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Conserved domains on  [gi|1372008885|ref|WP_106886571|]
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rhodanese-like domain-containing protein [Aeromonas rivipollensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08762 super family cl35741
molybdopterin-synthase adenylyltransferase MoeB;
17-121 3.18e-39

molybdopterin-synthase adenylyltransferase MoeB;


The actual alignment was detected with superfamily member PRK08762:

Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 134.75  E-value: 3.18e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  17 QIRETDVHQIRRWQEEGrfFHLIDVREDNEWAKGHLPGAEHLGRGVMERDIETRFPDPDTELYLYCGGGFRSILAADNLQ 96
Cdd:PRK08762    1 SIREISPAEARARAAQG--AVLIDVREAHERASGQAEGALRIPRGFLELRIETHLPDRDREIVLICASGTRSAHAAATLR 78

                          90       100
                  ....*....|....*....|....*
gi 1372008885  97 KMGYSRVVSVDGGFRGWCDAGYPVE 121
Cdd:PRK08762   79 ELGYTRVASVAGGFSAWKDAGLPLE 103
 
Name Accession Description Interval E-value
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
17-121 3.18e-39

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 134.75  E-value: 3.18e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  17 QIRETDVHQIRRWQEEGrfFHLIDVREDNEWAKGHLPGAEHLGRGVMERDIETRFPDPDTELYLYCGGGFRSILAADNLQ 96
Cdd:PRK08762    1 SIREISPAEARARAAQG--AVLIDVREAHERASGQAEGALRIPRGFLELRIETHLPDRDREIVLICASGTRSAHAAATLR 78

                          90       100
                  ....*....|....*....|....*
gi 1372008885  97 KMGYSRVVSVDGGFRGWCDAGYPVE 121
Cdd:PRK08762   79 ELGYTRVASVAGGFSAWKDAGLPLE 103
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 17-122 1.84e-33

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: 112.37  E-value: 1.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  17 QIRETDVHQIRRWQEEGRFFhLIDVREDNEWAKGHLPGAEHLGRGVMERDIETRfpDPDTELYLYCGGGFRSILAADNLQ 96
Cdd:COG0607     2 SVKEISPAELAELLESEDAV-LLDVREPEEFAAGHIPGAINIPLGELAERLDEL--PKDKPIVVYCASGGRSAQAAALLR 78

                          90       100
                  ....*....|....*....|....*.
gi 1372008885  97 KMGYSRVVSVDGGFRGWCDAGYPVES 122
Cdd:COG0607    79 RAGYTNVYNLAGGIEAWKAAGLPVEK 104
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 25-113 2.75e-24

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: 88.51  E-value: 2.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  25 QIRRWQEEGRFFhLIDVREDNEWAKGHLPGAEHLGRGVMERDIETRFPDPDTELYLYCGGGFRSILAADNLQKMGYSRVV 104
Cdd:cd00158     1 ELKELLDDEDAV-LLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVY 79


                  ....*....
gi 1372008885 105 SVDGGFRGW 113
Cdd:cd00158    80 NLEGGMLAW 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 37-113 7.54e-19

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: 74.83  E-value: 7.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  37 HLIDVREDNEWAKGHLPGAEHL------GRGVMERDIETRFPD--PDTELYLYCGGGFRSILAADNLQKMGYSRVVSVDG 108
Cdd:pfam00581   7 VLIDVRPPEEYAKGHIPGAVNVplsslsLPPLPLLELLEKLLEllKDKPIVVYCNSGNRAAAAAALLKALGYKNVYVLDG 86


                  ....*
gi 1372008885 109 GFRGW 113
Cdd:pfam00581  87 GFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 36-119 7.05e-16

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: 67.48  E-value: 7.05e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885   36 FHLIDVREDNEWAKGHLPGAEHLGRG-VMERDIETRFP-----------DPDTELYLYCGGGFRSILAADNLQKMGYSRV 103
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPGAVNIPLSeLLDRRGELDILefeellkrlglDKDKPVVVYCRSGNRSAKAAWLLRELGFKNV 84

