NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488399826|ref|WP_002469211|]
View 

MULTISPECIES: DsrE/DsrF/DrsH-like family protein [Staphylococcus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
YrkE COG2210
Peroxiredoxin family protein [Energy production and conversion];
200-355 8.27e-81

Peroxiredoxin family protein [Energy production and conversion];


:

Pssm-ID: 441812  Cd Length: 156  Bit Score: 243.20  E-value: 8.27e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826 200 KSGTTIVLFSGELDKAVAAMIIANGAKAAGRDVTIFCTFWGLNALKKIQSQRIKKKGIAKLFDFMLPNSPINMPISKMNM 279
Cdd:COG2210    1 KKKLTIIVFSGDLDKAYAALILANGAAAMGKEVTIFFTFWGLNALRKDKKDSLKKPLGNPMFGMMMPKGPPKLPLSKPGM 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488399826 280 FGLGNLMMRYVMKKKNVDTLPSLIDQAVEQGVKLIACTMSMDVMGITKEELRDDVEYGGVGAYIGYTEQANHNLFI 355
Cdd:COG2210   81 GGLGTKMMKKRMKKKGVASLEELLELAKELGVKLYACQMSMDLMGIKKEELIDGVEIGGAATFLEEAEEADINLFI 156
SirA_YedF_YeeD super family cl00436
SirA, YedF, and YeeD. Two-layered alpha/beta sandwich domain. SirA (also known as UvrY, and ...
 120-188 7.59e-25

SirA, YedF, and YeeD. Two-layered alpha/beta sandwich domain. SirA (also known as UvrY, and YhhP) belongs to a family of bacterial two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding.


The actual alignment was detected with superfamily member cd03420:

Pssm-ID: 444904  Cd Length: 69  Bit Score: 95.91  E-value: 7.59e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488399826 120 TFNYSNLQCPGPIVNISKEIKNIAIGDQIEVVVTDHGFLNDIKSWVKQTGHTLVRLNDFGNEIRAIIQK 188
Cdd:cd03420    1 EVDACGLQCPGPILKLKKEIDKLQDGEQLEVKASDPGFARDAQAWCKSTGNTLISLETEKGKVKAVIEK 69
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 16-97 3.85e-22

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


:

Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 89.28  E-value: 3.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  16 ELQEL--GSKGQLIDVRQPEEFELGHIKNALLHSVENIET----FKQSKNKTYYIYCKSDNRSRKASQFLAQRGY-DVVN 88
Cdd:cd00158    1 ELKELldDEDAVLLDVREPEEYAAGHIPGAINIPLSELEEraalLELDKDKPIVVYCRSGNRSARAAKLLRKAGGtNVYN 80


                 ....*....
gi 488399826  89 LDGGYTAYE 97
Cdd:cd00158   81 LEGGMLAWK 89
 
Name Accession Description Interval E-value
YrkE COG2210
Peroxiredoxin family protein [Energy production and conversion];
200-355 8.27e-81

Peroxiredoxin family protein [Energy production and conversion];


Pssm-ID: 441812  Cd Length: 156  Bit Score: 243.20  E-value: 8.27e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826 200 KSGTTIVLFSGELDKAVAAMIIANGAKAAGRDVTIFCTFWGLNALKKIQSQRIKKKGIAKLFDFMLPNSPINMPISKMNM 279
Cdd:COG2210    1 KKKLTIIVFSGDLDKAYAALILANGAAAMGKEVTIFFTFWGLNALRKDKKDSLKKPLGNPMFGMMMPKGPPKLPLSKPGM 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488399826 280 FGLGNLMMRYVMKKKNVDTLPSLIDQAVEQGVKLIACTMSMDVMGITKEELRDDVEYGGVGAYIGYTEQANHNLFI 355
Cdd:COG2210   81 GGLGTKMMKKRMKKKGVASLEELLELAKELGVKLYACQMSMDLMGIKKEELIDGVEIGGAATFLEEAEEADINLFI 156
DrsE_2 pfam13686
DsrE/DsrF/DrsH-like family; DsrE is a small soluble protein involved in intracellular sulfur ...
 203-354 4.63e-66

DsrE/DsrF/DrsH-like family; DsrE is a small soluble protein involved in intracellular sulfur reduction. The family also includes YrkE proteins.


