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Conserved domains on  [gi|489113642|ref|WP_003023495|]
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MULTISPECIES: thiosulfate sulfurtransferase GlpE [Citrobacter]

Protein Classification

thiosulfate sulfurtransferase GlpE( domain architecture ID 10791817)

thiosulfate sulfurtransferase GlpE catalyzes the sulfur transfer reaction from thiosulfate to cyanide

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
1-108 3.76e-73

thiosulfate sulfurtransferase GlpE;


:

Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 212.19  E-value: 3.76e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642   1 MDQFECINVEEAHQKLHQGAAVLVDIRDPQSYAMGHAPQAFHLTNDTLGSFMREHDFDTAVLVMCYHGNSSKGAAQYLLQ 80
Cdd:PRK00162   1 MDQFECINVEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQ 80

                         90       100
                 ....*....|....*....|....*...
gi 489113642  81 QGYDAVYSVDGGFDAWHRHFPAEVAYGS 108
Cdd:PRK00162  81 QGFDVVYSIDGGFEAWRRTFPAEVASGA 108
 
Name Accession Description Interval E-value
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
1-108 3.76e-73

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 212.19  E-value: 3.76e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642   1 MDQFECINVEEAHQKLHQGAAVLVDIRDPQSYAMGHAPQAFHLTNDTLGSFMREHDFDTAVLVMCYHGNSSKGAAQYLLQ 80
Cdd:PRK00162   1 MDQFECINVEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQ 80

                         90       100
                 ....*....|....*....|....*...
gi 489113642  81 QGYDAVYSVDGGFDAWHRHFPAEVAYGS 108
Cdd:PRK00162  81 QGFDVVYSIDGGFEAWRRTFPAEVASGA 108
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 6-98 3.06e-39

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: 126.22  E-value: 3.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642   6 CINVEEAHQKLHQG-AAVLVDIRDPQSYAM--GHAPQAFHLTNDTLGSFMREHDFDTAVLVMCYHGNSSKGAAQYLLQQG 82
Cdd:cd01444    1 RISVDELAELLAAGeAPVLLDVRDPASYAAlpDHIPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAG 80

                         90
                 ....*....|....*.
gi 489113642  83 YDAVYSVDGGFDAWHR 98
Cdd:cd01444   81 FTDVRSLAGGFEAWRR 96
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 2-98 1.00e-32

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: 110.06  E-value: 1.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642   2 DQFECINVEEAHQKLHQGAAVLVDIRDPQSYAMGHAPQAFHLTNDTLGSFMREHDFDTAVLVMCYHGNSSKGAAQYLLQQ 81
Cdd:COG0607    1 ASVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRA 80

                         90
                 ....*....|....*..
gi 489113642  82 GYDAVYSVDGGFDAWHR 98
Cdd:COG0607   81 GYTNVYNLAGGIEAWKA 97
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 17-102 1.44e-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: 68.64  E-value: 1.44e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642    17 HQGAAVLVDIRDPQSYAMGHAPQAFHLTNDTLGSFMREHDF--------------DTAVLVMCYHGNSSKGAAQYLLQQG 82
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDIlefeellkrlgldkDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 489113642    83 YDAVYSVDGGFDAWHRHFPA 102
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 16-97 2.09e-16

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: 68.28  E-value: 2.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642   16 LHQGAAVLVDIRDPQSYAMGHAPQAFHLT-----------NDTLGSFMREHDFDTAVLVmCYHGNSSKGAAQYLLQQGYD 84
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPlsslslpplplLELLEKLLELLKDKPIVVY-CNSGNRAAAAAALLKALGYK 79

                          90
                  ....*....|...
gi 489113642   85 AVYSVDGGFDAWH 97
Cdd:pfam00581  80 NVYVLDGGFEAWK 92
 
Name Accession Description Interval E-value
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
1-108 3.76e-73

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 212.19  E-value: 3.76e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642   1 MDQFECINVEEAHQKLHQGAAVLVDIRDPQSYAMGHAPQAFHLTNDTLGSFMREHDFDTAVLVMCYHGNSSKGAAQYLLQ 80
Cdd:PRK00162   1 MDQFECINVEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQ 80

