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Conserved domains on  [gi|112491353|pdb|2HHG|A]
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Chain A, Hypothetical protein RPA3614

Protein Classification

rhodanese-like domain-containing protein( domain architecture ID 10106649)

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
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 24-128 3.73e-58

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: 175.69  E-value: 3.73e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       24 LTTADAIALHKSGasDVVIVDIRDPREIERDGKIPGSFSCTRG*LEFWIDPQSPYAKPIFQEDKKFVFYCAGGLRSALAA 103
Cdd:cd01447   1 LSPEDARALLGSP--GVLLVDVRDPRELERTGMIPGAFHAPRGMLEFWADPDSPYHKPAFAEDKPFVFYCASGWRSALAG 78

                        90       100
                ....*....|....*....|....*
2HHG_A      104 KTAQD*GLKPVAHIEGGFGAWRDAG 128
Cdd:cd01447  79 KTLQDMGLKPVYNIEGGFKDWKEAG 103
 
Name Accession Description Interval E-value
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 24-128 3.73e-58

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: 175.69  E-value: 3.73e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       24 LTTADAIALHKSGasDVVIVDIRDPREIERDGKIPGSFSCTRG*LEFWIDPQSPYAKPIFQEDKKFVFYCAGGLRSALAA 103
Cdd:cd01447   1 LSPEDARALLGSP--GVLLVDVRDPRELERTGMIPGAFHAPRGMLEFWADPDSPYHKPAFAEDKPFVFYCASGWRSALAG 78

                        90       100
                ....*....|....*....|....*
2HHG_A      104 KTAQD*GLKPVAHIEGGFGAWRDAG 128
Cdd:cd01447  79 KTLQDMGLKPVYNIEGGFKDWKEAG 103
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 19-133 1.01e-27

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: 98.50  E-value: 1.01e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       19 SSIETLTTADAIALHKSGasDVVIVDIRDPREIERdGKIPGSFSCTRG*LEFWIDPqspyakpiFQEDKKFVFYCAGGLR 98
Cdd:COG0607   1 ASVKEISPAELAELLESE--DAVLLDVREPEEFAA-GHIPGAINIPLGELAERLDE--------LPKDKPIVVYCASGGR 69

                        90       100       110
                ....*....|....*....|....*....|....*
2HHG_A       99 SALAAKTAQD*GLKPVAHIEGGFGAWRDAGGPIEA 133
Cdd:COG0607  70 SAQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVEK 104
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
20-132 1.51e-21

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 88.14  E-value: 1.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A        20 SIETLTTADAIALHKSGAsdvVIVDIRDPREIErDGKIPGSFSCTRG*LEFWIDPQSPyakpifQEDKKFVFYCAGGLRS 99
Cdd:PRK08762   1 SIREISPAEARARAAQGA---VLIDVREAHERA-SGQAEGALRIPRGFLELRIETHLP------DRDREIVLICASGTRS 70

                         90       100       110
                 ....*....|....*....|....*....|...
2HHG_A       100 ALAAKTAQD*GLKPVAHIEGGFGAWRDAGGPIE 132
Cdd:PRK08762  71 AHAAATLRELGYTRVASVAGGFSAWKDAGLPLE 103
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 36-124 5.51e-17

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: 5.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A         36 GASDVVIVDIRDPREIERdGKIPGSFSCTRG*LEFWIDPQSPYAKPIFQ--EDKKFVFYCAGGLRSALAAKTAQD*GLKP 113
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAK-GHIPGAVNVPLSSLSLPPLPLLELLEKLLEllKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|.
2HHG_A        114 VAHIEGGFGAW 124
Cdd:pfam00581  81 VYVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 36-130 2.67e-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: 66.71  E-value: 2.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A          36 GASDVVIVDIRDPREIERdGKIPGSFSCTRG*LEFWIDPQSPYAKPIFQ------EDKKFVFYCAGGLRSALAAKTAQD* 109
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEG-GHIPGAVNIPLSELLDRRGELDILEFEELLkrlgldKDKPVVVYCRSGNRSAKAAWLLREL 79

                           90       100
                   ....*....|....*....|.
2HHG_A         110 GLKPVAHIEGGFGAWRDAGGP 130
Cdd:smart00450  80 GFKNVYLLDGGYKEWSAAGPP 100
 
