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Conserved domains on  [gi|488149983|ref|WP_002221191|]
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MULTISPECIES: rhodanese-like domain-containing protein [Neisseria]

Protein Classification

rhodanese-like domain-containing protein( domain architecture ID 10001806)

rhodanese-like domain-containing protein may have sulfurtransferase activity if an active site cysteine is present

CATH:  3.40.250.10
PubMed:  12151332|17454295

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 25-118 1.00e-28

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: 100.43  E-value: 1.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  25 KPLSAAQTAQ----HPAVWIDVRSEQEFSEGHLHNAVNIPVDQIVRRIHEAapDKDTPVNLYCRSGRRAKAALQELKKAG 100
Cdd:COG0607    4 KEISPAELAEllesEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDEL--PKDKPIVVYCASGGRSAQAAALLRRAG 81

                         90
                 ....*....|....*....
gi 488149983 101 YTNVAN-HGGYEDLLKKGM 118
Cdd:COG0607   82 YTNVYNlAGGIEAWKAAGL 100
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 25-118 1.00e-28

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: 100.43  E-value: 1.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  25 KPLSAAQTAQ----HPAVWIDVRSEQEFSEGHLHNAVNIPVDQIVRRIHEAapDKDTPVNLYCRSGRRAKAALQELKKAG 100
Cdd:COG0607    4 KEISPAELAEllesEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDEL--PKDKPIVVYCASGGRSAQAAALLRRAG 81

                         90
                 ....*....|....*....
gi 488149983 101 YTNVAN-HGGYEDLLKKGM 118
Cdd:COG0607   82 YTNVYNlAGGIEAWKAAGL 100
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 37-111 3.98e-28

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: 98.14  E-value: 3.98e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488149983  37 AVWIDVRSEQEFSEGHLHNAVNIPVDQIVRRIHEAAPDKDTPVNLYCRSGRRAKAALQELKKAGYTNVAN-HGGYE 111
Cdd:cd00158   11 AVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNlEGGML 86
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 37-117 2.20e-19

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: 76.34  E-value: 2.20e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983    37 AVWIDVRSEQEFSEGHLHNAVNIPVDQIVRR------------IHEAAPDKDTPVNLYCRSGRRAKAALQELKKAGYTNV 104
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPGAVNIPLSELLDRrgeldilefeelLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGFKNV 84

                           90
                   ....*....|....
gi 488149983   105 AN-HGGYEDLLKKG 117
Cdd:smart00450  85 YLlDGGYKEWSAAG 98
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 26-113 5.58e-19

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 75.27  E-value: 5.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  26 PLSAAQTaqhpavWIDVRSEQEFSEGHLHNAVNIPVDQIVRRIHEAAPDKDTPVNLYCRSGRRAKAALQELKKAGYTNVA 105
Cdd:PRK10287  16 PVFAAEH------WIDVRVPEQYQQEHVQGAINIPLKEVKERIATAVPDKNDTVKLYCNAGRQSGQAKEILSEMGYTHAE 89


                 ....*...
gi 488149983 106 NHGGYEDL 113
Cdd:PRK10287  90 NAGGLKDI 97
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 36-112 1.88e-18

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: 73.67  E-value: 1.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983   36 PAVWIDVRSEQEFSEGHLHNAVNIPVDQIVRRIHE--------AAPDKDTPVNLYCRSGRRAKAALQELKKAGYTNVAN- 106
Cdd:pfam00581   5 KVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPllelleklLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVYVl 84


                  ....*.
gi 488149983  107 HGGYED 112
Cdd:pfam00581  85 DGGFEA 90
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 40-110 4.42e-07

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: 46.82  E-value: 4.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983   40 IDVRSEQEFSEGHLHNAVNIPV------------------------------DQIVRRIHEAAPDKDTPVN--LYC-RSG 86
Cdd:TIGR03167   6 IDVRSPAEFAEGHLPGAINLPLlndeeraevgtlykqvgpfaaiklglalvsPNLAAHVEQWRAFADGPPQplLYCwRGG 85

