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Conserved domains on  [gi|502114521|ref|WP_012712671|]
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MULTISPECIES: rhodanese-like domain-containing protein [Sulfolobaceae]

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]; ...
 18-117 2.99e-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: 96.96  E-value: 2.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  18 DLPPSMVRKLWKSGKIIILDIRTPQEYEDHHIPGAILAPLNYLE-HLTELFEDREVAVVCEHGNRASYATYGMPHLYKKK 96
Cdd:COG0607    5 EISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAeRLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTN 84

                         90       100
                 ....*....|....*....|.
gi 502114521  97 AYYMIGGMALWMAMGYEVESG 117
Cdd:COG0607   85 VYNLAGGIEAWKAAGLPVEKG 105
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 18-117 2.99e-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: 96.96  E-value: 2.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  18 DLPPSMVRKLWKSGKIIILDIRTPQEYEDHHIPGAILAPLNYLE-HLTELFEDREVAVVCEHGNRASYATYGMPHLYKKK 96
Cdd:COG0607    5 EISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAeRLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTN 84

                         90       100
                 ....*....|....*....|.
gi 502114521  97 AYYMIGGMALWMAMGYEVESG 117
Cdd:COG0607   85 VYNLAGGIEAWKAAGLPVEKG 105
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 24-107 8.28e-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: 87.74  E-value: 8.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  24 VRKLWKSGKIIILDIRTPQEYEDHHIPGAILAPLNYLEH---LTELFEDREVAVVCEHGNRASYATYGMPHLYKKKAYYM 100
Cdd:cd00158    2 LKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEEraaLLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNL 81


                 ....*..
gi 502114521 101 IGGMALW 107
Cdd:cd00158   82 EGGMLAW 88
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 29-107 2.43e-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: 69.03  E-value: 2.43e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521    29 KSGKIIILDIRTPQEYEDHHIPGAILAPLNYLEHLTELF---------------EDREVAVVCEHGNRASYATYGMPHLY 93
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELdilefeellkrlgldKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90
                   ....*....|....
gi 502114521    94 KKKAYYMIGGMALW 107
Cdd:smart00450  81 FKNVYLLDGGYKEW 94
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 29-107 3.56e-15

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


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 65.97  E-value: 3.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521   29 KSGKIIILDIRTPQEYEDHHIPGAILAPLNYL-----------EHLTELFEDREVAVVCEHGNRASYATYGMPHLYKKKA 97
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLslpplpllellEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNV 81

                          90
                  ....*....|
gi 502114521   98 YYMIGGMALW 107
Cdd:pfam00581  82 YVLDGGFEAW 91
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
16-115 7.68e-12

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 60.80  E-value: 7.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  16 IIDLPPSMVRKLWKSGKIIIlDIRTPQEYEDHHIPGAILAPLNYLE-----HLTELfeDREVAVVCEHGNRASYATYGMP 90
Cdd:PRK08762   2 IREISPAEARARAAQGAVLI-DVREAHERASGQAEGALRIPRGFLElrietHLPDR--DREIVLICASGTRSAHAAATLR 78

                         90       100
                 ....*....|....*....|....*
gi 502114521  91 HLYKKKAYYMIGGMALWMAMGYEVE 115
Cdd:PRK08762  79 ELGYTRVASVAGGFSAWKDAGLPLE 103
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 18-117 2.99e-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: 96.96  E-value: 2.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  18 DLPPSMVRKLWKSGKIIILDIRTPQEYEDHHIPGAILAPLNYLE-HLTELFEDREVAVVCEHGNRASYATYGMPHLYKKK 96
Cdd:COG0607    5 EISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAeRLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTN 84

                         90       100
                 ....*....|....*....|.
gi 502114521  97 AYYMIGGMALWMAMGYEVESG 117
Cdd:COG0607   85 VYNLAGGIEAWKAAGLPVEKG 105
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 24-107 8.28e-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: 87.74  E-value: 8.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  24 VRKLWKSGKIIILDIRTPQEYEDHHIPGAILAPLNYLEH---LTELFEDREVAVVCEHGNRASYATYGMPHLYKKKAYYM 100
Cdd:cd00158    2 LKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEEraaLLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNL 81


                 ....*..
gi 502114521 101 IGGMALW 107
Cdd:cd00158   82 EGGMLAW 88
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 29-107 2.43e-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: 69.03  E-value: 2.43e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521    29 KSGKIIILDIRTPQEYEDHHIPGAILAPLNYLEHLTELF---------------EDREVAVVCEHGNRASYATYGMPHLY 93
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELdilefeellkrlgldKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90
                   ....*....|....
gi 502114521    94 KKKAYYMIGGMALW 107
Cdd:smart00450  81 FKNVYLLDGGYKEW 94
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 29-107 3.56e-15