Pssm-ID: 433404  Cd Length: 156  Bit Score: 205.63  E-value: 4.63e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  203 TTIVLFSGELDKAVAAMIIANGAKAAGRDVTIFCTFWGLNALKKIQSQRIKKKGIAKLFDFMLPNSPINMPISKMNMFGL 282
Cdd:pfam13686   5 TIIIFSKGTDDKAYAAFIIANGAAAMGMEVTMFFTFWGLNLLRKPEKVKVKKKPLEKMFGPMMPRGSKKLPLSKMNMGGI 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488399826  283 GNLMMRYVMKKKNVDTLPSLIDQAVEQGVKLIACTMSMDVMGITKEELRDDVEYGGVGAYIGYTEQANHNLF 354
Cdd:pfam13686  85 GTKMMKKVMKDKGVPSLEELLEMAQEKGVKLVACTMTMDLMGIKKEELIDGVEIAGAATYLGDAEESDVNLF 156
SirA_RHOD_Pry_redox cd03420
SirA_RHOD_Pry_redox. SirA-like domain located within a multidomain protein of unknown ...
 120-188 7.59e-25

SirA_RHOD_Pry_redox. SirA-like domain located within a multidomain protein of unknown function. Other domains include RHOD (rhodanese homology domain), and Pry_redox (pyridine nucleotide-disulphide oxidoreductase) as well as a C-terminal domain that corresponds to COG2210. This fold is referred to as a two-layered alpha/beta sandwich, structurally similar to that of translation initiation factor 3.


Pssm-ID: 239512  Cd Length: 69  Bit Score: 95.91  E-value: 7.59e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488399826 120 TFNYSNLQCPGPIVNISKEIKNIAIGDQIEVVVTDHGFLNDIKSWVKQTGHTLVRLNDFGNEIRAIIQK 188
Cdd:cd03420    1 EVDACGLQCPGPILKLKKEIDKLQDGEQLEVKASDPGFARDAQAWCKSTGNTLISLETEKGKVKAVIEK 69
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 16-97 3.85e-22

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 89.28  E-value: 3.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  16 ELQEL--GSKGQLIDVRQPEEFELGHIKNALLHSVENIET----FKQSKNKTYYIYCKSDNRSRKASQFLAQRGY-DVVN 88
Cdd:cd00158    1 ELKELldDEDAVLLDVREPEEYAAGHIPGAINIPLSELEEraalLELDKDKPIVVYCRSGNRSARAAKLLRKAGGtNVYN 80


                 ....*....
gi 488399826  89 LDGGYTAYE 97
Cdd:cd00158   81 LEGGMLAWK 89
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 9-99 2.69e-21

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 87.33  E-value: 2.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826   9 INDFTKKELQELGSKG--QLIDVRQPEEFELGHIKNALLHSVENIETF--KQSKNKTYYIYCKSDNRSRKASQFLAQRGY 84
Cdd:COG0607    3 VKEISPAELAELLESEdaVLLDVREPEEFAAGHIPGAINIPLGELAERldELPKDKPIVVYCASGGRSAQAAALLRRAGY 82

                         90
                 ....*....|....*.
gi 488399826  85 D-VVNLDGGYTAYEEQ 99
Cdd:COG0607   83 TnVYNLAGGIEAWKAA 98
TusA COG0425
Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ...
 126-188 1.98e-17

Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ribosomal structure and biogenesis, Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440194  Cd Length: 70  Bit Score: 75.62  E-value: 1.98e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488399826 126 LQCPGPIVNISKEIKNIAIGDQIEVVVTDHGFLNDIKSWVKQTGHTLVRLNDFGNEIRAIIQK 188
Cdd:COG0425    6 LSCPLPVLKTKKALEELKPGEVLEVLADDPGAVEDIPAWCRETGHELLSVEEEGGVYRILIRK 68
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 25-101 2.44e-15

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 70.95  E-value: 2.44e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826    25 QLIDVRQPEEFELGHIKNALLHSVENIETF----------------KQSKNKTYYIYCKSDNRSRKASQFLAQRGY-DVV 87
Cdd:smart00450   6 VLLDVRSPEEYEGGHIPGAVNIPLSELLDRrgeldilefeellkrlGLDKDKPVVVYCRSGNRSAKAAWLLRELGFkNVY 85

                           90
                   ....*....|....
gi 488399826    88 NLDGGYTAYEEQHH 101
Cdd:smart00450  86 LLDGGYKEWSAAGP 99
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 25-96 2.81e-15

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 70.59  E-value: 2.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826   25 QLIDVRQPEEFELGHIKNAL--------LHSVENIETFKQ----SKNKTYYIYCKSDNRSRKASQFLAQRGY-DVVNLDG 91
Cdd:pfam00581   7 VLIDVRPPEEYAKGHIPGAVnvplsslsLPPLPLLELLEKllelLKDKPIVVYCNSGNRAAAAAALLKALGYkNVYVLDG 86


                  ....*
gi 488399826   92 GYTAY 96
Cdd:pfam00581  87 GFEAW 91
TusA pfam01206
Sulfurtransferase TusA; This family includes the TusA sulfurtransferases.
 120-183 1.94e-14

Sulfurtransferase TusA; This family includes the TusA sulfurtransferases.