Name Accession Description Interval E-value
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 24-128 3.73e-58

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: 175.69  E-value: 3.73e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       24 LTTADAIALHKSGasDVVIVDIRDPREIERDGKIPGSFSCTRG*LEFWIDPQSPYAKPIFQEDKKFVFYCAGGLRSALAA 103
Cdd:cd01447   1 LSPEDARALLGSP--GVLLVDVRDPRELERTGMIPGAFHAPRGMLEFWADPDSPYHKPAFAEDKPFVFYCASGWRSALAG 78

                        90       100
                ....*....|....*....|....*
2HHG_A      104 KTAQD*GLKPVAHIEGGFGAWRDAG 128
Cdd:cd01447  79 KTLQDMGLKPVYNIEGGFKDWKEAG 103
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 19-133 1.01e-27

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: 98.50  E-value: 1.01e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       19 SSIETLTTADAIALHKSGasDVVIVDIRDPREIERdGKIPGSFSCTRG*LEFWIDPqspyakpiFQEDKKFVFYCAGGLR 98
Cdd:COG0607   1 ASVKEISPAELAELLESE--DAVLLDVREPEEFAA-GHIPGAINIPLGELAERLDE--------LPKDKPIVVYCASGGR 69

                        90       100       110
                ....*....|....*....|....*....|....*
2HHG_A       99 SALAAKTAQD*GLKPVAHIEGGFGAWRDAGGPIEA 133
Cdd:COG0607  70 SAQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVEK 104
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
20-132 1.51e-21

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 88.14  E-value: 1.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A        20 SIETLTTADAIALHKSGAsdvVIVDIRDPREIErDGKIPGSFSCTRG*LEFWIDPQSPyakpifQEDKKFVFYCAGGLRS 99
Cdd:PRK08762   1 SIREISPAEARARAAQGA---VLIDVREAHERA-SGQAEGALRIPRGFLELRIETHLP------DRDREIVLICASGTRS 70

                         90       100       110
                 ....*....|....*....|....*....|...
2HHG_A       100 ALAAKTAQD*GLKPVAHIEGGFGAWRDAGGPIE 132
Cdd:PRK08762  71 AHAAATLRELGYTRVASVAGGFSAWKDAGLPLE 103
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 36-124 5.51e-17

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: 5.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A         36 GASDVVIVDIRDPREIERdGKIPGSFSCTRG*LEFWIDPQSPYAKPIFQ--EDKKFVFYCAGGLRSALAAKTAQD*GLKP 113
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAK-GHIPGAVNVPLSSLSLPPLPLLELLEKLLEllKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|.
2HHG_A        114 VAHIEGGFGAW 124
Cdd:pfam00581  81 VYVLDGGFEAW 91
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 39-125 1.69e-15

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: 66.94  E-value: 1.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       39 DVVIVDIRDPREIERdGKIPGSFSCTRG*LEFWIDPQSPYAkpifqeDKKFVFYCAGGLRSALAAKTAQD*GLKPVAHIE 118
Cdd:cd00158  10 DAVLLDVREPEEYAA-GHIPGAINIPLSELEERAALLELDK------DKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLE 82


                ....*..
2HHG_A      119 GGFGAWR 125
Cdd:cd00158  83 GGMLAWK 89
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 36-130 2.67e-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: 66.71  E-value: 2.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A          36 GASDVVIVDIRDPREIERdGKIPGSFSCTRG*LEFWIDPQSPYAKPIFQ------EDKKFVFYCAGGLRSALAAKTAQD* 109
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEG-GHIPGAVNIPLSELLDRRGELDILEFEELLkrlgldKDKPVVVYCRSGNRSAKAAWLLREL 79

                           90       100
                   ....*....|....*....|.
2HHG_A         110 GLKPVAHIEGGFGAWRDAGGP 130
Cdd:smart00450  80 GFKNVYLLDGGYKEWSAAGPP 100
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 24-126 1.99e-12

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: 59.20  E-value: 1.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       24 LTTADAIALHKSGaSDVVIVDIRDPREIERD-GKIPGSFSCTRG*LEFWIdpqspyakPIFQEDKKFVFYCAGGLRSALA 102
Cdd:cd01444   2 ISVDELAELLAAG-EAPVLLDVRDPASYAALpDHIPGAIHLDEDSLDDWL--------GDLDRDRPVVVYCYHGNSSAQL 72