                           90
                   ....*....|....*.
gi 1372008885  104 VSVDGGFRGWCDAGYP 119
Cdd:smart00450  85 YLLDGGYKEWSAAGPP 100
phageshock_pspE TIGR02981
phage shock operon rhodanese PspE; Members of this very narrowly defined protein family are ...
 37-108 1.50e-08

phage shock operon rhodanese PspE; Members of this very narrowly defined protein family are proteins active as rhodanese (EC 2.8.1.1) and found in the extended variants of the phage shock protein (psp operon) in Escherichia coli and a few closely related species. Note that the designation phage shock protein PspE has been applied, incorrectly, in many instances where the genome lacks the phage shock regulon entirely.


Pssm-ID: 132026 [Multi-domain]  Cd Length: 101  Bit Score: 48.86  E-value: 1.50e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372008885  37 HLIDVREDNEWAKGHLPGAEHLGRGVMERDIETRFPDPDTELYLYCGGGFRSILAADNLQKMGYSRVVSVDG 108
Cdd:TIGR02981  20 HWIDVRIPEQYQQEHIQGAINIPLKEIKEHIATAVPDKNDTVKLYCNAGRQSGMAKDILLDMGYTHAENAGG 91
 
Name Accession Description Interval E-value
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
17-121 3.18e-39

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 134.75  E-value: 3.18e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  17 QIRETDVHQIRRWQEEGrfFHLIDVREDNEWAKGHLPGAEHLGRGVMERDIETRFPDPDTELYLYCGGGFRSILAADNLQ 96
Cdd:PRK08762    1 SIREISPAEARARAAQG--AVLIDVREAHERASGQAEGALRIPRGFLELRIETHLPDRDREIVLICASGTRSAHAAATLR 78

                          90       100
                  ....*....|....*....|....*
gi 1372008885  97 KMGYSRVVSVDGGFRGWCDAGYPVE 121
Cdd:PRK08762   79 ELGYTRVASVAGGFSAWKDAGLPLE 103
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 17-122 1.84e-33

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: 112.37  E-value: 1.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  17 QIRETDVHQIRRWQEEGRFFhLIDVREDNEWAKGHLPGAEHLGRGVMERDIETRfpDPDTELYLYCGGGFRSILAADNLQ 96
Cdd:COG0607     2 SVKEISPAELAELLESEDAV-LLDVREPEEFAAGHIPGAINIPLGELAERLDEL--PKDKPIVVYCASGGRSAQAAALLR 78

                          90       100
                  ....*....|....*....|....*.
gi 1372008885  97 KMGYSRVVSVDGGFRGWCDAGYPVES 122
Cdd:COG0607    79 RAGYTNVYNLAGGIEAWKAAGLPVEK 104
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 25-113 2.75e-24

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: 88.51  E-value: 2.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  25 QIRRWQEEGRFFhLIDVREDNEWAKGHLPGAEHLGRGVMERDIETRFPDPDTELYLYCGGGFRSILAADNLQKMGYSRVV 104
Cdd:cd00158     1 ELKELLDDEDAV-LLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVY 79


                  ....*....
gi 1372008885 105 SVDGGFRGW 113
Cdd:cd00158    80 NLEGGMLAW 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 37-113 7.54e-19

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: 74.83  E-value: 7.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  37 HLIDVREDNEWAKGHLPGAEHL------GRGVMERDIETRFPD--PDTELYLYCGGGFRSILAADNLQKMGYSRVVSVDG 108
Cdd:pfam00581   7 VLIDVRPPEEYAKGHIPGAVNVplsslsLPPLPLLELLEKLLEllKDKPIVVYCNSGNRAAAAAALLKALGYKNVYVLDG 86


                  ....*
gi 1372008885 109 GFRGW 113
Cdd:pfam00581  87 GFEAW 91
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 38-117 2.05e-16