Pssm-ID: 426125  Cd Length: 64  Bit Score: 67.21  E-value: 1.94e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488399826  120 TFNYSNLQCPGPIVNISKEIKNIAIGDQIEVVVTDHGFLNDIKSWVKQTGHTLVRLNDFGNEIR 183
Cdd:pfam01206   1 TLDLRGLACPMPLLKTKKALKKLKPGEVLEVLADDPGAVEDIPRWAKETGHEVLEVEEEDGEYR 64
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
9-99 2.97e-10

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 60.80  E-value: 2.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826   9 INDFTKKELQELGSKG-QLIDVRQPEEFELGHIKNAL------LHSVenIETFKQSKNKTYYIYCKSDNRSRKASQFLAQ 81
Cdd:PRK08762   2 IREISPAEARARAAQGaVLIDVREAHERASGQAEGALriprgfLELR--IETHLPDRDREIVLICASGTRSAHAAATLRE 79

                         90
                 ....*....|....*....
gi 488399826  82 RGY-DVVNLDGGYTAYEEQ 99
Cdd:PRK08762  80 LGYtRVASVAGGFSAWKDA 98
 
Name Accession Description Interval E-value
YrkE COG2210
Peroxiredoxin family protein [Energy production and conversion];
200-355 8.27e-81

Peroxiredoxin family protein [Energy production and conversion];


Pssm-ID: 441812  Cd Length: 156  Bit Score: 243.20  E-value: 8.27e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826 200 KSGTTIVLFSGELDKAVAAMIIANGAKAAGRDVTIFCTFWGLNALKKIQSQRIKKKGIAKLFDFMLPNSPINMPISKMNM 279
Cdd:COG2210    1 KKKLTIIVFSGDLDKAYAALILANGAAAMGKEVTIFFTFWGLNALRKDKKDSLKKPLGNPMFGMMMPKGPPKLPLSKPGM 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488399826 280 FGLGNLMMRYVMKKKNVDTLPSLIDQAVEQGVKLIACTMSMDVMGITKEELRDDVEYGGVGAYIGYTEQANHNLFI 355
Cdd:COG2210   81 GGLGTKMMKKRMKKKGVASLEELLELAKELGVKLYACQMSMDLMGIKKEELIDGVEIGGAATFLEEAEEADINLFI 156
DrsE_2 pfam13686
DsrE/DsrF/DrsH-like family; DsrE is a small soluble protein involved in intracellular sulfur ...
 203-354 4.63e-66

DsrE/DsrF/DrsH-like family; DsrE is a small soluble protein involved in intracellular sulfur reduction. The family also includes YrkE proteins.


Pssm-ID: 433404  Cd Length: 156  Bit Score: 205.63  E-value: 4.63e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  203 TTIVLFSGELDKAVAAMIIANGAKAAGRDVTIFCTFWGLNALKKIQSQRIKKKGIAKLFDFMLPNSPINMPISKMNMFGL 282
Cdd:pfam13686   5 TIIIFSKGTDDKAYAAFIIANGAAAMGMEVTMFFTFWGLNLLRKPEKVKVKKKPLEKMFGPMMPRGSKKLPLSKMNMGGI 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488399826  283 GNLMMRYVMKKKNVDTLPSLIDQAVEQGVKLIACTMSMDVMGITKEELRDDVEYGGVGAYIGYTEQANHNLF 354
Cdd:pfam13686  85 GTKMMKKVMKDKGVPSLEELLEMAQEKGVKLVACTMTMDLMGIKKEELIDGVEIAGAATYLGDAEESDVNLF 156
SirA_RHOD_Pry_redox cd03420
SirA_RHOD_Pry_redox. SirA-like domain located within a multidomain protein of unknown ...
 120-188 7.59e-25

SirA_RHOD_Pry_redox. SirA-like domain located within a multidomain protein of unknown function. Other domains include RHOD (rhodanese homology domain), and Pry_redox (pyridine nucleotide-disulphide oxidoreductase) as well as a C-terminal domain that corresponds to COG2210. This fold is referred to as a two-layered alpha/beta sandwich, structurally similar to that of translation initiation factor 3.