                        90       100
                ....*....|....*....|....
2HHG_A      103 AKTAQD*GLKPVAHIEGGFGAWRD 126
Cdd:cd01444  73 AQALREAGFTDVRSLAGGFEAWRR 96
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 39-126 7.09e-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: 55.35  E-value: 7.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       39 DVVIVDIRDPREIeRDGKIPGSFSCTRG*LE--FWIDPQS-----PYAKPIFqeDKKFVFYCAGGLRSALAAKTAQD*GL 111
Cdd:cd01519  15 NKVLIDVREPEEL-KTGKIPGAINIPLSSLPdaLALSEEEfekkyGFPKPSK--DKELIFYCKAGVRSKAAAELARSLGY 91

                        90
                ....*....|....*
2HHG_A      112 KPVAHIEggfGAWRD 126
Cdd:cd01519  92 ENVGNYP---GSWLD 103
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
1-130 1.90e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 51.27  E-value: 1.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A         1 G*PQTitrgiKA*LDEANSSIETLTTADAIALHKSGASDVVIVDIRDPREIERdGKIPGSFSCTRG*LEfwidpQSPYAK 80
Cdd:PRK07411 266 GIPQA-----KAAEAAQKAEIPEMTVTELKALLDSGADDFVLIDVRNPNEYEI-ARIPGSVLVPLPDIE-----NGPGVE 334

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
2HHG_A        81 PIFQ--EDKKFVFYCAGGLRSALAAKTAQD*GLKPVaHIEGGFGAWRDAGGP 130
Cdd:PRK07411 335 KVKEllNGHRLIAHCKMGGRSAKALGILKEAGIEGT-NVKGGITAWSREVDP 385
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 38-127 4.04e-07

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 47.56  E-value: 4.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A        38 SDVVIVDIRDPREIErDGKIPGSFSCTRG*LEfwidpqSPYAKPIFQEDKKFVFYCAGGLRSALAAKTAQD*GLKPVAHI 117
Cdd:PRK05597 273 DGVTLIDVREPSEFA-AYSIPGAHNVPLSAIR------EGANPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYTGMSSL 345

                         90
                 ....*....|
2HHG_A       118 EGGFGAWRDA 127
Cdd:PRK05597 346 DGGIEGWLDS 355
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 21-131 4.29e-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: 45.17  E-value: 4.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       21 IETLTTADAIALHKSGAsdvVIVDIRDPREIERDgKIPGSFSCTRG*LEfwidpQSPYAKPIFQEdkkFVFYCAGGLRSA 100
Cdd:cd01527   1 LTTISPNDACELLAQGA---VLVDIREPDEYLRE-RIPGARLVPLSQLE-----SEGLPLVGANA---IIFHCRSGMRTQ 68

                        90       100       110
                ....*....|....*....|....*....|.
2HHG_A      101 LAAKTAQD*GLKPVAHIEGGFGAWRDAGGPI 131
Cdd:cd01527  69 QNAERLAAISAGEAYVLEGGLDAWKAAGLPV 99
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 23-124 3.20e-06

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: 43.15  E-value: 3.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       23 TLTTADAIALHKSGASDVVIVDIRDPREIERdGKIPGSFSCTRG*LEFWIDpqspyAKPIFQEDKKFVFYCAGGLRSALA 102
Cdd:cd01528   1 QISVAELAEWLADEREEPVLIDVREPEELEI-AFLPGFLHLPMSEIPERSK-----ELDSDNPDKDIVVLCHHGGRSMQV 74

                        90       100
                ....*....|....*....|..
2HHG_A      103 AKTAQD*GLKPVAHIEGGFGAW 124
Cdd:cd01528  75 AQWLLRQGFENVYNLQGGIDAW 96
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 23-124 3.81e-06

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 44.70  E-value: 3.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A        23 TLTTADAIALHKSGAsDVVIVDIRDPREIERDgKIPGSFSCTRG*LEfwidpqSPYAKPIFQEDKKFVFYCAGGLRSALA 102
Cdd:PRK07878 288 TITPRELKEWLDSGK-KIALIDVREPVEWDIV-HIPGAQLIPKSEIL------SGEALAKLPQDRTIVLYCKTGVRSAEA 359

