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Conserved domains on  [gi|2222587737|ref|WP_244569677|]
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R3H domain-containing nucleic acid-binding protein [Aeriscardovia aeriphila]

Protein Classification

protein jag( domain architecture ID 11448923)

SpoIIIJ-associated protein jag is necessary for the third stage of sporulation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Jag COG1847
Predicted RNA-binding protein Jag (SpoIIIJ-associated), conains KH and R3H domains [General ...
 17-158 4.75e-53

Predicted RNA-binding protein Jag (SpoIIIJ-associated), conains KH and R3H domains [General function prediction only];


:

Pssm-ID: 441452 [Multi-domain]  Cd Length: 143  Bit Score: 166.05  E-value: 4.75e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587737  17 ADYLEGLLDVLDYDGDIELGVRNGRPLVQIVADDdtdIKQLIGKDGEVVEALQRLARLAVQQKTGERSGLIVDVDGFLAR 96
Cdd:COG1847     2 ADFLEELLDIMGLDGDIEIEVEGDRLTVDISGED---LGLLIGRRGETLDALQYLTNLAVNRKTGERSRVILDVEGYRER 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2222587737  97 KRRHLRNLALDAVDDVREDGEPVTLEDMNAYERKIIHDIVRQ-EGLKSRSHGDEPHRHVTVYL 158
Cdd:COG1847    79 REEELEELARRAAEKVKRTGKPVELEPMSPYERRIIHDALADdPGVETESEGEEPYRRVVISP 141
 
Name Accession Description Interval E-value
Jag COG1847
Predicted RNA-binding protein Jag (SpoIIIJ-associated), conains KH and R3H domains [General ...
 17-158 4.75e-53

Predicted RNA-binding protein Jag (SpoIIIJ-associated), conains KH and R3H domains [General function prediction only];


Pssm-ID: 441452 [Multi-domain]  Cd Length: 143  Bit Score: 166.05  E-value: 4.75e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587737  17 ADYLEGLLDVLDYDGDIELGVRNGRPLVQIVADDdtdIKQLIGKDGEVVEALQRLARLAVQQKTGERSGLIVDVDGFLAR 96
Cdd:COG1847     2 ADFLEELLDIMGLDGDIEIEVEGDRLTVDISGED---LGLLIGRRGETLDALQYLTNLAVNRKTGERSRVILDVEGYRER 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2222587737  97 KRRHLRNLALDAVDDVREDGEPVTLEDMNAYERKIIHDIVRQ-EGLKSRSHGDEPHRHVTVYL 158
Cdd:COG1847    79 REEELEELARRAAEKVKRTGKPVELEPMSPYERRIIHDALADdPGVETESEGEEPYRRVVISP 141
Jag_EloR NF041568
RNA-binding cell elongation regulator Jag/EloR; Members of this family are nucleic ...
 14-158 2.96e-24

RNA-binding cell elongation regulator Jag/EloR; Members of this family are nucleic acid-binding proteins (RNA or single-stranded DNA) with a KH domain at the N-terminus, an R3H domain at the C-terminus, and additional regions of homology. The founding member of this family was JAG (spoIIIJ Associated Gene) from Bacillus subtilis, but later work in other lineages, such as Streptococcus pneumoniae, as established a role in controlling cell elongation and the operation of the elongasome. The S. pneumoniae protein, a protein that undergoes regulatory phosphorylation and dephosphorylation, is also called RNA-binding cell elongation regulator EloR, and also KhpB.