Pssm-ID: 239512  Cd Length: 69  Bit Score: 95.91  E-value: 7.59e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488399826 120 TFNYSNLQCPGPIVNISKEIKNIAIGDQIEVVVTDHGFLNDIKSWVKQTGHTLVRLNDFGNEIRAIIQK 188
Cdd:cd03420    1 EVDACGLQCPGPILKLKKEIDKLQDGEQLEVKASDPGFARDAQAWCKSTGNTLISLETEKGKVKAVIEK 69
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 16-97 3.85e-22

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 89.28  E-value: 3.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  16 ELQEL--GSKGQLIDVRQPEEFELGHIKNALLHSVENIET----FKQSKNKTYYIYCKSDNRSRKASQFLAQRGY-DVVN 88
Cdd:cd00158    1 ELKELldDEDAVLLDVREPEEYAAGHIPGAINIPLSELEEraalLELDKDKPIVVYCRSGNRSARAAKLLRKAGGtNVYN 80


                 ....*....
gi 488399826  89 LDGGYTAYE 97
Cdd:cd00158   81 LEGGMLAWK 89
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 9-99 2.69e-21

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 87.33  E-value: 2.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826   9 INDFTKKELQELGSKG--QLIDVRQPEEFELGHIKNALLHSVENIETF--KQSKNKTYYIYCKSDNRSRKASQFLAQRGY 84
Cdd:COG0607    3 VKEISPAELAELLESEdaVLLDVREPEEFAAGHIPGAINIPLGELAERldELPKDKPIVVYCASGGRSAQAAALLRRAGY 82

                         90
                 ....*....|....*.
gi 488399826  85 D-VVNLDGGYTAYEEQ 99
Cdd:COG0607   83 TnVYNLAGGIEAWKAA 98
TusA COG0425
Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ...
 126-188 1.98e-17

Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ribosomal structure and biogenesis, Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440194  Cd Length: 70  Bit Score: 75.62  E-value: 1.98e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488399826 126 LQCPGPIVNISKEIKNIAIGDQIEVVVTDHGFLNDIKSWVKQTGHTLVRLNDFGNEIRAIIQK 188
Cdd:COG0425    6 LSCPLPVLKTKKALEELKPGEVLEVLADDPGAVEDIPAWCRETGHELLSVEEEGGVYRILIRK 68
COG2044 COG2044
Predicted peroxiredoxin, DsrE/DsrF-like family [General function prediction only];
205-350 5.30e-16

Predicted peroxiredoxin, DsrE/DsrF-like family [General function prediction only];


Pssm-ID: 441647  Cd Length: 121  Bit Score: 73.39  E-value: 5.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826 205 IVLFSG--ELDKAVAAMIIANGAKAAGRDVTIFCTFWGLNALKKIQSQRIKKKGiaklfdfmlpnspinmpiskmnmfgl 282
Cdd:COG2044    7 ILLTSGpdDPERATMAFVLAAAAAAMGAEVTIFLTGEGVRLAKKGVAEKIRAPG-------------------------- 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488399826 283 gnlmmryvmkkknVDTLPSLIDQAVEQGVKLIACTMSMDVMGITKEELRDDVEYGGVGAYIGYTEQAN 350
Cdd:COG2044   61 -------------GPPLADLLEEAIEAGVKVYVCEPCLKARGLTEEDLIPGVEIAGAADFAELALEAD 115
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 25-101 2.44e-15

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 70.95  E-value: 2.44e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826    25 QLIDVRQPEEFELGHIKNALLHSVENIETF----------------KQSKNKTYYIYCKSDNRSRKASQFLAQRGY-DVV 87
Cdd:smart00450   6 VLLDVRSPEEYEGGHIPGAVNIPLSELLDRrgeldilefeellkrlGLDKDKPVVVYCRSGNRSAKAAWLLRELGFkNVY 85

                           90
                   ....*....|....
gi 488399826    88 NLDGGYTAYEEQHH 101
Cdd:smart00450  86 LLDGGYKEWSAAGP 99
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 25-96 2.81e-15

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 70.59  E-value: 2.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826   25 QLIDVRQPEEFELGHIKNAL--------LHSVENIETFKQ----SKNKTYYIYCKSDNRSRKASQFLAQRGY-DVVNLDG 91
Cdd:pfam00581   7 VLIDVRPPEEYAKGHIPGAVnvplsslsLPPLPLLELLEKllelLKDKPIVVYCNSGNRAAAAAALLKALGYkNVYVLDG 86


                  ....*
gi 488399826   92 GYTAY 96
Cdd:pfam00581  87 GFEAW 91
SirA_YedF_YeeD cd00291
SirA, YedF, and YeeD. Two-layered alpha/beta sandwich domain. SirA (also known as UvrY, and ...
 120-188 1.20e-14

SirA, YedF, and YeeD. Two-layered alpha/beta sandwich domain. SirA (also known as UvrY, and YhhP) belongs to a family of bacterial two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding.


