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Conserved domains on  [gi|920628913|ref|WP_053030521|]
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rhodanese-like domain-containing protein [Staphylococcus borealis]

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]; ...
 1-97 2.72e-30

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: 103.51  E-value: 2.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   1 MESITVDQLKEKvLESNPVNIVDVRTDEETAMGVIPGAKTIPMDQIPDNLNYFNDKDTYYIICAAGMRSAKVVKYLE--G 78
Cdd:COG0607    3 VKEISPAELAEL-LESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRraG 81

                         90
                 ....*....|....*....
gi 920628913  79 HDiHAINVEGGMNEWGTAG 97
Cdd:COG0607   82 YT-NVYNLAGGIEAWKAAG 99
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 1-97 2.72e-30

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: 103.51  E-value: 2.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   1 MESITVDQLKEKvLESNPVNIVDVRTDEETAMGVIPGAKTIPMDQIPDNLNYFNDKDTYYIICAAGMRSAKVVKYLE--G 78
Cdd:COG0607    3 VKEISPAELAEL-LESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRraG 81

                         90
                 ....*....|....*....
gi 920628913  79 HDiHAINVEGGMNEWGTAG 97
Cdd:COG0607   82 YT-NVYNLAGGIEAWKAAG 99
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 8-93 1.76e-20

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: 78.11  E-value: 1.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   8 QLKEKvLESNPVNIVDVRTDEETAMGVIPGAKTIPMDQIPDNLNYF-NDKD-TYYIICAAGMRSAKVVKYLEGHD-IHAI 84
Cdd:cd00158    1 ELKEL-LDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLeLDKDkPIVVYCRSGNRSARAAKLLRKAGgTNVY 79


                 ....*....
gi 920628913  85 NVEGGMNEW 93
Cdd:cd00158   80 NLEGGMLAW 88
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 19-97 8.00e-13

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: 59.01  E-value: 8.00e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913    19 VNIVDVRTDEETAMGVIPGAKTIPMDQIPDNLNYFN-------------DKDTYYII-CAAGMRSAKVVKYLE--GHDiH 82
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDilefeellkrlglDKDKPVVVyCRSGNRSAKAAWLLRelGFK-N 83

                           90
                   ....*....|....*
gi 920628913    83 AINVEGGMNEWGTAG 97
Cdd:smart00450  84 VYLLDGGYKEWSAAG 98
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 14-93 2.31e-11

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: 55.18  E-value: 2.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   14 LESNPVNIVDVRTDEETAMGVIPGAKTIPMDQIPDNLNYFND----------KDTYYIICAAGMRSAKVVKYLE--GHDi 81
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLEllekllellkDKPIVVYCNSGNRAAAAAALLKalGYK- 79

                          90
                  ....*....|..
gi 920628913   82 HAINVEGGMNEW 93
Cdd:pfam00581  80 NVYVLDGGFEAW 91
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
1-97 5.79e-11

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 57.33  E-value: 5.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   1 MESITVDQLKEKVLESnpVNIVDVRTDEETAMGVIPGAKTIPMDQIPDNL-NYFNDKDT-YYIICAAGMRSAKVVKYLEG 78
Cdd:PRK08762   2 IREISPAEARARAAQG--AVLIDVREAHERASGQAEGALRIPRGFLELRIeTHLPDRDReIVLICASGTRSAHAAATLRE 79

                         90       100
                 ....*....|....*....|
gi 920628913  79 HDI-HAINVEGGMNEWGTAG 97
Cdd:PRK08762  80 LGYtRVASVAGGFSAWKDAG 99
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 1-97 2.72e-30

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: 103.51  E-value: 2.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   1 MESITVDQLKEKvLESNPVNIVDVRTDEETAMGVIPGAKTIPMDQIPDNLNYFNDKDTYYIICAAGMRSAKVVKYLE--G 78
Cdd:COG0607    3 VKEISPAELAEL-LESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRraG 81

                         90
                 ....*....|....*....
gi 920628913  79 HDiHAINVEGGMNEWGTAG 97
Cdd:COG0607   82 YT-NVYNLAGGIEAWKAAG 99
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 8-93 1.76e-20

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: 78.11  E-value: 1.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   8 QLKEKvLESNPVNIVDVRTDEETAMGVIPGAKTIPMDQIPDNLNYF-NDKD-TYYIICAAGMRSAKVVKYLEGHD-IHAI 84
Cdd:cd00158    1 ELKEL-LDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLeLDKDkPIVVYCRSGNRSARAAKLLRKAGgTNVY 79


                 ....*....
gi 920628913  85 NVEGGMNEW 93
Cdd:cd00158   80 NLEGGMLAW 88
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 19-97 8.00e-13