                          90       100
                  ....*....|....*....|....
gi 488149983   87 RRAKAALQELKKAGYTNVANHGGY 110
Cdd:TIGR03167  86 MRSGSLAWLLAQIGFRVPRLEGGY 109
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 25-118 1.00e-28

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: 100.43  E-value: 1.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  25 KPLSAAQTAQ----HPAVWIDVRSEQEFSEGHLHNAVNIPVDQIVRRIHEAapDKDTPVNLYCRSGRRAKAALQELKKAG 100
Cdd:COG0607    4 KEISPAELAEllesEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDEL--PKDKPIVVYCASGGRSAQAAALLRRAG 81

                         90
                 ....*....|....*....
gi 488149983 101 YTNVAN-HGGYEDLLKKGM 118
Cdd:COG0607   82 YTNVYNlAGGIEAWKAAGL 100
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 37-111 3.98e-28

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: 98.14  E-value: 3.98e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488149983  37 AVWIDVRSEQEFSEGHLHNAVNIPVDQIVRRIHEAAPDKDTPVNLYCRSGRRAKAALQELKKAGYTNVAN-HGGYE 111
Cdd:cd00158   11 AVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNlEGGML 86
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 37-117 2.20e-19

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: 76.34  E-value: 2.20e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983    37 AVWIDVRSEQEFSEGHLHNAVNIPVDQIVRR------------IHEAAPDKDTPVNLYCRSGRRAKAALQELKKAGYTNV 104
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPGAVNIPLSELLDRrgeldilefeelLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGFKNV 84

                           90
                   ....*....|....
gi 488149983   105 AN-HGGYEDLLKKG 117
Cdd:smart00450  85 YLlDGGYKEWSAAG 98
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 26-113 5.58e-19

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 75.27  E-value: 5.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  26 PLSAAQTaqhpavWIDVRSEQEFSEGHLHNAVNIPVDQIVRRIHEAAPDKDTPVNLYCRSGRRAKAALQELKKAGYTNVA 105
Cdd:PRK10287  16 PVFAAEH------WIDVRVPEQYQQEHVQGAINIPLKEVKERIATAVPDKNDTVKLYCNAGRQSGQAKEILSEMGYTHAE 89


                 ....*...
gi 488149983 106 NHGGYEDL 113
Cdd:PRK10287  90 NAGGLKDI 97
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 36-112 1.88e-18

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: 73.67  E-value: 1.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983   36 PAVWIDVRSEQEFSEGHLHNAVNIPVDQIVRRIHE--------AAPDKDTPVNLYCRSGRRAKAALQELKKAGYTNVAN- 106
Cdd:pfam00581   5 KVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPllelleklLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVYVl 84


                  ....*.
gi 488149983  107 HGGYED 112
Cdd:pfam00581  85 DGGFEA 90
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 32-115 3.20e-18

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: 73.46  E-value: 3.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  32 TAQHP-AVWIDVRSEQEFSEGHLHNAVNIPVDQIV-----------RRIHEAAPDKDTPVNLYCRSGRRAKAALQELKKA 99
Cdd:cd01519   10 PNPHPnKVLIDVREPEELKTGKIPGAINIPLSSLPdalalseeefeKKYGFPKPSKDKELIFYCKAGVRSKAAAELARSL 89

                         90
                 ....*....|....*..
gi 488149983 100 GYTNVANH-GGYEDLLK 115
Cdd:cd01519   90 GYENVGNYpGSWLDWAA 106
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 40-110 7.53e-16

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: 66.91  E-value: 7.53e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488149983  40 IDVRSEQEFSEGHLHNAVNIPVDQIVRRIHEAapDKDTPVNLYCRSGRRAKAALQELKKAGYtNVAN-HGGY 110
Cdd:cd01524   17 IDVRTPQEFEKGHIKGAINIPLDELRDRLNEL--PKDKEIIVYCAVGLRGYIAARILTQNGF-KVKNlDGGY 85
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
26-111 1.09e-15