Pssm-ID: 238180  Cd Length: 69  Bit Score: 67.97  E-value: 1.20e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488399826 120 TFNYSNLQCPGPIVNISKEIKNIAIGDQIEVVVTDHGFLNDIKSWVKQTGHTLVRLNDFGNEIRAIIQK 188
Cdd:cd00291    1 TLDLRGLPCPLPVLKTKKALEKLKSGEVLEVLLDDPGAVEDIPAWAKETGHEVLEVEEEGGVYRILIRK 69
TusA pfam01206
Sulfurtransferase TusA; This family includes the TusA sulfurtransferases.
 120-183 1.94e-14

Sulfurtransferase TusA; This family includes the TusA sulfurtransferases.


Pssm-ID: 426125  Cd Length: 64  Bit Score: 67.21  E-value: 1.94e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488399826  120 TFNYSNLQCPGPIVNISKEIKNIAIGDQIEVVVTDHGFLNDIKSWVKQTGHTLVRLNDFGNEIR 183
Cdd:pfam01206   1 TLDLRGLACPMPLLKTKKALKKLKPGEVLEVLADDPGAVEDIPRWAKETGHEVLEVEEEDGEYR 64
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 16-97 2.26e-14

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.


Pssm-ID: 238782 [Multi-domain]  Cd Length: 90  Bit Score: 67.68  E-value: 2.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  16 ELQELGSKG-QLIDVRQPEEFELGHIKNALLHSVENIETFKQS--KNKTYYIYCKSDNRSRKASQFLAQRGYDVVNLDGG 92
Cdd:cd01524    5 ELDNYRADGvTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNElpKDKEIIVYCAVGLRGYIAARILTQNGFKVKNLDGG 84


                 ....*
gi 488399826  93 YTAYE 97
Cdd:cd01524   85 YKTYS 89
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
9-99 2.97e-10

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 60.80  E-value: 2.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826   9 INDFTKKELQELGSKG-QLIDVRQPEEFELGHIKNAL------LHSVenIETFKQSKNKTYYIYCKSDNRSRKASQFLAQ 81
Cdd:PRK08762   2 IREISPAEARARAAQGaVLIDVREAHERASGQAEGALriprgfLELR--IETHLPDRDREIVLICASGTRSAHAAATLRE 79

                         90
                 ....*....|....*....
gi 488399826  82 RGY-DVVNLDGGYTAYEEQ 99
Cdd:PRK08762  80 LGYtRVASVAGGFSAWKDA 98
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 15-99 3.49e-09

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 57.80  E-value: 3.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  15 KELQELGSKGQLIDVRQPEEFELGHIKNALL------HSVENIETFKQskNKTYYIYCKSDNRSRKASQFLAQRGY-DVV 87
Cdd:PRK07878 295 KEWLDSGKKIALIDVREPVEWDIVHIPGAQLipkseiLSGEALAKLPQ--DRTIVLYCKTGVRSAEALAALKKAGFsDAV 372

                         90
                 ....*....|..
gi 488399826  88 NLDGGYTAYEEQ 99
Cdd:PRK07878 373 HLQGGVVAWAKQ 384
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
1-96 1.42e-08

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 51.95  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826   1 MSQYKtkHINdftKKELQELGSKGQ--LIDVRQPEEFELGHIKNALLHSVENIETFKQSKN--KTYYIYCKSDNRSRKAS 76
Cdd:PRK00162   1 MDQFE--CIN---VEQAHQKLQEGGavLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADfdTPVMVMCYHGNSSQGAA 75

                         90       100
                 ....*....|....*....|.
gi 488399826  77 QFLAQRGYDVV-NLDGGYTAY 96
Cdd:PRK00162  76 QYLLQQGFDVVySIDGGFEAW 96
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
9-99 3.61e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 54.74  E-value: 3.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826   9 INDFTKKELQELGSKGQ----LIDVRQPEEFELGHIKNAL---LHSVEN---IETFKQSKNKTYYI-YCKSDNRSRKASQ 77
Cdd:PRK07411 281 IPEMTVTELKALLDSGAddfvLIDVRNPNEYEIARIPGSVlvpLPDIENgpgVEKVKELLNGHRLIaHCKMGGRSAKALG 360

                         90       100
                 ....*....|....*....|..
gi 488399826  78 FLAQRGYDVVNLDGGYTAYEEQ 99
Cdd:PRK07411 361 ILKEAGIEGTNVKGGITAWSRE 382
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 27-91 9.83e-08

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 49.46  E-value: 9.83e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  27 IDVRQPEEFELGHIKNA----LLHSVENIETFKQSKNKTYYIYCKSDNRSRKASQFLAQRGY-DVVNLDG 91
Cdd:PRK10287  24 IDVRVPEQYQQEHVQGAinipLKEVKERIATAVPDKNDTVKLYCNAGRQSGQAKEILSEMGYtHAENAGG 93
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 15-98 9.93e-08