Pssm-ID: 469453 [Multi-domain]  Cd Length: 203  Bit Score: 94.04  E-value: 2.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587737  14 DIAADYLEGLLDVLDYDGDIELGVRNGRPLVQIVADDDTDIkqLIGKDGEVVEALQRLARLAVQQKTGERSGLIVDVDGF 93
Cdd:NF041568   60 EEAKEFLENVLEAMGIDEVEIEEEEDDDVIKFNLSGEKLGL--LIGKRGQTLDALQYLTNLVANRYSDEYVRVILDAENY 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2222587737  94 LARKRRHLRNLALDAVDDVREDGEPVTLEDMNAYERKIIHDIVRQ-EGLKSRSHGDEPHRHVTVYL 158
Cdd:NF041568  138 RERREETLEQLAERLADKVKRTKKPVVLEPMPSYERKIIHTALQNhPDVETYSEGEEPNRKVVIAP 203
R3H_jag cd02644
R3H domain found in proteins homologous to Bacillus subtilus Jag, which is associated with ...
 95-158 6.56e-22

R3H domain found in proteins homologous to Bacillus subtilus Jag, which is associated with SpoIIIJ. SpoIIIJ is necessary for the third stage of sporulation. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100073  Cd Length: 67  Bit Score: 84.06  E-value: 6.56e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2222587737  95 ARKRRHLRNLALDAVDDVREDGEPVTLEDMNAYERKIIHDIVRQ-EGLKSRSHGDEPHRHVTVYL 158
Cdd:cd02644     2 ERREETLIRLAERAAEKVRRTGKPVKLEPMNAYERRIIHDALANdEDVETESEGEGPYRRVVISP 66
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
81-157 1.52e-18

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 75.80  E-value: 1.52e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2222587737   81 GERSGLIVDVDGFLARKRRHLRNLALDAVDDVREDGEPVTLEDMNAYERKIIHDIVRQEGLKSRSHGDEPHRHVTVY 157
Cdd:smart00393   1 ADFLPVTLDALSYRPRRREELIELELEIARFVKSTKESVELPPMNSYERKIVHELAEKYGLESESFGEGPKRRVVIS 77
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
 101-157 1.67e-18

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 75.22  E-value: 1.67e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2222587737 101 LRNLALDAVDDVREDGEPVTLEDMNAYERKIIHDIVRQEGLKSRSHGDEPHRHVTVY 157
Cdd:pfam01424   3 LEQLAEKLAEFVKDTGKSLELPPMSSYERRIIHELAQKYGLESESEGEEPNRRVVVY 59
 
Name Accession Description Interval E-value
Jag COG1847
Predicted RNA-binding protein Jag (SpoIIIJ-associated), conains KH and R3H domains [General ...
 17-158 4.75e-53

Predicted RNA-binding protein Jag (SpoIIIJ-associated), conains KH and R3H domains [General function prediction only];


Pssm-ID: 441452 [Multi-domain]  Cd Length: 143  Bit Score: 166.05  E-value: 4.75e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587737  17 ADYLEGLLDVLDYDGDIELGVRNGRPLVQIVADDdtdIKQLIGKDGEVVEALQRLARLAVQQKTGERSGLIVDVDGFLAR 96
Cdd:COG1847     2 ADFLEELLDIMGLDGDIEIEVEGDRLTVDISGED---LGLLIGRRGETLDALQYLTNLAVNRKTGERSRVILDVEGYRER 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2222587737  97 KRRHLRNLALDAVDDVREDGEPVTLEDMNAYERKIIHDIVRQ-EGLKSRSHGDEPHRHVTVYL 158
Cdd:COG1847    79 REEELEELARRAAEKVKRTGKPVELEPMSPYERRIIHDALADdPGVETESEGEEPYRRVVISP 141
Jag_EloR NF041568
RNA-binding cell elongation regulator Jag/EloR; Members of this family are nucleic ...
 14-158 2.96e-24

RNA-binding cell elongation regulator Jag/EloR; Members of this family are nucleic acid-binding proteins (RNA or single-stranded DNA) with a KH domain at the N-terminus, an R3H domain at the C-terminus, and additional regions of homology. The founding member of this family was JAG (spoIIIJ Associated Gene) from Bacillus subtilis, but later work in other lineages, such as Streptococcus pneumoniae, as established a role in controlling cell elongation and the operation of the elongasome. The S. pneumoniae protein, a protein that undergoes regulatory phosphorylation and dephosphorylation, is also called RNA-binding cell elongation regulator EloR, and also KhpB.