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: 68.99  E-value: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  38 LIDVREDNEW-AKGHLPGAEHLGRGVMERDIETRFP------DPDTELYLYCGGGFRSILAADNLQKMGYSRVVSVDGGF 110
Cdd:cd01447    17 LVDVRDPRELeRTGMIPGAFHAPRGMLEFWADPDSPyhkpafAEDKPFVFYCASGWRSALAGKTLQDMGLKPVYNIEGGF 96


                  ....*..
gi 1372008885 111 RGWCDAG 117
Cdd:cd01447    97 KDWKEAG 103
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 36-119 7.05e-16

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: 67.48  E-value: 7.05e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885   36 FHLIDVREDNEWAKGHLPGAEHLGRG-VMERDIETRFP-----------DPDTELYLYCGGGFRSILAADNLQKMGYSRV 103
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPGAVNIPLSeLLDRRGELDILefeellkrlglDKDKPVVVYCRSGNRSAKAAWLLRELGFKNV 84

                           90
                   ....*....|....*.
gi 1372008885  104 VSVDGGFRGWCDAGYP 119
Cdd:smart00450  85 YLLDGGYKEWSAAGPP 100
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 16-116 1.05e-15

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 71.44  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  16 PQIRETDVHQIRRWQEEGRFFHLIDVREDNEWAKGHLPGAEHLGRGVMERDIETRFPDPDTELYLYCGGGFRSILAADNL 95
Cdd:PRK05597  255 ISGGFGEVLDVPRVSALPDGVTLIDVREPSEFAAYSIPGAHNVPLSAIREGANPPSVSAGDEVVVYCAAGVRSAQAVAIL 334

                          90       100
                  ....*....|....*....|.
gi 1372008885  96 QKMGYSRVVSVDGGFRGWCDA 116
Cdd:PRK05597  335 ERAGYTGMSSLDGGIEGWLDS 355
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 28-113 1.99e-15

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: 66.16  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  28 RWQEEG-RFFHLIDVREDNEWAKGHLPGAEHL--GRGVMERD--IETRFPDPDTELYLYCGGGFRSILAADNLQKMGYSR 102
Cdd:cd01529     4 DWLGEHePGTALLDVRAEDEYAAGHLPGKRSIpgAALVLRSQelQALEAPGRATRYVLTCDGSLLARFAAQELLALGGKP 83

                          90
                  ....*....|.
gi 1372008885 103 VVSVDGGFRGW 113
Cdd:cd01529    84 VALLDGGTSAW 94
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 25-113 4.59e-12

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 61.26  E-value: 4.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  25 QIRRWQEEGRFFHLIDVREDNEWAKGHLPGAEHLGRGVMERDIETRFPDPDTELYLYCGGGFRSILAADNLQKMGYSRVV 104
Cdd:PRK07878  293 ELKEWLDSGKKIALIDVREPVEWDIVHIPGAQLIPKSEILSGEALAKLPQDRTIVLYCKTGVRSAEALAALKKAGFSDAV 372


                  ....*....
gi 1372008885 105 SVDGGFRGW 113
Cdd:PRK07878  373 HLQGGVVAW 381
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 38-113 2.74e-11

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: 55.74  E-value: 2.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  38 LIDVREDNEWAKGHLPGAEHLGRGVM-------ERDIETRF----PDPDTELYLYCGGGFRSILAADNLQKMGYSRVVSV 106
Cdd:cd01519    18 LIDVREPEELKTGKIPGAINIPLSSLpdalalsEEEFEKKYgfpkPSKDKELIFYCKAGVRSKAAAELARSLGYENVGNY 97


                  ....*..
gi 1372008885 107 DGGFRGW 113
Cdd:cd01519    98 PGSWLDW 104
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 24-113 4.47e-10

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: 52.27  E-value: 4.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  24 HQIRRWQEEGRFfhLIDVREDNEWAKGHLPGAEHLgrGVME-RDIETRFPdPDTELYLYCGGGFRSILAADNLQKMGYsR 102
Cdd:cd01524     4 HELDNYRADGVT--LIDVRTPQEFEKGHIKGAINI--PLDElRDRLNELP-KDKEIIVYCAVGLRGYIAARILTQNGF-K 77

                          90
                  ....*....|.
gi 1372008885 103 VVSVDGGFRGW 113
Cdd:cd01524    78 VKNLDGGYKTY 88
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 38-113 7.01e-10

Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 1st repeat which does not contain the putative catalytic Cys residue.