                         90       100
                 ....*....|....*....|....*...
gi 489113642  81 QGYDAVYSVDGGFDAWHRHFPAEVAYGS 108
Cdd:PRK00162  81 QGFDVVYSIDGGFEAWRRTFPAEVASGA 108
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 6-98 3.06e-39

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: 126.22  E-value: 3.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642   6 CINVEEAHQKLHQG-AAVLVDIRDPQSYAM--GHAPQAFHLTNDTLGSFMREHDFDTAVLVMCYHGNSSKGAAQYLLQQG 82
Cdd:cd01444    1 RISVDELAELLAAGeAPVLLDVRDPASYAAlpDHIPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAG 80

                         90
                 ....*....|....*.
gi 489113642  83 YDAVYSVDGGFDAWHR 98
Cdd:cd01444   81 FTDVRSLAGGFEAWRR 96
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 2-98 1.00e-32

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: 110.06  E-value: 1.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642   2 DQFECINVEEAHQKLHQGAAVLVDIRDPQSYAMGHAPQAFHLTNDTLGSFMREHDFDTAVLVMCYHGNSSKGAAQYLLQQ 81
Cdd:COG0607    1 ASVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRA 80

                         90
                 ....*....|....*..
gi 489113642  82 GYDAVYSVDGGFDAWHR 98
Cdd:COG0607   81 GYTNVYNLAGGIEAWKA 97
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 11-96 3.47e-23

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: 85.04  E-value: 3.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642  11 EAHQKLHQGAAVLVDIRDPQSYAMGHAPQAFHLTNDTLGSFMREH--DFDTAVLVMCYHGNSSKGAAQYLLQQGYDAVYS 88
Cdd:cd00158    1 ELKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLelDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYN 80


                 ....*...
gi 489113642  89 VDGGFDAW 96
Cdd:cd00158   81 LEGGMLAW 88
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
7-98 1.18e-20

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 84.68  E-value: 1.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642   7 INVEEAHQKLHQGAaVLVDIRDPQSYAMGHAPQAFHLTNDTLGSFMREH--DFDTAVLVMCYHGNSSKGAAQYLLQQGYD 84
Cdd:PRK08762   5 ISPAEARARAAQGA-VLIDVREAHERASGQAEGALRIPRGFLELRIETHlpDRDREIVLICASGTRSAHAAATLRELGYT 83

                         90
                 ....*....|....
gi 489113642  85 AVYSVDGGFDAWHR 98
Cdd:PRK08762  84 RVASVAGGFSAWKD 97
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 17-102 1.44e-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: 68.64  E-value: 1.44e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642    17 HQGAAVLVDIRDPQSYAMGHAPQAFHLTNDTLGSFMREHDF--------------DTAVLVMCYHGNSSKGAAQYLLQQG 82
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDIlefeellkrlgldkDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 489113642    83 YDAVYSVDGGFDAWHRHFPA 102
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 16-97 2.09e-16

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: 68.28  E-value: 2.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642   16 LHQGAAVLVDIRDPQSYAMGHAPQAFHLT-----------NDTLGSFMREHDFDTAVLVmCYHGNSSKGAAQYLLQQGYD 84
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPlsslslpplplLELLEKLLELLKDKPIVVY-CNSGNRAAAAAALLKALGYK 79

                          90
                  ....*....|...
gi 489113642   85 AVYSVDGGFDAWH 97
Cdd:pfam00581  80 NVYVLDGGFEAWK 92
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 7-96 1.51e-15

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: 66.26  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642   7 INVEEAHQKLHQGAA--VLVDIRDPQSYAMGHAPQAFHLTNDTLGSFMRE---HDFDTAVLVMCYHGNSSKGAAQYLLQQ 81
Cdd:cd01528    2 ISVAELAEWLADEREepVLIDVREPEELEIAFLPGFLHLPMSEIPERSKEldsDNPDKDIVVLCHHGGRSMQVAQWLLRQ 81

                         90
                 ....*....|....*
gi 489113642  82 GYDAVYSVDGGFDAW 96
Cdd:cd01528   82 GFENVYNLQGGIDAW 96
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 7-96 9.85e-13