Pssm-ID: 469453 [Multi-domain]  Cd Length: 203  Bit Score: 94.04  E-value: 2.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587737  14 DIAADYLEGLLDVLDYDGDIELGVRNGRPLVQIVADDDTDIkqLIGKDGEVVEALQRLARLAVQQKTGERSGLIVDVDGF 93
Cdd:NF041568   60 EEAKEFLENVLEAMGIDEVEIEEEEDDDVIKFNLSGEKLGL--LIGKRGQTLDALQYLTNLVANRYSDEYVRVILDAENY 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2222587737  94 LARKRRHLRNLALDAVDDVREDGEPVTLEDMNAYERKIIHDIVRQ-EGLKSRSHGDEPHRHVTVYL 158
Cdd:NF041568  138 RERREETLEQLAERLADKVKRTKKPVVLEPMPSYERKIIHTALQNhPDVETYSEGEEPNRKVVIAP 203
R3H_jag cd02644
R3H domain found in proteins homologous to Bacillus subtilus Jag, which is associated with ...
 95-158 6.56e-22

R3H domain found in proteins homologous to Bacillus subtilus Jag, which is associated with SpoIIIJ. SpoIIIJ is necessary for the third stage of sporulation. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100073  Cd Length: 67  Bit Score: 84.06  E-value: 6.56e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2222587737  95 ARKRRHLRNLALDAVDDVREDGEPVTLEDMNAYERKIIHDIVRQ-EGLKSRSHGDEPHRHVTVYL 158
Cdd:cd02644     2 ERREETLIRLAERAAEKVRRTGKPVKLEPMNAYERRIIHDALANdEDVETESEGEGPYRRVVISP 66
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
81-157 1.52e-18

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 75.80  E-value: 1.52e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2222587737   81 GERSGLIVDVDGFLARKRRHLRNLALDAVDDVREDGEPVTLEDMNAYERKIIHDIVRQEGLKSRSHGDEPHRHVTVY 157
Cdd:smart00393   1 ADFLPVTLDALSYRPRRREELIELELEIARFVKSTKESVELPPMNSYERKIVHELAEKYGLESESFGEGPKRRVVIS 77
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
 101-157 1.67e-18

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 75.22  E-value: 1.67e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2222587737 101 LRNLALDAVDDVREDGEPVTLEDMNAYERKIIHDIVRQEGLKSRSHGDEPHRHVTVY 157
Cdd:pfam01424   3 LEQLAEKLAEFVKDTGKSLELPPMSSYERRIIHELAQKYGLESESEGEEPNRRVVVY 59
R3H cd02325
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ...
 94-157 3.58e-15

R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100064  Cd Length: 59  Bit Score: 66.48  E-value: 3.58e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2222587737  94 LARKRRHLRNLALDAvddvreDGEPVTLEDMNAYERKIIHDIVRQEGLKSRSHGDEPHRHVTVY 157
Cdd:cd02325     1 REEREEELEAFAKDA------AGKSLELPPMNSYERKLIHDLAEYYGLKSESEGEGPNRRVVIT 58
KH-II_Jag cd02414
type II K-homology (KH) RNA-binding domain found in protein Jag and similar proteins; Protein ...
 16-96 5.39e-11

type II K-homology (KH) RNA-binding domain found in protein Jag and similar proteins; Protein Jag, also called SpoIIIJ-associated protein, is associated with SpoIIIJ and is necessary for the third stage of sporulation. Members of this family are mainly from bacteria and contain only one canonical type II K-homology (KH) domain that has the signature motif GXXG (where X represents any amino acid).