Pssm-ID: 238790 [Multi-domain]  Cd Length: 92  Bit Score: 51.72  E-value: 7.01e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372008885  38 LIDVREDNEWAKGHLPGAEHLGRGVMERDIETRFPDPDTELYLYCGGGFRSI--LAADNLQKMGYSRVVSVDGGFRGW 113
Cdd:cd01532    13 LIDVREEDPFAQSHPLWAANLPLSRLELDAWVRIPRRDTPIVVYGEGGGEDLapRAARRLSELGYTDVALLEGGLQGW 90
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 23-115 7.40e-10

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: 51.88  E-value: 7.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  23 VHQIRRWQEEGRFFHLIDVREDNEWAK--GHLPGAEHLGrgvMER--DIETRFPDpDTELYLYCGGGFRSILAADNLQKM 98
Cdd:cd01444     4 VDELAELLAAGEAPVLLDVRDPASYAAlpDHIPGAIHLD---EDSldDWLGDLDR-DRPVVVYCYHGNSSAQLAQALREA 79

                          90
                  ....*....|....*..
gi 1372008885  99 GYSRVVSVDGGFRGWCD 115
Cdd:cd01444    80 GFTDVRSLAGGFEAWRR 96
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 17-113 9.04e-10

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: 51.63  E-value: 9.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  17 QIRETDVHQIRrwQEEGRFFHLIDVREDNEWAKGHLPGAEHLGRG-VMERDIETRFPDPDTELYLYCGGGFRSILAADNL 95
Cdd:cd01528     1 QISVAELAEWL--ADEREEPVLIDVREPEELEIAFLPGFLHLPMSeIPERSKELDSDNPDKDIVVLCHHGGRSMQVAQWL 78

                          90
                  ....*....|....*...
gi 1372008885  96 QKMGYSRVVSVDGGFRGW 113
Cdd:cd01528    79 LRQGFENVYNLQGGIDAW 96
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 10-117 4.06e-09

Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 2nd repeat which does contain the putative catalytic Cys residue.


Pssm-ID: 238791 [Multi-domain]  Cd Length: 109  Bit Score: 50.15  E-value: 4.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  10 LVEAIR--PQIRETdvhQIRRWQEEGRFFHLIDVREDNEWAKGHLPGAEHLGRGVMERDIETRFPDPDTELYLYCGGGFR 87
Cdd:cd01533     2 LVEAVRhtPSVSAD---ELAALQARGAPLVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGELAPDPRTPIVVNCAGRTR 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1372008885  88 SILAADNLQKMGY-SRVVSVDGGFRGWCDAG 117
Cdd:cd01533    79 SIIGAQSLINAGLpNPVAALRNGTQGWTLAG 109
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
28-113 6.81e-09

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 49.63  E-value: 6.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  28 RWQEEGRffHLIDVREDNEWAKGHLPGAEHLGRGVMERDIetRFPDPDTELYLYCGGGFRSILAADNLQKMGYSRVVSVD 107
Cdd:PRK00162   15 KLQEGGA--VLVDIRDPQSFAMGHAPGAFHLTNDSLGAFM--RQADFDTPVMVMCYHGNSSQGAAQYLLQQGFDVVYSID 90


                  ....*.
gi 1372008885 108 GGFRGW 113
Cdd:PRK00162   91 GGFEAW 96
phageshock_pspE TIGR02981
phage shock operon rhodanese PspE; Members of this very narrowly defined protein family are ...
 37-108 1.50e-08

phage shock operon rhodanese PspE; Members of this very narrowly defined protein family are proteins active as rhodanese (EC 2.8.1.1) and found in the extended variants of the phage shock protein (psp operon) in Escherichia coli and a few closely related species. Note that the designation phage shock protein PspE has been applied, incorrectly, in many instances where the genome lacks the phage shock regulon entirely.