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: 59.04  E-value: 9.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642   7 INVEEAHQKLHQGAaVLVDIRDPQSYAMGHAPQAFHLTNDTLGSFMREHDFDTAVLVMCYHGNSSKGAAQYLLQQGYDAV 86
Cdd:cd01527    4 ISPNDACELLAQGA-VLVDIREPDEYLRERIPGARLVPLSQLESEGLPLVGANAIIFHCRSGMRTQQNAERLAAISAGEA 82

                         90
                 ....*....|
gi 489113642  87 YSVDGGFDAW 96
Cdd:cd01527   83 YVLEGGLDAW 92
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 10-98 1.62e-11

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: 56.18  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642  10 EEAHQKL-HQGAAVLVDIR-DPQSYAMGHAPQAFHLTNDTLGSFMREHDF----------DTAVLVMCYHGNSSKGAAQY 77
Cdd:cd01522    4 AEAWALLqADPQAVLVDVRtEAEWKFVGGVPDAVHVAWQVYPDMEINPNFlaeleekvgkDRPVLLLCRSGNRSIAAAEA 83

                         90       100
                 ....*....|....*....|....*.
gi 489113642  78 LLQQGYDAVYSVDGGF-----DAWHR 98
Cdd:cd01522   84 AAQAGFTNVYNVLEGFegdldAAGHR 109
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 7-96 7.72e-11

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: 53.97  E-value: 7.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642   7 INVEEAHQKLHQGAAVLVDIRDPQSY-AMGHAPQAFHLTNDTL-------GSFMREH-DFDTAVLVMCYHGNSSKGAAQY 77
Cdd:cd01447    1 LSPEDARALLGSPGVLLVDVRDPRELeRTGMIPGAFHAPRGMLefwadpdSPYHKPAfAEDKPFVFYCASGWRSALAGKT 80

                         90
                 ....*....|....*....
gi 489113642  78 LLQQGYDAVYSVDGGFDAW 96
Cdd:cd01447   81 LQDMGLKPVYNIEGGFKDW 99
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 3-99 2.54e-10

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: 53.13  E-value: 2.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642   3 QFEcINVEEAHQKLHQGAA--VLVDIRDPQSYAMGHAPQAFHLTNDTLgSFMREHDFDTAVLVMCY----HGNSSKGAAQ 76
Cdd:cd01521    7 AFE-TDCWDVAIALKNGKPdfVLVDVRSAEAYARGHVPGAINLPHREI-CENATAKLDKEKLFVVYcdgpGCNGATKAAL 84

                         90       100
                 ....*....|....*....|...
gi 489113642  77 YLLQQGYDaVYSVDGGFDAWHRH 99
Cdd:cd01521   85 KLAELGFP-VKEMIGGLDWWKRE 106
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 22-98 1.12e-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: 50.73  E-value: 1.12e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489113642  22 VLVDIRDPQSYAMGHAPQAFHLTNDTLGSFMREHDFDTAVLVMCYHGNSSKGAAQYLLQQGYDaVYSVDGGFDAWHR 98
Cdd:cd01524   15 TLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGFK-VKNLDGGYKTYST 90
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 5-96 1.15e-07

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 46.15  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642   5 ECINVEEAHQKLHQGAA-VLVDIRDPQSYAMGHAPQAFHLTndtLGSFMR-------------EHDFDTAVLVMCYHGNS 70
Cdd:cd01526    8 ERVSVKDYKNILQAGKKhVLLDVRPKVHFEICRLPEAINIP---LSELLSkaaelkslqelplDNDKDSPIYVVCRRGND 84

                         90       100
                 ....*....|....*....|....*..
gi 489113642  71 SKGAAQYLLQQGYDA-VYSVDGGFDAW 96
Cdd:cd01526   85 SQTAVRKLKELGLERfVRDIIGGLKAW 111
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 21-99 3.55e-07