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 71.20  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  26 PLSAAQTAQHPAVWIDVRSEQEFSEGHLHNAVNIPVDQIVRRIHEAAPDKDTPVNLYCRSGRRAKAALQELKKAGYTNVA 105
Cdd:PRK08762   7 PAEARARAAQGAVLIDVREAHERASGQAEGALRIPRGFLELRIETHLPDRDREIVLICASGTRSAHAAATLRELGYTRVA 86


                 ....*..
gi 488149983 106 N-HGGYE 111
Cdd:PRK08762  87 SvAGGFS 93
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 40-111 6.13e-11

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 57.96  E-value: 6.13e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488149983  40 IDVRSEQEFSEGHLHNAVNIPVDQIVRRIHEAAPDKDTPVNLYCRSGRRAKAALQELKKAGYTNVAN-HGGYE 111
Cdd:PRK05597 278 IDVREPSEFAAYSIPGAHNVPLSAIREGANPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYTGMSSlDGGIE 350
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 40-105 2.68e-10

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: 53.06  E-value: 2.68e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  40 IDVRSEQEFSEGHLHNAVNIPVDQIVRRIHE----AAPDKDTPVNLYCRSGRRAKAALQELKKAGYTNVA 105
Cdd:cd01529   16 LDVRAEDEYAAGHLPGKRSIPGAALVLRSQElqalEAPGRATRYVLTCDGSLLARFAAQELLALGGKPVA 85
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 26-106 3.86e-10

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: 53.10  E-value: 3.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  26 PLSAAQTAQHP--AVWIDVRSEQEFSE-GHLHNAVNIP-------------VDQIvrrihEAAPDKDTPVNLYCRSGRRA 89
Cdd:cd01522    3 PAEAWALLQADpqAVLVDVRTEAEWKFvGGVPDAVHVAwqvypdmeinpnfLAEL-----EEKVGKDRPVLLLCRSGNRS 77

                         90
                 ....*....|....*..
gi 488149983  90 KAALQELKKAGYTNVAN 106
Cdd:cd01522   78 IAAAEAAAQAGFTNVYN 94
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 40-105 7.90e-09

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: 49.02  E-value: 7.90e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488149983  40 IDVRSEQEFSEGHLHNAVNIPVDQIVRRIHEAAPDKDTPVNLYCRSGRR--AKAALQELKKAGYTNVA 105
Cdd:cd01532   14 IDVREEDPFAQSHPLWAANLPLSRLELDAWVRIPRRDTPIVVYGEGGGEdlAPRAARRLSELGYTDVA 81
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 31-102 2.42e-08

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: 2.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  31 QTAQHPaVWIDVRSEQEFSEGHLHNAVNIPVDQIVRRIHEAAP--------DKDTPVNLYCRSGRRAKAALQELKKAGYT 102
Cdd:cd01526   20 QAGKKH-VLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKSlqelpldnDKDSPIYVVCRRGNDSQTAVRKLKELGLE 98
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 40-109 2.75e-08

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 50.09  E-value: 2.75e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  40 IDVRSEQEFSEGHLHNAVNIPVDQIVRRIHEAAPDKDTPVNLYCRSGRRAKAALQELKKAGYTNVANHGG 109
Cdd:PRK07878 307 IDVREPVEWDIVHIPGAQLIPKSEILSGEALAKLPQDRTIVLYCKTGVRSAEALAALKKAGFSDAVHLQG 376
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 40-109 2.99e-08

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: 48.01  E-value: 2.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  40 IDVRSEQEFS-----------EGHLHNAVNIP-------------VDQIVRRIHEAAPDKDTPVNLYCRSGRRA---KAA 92
Cdd:cd01449   18 VDARSPERFRgevpeprpglrSGHIPGAVNIPwtslldedgtfksPEELRALFAALGITPDKPVIVYCGSGVTAcvlLLA 97

                         90
                 ....*....|....*..
gi 488149983  93 LQELkkaGYTNVANHGG 109
Cdd:cd01449   98 LELL---GYKNVRLYDG 111
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 40-106 5.90e-08