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 52.95  E-value: 9.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  15 KELQELGSKGQLIDVRQPEEFELGHIKNALLHSVENIE----TFKQSKNKTYYIYCKSDNRSRKASQFLAQRGY-DVVNL 89
Cdd:PRK05597 266 PRVSALPDGVTLIDVREPSEFAAYSIPGAHNVPLSAIReganPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYtGMSSL 345


                 ....*....
gi 488399826  90 DGGYTAYEE 98
Cdd:PRK05597 346 DGGIEGWLD 354
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 15-99 4.01e-07

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 48.46  E-value: 4.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  15 KELQELGSKGQ---LIDVRQPEEFELGHIKNAL------------LHSVENIETFKQSKNKTYYIYCKSDNRSRKASQFL 79
Cdd:cd01526   13 KDYKNILQAGKkhvLLDVRPKVHFEICRLPEAIniplsellskaaELKSLQELPLDNDKDSPIYVVCRRGNDSQTAVRKL 92

                         90       100
                 ....*....|....*....|..
gi 488399826  80 AQRGY--DVVNLDGGYTAYEEQ 99
Cdd:cd01526   93 KELGLerFVRDIIGGLKAWADK 114
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 26-94 8.51e-07

Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein 67B2 of Drosophila melanogaster and other similar proteins, many of which are uncharacterized.


Pssm-ID: 238777 [Multi-domain]  Cd Length: 106  Bit Score: 46.88  E-value: 8.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  26 LIDVRQPEEFELGHIKNAL---LHSVE-----NIETFKQ-------SKNKTYYIYCKSDNRSRKASQFLAQRGY-DVVNL 89
Cdd:cd01519   18 LIDVREPEELKTGKIPGAInipLSSLPdalalSEEEFEKkygfpkpSKDKELIFYCKAGVRSKAAAELARSLGYeNVGNY 97


                 ....*
gi 488399826  90 DGGYT 94
Cdd:cd01519   98 PGSWL 102
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 17-99 9.44e-07

Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes uncharacterized putative rhodanese-related domains.


Pssm-ID: 238786 [Multi-domain]  Cd Length: 101  Bit Score: 46.62  E-value: 9.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  17 LQELGSKGQLIDVRQPEEFELGHIKNALLHSVENIETF-----KQSKNKTYYIYCKSDNRSRKASQFLAQRGYD-VVNLD 90
Cdd:cd01528   11 LADEREEPVLIDVREPEELEIAFLPGFLHLPMSEIPERskeldSDNPDKDIVVLCHHGGRSMQVAQWLLRQGFEnVYNLQ 90


                 ....*....
gi 488399826  91 GGYTAYEEQ 99
Cdd:cd01528   91 GGIDAWSLE 99
SirA cd03423
SirA (also known as UvrY, and YhhP) belongs to a family of two-component response regulators ...
 120-188 9.52e-07

SirA (also known as UvrY, and YhhP) belongs to a family of two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is thought to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding.


Pssm-ID: 239515  Cd Length: 69  Bit Score: 45.81  E-value: 9.52e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488399826 120 TFNYSNLQCPGPIVNISKEIKNIAIGDQIEVVVTDHGFLNDIKSWVKQTGHTLVRLNDFGNEIRAIIQK 188
Cdd:cd03423    1 ILDTRGLRCPEPVMMLHKKVRKMKPGDTLLVLATDPSTTRDIPKFCTFLGHELLAQETEDEPYRYLIRK 69
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 26-98 1.14e-06

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins.


Pssm-ID: 238776 [Multi-domain]  Cd Length: 101  Bit Score: 46.42  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  26 LIDVRQPEEFELGHIKNALlhsVENIETF-----------KQSKNKTYYIYCKSDNRSRKASQFLAQRGY-DVVNLDGGY 93
Cdd:cd01518   20 LLDVRNDYEYDIGHFKGAV---NPDVDTFrefpfwldenlDLLKGKKVLMYCTGGIRCEKASAYLKERGFkNVYQLKGGI 96


                 ....*
gi 488399826  94 TAYEE 98
Cdd:cd01518   97 LKYLE 101
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 22-96 1.29e-06

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 49.44  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  22 SKGQLIDVRQPEEFELGHIKNA----LLHSVENIE---TFKQ------------------------------SKNKTYYI 64
Cdd:PRK11784  14 NDTPLIDVRSPIEFAEGHIPGAinlpLLNDEERAEvgtCYKQqgqfaaialghalvagniaahreeawadfpRANPRGLL 93

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488399826  65 YC-KSDNRSRKASQFLAQRGYDVVNLDGGYTAY 96
Cdd:PRK11784  94 YCwRGGLRSGSVQQWLKEAGIDVPRLEGGYKAY 126
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 16-98 2.98e-06

GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.


