGIGEAKAIQLKAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514   90 LEMASRINSERLMicsERFT--SPEQVYNHYHYAFRDRRKEYFMALLLDGKNRIMREIQVSEGSLNQSIVHPREVFNPAV 167
Cdd:TIGR00608  80 VELAKRYAKSRML---ERPVirSPEAAAEFLHTDLAHETREHFMVLFLDRKNRLIAKEVVFIGTVNHVPVHPREIFKEAL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499243514  168 RESAAAVILVHNHPTGDPAPSREDLEITRRLREAGDIMGIRVLDHIIIGDGRFTSFVSAGLL 229
Cdd:TIGR00608 157 KLSASALILAHNHPSGEPSPSQEDILITERLRKAAELLGIELLDHLIIGKGRYVSFREEGLL 218
RadC pfam04002
RadC-like JAB domain; A family of proteins present widely across the bacteria. This family was ...
 108-220 1.06e-60

RadC-like JAB domain; A family of proteins present widely across the bacteria. This family was named initially with reference to the E. coli radC102 mutation which suggested that RadC was involved in repair of DNA lesions. However the relevant mutation has subsequently been shown to be in recG, where radC is in fact an allele of recG. In addition, a personal communication from Claverys, J-P, et al, indicates a total failure of all attempts to characterize a radiation-related function for RadC in Streptococcus pneumoniae, suggesting that it is not involved in repair of DNA lesions, in recombination during transformation, in gene conversion, nor in mismatch repair. Computational analysis, however, provides a possible function. The RadC-like family belong to the JAB superfamily of metalloproteins. The domain shows fusions to an N-terminal Helix-hairpin-Helix (HhH) domain in most instances. Other domain combinations include fusions to the anti-restriction module ArdC, the DinG/RAD3-like superfamily II helicases and the DNAG-like primase. In some bacteria, closely related DinG/Rad3- like superfamily II helicases are fused to a 3'-5' exonuclease in the same position as the RadC-like JAB domain. These conserved domain associations lead to the hypothesis that the RadC-like JAB domains might function as a nuclease.


Pssm-ID: 461124  Cd Length: 113  Bit Score: 186.07  E-value: 1.06e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514  108 FTSPEQVYNHYHYAFRDRRKEYFMALLLDGKNRIMREIQVSEGSLNQSIVHPREVFNPAVRESAAAVILVHNHPTGDPAP 187
Cdd:pfam04002   1 ITSPEDVAEYLMEELRDLDQEVFRVLFLDTKNRLIADEELSEGTLNSTLVHPREIFKRALRLNAAAVILAHNHPSGDPEP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 499243514  188 SREDLEITRRLREAGDIMGIRVLDHIIIGDGRF 220
Cdd:pfam04002  81 SREDIELTRRLKEAGELLGIRLLDHIIIGDGGY 113
MPN_DUF2466 cd08071
Mov34/MPN/PAD-1 family; Mov34 DUF2466 (also known as DNA repair protein RadC) domain of ...
 112-223 7.41e-60

Mov34/MPN/PAD-1 family; Mov34 DUF2466 (also known as DNA repair protein RadC) domain of unknown function contains the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity. However, to date, the name RadC has been misleading and no function has been determined.


Pssm-ID: 163702  Cd Length: 113  Bit Score: 183.73  E-value: 7.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514 112 EQVYNHYHYAFRDRRKEYFMALLLDGKNRIMREIQVSEGSLNQSIVHPREVFNPAVRESAAAVILVHNHPTGDPAPSRED 191
Cdd:cd08071    1 EDVAEYLREELGDLDQEEFVVLLLDTKNRLIAVETISVGTLNSSLVHPREIFKEALRHNAAAIILAHNHPSGDPTPSRED 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 499243514 192 LEITRRLREAGDIMGIRVLDHIIIGDGRFTSF 223
Cdd:cd08071   81 IELTKRLKEAGELLGIRLLDHIIVGDGGYFSF 112
 