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 49.02  E-value: 5.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  40 IDVRSEQEFS---E------GHLHNAVNIP-------------VDQIVRRIHEAAPDKDTPVNLYCRSGRRAKAALQELK 97
Cdd:COG2897  157 VDARSPERYRgevEpidpraGHIPGAVNLPwtdlldedgtfksAEELRALFAALGIDPDKPVITYCGSGVRAAHTWLALE 236


                 ....*....
gi 488149983  98 KAGYTNVAN 106
Cdd:COG2897  237 LLGYPNVRL 245
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 33-111 1.47e-07

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: 45.71  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  33 AQHPAVWIDVRSEQEF--SEGHLHNAV---NIPVDQIVRRIheaapDKDTPVNLYCRSGRRAKAALQELKKAGYTNV-AN 106
Cdd:cd01444   13 AGEAPVLLDVRDPASYaaLPDHIPGAIhldEDSLDDWLGDL-----DRDRPVVVYCYHGNSSAQLAQALREAGFTDVrSL 87


                 ....*
gi 488149983 107 HGGYE 111
Cdd:cd01444   88 AGGFE 92
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 40-110 3.80e-07

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 46.75  E-value: 3.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  40 IDVRSEQEFSEGHLHNAVNIPV---------------------------------DQIVRRIHEAAPDKDTPVNLYC-RS 85
Cdd:PRK11784  19 IDVRSPIEFAEGHIPGAINLPLlndeeraevgtcykqqgqfaaialghalvagniAAHREEAWADFPRANPRGLLYCwRG 98

                         90       100
                 ....*....|....*....|....*
gi 488149983  86 GRRAKAALQELKKAGYTNVANHGGY 110
Cdd:PRK11784  99 GLRSGSVQQWLKEAGIDVPRLEGGY 123
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 40-110 4.42e-07

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: 46.82  E-value: 4.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983   40 IDVRSEQEFSEGHLHNAVNIPV------------------------------DQIVRRIHEAAPDKDTPVN--LYC-RSG 86
Cdd:TIGR03167   6 IDVRSPAEFAEGHLPGAINLPLlndeeraevgtlykqvgpfaaiklglalvsPNLAAHVEQWRAFADGPPQplLYCwRGG 85

                          90       100
                  ....*....|....*....|....
gi 488149983   87 RRAKAALQELKKAGYTNVANHGGY 110
Cdd:TIGR03167  86 MRSGSLAWLLAQIGFRVPRLEGGY 109
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 29-117 5.67e-07

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: 44.34  E-value: 5.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  29 AAQTAQHPAVWIDVRSEQEF-SEGHLHNAVNIPVDQIVRRI------HEAAPDKDTPVNLYCRSGRRAKAALQELKKAGY 101
Cdd:cd01447    7 RALLGSPGVLLVDVRDPRELeRTGMIPGAFHAPRGMLEFWAdpdspyHKPAFAEDKPFVFYCASGWRSALAGKTLQDMGL 86

                         90
                 ....*....|....*..
gi 488149983 102 TNVAN-HGGYEDLLKKG 117
Cdd:cd01447   87 KPVYNiEGGFKDWKEAG 103
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 37-106 5.81e-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: 44.31  E-value: 5.81e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488149983  37 AVWIDVRSEQEFSEGHLHNAVNIPVDQIVRR---IHEAAPDKDTPVnlYCRSGRRAKAALQELKKAGYTNVAN 106
Cdd:cd01528   18 PVLIDVREPEELEIAFLPGFLHLPMSEIPERskeLDSDNPDKDIVV--LCHHGGRSMQVAQWLLRQGFENVYN 88
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 27-103 2.47e-06

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: 42.83  E-value: 2.47e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488149983  27 LSAAQTAQHPAVWIDVRSEQEFSEGHLHNAVNIPVDQIVRRIHEAAPDKDTPVNLYCRSGRRAKAALQELKKAGYTN 103
Cdd:cd01533   17 LAALQARGAPLVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGELAPDPRTPIVVNCAGRTRSIIGAQSLINAGLPN 93
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
34-111 2.55e-06