Pssm-ID: 238721 [Multi-domain]  Cd Length: 96  Bit Score: 44.94  E-value: 2.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  16 ELQELGSKGQLIDVRQPEEFE--LGHIKNALLHSVENIETF--KQSKNKTYYIYCKSDNRSRKASQFLAQRGY-DVVNLD 90
Cdd:cd01444    9 ELLAAGEAPVLLDVRDPASYAalPDHIPGAIHLDEDSLDDWlgDLDRDRPVVVYCYHGNSSAQLAQALREAGFtDVRSLA 88


                 ....*...
gi 488399826  91 GGYTAYEE 98
Cdd:cd01444   89 GGFEAWRR 96
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 25-94 5.56e-06

Member of the Rhodanese Homology Domain superfamily. This CD includes the putative rhodanese-like protein, Psp2, of Yersinia pestis biovar Medievalis and other similar uncharacterized proteins.


Pssm-ID: 238779 [Multi-domain]  Cd Length: 110  Bit Score: 44.65  E-value: 5.56e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488399826  25 QLIDVRQPEEFELGHIKNAL---LHSVENIETFKQSKNKTYYIYCKSD--NRSRKASQFLAQRGYDVVNLDGGYT 94
Cdd:cd01521   27 VLVDVRSAEAYARGHVPGAInlpHREICENATAKLDKEKLFVVYCDGPgcNGATKAALKLAELGFPVKEMIGGLD 101
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 20-98 3.09e-05

Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as a polysulfide binding and transferase domain in anaerobic gram-negative bacteria, functioning in oxidative phosphorylation with polysulfide-sulfur as a terminal electron acceptor. The active site contains the same conserved cysteine that is the catalytic residue in other Rhodanese Homology Domain proteins.


Pssm-ID: 238724 [Multi-domain]  Cd Length: 103  Bit Score: 42.41  E-value: 3.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  20 LGSKG-QLIDVRQPEEFEL-GHIKNALlHSVENIETF---KQS--------KNKTYYIYCKSDNRSRKASQFLAQRGYD- 85
Cdd:cd01447   10 LGSPGvLLVDVRDPRELERtGMIPGAF-HAPRGMLEFwadPDSpyhkpafaEDKPFVFYCASGWRSALAGKTLQDMGLKp 88

                         90
                 ....*....|...
gi 488399826  86 VVNLDGGYTAYEE 98
Cdd:cd01447   89 VYNIEGGFKDWKE 101
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 26-96 3.12e-05

Member of the Rhodanese Homology Domain superfamily. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. Only the second and most of the fourth repeats contain the putative catalytic Cys residue. This CD aligns the 1st , 2nd, 3rd, and 4th repeats.


Pssm-ID: 238787 [Multi-domain]  Cd Length: 96  Bit Score: 42.28  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  26 LIDVRQPEEFELGHIKNA-------LLHSVENIETFKQSKNKTYYI-YCKSDNRSRKASQFLAQRGY-DVVNLDGGYTAY 96
Cdd:cd01529   15 LLDVRAEDEYAAGHLPGKrsipgaaLVLRSQELQALEAPGRATRYVlTCDGSLLARFAAQELLALGGkPVALLDGGTSAW 94
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
26-96 3.34e-05

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 45.22  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  26 LIDVRQPEEFELGHIKNALlhsVENIETF-----------KQSKNKTYYIYCKSDNRSRKASQFLAQRGYDVVN-LDGGY 93
Cdd:PRK00142 130 FIDMRNDYEYEIGHFENAI---EPDIETFrefppwveenlDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYqLEGGI 206


                 ...
gi 488399826  94 TAY 96
Cdd:PRK00142 207 ITY 209
DrsE pfam02635
DsrE/DsrF-like family; DsrE is a small soluble protein involved in intracellular sulfur ...
 292-349 3.25e-04

DsrE/DsrF-like family; DsrE is a small soluble protein involved in intracellular sulfur reduction. This family also includes DsrF.


Pssm-ID: 426894  Cd Length: 117  Bit Score: 40.01  E-value: 3.25e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488399826  292 KKKNVDTLPSLIDQAVEQGVKLIACTMSMDVMGIT-KEELRDDVEYGGVGAYIGYTEQA 349
Cdd:pfam02635  53 NPIGEKNLAELLKALAEYGVKVYVCGQSLKARGITeDELLGVGVEVSGLGELAELQLEG 111
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 21-98 3.66e-04

Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included in this CD are eukaryotic arsenate resistance proteins such as Saccharomyces cerevisiae Acr2p and similar proteins. Cdc25 phosphatases activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. The Cdc25 and Acr2p RHOD domains have the signature motif (H/YCxxxxxR).