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: 59.01  E-value: 8.00e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913    19 VNIVDVRTDEETAMGVIPGAKTIPMDQIPDNLNYFN-------------DKDTYYII-CAAGMRSAKVVKYLE--GHDiH 82
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDilefeellkrlglDKDKPVVVyCRSGNRSAKAAWLLRelGFK-N 83

                           90
                   ....*....|....*
gi 920628913    83 AINVEGGMNEWGTAG 97
Cdd:smart00450  84 VYLLDGGYKEWSAAG 98
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 4-93 1.54e-12

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: 58.17  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   4 ITVDQLKEKVLES--NPVnIVDVRTDEETAMGVIPGAKTIPMDQIPDNLNYFN----DKDTyYIICAAGMRSAKVVKYLE 77
Cdd:cd01528    2 ISVAELAEWLADEreEPV-LIDVREPEELEIAFLPGFLHLPMSEIPERSKELDsdnpDKDI-VVLCHHGGRSMQVAQWLL 79

                         90
                 ....*....|....*..
gi 920628913  78 GHDIHAI-NVEGGMNEW 93
Cdd:cd01528   80 RQGFENVyNLQGGIDAW 96
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 14-93 2.31e-11

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: 55.18  E-value: 2.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   14 LESNPVNIVDVRTDEETAMGVIPGAKTIPMDQIPDNLNYFND----------KDTYYIICAAGMRSAKVVKYLE--GHDi 81
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLEllekllellkDKPIVVYCNSGNRAAAAAALLKalGYK- 79

                          90
                  ....*....|..
gi 920628913   82 HAINVEGGMNEW 93
Cdd:pfam00581  80 NVYVLDGGFEAW 91
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
1-97 5.79e-11

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 57.33  E-value: 5.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   1 MESITVDQLKEKVLESnpVNIVDVRTDEETAMGVIPGAKTIPMDQIPDNL-NYFNDKDT-YYIICAAGMRSAKVVKYLEG 78
Cdd:PRK08762   2 IREISPAEARARAAQG--AVLIDVREAHERASGQAEGALRIPRGFLELRIeTHLPDRDReIVLICASGTRSAHAAATLRE 79

                         90       100
                 ....*....|....*....|
gi 920628913  79 HDI-HAINVEGGMNEWGTAG 97
Cdd:PRK08762  80 LGYtRVASVAGGFSAWKDAG 99
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 19-93 8.52e-11

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 56.80  E-value: 8.52e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 920628913  19 VNIVDVRTDEETAMGVIPGAKTIPMDQIPDNLN--YFNDKDTYYIICAAGMRSAKVVKYLEGHDIHAI-NVEGGMNEW 93
Cdd:PRK05597 275 VTLIDVREPSEFAAYSIPGAHNVPLSAIREGANppSVSAGDEVVVYCAAGVRSAQAVAILERAGYTGMsSLDGGIEGW 352
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
1-93 1.73e-09

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 53.20  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   1 MESITVDQLKEkVLESNPVNIV--DVRTDEETAMGVIPGAKTIPMDQIPDNLNYFNDK---DTYYII--CAAGMRSAKVV 73
Cdd:PRK07411 281 IPEMTVTELKA-LLDSGADDFVliDVRNPNEYEIARIPGSVLVPLPDIENGPGVEKVKellNGHRLIahCKMGGRSAKAL 359

                         90       100
                 ....*....|....*....|
gi 920628913  74 KYLEGHDIHAINVEGGMNEW 93
Cdd:PRK07411 360 GILKEAGIEGTNVKGGITAW 379
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 21-95 6.66e-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: 48.80  E-value: 6.66e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 920628913  21 IVDVRTDEETAMGVIPGAKTIPMDQIPDNLNYFNDKDTYYIICAAGMRSAKVVKYLEGHDIHAINVEGGMNEWGT 95
Cdd:cd01524   16 LIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGFKVKNLDGGYKTYST 90
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 2-93 5.22e-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: 46.92  E-value: 5.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   2 ESITVDQLKEKVLESNPVNIVDVRTDEETAMGVIPGAKTIPMDQIPD---------NLNYFNDKDT-YYIICAAGMRSAK 71
Cdd:cd01526    8 ERVSVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSkaaelkslqELPLDNDKDSpIYVVCRRGNDSQT 87

                         90       100
                 ....*....|....*....|....
gi 920628913  72 VVKYLE--GHDIHAINVEGGMNEW 93
Cdd:cd01526   88 AVRKLKelGLERFVRDIIGGLKAW 111
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 5-93 6.83e-08

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


Pssm-ID: 238777 [Multi-domain]  Cd Length: 106  Bit Score: 46.49  E-value: 6.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   5 TVDQLKeKVLESNP-VNIVDVRTDEETAMGVIPGAKTIPMDQIPDNLNYFND--KDTY---------YII--CAAGMRS- 69
Cdd:cd01519    2 SFEEVK-NLPNPHPnKVLIDVREPEELKTGKIPGAINIPLSSLPDALALSEEefEKKYgfpkpskdkELIfyCKAGVRSk 80