Pssm-ID: 132026 [Multi-domain]  Cd Length: 101  Bit Score: 48.86  E-value: 1.50e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372008885  37 HLIDVREDNEWAKGHLPGAEHLGRGVMERDIETRFPDPDTELYLYCGGGFRSILAADNLQKMGYSRVVSVDG 108
Cdd:TIGR02981  20 HWIDVRIPEQYQQEHIQGAINIPLKEIKEHIATAVPDKNDTVKLYCNAGRQSGMAKDILLDMGYTHAENAGG 91
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 37-108 1.73e-08

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 48.69  E-value: 1.73e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372008885  37 HLIDVREDNEWAKGHLPGAEHLGRGVMERDIETRFPDPDTELYLYCGGGFRSILAADNLQKMGYSRVVSVDG 108
Cdd:PRK10287   22 HWIDVRVPEQYQQEHVQGAINIPLKEVKERIATAVPDKNDTVKLYCNAGRQSGQAKEILSEMGYTHAENAGG 93
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 38-116 3.10e-08

Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative rhodanese-related sulfurtransferases of several uncharacterized proteins.


Pssm-ID: 238780 [Multi-domain]  Cd Length: 117  Bit Score: 48.09  E-value: 3.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  38 LIDVREDNEWAK-GHLPGAEHLGRGV---MER-----DIETRFPDPDTELYLYCGGGFRSILAADNLQKMGYSRVVSVDG 108
Cdd:cd01522    18 LVDVRTEAEWKFvGGVPDAVHVAWQVypdMEInpnflAELEEKVGKDRPVLLLCRSGNRSIAAAEAAAQAGFTNVYNVLE 97


                  ....*...
gi 1372008885 109 GFRGWCDA 116
Cdd:cd01522    98 GFEGDLDA 105
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 22-120 7.20e-08

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: 46.96  E-value: 7.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  22 DVHQIRRwqEEGRFFHLIDVREDNEWAKGHLPGAEHLGRGVMERDIETRFPdPDTELYLYCGG----GfrSILAADNLQK 97
Cdd:cd01521    14 DVAIALK--NGKPDFVLVDVRSAEAYARGHVPGAINLPHREICENATAKLD-KEKLFVVYCDGpgcnG--ATKAALKLAE 88

                          90       100
                  ....*....|....*....|...
gi 1372008885  98 MGYsRVVSVDGGFRGWCDAGYPV 120
Cdd:cd01521    89 LGF-PVKEMIGGLDWWKREGYAT 110
4RHOD_Repeat_4 cd01535
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative ...
 29-122 1.33e-07

Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 4th repeat which, in general, contains the putative catalytic Cys residue.


Pssm-ID: 238793 [Multi-domain]  Cd Length: 145  Bit Score: 47.12  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  29 WQEEGRFFHLIDVREDNEWAKGHLPGAEHLGRGVMERDIEtRFPDPDTELyLYCGGGFRSILAADNLQKMGYSRVVSVDG 108
Cdd:cd01535     5 WLGEGGQTAVVDVTASANYVKRHIPGAWWVLRAQLAQALE-KLPAAERYV-LTCGSSLLARFAAADLAALTVKPVFVLEG 82

                          90
                  ....*....|....
gi 1372008885 109 GFRGWCDAGYPVES 122
Cdd:cd01535    83 GTAAWIAAGLPVES 96
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 38-120 1.38e-07

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: 45.94  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  38 LIDVREDNEWAKGHLPGAEHLGRGVMErdiETRFPDPDTELYLY-CGGGFRSILAADNLQKMGYSRVVSVDGGFRGWCDA 116
Cdd:cd01527    19 LVDIREPDEYLRERIPGARLVPLSQLE---SEGLPLVGANAIIFhCRSGMRTQQNAERLAAISAGEAYVLEGGLDAWKAA 95


                  ....
gi 1372008885 117 GYPV 120
Cdd:cd01527    96 GLPV 99
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 21-113 1.66e-07

