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Conserved domains on  [gi|2315639811|dbj|GIW25270|]
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MAG: sulfurtransferase [Meiothermus sp.]

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]; ...
 13-116 7.70e-43

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: 135.87  E-value: 7.70e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  13 SKVPRITAKEAQEKLKA-GAVMIDVRTPLERKLSKIPGSQGMPLAELAKRWESLPKDKPIICLCESGNRSQQAAEFLAQK 91
Cdd:COG0607     1 ASVKEISPAELAELLESeDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRA 80

                          90       100
                  ....*....|....*....|....*.
gi 2315639811  92 GFE-VYNLAGGISAWQAAGLPVKKGD 116
Cdd:COG0607    81 GYTnVYNLAGGIEAWKAAGLPVEKGK 106
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 13-116 7.70e-43

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: 135.87  E-value: 7.70e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  13 SKVPRITAKEAQEKLKA-GAVMIDVRTPLERKLSKIPGSQGMPLAELAKRWESLPKDKPIICLCESGNRSQQAAEFLAQK 91
Cdd:COG0607     1 ASVKEISPAELAELLESeDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRA 80

                          90       100
                  ....*....|....*....|....*.
gi 2315639811  92 GFE-VYNLAGGISAWQAAGLPVKKGD 116
Cdd:COG0607    81 GYTnVYNLAGGIEAWKAAGLPVEKGK 106
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 22-106 2.36e-27

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: 96.21  E-value: 2.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  22 EAQEKLKA-GAVMIDVRTPLERKLSKIPGSQGMPLAELAKRW--ESLPKDKPIICLCESGNRSQQAAEFLAQKGF-EVYN 97
Cdd:cd00158     1 ELKELLDDeDAVLLDVREPEEYAAGHIPGAINIPLSELEERAalLELDKDKPIVVYCRSGNRSARAAKLLRKAGGtNVYN 80


                  ....*....
gi 2315639811  98 LAGGISAWQ 106
Cdd:cd00158    81 LEGGMLAWK 89
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
15-114 2.22e-25

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 97.77  E-value: 2.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  15 VPRITAKEAQEKLKAGAVMIDVRTPLERKLSKIPGSQGMPLAELAKRWES-LP-KDKPIICLCESGNRSQQAAEFLAQKG 92
Cdd:PRK08762    2 IREISPAEARARAAQGAVLIDVREAHERASGQAEGALRIPRGFLELRIEThLPdRDREIVLICASGTRSAHAAATLRELG 81

                          90       100
                  ....*....|....*....|...
gi 2315639811  93 FE-VYNLAGGISAWQAAGLPVKK 114
Cdd:PRK08762   82 YTrVASVAGGFSAWKDAGLPLER 104
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 28-106 3.19e-21

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: 80.99  E-value: 3.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  28 KAGAVMIDVRTPLERKLSKIPGSQ----------GMPLAELAKRWESLPKDKPIICLCESGNRSQQAAEFLAQKGF-EVY 96
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVnvplsslslpPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYkNVY 82

                          90
                  ....*....|
gi 2315639811  97 NLAGGISAWQ 106
Cdd:pfam00581  83 VLDGGFEAWK 92
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 28-111 9.71e-21

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: 79.81  E-value: 9.71e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811   28 KAGAVMIDVRTPLERKLSKIPGSQGMPLAELAKRWE--------------SLPKDKPIICLCESGNRSQQAAEFLAQKGF 93
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGeldilefeellkrlGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81

                           90
                   ....*....|....*....
gi 2315639811   94 E-VYNLAGGISAWQAAGLP 111
Cdd:smart00450  82 KnVYLLDGGYKEWSAAGPP 100
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 13-116 7.70e-43

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: 135.87  E-value: 7.70e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  13 SKVPRITAKEAQEKLKA-GAVMIDVRTPLERKLSKIPGSQGMPLAELAKRWESLPKDKPIICLCESGNRSQQAAEFLAQK 91
Cdd:COG0607     1 ASVKEISPAELAELLESeDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRA 80

                          90       100
                  ....*....|....*....|....*.
gi 2315639811  92 GFE-VYNLAGGISAWQAAGLPVKKGD 116
Cdd:COG0607    81 GYTnVYNLAGGIEAWKAAGLPVEKGK 106
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 22-106 2.36e-27

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: 96.21  E-value: 2.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  22 EAQEKLKA-GAVMIDVRTPLERKLSKIPGSQGMPLAELAKRW--ESLPKDKPIICLCESGNRSQQAAEFLAQKGF-EVYN 97
Cdd:cd00158     1 ELKELLDDeDAVLLDVREPEEYAAGHIPGAINIPLSELEERAalLELDKDKPIVVYCRSGNRSARAAKLLRKAGGtNVYN 80


                  ....*....
gi 2315639811  98 LAGGISAWQ 106
Cdd:cd00158    81 LEGGMLAWK 89
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 30-106 1.24e-25

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: 91.94  E-value: 1.24e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2315639811  30 GAVMIDVRTPLERKLSKIPGSQGMPLAELAKRWESLPKDKPIICLCESGNRSQQAAEFLAQKGFEVYNLAGGISAWQ 106
Cdd:cd01524    13 GVTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGFKVKNLDGGYKTYS 89
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
15-114 2.22e-25

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 97.77  E-value: 2.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  15 VPRITAKEAQEKLKAGAVMIDVRTPLERKLSKIPGSQGMPLAELAKRWES-LP-KDKPIICLCESGNRSQQAAEFLAQKG 92
Cdd:PRK08762    2 IREISPAEARARAAQGAVLIDVREAHERASGQAEGALRIPRGFLELRIEThLPdRDREIVLICASGTRSAHAAATLRELG 81

                          90       100
                  ....*....|....*....|...
gi 2315639811  93 FE-VYNLAGGISAWQAAGLPVKK 114
Cdd:PRK08762   82 YTrVASVAGGFSAWKDAGLPLER 104
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 18-105 2.84e-25

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: 91.30  E-value: 2.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  18 ITAKEAQEKL---KAGAVMIDVRTPLERKLSKIPGSQGMPLAELAKRWESLP---KDKPIICLCESGNRSQQAAEFLAQK 91
Cdd:cd01528     2 ISVAELAEWLadeREEPVLIDVREPEELEIAFLPGFLHLPMSEIPERSKELDsdnPDKDIVVLCHHGGRSMQVAQWLLRQ 81

                          90
                  ....*....|....*
gi 2315639811  92 GFE-VYNLAGGISAW 105
Cdd:cd01528    82 GFEnVYNLQGGIDAW 96
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 15-112 5.81e-23

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: 85.62  E-value: 5.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  15 VPRITAKEAQEKLKAGAVMIDVRTPLERKLSKIPGSQGMPLAELAKRWESLPKDKPIICLCESGNRSQQAAEFLAQ-KGF 93
Cdd:cd01527     1 LTTISPNDACELLAQGAVLVDIREPDEYLRERIPGARLVPLSQLESEGLPLVGANAIIFHCRSGMRTQQNAERLAAiSAG 80

                          90
                  ....*....|....*....
gi 2315639811  94 EVYNLAGGISAWQAAGLPV 112
Cdd:cd01527    81 EAYVLEGGLDAWKAAGLPV 99
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 28-106 3.19e-21

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: 80.99  E-value: 3.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  28 KAGAVMIDVRTPLERKLSKIPGSQ----------GMPLAELAKRWESLPKDKPIICLCESGNRSQQAAEFLAQKGF-EVY 96
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVnvplsslslpPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYkNVY 82

                          90
                  ....*....|
gi 2315639811  97 NLAGGISAWQ 106
Cdd:pfam00581  83 VLDGGFEAWK 92
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 28-111 9.71e-21

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: 79.81  E-value: 9.71e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811   28 KAGAVMIDVRTPLERKLSKIPGSQGMPLAELAKRWE--------------SLPKDKPIICLCESGNRSQQAAEFLAQKGF 93
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGeldilefeellkrlGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81

                           90
                   ....*....|....*....
gi 2315639811   94 E-VYNLAGGISAWQAAGLP 111
Cdd:smart00450  82 KnVYLLDGGYKEWSAAGPP 100
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 17-107 4.22e-19

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: 75.38  E-value: 4.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  17 RITAKEAQEKLKAG--AVMIDVRTPL--ERKLSKIPGSQGMPLAELAKRWESLPKDKPIICLCESGNRSQQAAEFLAQKG 92
Cdd:cd01444     1 RISVDELAELLAAGeaPVLLDVRDPAsyAALPDHIPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAG 80

                          90
                  ....*....|....*.
gi 2315639811  93 F-EVYNLAGGISAWQA 107
Cdd:cd01444    81 FtDVRSLAGGFEAWRR 96
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
17-112 5.50e-18

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 73.13  E-value: 5.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  17 RITAKEAQEKLKA-GAVMIDVRTPLERKLSKIPGSQGMPLAELAKRWESLPKDKPIICLCESGNRSQQAAEFLAQKGFE- 94
Cdd:PRK00162    6 CINVEQAHQKLQEgGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQQGFDv 85

                          90
                  ....*....|....*...
gi 2315639811  95 VYNLAGGISAWQAAGLPV 112
Cdd:PRK00162   86 VYSIDGGFEAWRRTFPAE 103
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 17-105 1.36e-15

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: 67.33  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  17 RITAKEAQEKLKAGA--VMIDVRTPLERKLSKIPGSQGMPLAEL-AKRWESLP---------KDKPIICLCESGNRSQQA 84
Cdd:cd01526     9 RVSVKDYKNILQAGKkhVLLDVRPKVHFEICRLPEAINIPLSELlSKAAELKSlqelpldndKDSPIYVVCRRGNDSQTA 88

                          90       100
                  ....*....|....*....|...
gi 2315639811  85 AEFLAQKGFE--VYNLAGGISAW 105
Cdd:cd01526    89 VRKLKELGLErfVRDIIGGLKAW 111
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
13-105 9.75e-15

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 68.61  E-value: 9.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  13 SKVPRITAKEAQEKLKAGA---VMIDVRTPLERKLSKIPGSQGMPLAELAK-----RWESLPKDKPIICLCESGNRSQQA 84
Cdd:PRK07411  279 AEIPEMTVTELKALLDSGAddfVLIDVRNPNEYEIARIPGSVLVPLPDIENgpgveKVKELLNGHRLIAHCKMGGRSAKA 358

                          90       100
                  ....*....|....*....|.
gi 2315639811  85 AEFLAQKGFEVYNLAGGISAW 105
Cdd:PRK07411  359 LGILKEAGIEGTNVKGGITAW 379
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 15-108 3.09e-14

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 67.20  E-value: 3.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  15 VPRITAkeaqekLKAGAVMIDVRTPLERKLSKIPGSQGMPLAEL---AKRWESLPKDKPIIcLCESGNRSQQAAEFLAQK 91
Cdd:PRK05597  265 VPRVSA------LPDGVTLIDVREPSEFAAYSIPGAHNVPLSAIregANPPSVSAGDEVVV-YCAAGVRSAQAVAILERA 337

                          90
                  ....*....|....*...
gi 2315639811  92 GFE-VYNLAGGISAWQAA 108
Cdd:PRK05597  338 GYTgMSSLDGGIEGWLDS 355
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 18-105 5.89e-14

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 66.27  E-value: 5.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  18 ITAKEAQEKLKAGA--VMIDVRTPLERKLSKIPGSQGMPLAEL--AKRWESLPKDKPIICLCESGNRSQQAAEFLAQKGF 93
Cdd:PRK07878  289 ITPRELKEWLDSGKkiALIDVREPVEWDIVHIPGAQLIPKSEIlsGEALAKLPQDRTIVLYCKTGVRSAEALAALKKAGF 368

                          90
                  ....*....|...
gi 2315639811  94 -EVYNLAGGISAW 105
Cdd:PRK07878  369 sDAVHLQGGVVAW 381
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 18-101 1.04e-12

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: 59.65  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  18 ITAKEAQEKLKAG--AVMIDVRTPLERKL-SKIPGSQGMP-------------LAELAKRwesLPKDKPIICLCESGNRS 81
Cdd:cd01522     1 LTPAEAWALLQADpqAVLVDVRTEAEWKFvGGVPDAVHVAwqvypdmeinpnfLAELEEK---VGKDRPVLLLCRSGNRS 77

                          90       100
                  ....*....|....*....|.
gi 2315639811  82 QQAAEFLAQKGF-EVYNLAGG 101
Cdd:cd01522    78 IAAAEAAAQAGFtNVYNVLEG 98
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 18-109 2.56e-12

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: 58.21  E-value: 2.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  18 ITAKEAQEKLKA-GAVMIDVRTP--LERKlSKIPGSQGMPLAELAKRWE--------SLPKDKPIICLCESGNRSQQAAE 86
Cdd:cd01447     1 LSPEDARALLGSpGVLLVDVRDPreLERT-GMIPGAFHAPRGMLEFWADpdspyhkpAFAEDKPFVFYCASGWRSALAGK 79

                          90       100
                  ....*....|....*....|....
gi 2315639811  87 FLAQKGFE-VYNLAGGISAWQAAG 109
Cdd:cd01447    80 TLQDMGLKpVYNIEGGFKDWKEAG 103
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 32-107 8.30e-12

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: 56.89  E-value: 8.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  32 VMIDVRTPLERKLSKIPGSQGMPLAELAKRW-------------ESLPKDKPIICLCESGNRSQQAAEFLAQKGFE-VYN 97
Cdd:cd01519    17 VLIDVREPEELKTGKIPGAINIPLSSLPDALalseeefekkygfPKPSKDKELIFYCKAGVRSKAAAELARSLGYEnVGN 96

                          90
                  ....*....|
gi 2315639811  98 LAGGISAWQA 107
Cdd:cd01519    97 YPGSWLDWAA 106
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 18-105 3.81e-11

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: 55.19  E-value: 3.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  18 ITAKEAQEKLKAGAVM--IDVRTPLERKLSKIPGSQGMPL----AELAKRWES----LPKDKPIICLCESGNRSQQAAEF 87
Cdd:cd01523     1 LDPEDLYARLLAGQPLfiLDVRNESDYERWKIDGENNTPYfdpyFDFLEIEEDildqLPDDQEVTVICAKEGSSQFVAEL 80

                          90
                  ....*....|....*...
gi 2315639811  88 LAQKGFEVYNLAGGISAW 105
Cdd:cd01523    81 LAERGYDVDYLAGGMKAW 98
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 28-112 2.91e-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: 2.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  28 KAGAVMIDVRTPLERKLSKIPGSQGMPLAEL-AKRWESLPKDKPIICLCES--GNRSQQAAEFLAQKGFEVYNLAGGISA 104
Cdd:cd01521    23 KPDFVLVDVRSAEAYARGHVPGAINLPHREIcENATAKLDKEKLFVVYCDGpgCNGATKAALKLAELGFPVKEMIGGLDW 102


                  ....*...
gi 2315639811 105 WQAAGLPV 112
Cdd:cd01521   103 WKREGYAT 110
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 12-109 3.25e-09

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: 50.54  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  12 GSKVPRITAKEAQEKLKAGA--VMIDVRTPLERKLSKIPGSQGMPLAELAKRWESLPKD--KPIICLCESGNRSQQAAEF 87
Cdd:cd01533     6 VRHTPSVSADELAALQARGAplVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGELAPDprTPIVVNCAGRTRSIIGAQS 85

                          90       100
                  ....*....|....*....|....
gi 2315639811  88 LAQKGFE--VYNLAGGISAWQAAG 109
Cdd:cd01533    86 LINAGLPnpVAALRNGTQGWTLAG 109
4RHOD_Repeat_4 cd01535
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative ...
 19-116 8.99e-09

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: 50.20  E-value: 8.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  19 TAKEAQEKLKAGAVmIDVRTPLERKLSKIPGSQGMPLAELAKRWESLPKDKPIICLCESGNRSQQA-AEFLAQKGFEVYN 97
Cdd:cd01535     1 TLAAWLGEGGQTAV-VDVTASANYVKRHIPGAWWVLRAQLAQALEKLPAAERYVLTCGSSLLARFAaADLAALTVKPVFV 79

                          90
                  ....*....|....*....
gi 2315639811  98 LAGGISAWQAAGLPVKKGD 116
Cdd:cd01535    80 LEGGTAAWIAAGLPVESGE 98
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 34-103 6.97e-07

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 44.45  E-value: 6.97e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2315639811  34 IDVRTPLERKLSKIPGSQGMPLAELAKRWESLPKDK--PIICLCESGNRSQQAAEFLAQKGFEVYNLAGGIS 103
Cdd:PRK10287   24 IDVRVPEQYQQEHVQGAINIPLKEVKERIATAVPDKndTVKLYCNAGRQSGQAKEILSEMGYTHAENAGGLK 95
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 35-107 4.68e-06