                         90       100
                 ....*....|....*....|....*.
gi 920628913  70 --AKVVKYLEGHDIHaiNVEGGMNEW 93
Cdd:cd01519   81 aaAELARSLGYENVG--NYPGSWLDW 104
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 4-93 1.15e-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: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   4 ITVDQLKEKVLESNPVNIVDVRTDEETAM--GVIPGAktIPMDqiPDNLNYF---NDKDTYYII-CAAGMRSAKVVKYL- 76
Cdd:cd01444    2 ISVDELAELLAAGEAPVLLDVRDPASYAAlpDHIPGA--IHLD--EDSLDDWlgdLDRDRPVVVyCYHGNSSAQLAQALr 77

                         90
                 ....*....|....*....
gi 920628913  77 --EGHDIHAinVEGGMNEW 93
Cdd:cd01444   78 eaGFTDVRS--LAGGFEAW 94
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 4-94 1.56e-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: 45.56  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   4 ITVDQLKEKVLESNPVNIVDVRTDEETAMGVIPGAKTIP---------------MDQIPDnlnyfnDKDtYYIICAAGMR 68
Cdd:cd01523    1 LDPEDLYARLLAGQPLFILDVRNESDYERWKIDGENNTPyfdpyfdfleieediLDQLPD------DQE-VTVICAKEGS 73

                         90       100
                 ....*....|....*....|....*.
gi 920628913  69 SAKVVKYLEGHDIHAINVEGGMNEWG 94
Cdd:cd01523   74 SQFVAELLAERGYDVDYLAGGMKAWS 99
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 3-94 1.21e-06

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 45.08  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   3 SITVDQLKEKVLESNPVNIVDVRTDEETAMGVIPGAKTIPMDQIP--DNLNYFNDKDTYYIICAAGMRSAKVVKYLEGHD 80
Cdd:PRK07878 288 TITPRELKEWLDSGKKIALIDVREPVEWDIVHIPGAQLIPKSEILsgEALAKLPQDRTIVLYCKTGVRSAEALAALKKAG 367

                         90
                 ....*....|....*
gi 920628913  81 IH-AINVEGGMNEWG 94
Cdd:PRK07878 368 FSdAVHLQGGVVAWA 382
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 1-97 1.24e-04

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


Pssm-ID: 238785 [Multi-domain]  Cd Length: 99  Bit Score: 37.85  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   1 MESITVDQLKEKVleSNPVNIVDVRTDEETAMGVIPGAKTIPMDQIPDNLNYFNDKDTYYIICAAGMRSAKVVKYLEG-H 79
Cdd:cd01527    1 LTTISPNDACELL--AQGAVLVDIREPDEYLRERIPGARLVPLSQLESEGLPLVGANAIIFHCRSGMRTQQNAERLAAiS 78

                         90
                 ....*....|....*...
gi 920628913  80 DIHAINVEGGMNEWGTAG 97
Cdd:cd01527   79 AGEAYVLEGGLDAWKAAG 96
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 4-94 1.29e-03

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 36.31  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913   4 ITVDQLKEkVLESNPVNIVDVRTDE----ETAMGV-----IPGAKTIPMDQIPDNLNYFNDKD----------------- 57
Cdd:COG2897  140 ADADEVLA-ALGDPDAVLVDARSPEryrgEVEPIDpraghIPGAVNLPWTDLLDEDGTFKSAEelralfaalgidpdkpv 218

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 920628913  58 -TYyiiCAAGMRSAKVVKYLE--GHDIHAiNVEGGMNEWG 94
Cdd:COG2897  219 iTY---CGSGVRAAHTWLALEllGYPNVR-LYDGSWSEWG 254
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 22-92 1.88e-03

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 36.01  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 920628913  22 VDVRTDEETAMGVIP--GAK-TIPMDQIPDNLNYFN-----DKDTYYIICAAGMRSAKVV-KYLE-GHDIHAINVEGGMN 91
Cdd:PRK05600 290 LDVREPHEVLLKDLPegGASlKLPLSAITDDADILHalspiDGDNVVVYCASGIRSADFIeKYSHlGHELTLHNLPGGVN 369


                 .
gi 920628913  92 E 92
Cdd:PRK05600 370 A 370
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 3-42 5.76e-03

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: 33.59  E-value: 5.76e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 920628913   3 SITVDQLKEKVLESNPVNIVDVRTDEETAMGVIPGAKTIP 42
Cdd:cd01533   11 SVSADELAALQARGAPLVVLDGRRFDEYRKMTIPGSVSCP 50
 
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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