Pssm-ID: 238720 [Multi-domain]  Cd Length: 113  Bit Score: 39.70  E-value: 3.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  21 GSKGQLIDVRQPEeFELGHIKNAL---LHSVEN-----IETFKQSKNKTYYIYC-KSDNRSRKASQFLAQR----GYD-- 85
Cdd:cd01443   21 GKDFVVVDLRRDD-YEGGHIKGSInlpAQSCYQtlpqvYALFSLAGVKLAIFYCgSSQGRGPRAARWFADYlrkvGESlp 99

                         90
                 ....*....|....
gi 488399826  86 -VVNLDGGYTAYEE 98
Cdd:cd01443  100 kSYILTGGIKAWYH 113
PRK01415 PRK01415
hypothetical protein; Validated
 26-104 5.88e-04

hypothetical protein; Validated


Pssm-ID: 167229 [Multi-domain]  Cd Length: 247  Bit Score: 41.08  E-value: 5.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  26 LIDVRQPEEFELGHIKNALlhsVENIETFKQS-----------KNKTYYIYCKSDNRSRKASQFLAQRGYD-VVNLDGGY 93
Cdd:PRK01415 130 VIDTRNDYEVEVGTFKSAI---NPNTKTFKQFpawvqqnqellKGKKIAMVCTGGIRCEKSTSLLKSIGYDeVYHLKGGI 206

                         90
                 ....*....|.
gi 488399826  94 TAYEEQHHNDN 104
Cdd:PRK01415 207 LQYLEDTQNKN 217
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 16-95 6.71e-04

Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 3rd repeat which does not contain the putative catalytic Cys residue.


Pssm-ID: 238792 [Multi-domain]  Cd Length: 95  Bit Score: 38.60  E-value: 6.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  16 ELQELGSKGQ----LIDVRQPEEFELGHIKNAlLHS-----VENIETFKQSKNKTYYIYCKSDNRSRKASQFLAQRGYDV 86
Cdd:cd01534    5 ELARWAAEGDrtvyRFDVRTPEEYEAGHLPGF-RHTpggqlVQETDHFAPVRGARIVLADDDGVRADMTASWLAQMGWEV 83


                 ....*....
gi 488399826  87 VNLDGGYTA 95
Cdd:cd01534   84 YVLEGGLAA 92
COG3370 COG3370
Uncharacterized conserved protein AF1964, DsrE/DsrF-like family [General function prediction ...
 273-339 1.06e-03

Uncharacterized conserved protein AF1964, DsrE/DsrF-like family [General function prediction only];


Pssm-ID: 442597  Cd Length: 112  Bit Score: 38.32  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826 273 PISKMNMfglgNLMMRYVMKKKN----V----------------DTLPSLIDQAVEQGVKLIACTMSMDVMGITKE--EL 330
Cdd:COG3370   13 DEEKAKM----ALMYALNSLKKNwwedVkvifwgpsvkllaedeEEVQELIKELIKAGVKVSACKACADNLGVTEKleKL 88


                 ....*....
gi 488399826 331 RDDVEYGGV 339
Cdd:COG3370   89 GIEVEYAGE 97
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 18-100 2.00e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, and similar uncharacterized putative rhodanese-related sulfurtransferases.


Pssm-ID: 238785 [Multi-domain]  Cd Length: 99  Bit Score: 37.08  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399826  18 QELGSKGQ-LIDVRQPEEFELGHIKNALLHSVENIET---FKQSKNKTYYiYCKSDNRSRKASQFLAQ-RGYDVVNLDGG 92
Cdd:cd01527   10 CELLAQGAvLVDIREPDEYLRERIPGARLVPLSQLESeglPLVGANAIIF-HCRSGMRTQQNAERLAAiSAGEAYVLEGG 88


                 ....*...
gi 488399826  93 YTAYEEQH 100
Cdd:cd01527   89 LDAWKAAG 96
COG1416 COG1416
Intracellular sulfur oxidation protein, DsrE/DsrF family [Inorganic ion transport and ...
 294-341 4.32e-03

Intracellular sulfur oxidation protein, DsrE/DsrF family [Inorganic ion transport and metabolism];


Pssm-ID: 441026  Cd Length: 139  Bit Score: 37.22  E-value: 4.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 488399826 294 KNVDTLPSLIDQAVEQGVKLIACTMSMDVMGITKEELRDDVEY--GGVGA 341
Cdd:COG1416   76 KDNNPLAERIAALAEKGVKFVACGNTLKARGIDKDDLLPGVEVvpSGVVE 125
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH