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Conserved domains on  [gi|79558700|ref|NP_565497|]
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Rhodanese/Cell cycle control phosphatase superfamily protein [Arabidopsis thaliana]

Protein Classification

rhodanese-like domain-containing protein( domain architecture ID 13)

rhodanese-like domain-containing protein may have sulfurtransferase activity if an active site cysteine is present

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
39-149 2.71e-35

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.


The actual alignment was detected with superfamily member PLN02160:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 136  Bit Score: 119.81  E-value: 2.71e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700   39 EDVETVDVYTAKGFLSTGHRYLDVRTNEEFAKSHVEEA--LNIPYMFKTDEGRVINPDFLSQVASVCKKDEHLIVACNAG 116
Cdd:PLN02160  12 EEVVSVDVSQAKTLLQSGHQYLDVRTQDEFRRGHCEAAkiVNIPYMLNTPQGRVKNQEFLEQVSSLLNPADDILVGCQSG 91
                         90       100       110
                 ....*....|....*....|....*....|...
gi 79558700  117 GRGSRACVDLLNEGYDHVANMGGGYSAWVDAGF 149
Cdd:PLN02160  92 ARSLKATTELVAAGYKKVRNKGGGYLAWVDHSF 124
 
Name Accession Description Interval E-value
PLN02160 PLN02160
thiosulfate sulfurtransferase
39-149 2.71e-35

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 119.81  E-value: 2.71e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700   39 EDVETVDVYTAKGFLSTGHRYLDVRTNEEFAKSHVEEA--LNIPYMFKTDEGRVINPDFLSQVASVCKKDEHLIVACNAG 116
Cdd:PLN02160  12 EEVVSVDVSQAKTLLQSGHQYLDVRTQDEFRRGHCEAAkiVNIPYMLNTPQGRVKNQEFLEQVSSLLNPADDILVGCQSG 91
                         90       100       110
                 ....*....|....*....|....*....|...
gi 79558700  117 GRGSRACVDLLNEGYDHVANMGGGYSAWVDAGF 149
Cdd:PLN02160  92 ARSLKATTELVAAGYKKVRNKGGGYLAWVDHSF 124
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
40-154 1.69e-22

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: 86.17  E-value: 1.69e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700  40 DVETVDVYTAKGFLSTGH-RYLDVRTNEEFAKSHVEEALNIPYmfktdegrvinPDFLSQVASVcKKDEHLIVACNAGGR 118
Cdd:COG0607   2 SVKEISPAELAELLESEDaVLLDVREPEEFAAGHIPGAINIPL-----------GELAERLDEL-PKDKPIVVYCASGGR 69
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 79558700 119 GSRACVDLLNEGYDHVANMGGGYSAWVDAGFAGDKP 154
Cdd:COG0607  70 SAQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVEKG 105
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
60-145 4.88e-19

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: 76.95  E-value: 4.88e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700  60 LDVRTNEEFAKSHVEEALNIPYMFKTDEGRVINPDflsqvasvckKDEHLIVACNAGGRGSRACVDLLNEGYDHVANMGG 139
Cdd:cd00158  14 LDVREPEEYAAGHIPGAINIPLSELEERAALLELD----------KDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLEG 83

                ....*.
gi 79558700 140 GYSAWV 145
Cdd:cd00158  84 GMLAWK 89
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
56-150 2.66e-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: 70.18  E-value: 2.66e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700     56 GHRYLDVRTNEEFAKSHVEEALNIPYM-FKTDEGRVINPDFLSQVASV-CKKDEHLIVACNAGGRGSRACVDLLNEGYDH 133
Cdd:smart00450   4 KVVLLDVRSPEEYEGGHIPGAVNIPLSeLLDRRGELDILEFEELLKRLgLDKDKPVVVYCRSGNRSAKAAWLLRELGFKN 83
                           90
                   ....*....|....*..
gi 79558700    134 VANMGGGYSAWVDAGFA 150
Cdd:smart00450  84 VYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
60-145 1.02e-14

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: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700    60 LDVRTNEEFAKSHVEEALNIPYMFKTDEGRVINPDFLSQVASVckKDEHLIVACNAGGRGSRACVDLLNEGYDHVANMGG 139
Cdd:pfam00581   9 IDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLLELL--KDKPIVVYCNSGNRAAAAAALLKALGYKNVYVLDG 86