                         90       100
                 ....*....|....*....|..
2HHG_A       103 AKTAQD*GLKPVAHIEGGFGAW 124
Cdd:PRK07878 360 LAALKKAGFSDAVHLQGGVVAW 381
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
28-133 3.98e-06

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 42.70  E-value: 3.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A        28 DAIALHKSGasDVVIVDIRDPREIERdGKIPGSFSCTRG*LEFWIDpQSPYAKPIfqedkkfVFYCAGGLRSALAAKTAQ 107
Cdd:PRK00162  11 QAHQKLQEG--GAVLVDIRDPQSFAM-GHAPGAFHLTNDSLGAFMR-QADFDTPV-------MVMCYHGNSSQGAAQYLL 79

                         90       100
                 ....*....|....*....|....*.
2HHG_A       108 D*GLKPVAHIEGGFGAWRDAGGPIEA 133
Cdd:PRK00162  80 QQGFDVVYSIDGGFEAWRRTFPAEVA 105
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 42-125 1.10e-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: 41.51  E-value: 1.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       42 IVDIRDPREIERdGKIPGSFSCTRG*LEFWIDPQSPYAKPIfqEDKKFVFYCAGGLRSALAAKTAQD*GLKPVAHIEGGF 121
Cdd:cd01529  15 LLDVRAEDEYAA-GHLPGKRSIPGAALVLRSQELQALEAPG--RATRYVLTCDGSLLARFAAQELLALGGKPVALLDGGT 91


                ....
2HHG_A      122 GAWR 125
Cdd:cd01529  92 SAWV 95
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 40-124 6.37e-05

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: 39.17  E-value: 6.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       40 VVIVDIRDPREIERdGKIPGSFSCTRG*LEFWIDPqspyakpiFQEDKKFVFYCAGGLRSALAAKTAQD*GLKpVAHIEG 119
Cdd:cd01524  14 VTLIDVRTPQEFEK-GHIKGAINIPLDELRDRLNE--------LPKDKEIIVYCAVGLRGYIAARILTQNGFK-VKNLDG 83


                ....*
2HHG_A      120 GFGAW 124
Cdd:cd01524  84 GYKTY 88
4RHOD_Repeat_4 cd01535
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative ...
 53-132 8.94e-05

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: 39.80  E-value: 8.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       53 RDGKIPGSFSCTRG*LefwidPQSPYAKPIFQedkKFVFYCAGGLRSALAAKTAQD*GLKPVAHIEGGFGAWRDAGGPIE 132
Cdd:cd01535  24 VKRHIPGAWWVLRAQL-----AQALEKLPAAE---RYVLTCGSSLLARFAAADLAALTVKPVFVLEGGTAAWIAAGLPVE 95
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 39-120 1.30e-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: 38.71  E-value: 1.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       39 DVVIVDIRDPREIerdgKIpGSFsctRG*LEFWIDP---QSPYAK--PIFQEDKKFVFYCAGGLRSALAAKTAQD*GLKP 113
Cdd:cd01518  17 EVVLLDVRNDYEY----DI-GHF---KGAVNPDVDTfreFPFWLDenLDLLKGKKVLMYCTGGIRCEKASAYLKERGFKN 88


                ....*..
2HHG_A      114 VAHIEGG 120
Cdd:cd01518  89 VYQLKGG 95
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 29-130 2.15e-04

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: 38.10  E-value: 2.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       29 AIALhKSGASDVVIVDIRDPREIERdGKIPGSFSCTRG*LEFWIDPQSPYAKPifqedkkFVFYCAGgLRSALAAKTAqd 108
Cdd:cd01521  16 AIAL-KNGKPDFVLVDVRSAEAYAR-GHVPGAINLPHREICENATAKLDKEKL-------FVVYCDG-PGCNGATKAA-- 83

                        90       100
                ....*....|....*....|....*...
2HHG_A      109 *gLK------PVAHIEGGFGAWRDAGGP 130
Cdd:cd01521  84 --LKlaelgfPVKEMIGGLDWWKREGYA 109
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 36-132 6.23e-04