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: 45.92  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  21 TDVHQIRRWQEEG-RFFHLIDVREDNEWAKGHLPGAEHLGRGVMERDIETRFPDPDTELYLYCGGGFRSILAADNLQKMG 99
Cdd:cd01534     1 IGAAELARWAAEGdRTVYRFDVRTPEEYEAGHLPGFRHTPGGQLVQETDHFAPVRGARIVLADDDGVRADMTASWLAQMG 80

                          90
                  ....*....|....
gi 1372008885 100 YSrVVSVDGGFRGW 113
Cdd:cd01534    81 WE-VYVLEGGLAAA 93
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 31-115 8.36e-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: 44.61  E-value: 8.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  31 EEGRFFHLIDVREDNEWAKGHLPGAEHLGRGVMER---DIETRFP-----DPDTELYLYCGGGFRSILAADNLQKMGYSR 102
Cdd:cd01526    20 QAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSkaaELKSLQElpldnDKDSPIYVVCRRGNDSQTAVRKLKELGLER 99

                          90
                  ....*....|....
gi 1372008885 103 -VVSVDGGFRGWCD 115
Cdd:cd01526   100 fVRDIIGGLKAWAD 113
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 38-121 1.07e-06

3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 45.55  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  38 LIDVREDNEWA---------KGHLPGAEHL-GRGVMERD--------IETRF----PDPDTELYLYCGGGFRS---ILAa 92
Cdd:COG2897   156 LVDARSPERYRgevepidprAGHIPGAVNLpWTDLLDEDgtfksaeeLRALFaalgIDPDKPVITYCGSGVRAahtWLA- 234

                          90       100       110
                  ....*....|....*....|....*....|
gi 1372008885  93 dnLQKMGYSRVVSVDGGFRGWC-DAGYPVE 121
Cdd:COG2897   235 --LELLGYPNVRLYDGSWSEWGsDPDLPVE 262
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 38-122 1.37e-05

3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 42.47  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  38 LIDVRED-----NEWAKGHLPGAEHLgrgvmerDIETRFPDPDTELY--LYCGGGFRSILAA------------DN---- 94
Cdd:COG2897    12 ILDVRWDlpdgrAAYEAGHIPGAVFL-------DLDTDLSDPRSPGRhpLPSPEAFAALLGAlgisndttvvvyDDgggl 84

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1372008885  95 --------LQKMGYSRVVSVDGGFRGWCDAGYPVES 122
Cdd:COG2897    85 faarawwlLRYAGHEDVRVLDGGLAAWKAAGLPLET 120
PLN02160 PLN02160
thiosulfate sulfurtransferase
 17-122 2.47e-05

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 40.84  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  17 QIRETDVHQIRRWQEEGRFFhlIDVREDNEWAKGHLPGAEHL----------GRGVMERDIE--TRFPDPDTELYLYCGG 84
Cdd:PLN02160   13 EVVSVDVSQAKTLLQSGHQY--LDVRTQDEFRRGHCEAAKIVnipymlntpqGRVKNQEFLEqvSSLLNPADDILVGCQS 90

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1372008885  85 GFRSILAADNLQKMGYSRVVSVDGGFRGWCDAGYPVES 122
Cdd:PLN02160   91 GARSLKATTELVAAGYKKVRNKGGGYLAWVDHSFPINQ 128
RHOD_YbbB cd01520
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ...
 38-113 3.89e-05

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP /GTP binding proteins including E. coli YbbB.


Pssm-ID: 238778 [Multi-domain]  Cd Length: 128  Bit Score: 39.97  E-value: 3.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  38 LIDVREDNEWAKGHLPG--------------------------AEHLGRGVMERDIE-------TRFPDPDTELYLYCG- 83
Cdd:cd01520    16 LIDVRSPKEFFEGHLPGainlpllddeeralvgtlykqqgreaAIELGLELVSGKLKrilneawEARLERDPKLLIYCAr 95

                          90       100       110
                  ....*....|....*....|....*....|
gi 1372008885  84 GGFRSILAADNLQKMGYsRVVSVDGGFRGW 113
Cdd:cd01520    96 GGMRSQSLAWLLESLGI-DVPLLEGGYKAY 124
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 36-113 6.86e-05

Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the second repeat. Only the second repeat contains the catalytically active Cys residue.