Name Accession Description Interval E-value
PRK00024 PRK00024
DNA repair protein RadC;
5-229 1.77e-119

DNA repair protein RadC;


Pssm-ID: 178801 [Multi-domain]  Cd Length: 224  Bit Score: 338.97  E-value: 1.77e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514   5 IKAWPEDERPREKLLRRGAPVLSDAELLALIIRTGdsVTGRSAIDLGRALLQECGDLRTLAGATVSELCAVKGMGTAKAT 84
Cdd:PRK00024   3 IKDWPEEERPRERLLKYGAAALSDAELLAILLRTG--TKGKSVLDLARELLQRFGSLRGLLDASLEELQSIKGIGPAKAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514  85 SIKAALEMASRINSERLMIcSERFTSPEQVYNHYHYAFRDRRKEYFMALLLDGKNRIMREIQVSEGSLNQSIVHPREVFN 164
Cdd:PRK00024  81 QLKAALELARRILAERLRE-REVLLSPEDVADYLMAELRDEEQEHFVVLFLDTKNRVIADEELFIGTLNSSIVHPREIVK 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499243514 165 PAVRESAAAVILVHNHPTGDPAPSREDLEITRRLREAGDIMGIRVLDHIIIGDGRFTSFVSAGLL 229
Cdd:PRK00024 160 RALKLNAAALILAHNHPSGDPEPSQADILITKRLKEAGELLGIRLLDHIIIGDGEYVSFAERGLL 224
RadC COG2003
DNA repair protein RadC, contains a helix-hairpin-helix DNA-binding motif [Replication, ...
 4-229 1.20e-113

DNA repair protein RadC, contains a helix-hairpin-helix DNA-binding motif [Replication, recombination and repair];


Pssm-ID: 441606 [Multi-domain]  Cd Length: 224  Bit Score: 324.32  E-value: 1.20e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514   4 GIKAWPEDERPREKLLRRGAPVLSDAELLALIIRTGdsVTGRSAIDLGRALLQECGDLRTLAGATVSELCAVKGMGTAKA 83
Cdd:COG2003    2 KIKDLPHRERPRERLLAKGAAALSDAELLAILLRTG--TPGKDAVELAKELLARFGSLRGLLRASVEELRKIKGIGEAKA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514  84 TSIKAALEMASRINSERLMIcSERFTSPEQVYNHYHYAFRDRRKEYFMALLLDGKNRIMREIQVSEGSLNQSIVHPREVF 163
Cdd:COG2003   80 AQLKAALELGRRLLREELEE-RPVISSPEDVADYLRARLAHLPREVFRVLFLDTKNRLIADEELSIGTLNHTPVYPREVF 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499243514 164 NPAVRESAAAVILVHNHPTGDPAPSREDLEITRRLREAGDIMGIRVLDHIIIGDGRFTSFVSAGLL 229
Cdd:COG2003  159 KRALRLNAAAIILAHNHPSGDPEPSRADIELTRRLKEAGELLGIRLLDHIIIGDGGYVSFAEEGLL 224
radc TIGR00608
DNA repair protein radc; The genes in this family for which the functions are known have an as ...
 13-229 1.28e-74