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


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 65.97  E-value: 3.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521   29 KSGKIIILDIRTPQEYEDHHIPGAILAPLNYL-----------EHLTELFEDREVAVVCEHGNRASYATYGMPHLYKKKA 97
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLslpplpllellEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNV 81

                          90
                  ....*....|
gi 502114521   98 YYMIGGMALW 107
Cdd:pfam00581  82 YVLDGGFEAW 91
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 19-109 1.81e-13

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: 61.51  E-value: 1.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  19 LPPSMVRKLWKSGK-IIILDIRTPQEYED--HHIPGAI-LAPLNYLEHLTELFEDREVAVVCEHGNRAS-YATYGMPHLY 93
Cdd:cd01444    2 ISVDELAELLAAGEaPVLLDVRDPASYAAlpDHIPGAIhLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAqLAQALREAGF 81

                         90
                 ....*....|....*.
gi 502114521  94 kKKAYYMIGGMALWMA 109
Cdd:cd01444   82 -TDVRSLAGGFEAWRR 96
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
16-115 7.68e-12

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 60.80  E-value: 7.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  16 IIDLPPSMVRKLWKSGKIIIlDIRTPQEYEDHHIPGAILAPLNYLE-----HLTELfeDREVAVVCEHGNRASYATYGMP 90
Cdd:PRK08762   2 IREISPAEARARAAQGAVLI-DVREAHERASGQAEGALRIPRGFLElrietHLPDR--DREIVLICASGTRSAHAAATLR 78

                         90       100
                 ....*....|....*....|....*
gi 502114521  91 HLYKKKAYYMIGGMALWMAMGYEVE 115
Cdd:PRK08762  79 ELGYTRVASVAGGFSAWKDAGLPLE 103
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 34-107 1.41e-09

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: 51.50  E-value: 1.41e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502114521  34 IILDIRTPQEYEDHHIPGAILAPLNYL-EHLTELFEDREVAVVCEHGNRaSYATYGMPHLYKKKAYYMIGGMALW 107
Cdd:cd01524   15 TLIDVRTPQEFEKGHIKGAINIPLDELrDRLNELPKDKEIIVYCAVGLR-GYIAARILTQNGFKVKNLDGGYKTY 88
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 19-114 1.01e-08

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: 49.41  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  19 LPPSMVRKLWKSGKIIIlDIRTPQEYEDHHIPGAILAPLNYLEHL-TELFEDREVAVVCEHGNRASYATYGMPHLYKKKA 97
Cdd:cd01527    4 ISPNDACELLAQGAVLV-DIREPDEYLRERIPGARLVPLSQLESEgLPLVGANAIIFHCRSGMRTQQNAERLAAISAGEA 82

                         90
                 ....*....|....*..
gi 502114521  98 YYMIGGMALWMAMGYEV 114
Cdd:cd01527   83 YVLEGGLDAWKAAGLPV 99
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 19-111 5.68e-08

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: 47.42  E-value: 5.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  19 LPPSMVRKLWKSGKIIILDIRTPQEYE-DHHIPGAILAPLNYLE---------HLTELFEDREVAVVCEHGNRASYATYG 88
Cdd:cd01447    1 LSPEDARALLGSPGVLLVDVRDPRELErTGMIPGAFHAPRGMLEfwadpdspyHKPAFAEDKPFVFYCASGWRSALAGKT 80

                         90       100
                 ....*....|....*....|...
gi 502114521  89 MPHLYKKKAYYMIGGMALWMAMG 111
Cdd:cd01447   81 LQDMGLKPVYNIEGGFKDWKEAG 103
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 32-81 2.29e-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: 45.85  E-value: 2.29e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502114521  32 KIIILDIRTPQEYEDHHIPGAILAPLN----YLEHLTELFEDREVAVVCEHGNR 81
Cdd:cd01528   17 EPVLIDVREPEELEIAFLPGFLHLPMSeipeRSKELDSDNPDKDIVVLCHHGGR 70
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 20-107 2.30e-07

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: 45.95  E-value: 2.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  20 PPSMVRKLWKSGKIIILDIRTPQEYEDHHIPGAILAPLNYL---------EHLTELFEDREVAVVCEHGNRASYATyGMP 90
Cdd:cd01523    3 PEDLYARLLAGQPLFILDVRNESDYERWKIDGENNTPYFDPyfdfleieeDILDQLPDDQEVTVICAKEGSSQFVA-ELL 81

                         90
                 ....*....|....*..
gi 502114521  91 HLYKKKAYYMIGGMALW 107
Cdd:cd01523   82 AERGYDVDYLAGGMKAW 98
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 21-85 2.42e-07