Pssm-ID: 238726 [Multi-domain]  Cd Length: 118  Bit Score: 39.15  E-value: 6.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  36 FHLIDVREDNEWA-----------KGHLPGAEHL---------GRGVMERDIETRFP----DPDTELYLYCGGGFRS--- 88
Cdd:cd01449    15 VQLVDARSPERFRgevpeprpglrSGHIPGAVNIpwtslldedGTFKSPEELRALFAalgiTPDKPVIVYCGSGVTAcvl 94

                          90       100
                  ....*....|....*....|....*
gi 1372008885  89 ILAADNLqkmGYSRVVSVDGGFRGW 113
Cdd:cd01449    95 LLALELL---GYKNVRLYDGSWSEW 116
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 38-109 4.75e-04

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: 36.79  E-value: 4.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  38 LIDVREDNEWAKGHLPGAehlgrgvMERDIET--RFPD---------PDTELYLYCGGGFRSILAADNLQKMGYSRVVSV 106
Cdd:cd01518    20 LLDVRNDYEYDIGHFKGA-------VNPDVDTfrEFPFwldenldllKGKKVLMYCTGGIRCEKASAYLKERGFKNVYQL 92


                  ...
gi 1372008885 107 DGG 109
Cdd:cd01518    93 KGG 95
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 35-113 5.15e-04

tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a selenophosphate-dependent tRNA 2-selenouridine synthase, essential for modification of some tRNAs to replace a sulfur atom with selenium. This enzyme works with SelD, the selenium donor protein, which also acts in selenocysteine incorporation. Although the members of this protein family show a fairly deep split, sequences from both sides of the split are supported by co-occurence with, and often proximity to, the selD gene. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274463 [Multi-domain]  Cd Length: 311  Bit Score: 37.96  E-value: 5.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  35 FFHLIDVREDNEWAKGHLPGAEHL-------------------------------GRGVMER-DIETRFPDPDTELYLYC 82
Cdd:TIGR03167   2 FDPLIDVRSPAEFAEGHLPGAINLpllndeeraevgtlykqvgpfaaiklglalvSPNLAAHvEQWRAFADGPPQPLLYC 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1372008885  83 G-GGFRSILAADNLQKMGYsRVVSVDGGFRGW 113
Cdd:TIGR03167  82 WrGGMRSGSLAWLLAQIGF-RVPRLEGGYKAY 112
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 38-115 9.66e-04

Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with rhodanese-like domains found N-terminal of the metallo-beta-lactamase domain.


Pssm-ID: 238781 [Multi-domain]  Cd Length: 100  Bit Score: 35.93  E-value: 9.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  38 LIDVREDNEWAKGHLPGAEHL-------GRGVMERDIETRFPDpDTELYLYCGGGFRSILAADNLQKMGYsRVVSVDGGF 110
Cdd:cd01523    18 ILDVRNESDYERWKIDGENNTpyfdpyfDFLEIEEDILDQLPD-DQEVTVICAKEGSSQFVAELLAERGY-DVDYLAGGM 95


                  ....*
gi 1372008885 111 RGWCD 115
Cdd:cd01523    96 KAWSE 100
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 38-113 1.05e-03

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 37.12  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372008885  38 LIDVREDNEWAKGHLPGAEHL------------------GR------------GVMERDIETRFPDPDT---ELYLYCG- 83
Cdd:PRK11784   18 LIDVRSPIEFAEGHIPGAINLpllndeeraevgtcykqqGQfaaialghalvaGNIAAHREEAWADFPRanpRGLLYCWr 97

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1372008885  84 GGFRSILAADNLQKMGYsRVVSVDGG---FRGW 113
Cdd:PRK11784   98 GGLRSGSVQQWLKEAGI-DVPRLEGGykaYRRF 129
 
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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