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 46.79  E-value: 3.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642  21 AVLVDIRDPQSYAMGHAPQAFHLTNDTL--GSFMREHDFDTAVLVMCYHGNSSKGAAQYLLQQGYDAVYSVDGGFDAWHR 98
Cdd:PRK05597 275 VTLIDVREPSEFAAYSIPGAHNVPLSAIreGANPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYTGMSSLDGGIEGWLD 354


                 .
gi 489113642  99 H 99
Cdd:PRK05597 355 S 355
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 11-96 1.40e-06

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: 43.05  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642  11 EAHQKLHQGAAVLVDIRDPQSYAMGHAPQAFHLTNDTL------GSFMREHDFDTAVLVMCYHGNSSKGAAQYLLQQGYD 84
Cdd:cd01529    3 ADWLGEHEPGTALLDVRAEDEYAAGHLPGKRSIPGAALvlrsqeLQALEAPGRATRYVLTCDGSLLARFAAQELLALGGK 82

                         90
                 ....*....|..
gi 489113642  85 AVYSVDGGFDAW 96
Cdd:cd01529   83 PVALLDGGTSAW 94
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 17-96 9.11e-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: 38.40  E-value: 9.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642  17 HQGAAVLVDIRDPQSYAMGH-----------APQAFHLTNDtlgSFMREHDF-----DTAVLVMCYHGNSSKGAAQYLLQ 80
Cdd:cd01519   12 PHPNKVLIDVREPEELKTGKipgainiplssLPDALALSEE---EFEKKYGFpkpskDKELIFYCKAGVRSKAAAELARS 88

                         90
                 ....*....|....*.
gi 489113642  81 QGYDAVYSVDGGFDAW 96
Cdd:cd01519   89 LGYENVGNYPGSWLDW 104
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 23-96 1.69e-04

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: 37.47  E-value: 1.69e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489113642  23 LVDIRDPQSYAMGHAPQA--FHLTNDTLGSFMREHDFDTAVLVMCYHGNS--SKGAAQYLLQQGYDAVYSVDGGFDAW 96
Cdd:cd01532   13 LIDVREEDPFAQSHPLWAanLPLSRLELDAWVRIPRRDTPIVVYGEGGGEdlAPRAARRLSELGYTDVALLEGGLQGW 90
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 23-96 4.80e-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: 36.29  E-value: 4.80e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489113642  23 LVDIRDPQSYAMGHAPQAFHLTNdtlGSFMREHDFDTAV----LVMC-YHGNSSKGAAQYLLQQGYDaVYSVDGGFDAW 96
Cdd:cd01534   19 RFDVRTPEEYEAGHLPGFRHTPG---GQLVQETDHFAPVrgarIVLAdDDGVRADMTASWLAQMGWE-VYVLEGGLAAA 93
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 10-92 2.44e-03

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: 34.48  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642  10 EEAHQKLHQGAAVLVDIRDPQSYAMGHAPQAFHLTNDTLGSFMR-----EHDF-DTAVLVMCYHGNSSKGAAQYLLQQGY 83
Cdd:cd01518    7 AEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFwldenLDLLkGKKVLMYCTGGIRCEKASAYLKERGF 86


                 ....*....
gi 489113642  84 DAVYSVDGG 92
Cdd:cd01518   87 KNVYQLKGG 95
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 58-98 2.50e-03

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: 34.39  E-value: 2.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489113642  58 DTAVLVMCYHGNSSKGAAQYLLQQGYDAVYsVDGGFDAWHR 98
Cdd:cd01523   61 DQEVTVICAKEGSSQFVAELLAERGYDVDY-LAGGMKAWSE 100
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 13-96 2.64e-03

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 35.54  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489113642  13 HQKLHQGAAVLVDIR-----DPQSYAMGHAPQAFHL------------------TNDTLGSFMREH--DFDTAVLVmcYH 67
Cdd:COG2897    2 AAHLDDPDVVILDVRwdlpdGRAAYEAGHIPGAVFLdldtdlsdprspgrhplpSPEAFAALLGALgiSNDTTVVV--YD 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489113642  68 GNSSKGAA------QYLlqqGYDAVYSVDGGFDAW 96
Cdd:COG2897   80 DGGGLFAArawwllRYA---GHEDVRVLDGGLAAW 111
 
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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