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 48.17  E-value: 2.42e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502114521  21 PSMVRKLWKSGK-IIILDIRTPQEYEDHHIPGAILAP---LNYLEHLTELFEDREVAVVCEHGNRASYA 85
Cdd:PRK07878 291 PRELKEWLDSGKkIALIDVREPVEWDIVHIPGAQLIPkseILSGEALAKLPQDRTIVLYCKTGVRSAEA 359
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
19-107 5.34e-07

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 45.01  E-value: 5.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  19 LPPSMVRKLWKSGKIIILDIRTPQEYEDHHIPGAIlaplnyleHLT-----------ELfeDREVAVVCEHGNRA-SYAT 86
Cdd:PRK00162   7 INVEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAF--------HLTndslgafmrqaDF--DTPVMVMCYHGNSSqGAAQ 76

                         90       100
                 ....*....|....*....|.
gi 502114521  87 YGMPHLYkKKAYYMIGGMALW 107
Cdd:PRK00162  77 YLLQQGF-DVVYSIDGGFEAW 96
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 30-117 2.76e-06

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 44.78  E-value: 2.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  30 SGKIIILDIRT-----PQEYEDHHIPGAILAPLNY---------------LEHLTELFE----DREVAVVC---EHGNRA 82
Cdd:COG2897    7 DPDVVILDVRWdlpdgRAAYEAGHIPGAVFLDLDTdlsdprspgrhplpsPEAFAALLGalgiSNDTTVVVyddGGGLFA 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 502114521  83 SYA-----TYGmpHlykKKAYYMIGGMALWMAMGYEVESG 117
Cdd:COG2897   87 ARAwwllrYAG--H---EDVRVLDGGLAAWKAAGLPLETG 121
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
24-85 4.26e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 44.34  E-value: 4.26e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  24 VRKLWKSGK--IIILDIRTPQEYEDHHIPGAILAPL------NYLEHLTELFEDREVAVVCEHGNRASYA 85
Cdd:PRK07411 289 LKALLDSGAddFVLIDVRNPNEYEIARIPGSVLVPLpdiengPGVEKVKELLNGHRLIAHCKMGGRSAKA 358
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 35-109 1.21e-05

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 43.32  E-value: 1.21e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502114521  35 ILDIRTPQEYEDHHIPGAILAPLNYLEH---LTELFEDREVAVVCEHGNRASYATYGMPHLYKKKAYYMIGGMALWMA 109
Cdd:PRK05597 277 LIDVREPSEFAAYSIPGAHNVPLSAIREganPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYTGMSSLDGGIEGWLD 354
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 24-107 2.62e-05

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 42.08  E-value: 2.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  24 VRKLWKSGKIIILDIRTPQEY--EDH-------HIPGAILAPLNYL----------EHLTELFE------DREVAVVCEH 78
Cdd:COG2897  145 VLAALGDPDAVLVDARSPERYrgEVEpidpragHIPGAVNLPWTDLldedgtfksaEELRALFAalgidpDKPVITYCGS 224

                         90       100       110
                 ....*....|....*....|....*....|
gi 502114521  79 GNRASYATYGMPHL-YKKKAYYmIGGMALW 107
Cdd:COG2897  225 GVRAAHTWLALELLgYPNVRLY-DGSWSEW 253
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 32-114 3.52e-05

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: 40.41  E-value: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  32 KIIILDIRTPQEYEDHHIPGAILAPLNYLEHLTELFEDREVAVVC----EHGNRASYATYGMPHL-YKKKAyyMIGGMAL 106
Cdd:cd01521   25 DFVLVDVRSAEAYARGHVPGAINLPHREICENATAKLDKEKLFVVycdgPGCNGATKAALKLAELgFPVKE--MIGGLDW 102


                 ....*...
gi 502114521 107 WMAMGYEV 114
Cdd:cd01521  103 WKREGYAT 110
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 36-56 3.57e-05

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: 40.14  E-value: 3.57e-05
                         10        20
                 ....*....|....*....|.
gi 502114521  36 LDIRTPQEYEDHHIPGAILAP 56
Cdd:cd01534   20 FDVRTPEEYEAGHLPGFRHTP 40
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 13-107 3.73e-05

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: 40.37  E-value: 3.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  13 YKNIIDlppsmvrklwKSGKIIILDIRTPQEYEDHHIPGAILAPLNYL-----EHLTELF------EDREVAVVCEHGNR 81
Cdd:cd01526   15 YKNILQ----------AGKKHVLLDVRPKVHFEICRLPEAINIPLSELlskaaELKSLQElpldndKDSPIYVVCRRGND 84