DNA repair protein radc; The genes in this family for which the functions are known have an as yet porrly defined role in determining sensitivity to DNA damaging agents such as UV irradiation. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273171 [Multi-domain]  Cd Length: 218  Bit Score: 225.01  E-value: 1.28e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514   13 RPREKLLRRGAPVLSDAELLALIIRTGdSVTGRSAIDLGRALLQECGD---LRTLAGATVSELCAVKGMGTAKATSIKAA 89
Cdd:TIGR00608   1 MPREKLLKFGAEALSDYELLAIILRTG-TPKGLDVLSLSKRLLDVFGRqdsLGHLLSAPPEELSSVPGIGEAKAIQLKAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514   90 LEMASRINSERLMicsERFT--SPEQVYNHYHYAFRDRRKEYFMALLLDGKNRIMREIQVSEGSLNQSIVHPREVFNPAV 167
Cdd:TIGR00608  80 VELAKRYAKSRML---ERPVirSPEAAAEFLHTDLAHETREHFMVLFLDRKNRLIAKEVVFIGTVNHVPVHPREIFKEAL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499243514  168 RESAAAVILVHNHPTGDPAPSREDLEITRRLREAGDIMGIRVLDHIIIGDGRFTSFVSAGLL 229
Cdd:TIGR00608 157 KLSASALILAHNHPSGEPSPSQEDILITERLRKAAELLGIELLDHLIIGKGRYVSFREEGLL 218
RadC pfam04002
RadC-like JAB domain; A family of proteins present widely across the bacteria. This family was ...
 108-220 1.06e-60

RadC-like JAB domain; A family of proteins present widely across the bacteria. This family was named initially with reference to the E. coli radC102 mutation which suggested that RadC was involved in repair of DNA lesions. However the relevant mutation has subsequently been shown to be in recG, where radC is in fact an allele of recG. In addition, a personal communication from Claverys, J-P, et al, indicates a total failure of all attempts to characterize a radiation-related function for RadC in Streptococcus pneumoniae, suggesting that it is not involved in repair of DNA lesions, in recombination during transformation, in gene conversion, nor in mismatch repair. Computational analysis, however, provides a possible function. The RadC-like family belong to the JAB superfamily of metalloproteins. The domain shows fusions to an N-terminal Helix-hairpin-Helix (HhH) domain in most instances. Other domain combinations include fusions to the anti-restriction module ArdC, the DinG/RAD3-like superfamily II helicases and the DNAG-like primase. In some bacteria, closely related DinG/Rad3- like superfamily II helicases are fused to a 3'-5' exonuclease in the same position as the RadC-like JAB domain. These conserved domain associations lead to the hypothesis that the RadC-like JAB domains might function as a nuclease.


Pssm-ID: 461124  Cd Length: 113  Bit Score: 186.07  E-value: 1.06e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514  108 FTSPEQVYNHYHYAFRDRRKEYFMALLLDGKNRIMREIQVSEGSLNQSIVHPREVFNPAVRESAAAVILVHNHPTGDPAP 187
Cdd:pfam04002   1 ITSPEDVAEYLMEELRDLDQEVFRVLFLDTKNRLIADEELSEGTLNSTLVHPREIFKRALRLNAAAVILAHNHPSGDPEP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 499243514  188 SREDLEITRRLREAGDIMGIRVLDHIIIGDGRF 220
Cdd:pfam04002  81 SREDIELTRRLKEAGELLGIRLLDHIIIGDGGY 113
MPN_DUF2466 cd08071
Mov34/MPN/PAD-1 family; Mov34 DUF2466 (also known as DNA repair protein RadC) domain of ...
 112-223 7.41e-60

Mov34/MPN/PAD-1 family; Mov34 DUF2466 (also known as DNA repair protein RadC) domain of unknown function contains the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity. However, to date, the name RadC has been misleading and no function has been determined.


Pssm-ID: 163702  Cd Length: 113  Bit Score: 183.73  E-value: 7.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514 112 EQVYNHYHYAFRDRRKEYFMALLLDGKNRIMREIQVSEGSLNQSIVHPREVFNPAVRESAAAVILVHNHPTGDPAPSRED 191
Cdd:cd08071    1 EDVAEYLREELGDLDQEEFVVLLLDTKNRLIAVETISVGTLNSSLVHPREIFKEALRHNAAAIILAHNHPSGDPTPSRED 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 499243514 192 LEITRRLREAGDIMGIRVLDHIIIGDGRFTSF 223
Cdd:cd08071   81 IELTKRLKEAGELLGIRLLDHIIVGDGGYFSF 112
UPF0758_N pfam20582
UPF0758 N-terminal; This domain is functionally uncharacterized, found at the N-terminal of ...
 5-78 7.19e-32