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 38.23  E-value: 6.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       36 GASDVVIVDIR----DPREIERDGKIPGS-FSCTRG*LEfwiDPQSPYAKPI-----FQE---------DKKFVFY-CAG 95
Cdd:COG2897   6 DDPDVVILDVRwdlpDGRAAYEAGHIPGAvFLDLDTDLS---DPRSPGRHPLpspeaFAAllgalgisnDTTVVVYdDGG 82

                        90       100       110
                ....*....|....*....|....*....|....*..
2HHG_A       96 GLRSALAAKTAQD*GLKPVAHIEGGFGAWRDAGGPIE 132
Cdd:COG2897  83 GLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLE 119
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 24-132 2.00e-03

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 36.69  E-value: 2.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       24 LTTADAIaLHKSGASDVVIVDIRDPRE--------IERDGKIPGSFSctrg*LEF--WIDPQ----SP------YAKPIF 83
Cdd:COG2897 139 LADADEV-LAALGDPDAVLVDARSPERyrgevepiDPRAGHIPGAVN-----LPWtdLLDEDgtfkSAeelralFAALGI 212

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
2HHG_A       84 QEDKKFVFYCAGGLRSA---LAAKTAqd*GLKPVAHIEGGFGAW-RDAGGPIE 132
Cdd:COG2897 213 DPDKPVITYCGSGVRAAhtwLALELL---GYPNVRLYDGSWSEWgSDPDLPVE 262
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 32-124 2.21e-03

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: 35.69  E-value: 2.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       32 LHKSGASDVVIVDIRD----------PREIERDGKIPGSF-----SCTRG*LEFwIDPQspYAKPIFQE-----DKKFVF 91
Cdd:cd01449   7 LANLDSGDVQLVDARSperfrgevpePRPGLRSGHIPGAVnipwtSLLDEDGTF-KSPE--ELRALFAAlgitpDKPVIV 83

                        90       100       110
                ....*....|....*....|....*....|....*.
2HHG_A       92 YCAGGLRSA---LAAKTAqd*GLKPVAHIEGGFGAW 124
Cdd:cd01449  84 YCGSGVTACvllLALELL---GYKNVRLYDGSWSEW 116
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
39-120 2.92e-03

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 36.36  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A        39 DVVIVDIRDPREIErdgkIpGSFsctRG*LEFWIDP---QSPYAKPIFQ--EDKKFVFYCAGGLR----SALAAKtaqd* 109
Cdd:PRK00142 127 DVVFIDMRNDYEYE----I-GHF---ENAIEPDIETfreFPPWVEENLDplKDKKVVMYCTGGIRcekaSAWMKH----E 194

                         90
                 ....*....|.
2HHG_A       110 GLKPVAHIEGG 120
Cdd:PRK00142 195 GFKEVYQLEGG 205
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 24-134 6.93e-03

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: 34.23  E-value: 6.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A       24 LTTADAIALhKSGASDVVIVDIRDPREIERDGKIPGSFSCTRG*LEFW-IDPQ-SPYAKPIFQEDKKFVFYCAGGLRSAL 101
Cdd:cd01522   1 LTPAEAWAL-LQADPQAVLVDVRTEAEWKFVGGVPDAVHVAWQVYPDMeINPNfLAELEEKVGKDRPVLLLCRSGNRSIA 79

                        90       100       110
                ....*....|....*....|....*....|....*.
2HHG_A      102 AAKTAQD*GLKPVAHIEGGF-GAWRDAG--GPIEAW 134
Cdd:cd01522  80 AAEAAAQAGFTNVYNVLEGFeGDLDAAGhrGGVNGW 115
PRK05320 PRK05320
rhodanese superfamily protein; Provisional
 40-120 8.65e-03

rhodanese superfamily protein; Provisional


Pssm-ID: 235405 [Multi-domain]  Cd Length: 257  Bit Score: 35.00  E-value: 8.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2HHG_A        40 VVIVDIRDPREIERdgkipGSFsctRG*LEFWIDPQSPYAKPIFQ-----EDKKFVFYCAGGLRSALAAKTAQD*GLKPV 114
Cdd:PRK05320 132 VVMLDTRNAFEVDV-----GTF---DGALDYRIDKFTEFPEALAAhradlAGKTVVSFCTGGIRCEKAAIHMQEVGIDNV 203


                 ....*.
2HHG_A       115 AHIEGG 120
Cdd:PRK05320 204 YQLEGG 209
 
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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