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: 42.07  E-value: 4.68e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2315639811  35 DVRTPLERKLSKIPGSQGMPLAELAKRW-ESLPKDKPIICLCES-GNRSQQAAEFLAQKGFEVYNLAGGISAWQA 107
Cdd:cd01534    21 DVRTPEEYEAGHLPGFRHTPGGQLVQETdHFAPVRGARIVLADDdGVRADMTASWLAQMGWEVYVLEGGLAAALA 95
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 33-107 5.05e-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: 41.89  E-value: 5.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  33 MIDVRTPLERKLSKIPGSQGMPLAELAKR------WESLPKDKPIICLCESGNRSQQAAEFLAQKGF-EVYNLAGGISAW 105
Cdd:cd01529    15 LLDVRAEDEYAAGHLPGKRSIPGAALVLRsqelqaLEAPGRATRYVLTCDGSLLARFAAQELLALGGkPVALLDGGTSAW 94


                  ..
gi 2315639811 106 QA 107
Cdd:cd01529    95 VA 96
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 32-103 8.79e-06

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins.


Pssm-ID: 238776 [Multi-domain]  Cd Length: 101  Bit Score: 41.41  E-value: 8.79e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2315639811  32 VMIDVRTPLERKLSKIPGSQGMPL------AELAKRWESLPKDKPIICLCESGNRSQQAAEFLAQKGF-EVYNLAGGIS 103
Cdd:cd01518    19 VLLDVRNDYEYDIGHFKGAVNPDVdtfrefPFWLDENLDLLKGKKVLMYCTGGIRCEKASAYLKERGFkNVYQLKGGIL 97
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 16-112 1.74e-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: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  16 PRITAKEAQEKLKAG-AVMIDVRTPlER---KLSK-------IPGS-----------QGM--PLAELAKRWESL--PKDK 69
Cdd:COG2897   138 LLADADEVLAALGDPdAVLVDARSP-ERyrgEVEPidpraghIPGAvnlpwtdlldeDGTfkSAEELRALFAALgiDPDK 216

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2315639811  70 PIICLCESGNRSqqAAEFLAQK--GFE-VYNLAGGISAWQA-AGLPV 112
Cdd:COG2897   217 PVITYCGSGVRA--AHTWLALEllGYPnVRLYDGSWSEWGSdPDLPV 261
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
30-102 1.73e-03

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 36.36  E-value: 1.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2315639811  30 GAVMIDVRTPLErklskipgsqgmpLAELAKRWESLPKDKPIICLCESGNRSQQAAEFLAQKGF-EVYNLAGGI 102
Cdd:PRK00142  146 NAIEPDIETFRE-------------FPPWVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFkEVYQLEGGI 206
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 18-107 3.87e-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: 34.53  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  18 ITAKEAQEKLKAG-AVMIDVRTPlERKLSK------------IPGSQGMP-------------LAELAKRWESLPK--DK 69
Cdd:cd01449     1 VTAEEVLANLDSGdVQLVDARSP-ERFRGEvpeprpglrsghIPGAVNIPwtslldedgtfksPEELRALFAALGItpDK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2315639811  70 PIICLCESGNRSQQ---AAEFLAQKGFEVYnlAGGISAWQA 107
Cdd:cd01449    80 PVIVYCGSGVTACVlllALELLGYKNVRLY--DGSWSEWGS 118
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 31-106 5.82e-03

Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included in this CD are eukaryotic arsenate resistance proteins such as Saccharomyces cerevisiae Acr2p and similar proteins. Cdc25 phosphatases activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. The Cdc25 and Acr2p RHOD domains have the signature motif (H/YCxxxxxR).


Pssm-ID: 238720 [Multi-domain]  Cd Length: 113  Bit Score: 33.92  E-value: 5.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639811  31 AVMIDVRTPlERKLSKIPGSQGMPL----AELAKRWE--SLPKDKPIICLCE-SGNRSQQAAEFLA----QKG---FEVY 96
Cdd:cd01443    24 FVVVDLRRD-DYEGGHIKGSINLPAqscyQTLPQVYAlfSLAGVKLAIFYCGsSQGRGPRAARWFAdylrKVGeslPKSY 102

                          90
                  ....*....|
gi 2315639811  97 NLAGGISAWQ 106
Cdd:cd01443   103 ILTGGIKAWY 112
 
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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