Pssm-ID: 411785  Cd Length: 79  Bit Score: 55.99  E-value: 5.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2222587737  16 AADYLEGLLDVLDYDGDIELGVRNGRPLVQIvadDDTDIKQLIGKDGEVVEALQRLARLAVQQKTGERSGLIVDVDGFLA 95
Cdd:cd02414     2 AKEFLEELLDAMGIEAEVEVEEEEGTVKLNI---DGEDPGLLIGKHGETLDALQYLANLVLNKEFGKRVRVVLDVEGYRE 78


                  .
gi 2222587737  96 R 96
Cdd:cd02414    79 R 79
R3H_DEXH_helicase cd06007
R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may ...
 107-157 2.05e-06

R3H domain of a group of proteins which also contain a DEXH-box helicase domain, and may function as ATP-dependent DNA or RNA helicases. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100077  Cd Length: 59  Bit Score: 43.46  E-value: 2.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2222587737 107 DAVDDVREDGEPV-TLE-DMNAYERKIIHDIVRQEGLKSRSHGDEPHRHVTVY 157
Cdd:cd06007     6 KALEDFRASDNEEyEFPsSLTNHERAVIHRLCRKLGLKSKSKGKGSNRRLSVY 58
R3H_AAA cd02645
R3H domain of a group of proteins with unknown function, who also contain a AAA-ATPase (AAA) ...
 112-157 3.61e-05

R3H domain of a group of proteins with unknown function, who also contain a AAA-ATPase (AAA) domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100074  Cd Length: 60  Bit Score: 39.95  E-value: 3.61e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2222587737 112 VREDGEPVTLEDMNAYERKIIHDIVRQEGLKSRSHGDEPHRHVTVY 157
Cdd:cd02645    14 VIPKGEPVELLPRSAYIRRLQHDLVERYQLRSESFGSEPNRRLRIL 59
R3H_NRF cd02640
R3H domain of the NF-kappaB-repression factor (NRF). NRF is a nuclear inhibitor of NF-kappaB ...
 127-156 1.04e-03

R3H domain of the NF-kappaB-repression factor (NRF). NRF is a nuclear inhibitor of NF-kappaB proteins that can silence the IFNbeta promoter via binding to a negative regulatory element (NRE). Beside R3H NRF also contains a G-patch domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100069  Cd Length: 60  Bit Score: 35.84  E-value: 1.04e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2222587737 127 YERKIIHDIVRQEGLKSRSHGDEPHRHVTV 156
Cdd:cd02640    29 EERALIHQIAQKYGLKSRSYGSGNDRYLVI 58
R3H_NF-X1 cd02643
R3H domain of the X1 box binding protein (NF-X1) and related proteins. Human NF-X1 is a ...
 120-156 2.02e-03

R3H domain of the X1 box binding protein (NF-X1) and related proteins. Human NF-X1 is a transcription factor that regulates the expression of class II major histocompatibility complex (MHC) genes. The Drosophila homolog shuttle craft (STC) has been shown to be a DNA- or RNA-binding protein required for proper axon guidance in the central nervous system and, the yeast homolog FAP1 encodes a dosage suppressor of rapamycin toxicity. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100072  Cd Length: 74  Bit Score: 35.41  E-value: 2.02e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2222587737 120 TLEDMNAYERKIIHDIVRQEGLKSRSHGDEPHRHVTV 156
Cdd:cd02643    36 SFPPMNREKRRIVHELAEHFGIESVSYDQEPKRNVVA 72
R3H_unknown_2 cd06006
R3H domain of a group of fungal proteins with unknown function. The name of the R3H domain ...
 124-157 5.25e-03

R3H domain of a group of fungal proteins with unknown function. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100076  Cd Length: 59  Bit Score: 33.88  E-value: 5.25e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2222587737 124 MNAYERKIIHDIVRQEGLKSRSHGDEPHRHVTVY 157
Cdd:cd06006    25 MRSPQRAFIHELAKDYGLYSESQDPEPKRSVFVK 58
R3H_G-patch cd02646
R3H domain of a group of fungal and plant proteins with unknown function, who also contain a ...
 124-157 7.00e-03

R3H domain of a group of fungal and plant proteins with unknown function, who also contain a G-patch domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the R3H domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100075  Cd Length: 58  Bit Score: 33.70  E-value: 7.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2222587737 124 MNAYERKIIHDIVRQEGLKSRSHGDEPHRHVTVY 157
Cdd:cd02646    24 MDKHGRKTIHKLANCYNLKSKSRGKGKKRFVTVT 57
 
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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