                         90       100       110
                 ....*....|....*....|....*....|.
gi 502114521  82 ASYATygmpHLYKKKAYYM-----IGGMALW 107
Cdd:cd01526   85 SQTAV----RKLKELGLERfvrdiIGGLKAW 111
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 13-86 7.49e-05

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: 39.18  E-value: 7.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  13 YKNIIDLPPSmvrklwkSGKIIILDIRTPQEYEDHHIPGAILAPLNYLE---HLTEL-FE----------DREVAVVCEH 78
Cdd:cd01519    3 FEEVKNLPNP-------HPNKVLIDVREPEELKTGKIPGAINIPLSSLPdalALSEEeFEkkygfpkpskDKELIFYCKA 75


                 ....*...
gi 502114521  79 GNRASYAT 86
Cdd:cd01519   76 GVRSKAAA 83
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 24-84 1.31e-04

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: 38.77  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  24 VRKLWKSGKIIILDIRTPQEYE--------DH---HIPGAI-------LAPLNYL---EHLTELFE------DREVAVVC 76
Cdd:cd01449    6 VLANLDSGDVQLVDARSPERFRgevpeprpGLrsgHIPGAVnipwtslLDEDGTFkspEELRALFAalgitpDKPVIVYC 85


                 ....*...
gi 502114521  77 EHGNRASY 84
Cdd:cd01449   86 GSGVTACV 93
4RHOD_Repeat_4 cd01535
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative ...
 31-117 1.33e-04

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: 39.41  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  31 GKIIILDIRTPQEYEDHHIPGA---ILAPLNylEHLTELFEDREVAVVCEHGNRASYATYGMPHLYKKKAYYMIGGMALW 107
Cdd:cd01535   10 GQTAVVDVTASANYVKRHIPGAwwvLRAQLA--QALEKLPAAERYVLTCGSSLLARFAAADLAALTVKPVFVLEGGTAAW 87

                         90
                 ....*....|
gi 502114521 108 MAMGYEVESG 117
Cdd:cd01535   88 IAAGLPVESG 97
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 35-109 1.59e-03

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: 35.73  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  35 ILDIRTPQEYEDHHIPGAILAP-------LNYLEHLTELFEDREVAVVCEHGNRASYATYGMPHLYKKKAYYMIGGMALW 107
Cdd:cd01529   15 LLDVRAEDEYAAGHLPGKRSIPgaalvlrSQELQALEAPGRATRYVLTCDGSLLARFAAQELLALGGKPVALLDGGTSAW 94


                 ..
gi 502114521 108 MA 109
Cdd:cd01529   95 VA 96
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 32-57 2.86e-03

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 36.35  E-value: 2.86e-03
                         10        20
                 ....*....|....*....|....*.
gi 502114521  32 KIIILDIRTPQEYEDHHIPGAILAPL 57
Cdd:PRK11784  15 DTPLIDVRSPIEFAEGHIPGAINLPL 40
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 36-85 2.93e-03

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 35.21  E-value: 2.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 502114521  36 LDIRTPQEYEDHHIPGAILAPL-NYLEHLTELFEDRE--VAVVCEHGNRASYA 85
Cdd:PRK10287  24 IDVRVPEQYQQEHVQGAINIPLkEVKERIATAVPDKNdtVKLYCNAGRQSGQA 76
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 29-111 4.15e-03

Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the 1st repeat, which does not contain the catalytically active Cys residue. The role of the 1st repeat is uncertain, but it is believed to be involved in protein interaction.


Pssm-ID: 238725 [Multi-domain]  Cd Length: 122  Bit Score: 34.90  E-value: 4.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502114521  29 KSGKIIILDIRT-------PQEYEDHHIPGAILAPLNYL--------------EHLTELFE------DREVAVVCEHGNR 81
Cdd:cd01448   12 DDPDVRILDARWylpdrdgRKEYLEGHIPGAVFFDLDEDlddkspgphmlpspEEFAELLGslgisnDDTVVVYDDGGGF 91

                         90       100       110
                 ....*....|....*....|....*....|.
gi 502114521  82 ASYATYGMPHLY-KKKAYYMIGGMALWMAMG 111
Cdd:cd01448   92 FAARAWWTLRYFgHENVRVLDGGLQAWKAEG 122
RHOD_YbbB cd01520
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ...
 34-75 6.45e-03

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: 34.58  E-value: 6.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 502114521  34 IILDIRTPQEYEDHHIPGAILAPlnylehlteLFEDREVAVV 75
Cdd:cd01520   15 PLIDVRSPKEFFEGHLPGAINLP---------LLDDEERALV 47
 
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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