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 42.70  E-value: 2.55e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488149983  34 QHPAVWIDVRSEQEFSEGHLHNAVNIPVDQIVRRIHEAapDKDTPVNLYCRSGRRAKAALQELKKAGYTNVAN-HGGYE 111
Cdd:PRK00162  18 EGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQA--DFDTPVMVMCYHGNSSQGAAQYLLQQGFDVVYSiDGGFE 94
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 27-109 4.87e-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: 41.80  E-value: 4.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  27 LSAAQTAQH----PAVWIDVRSEQEFSEGHLHNAVNIPVDQIvRRIHEAAPD-----KDTPVNLYCRSGRRAKAALQELK 97
Cdd:cd01518    4 LSPAEWNELledpEVVLLDVRNDYEYDIGHFKGAVNPDVDTF-REFPFWLDEnldllKGKKVLMYCTGGIRCEKASAYLK 82

                         90
                 ....*....|...
gi 488149983  98 KAGYTNVAN-HGG 109
Cdd:cd01518   83 ERGFKNVYQlKGG 95
PLN02160 PLN02160
thiosulfate sulfurtransferase
 27-109 4.93e-06

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 42.77  E-value: 4.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488149983  27 LSAAQTA-QHPAVWIDVRSEQEFSEGHLHNA--VNIP---------------VDQIVRRIHeaaPDKDTPVNlyCRSGRR 88
Cdd:PLN02160  19 VSQAKTLlQSGHQYLDVRTQDEFRRGHCEAAkiVNIPymlntpqgrvknqefLEQVSSLLN---PADDILVG--CQSGAR 93

                         90       100
                 ....*....|....*....|.
gi 488149983  89 AKAALQELKKAGYTNVANHGG 109
Cdd:PLN02160  94 SLKATTELVAAGYKKVRNKGG 114
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
37-109 3.16e-05

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 41.37  E-value: 3.16e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488149983  37 AVWIDVRSEQEFSEGHLHNAVNIPVD---QIVRRIHEA-APDKDTPVNLYCRSGRRAKAALQELKKAGYTNVAN-HGG 109
Cdd:PRK00142 128 VVFIDMRNDYEYEIGHFENAIEPDIEtfrEFPPWVEENlDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQlEGG 205
RHOD_YbbB cd01520
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ...
 40-61 3.74e-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: 3.74e-05
                         10        20
                 ....*....|....*....|..
gi 488149983  40 IDVRSEQEFSEGHLHNAVNIPV 61
Cdd:cd01520   17 IDVRSPKEFFEGHLPGAINLPL 38
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 41-101 8.51e-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: 35.91  E-value: 8.51e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488149983  41 DVRSEQEFSEGHLHNAVNIPVDQIVRRIHEAAPDKDTPVNLYCRSGRRAKAALQELKKAGY 101
Cdd:cd01534   21 DVRTPEEYEAGHLPGFRHTPGGQLVQETDHFAPVRGARIVLADDDGVRADMTASWLAQMGW 81
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 40-67 9.86e-04

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 36.49  E-value: 9.86e-04
                         10        20
                 ....*....|....*....|....*...
gi 488149983  40 IDVRSEQEFSEGHLHNAVNIPVDQIVRR 67
Cdd:cd01446   21 LDCRPFLEYSSSHIRGAVNVCCPTILRR 48
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 26-96 3.38e-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: 34.38  E-value: 3.38e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488149983  26 PLSAAQTAQHPAVWIDVRSEQEFSEGHLHNAVNIPVDQIvRRIHEAAPDKDTpVNLYCRSGRRAKAALQEL 96
Cdd:cd01527    6 PNDACELLAQGAVLVDIREPDEYLRERIPGARLVPLSQL-ESEGLPLVGANA-IIFHCRSGMRTQQNAERL 74
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 38-94 4.78e-03

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: 34.25  E-value: 4.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488149983  38 VWIDVRSEQEFSEGHLHNAVNIPvdqiVRRIHEAAP---DKDTPVNLYCRS---GRRAKAALQ 94
Cdd:cd01521   27 VLVDVRSAEAYARGHVPGAINLP----HREICENATaklDKEKLFVVYCDGpgcNGATKAALK 85
 
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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