UPF0758 N-terminal; This domain is functionally uncharacterized, found at the N-terminal of the uncharacterized UPF0758 proteins from bacteria and archaea, and is approximately 90 amino acids in length. UPF0758 was previously known as the radC family, a name that was assigned according to the radC102 mutant of E. coli which was later demonstrated to be an allele of the transcription-repair-coupling factor recG. UPF0758 has been described as a putative JAMM-family deubiquitinating enzyme, but its function remains to be determined. Structure prediction using Colab notebook from AlphaFold DB suggests that it has an alpha bundle fold. It may contain two helix-hairpin-helix (HhH) motifs. This domain is found in association with pfam04002.


Pssm-ID: 466731 [Multi-domain]  Cd Length: 71  Bit Score: 110.83  E-value: 7.19e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499243514    5 IKAWPEDERPREKLLRRGAPVLSDAELLALIIRTGdsVTGRSAIDLGRALLQeCGDLRTLAGATVSELCAVKGM 78
Cdd:pfam20582   1 IKDWPEDERPREKLLRYGAEALSDAELLAILLGSG--TKGESAVDLARRLLH-FGGLRGLLKASVEELMKIKGI 71
MPN_prok_mb cd08059
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 127-225 2.08e-11

Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); prokaryotic; This family contains bacterial and archaeal MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains. These catalytically active domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site.


Pssm-ID: 163690  Cd Length: 101  Bit Score: 58.73  E-value: 2.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499243514 127 KEYFMALLLDGKNRIMREIQVSEGSLNQSIVHprevFNPAVRESAAAVILVHNHPTGDPAPSREDLEITRRLreagdimg 206
Cdd:cd08059   16 DEFCGFLSGSKDNVMDELIFLPFVSGSVSAVI----DLAALEIGMKVVGLVHSHPSGSCRPSEADLSLFTRF-------- 83

                         90
                 ....*....|....*....
gi 499243514 207 irVLDHIIIGDGRFTSFVS 225
Cdd:cd08059   84 --GLYHVIVCYPYENSWKC 100
PRK13482 PRK13482
DNA integrity scanning protein DisA; Provisional
 54-100 9.67e-04

DNA integrity scanning protein DisA; Provisional


Pssm-ID: 237395 [Multi-domain]  Cd Length: 352  Bit Score: 39.38  E-value: 9.67e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 499243514  54 LLQECGDLRTLAGATVSELCAVKGMGTAKATSIKAALE-MASRINSER 100
Cdd:PRK13482 303 LVEHFGSLQGLLAASIEDLDEVEGIGEVRARAIREGLSrLAEQSILDR 350
uvrC PRK00558
excinuclease ABC subunit UvrC;
52-90 9.88e-04

excinuclease ABC subunit UvrC;


Pssm-ID: 234792 [Multi-domain]  Cd Length: 598  Bit Score: 39.72  E-value: 9.88e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 499243514  52 RALLQECGDLRTLAGATVSELCAVKGMGTAKATSIKAAL 90
Cdd:PRK00558 557 KALLKHFGSLKAIKEASVEELAKVPGISKKLAEAIYEAL 595
MPN_archaeal cd08072
Mov34/MPN/PAD-1 family: archaeal JAB1/MPN/Mov34 metalloenzyme; This family contains only ...
 132-192 5.30e-03

Mov34/MPN/PAD-1 family: archaeal JAB1/MPN/Mov34 metalloenzyme; This family contains only archaeal MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains. These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site.


Pssm-ID: 163703  Cd Length: 117  Bit Score: 35.70  E-value: 5.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499243514 132 ALLLDGKNRIMREIQV---SEGSLNQSIVHPREVfnPAVREsaaAVILVHNHPTGDPAPSREDL 192
Cdd:cd08072   22 AALLRGKDGVITELLIlpgTESGEVSAVFPLLML--PLDMS---IVGSVHSHPSGSPRPSDADL 80
 
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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