                  ....*.
gi 79558700   140 GYSAWV 145
Cdd:pfam00581  87 GFEAWK 92
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
60-144 2.58e-06

tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a selenophosphate-dependent tRNA 2-selenouridine synthase, essential for modification of some tRNAs to replace a sulfur atom with selenium. This enzyme works with SelD, the selenium donor protein, which also acts in selenocysteine incorporation. Although the members of this protein family show a fairly deep split, sequences from both sides of the split are supported by co-occurence with, and often proximity to, the selD gene. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274463 [Multi-domain]  Cd Length: 311  Bit Score: 46.05  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700    60 LDVRTNEEFAKSHVEEALNIPYMfkTDEGRVI------------------------NPDFLSQVASVCKKDEHLIVACNA 115
Cdd:TIGR03167   6 IDVRSPAEFAEGHLPGAINLPLL--NDEERAEvgtlykqvgpfaaiklglalvspnLAAHVEQWRAFADGPPQPLLYCWR 83
                          90       100       110
                  ....*....|....*....|....*....|
gi 79558700   116 GGRGSRACVDLLNE-GYDhVANMGGGYSAW 144
Cdd:TIGR03167  84 GGMRSGSLAWLLAQiGFR-VPRLEGGYKAY 112
 
Name Accession Description Interval E-value
PLN02160 PLN02160
thiosulfate sulfurtransferase
39-149 2.71e-35

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 119.81  E-value: 2.71e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700   39 EDVETVDVYTAKGFLSTGHRYLDVRTNEEFAKSHVEEA--LNIPYMFKTDEGRVINPDFLSQVASVCKKDEHLIVACNAG 116
Cdd:PLN02160  12 EEVVSVDVSQAKTLLQSGHQYLDVRTQDEFRRGHCEAAkiVNIPYMLNTPQGRVKNQEFLEQVSSLLNPADDILVGCQSG 91
                         90       100       110
                 ....*....|....*....|....*....|...
gi 79558700  117 GRGSRACVDLLNEGYDHVANMGGGYSAWVDAGF 149
Cdd:PLN02160  92 ARSLKATTELVAAGYKKVRNKGGGYLAWVDHSF 124
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
40-154 1.69e-22

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: 86.17  E-value: 1.69e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700  40 DVETVDVYTAKGFLSTGH-RYLDVRTNEEFAKSHVEEALNIPYmfktdegrvinPDFLSQVASVcKKDEHLIVACNAGGR 118
Cdd:COG0607   2 SVKEISPAELAELLESEDaVLLDVREPEEFAAGHIPGAINIPL-----------GELAERLDEL-PKDKPIVVYCASGGR 69
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 79558700 119 GSRACVDLLNEGYDHVANMGGGYSAWVDAGFAGDKP 154
Cdd:COG0607  70 SAQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVEKG 105
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
60-145 4.88e-19

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: 76.95  E-value: 4.88e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700  60 LDVRTNEEFAKSHVEEALNIPYMFKTDEGRVINPDflsqvasvckKDEHLIVACNAGGRGSRACVDLLNEGYDHVANMGG 139
Cdd:cd00158  14 LDVREPEEYAAGHIPGAINIPLSELEERAALLELD----------KDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLEG 83

                ....*.
gi 79558700 140 GYSAWV 145
Cdd:cd00158  84 GMLAWK 89
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
56-150 2.66e-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: 70.18  E-value: 2.66e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700     56 GHRYLDVRTNEEFAKSHVEEALNIPYM-FKTDEGRVINPDFLSQVASV-CKKDEHLIVACNAGGRGSRACVDLLNEGYDH 133
Cdd:smart00450   4 KVVLLDVRSPEEYEGGHIPGAVNIPLSeLLDRRGELDILEFEELLKRLgLDKDKPVVVYCRSGNRSAKAAWLLRELGFKN 83
                           90
                   ....*....|....*..
gi 79558700    134 VANMGGGYSAWVDAGFA 150
Cdd:smart00450  84 VYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
60-145 1.02e-14

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: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700    60 LDVRTNEEFAKSHVEEALNIPYMFKTDEGRVINPDFLSQVASVckKDEHLIVACNAGGRGSRACVDLLNEGYDHVANMGG 139
Cdd:pfam00581   9 IDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLLELL--KDKPIVVYCNSGNRAAAAAALLKALGYKNVYVLDG 86

                  ....*.
gi 79558700   140 GYSAWV 145
Cdd:pfam00581  87 GFEAWK 92
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
44-155 1.52e-13

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 66.96  E-value: 1.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700   44 VDVYTAKGFLSTGHRYLDVRTNEEFAKSHVEEALNIPYMFKtdEGRVinpdflsqVASVCKKDEHLIVACNAGGRGSRAC 123
Cdd:PRK08762   5 ISPAEARARAAQGAVLIDVREAHERASGQAEGALRIPRGFL--ELRI--------ETHLPDRDREIVLICASGTRSAHAA 74
                         90       100       110
                 ....*....|....*....|....*....|..
gi 79558700  124 VDLLNEGYDHVANMGGGYSAWVDAGFAGDKPP 155
Cdd:PRK08762  75 ATLRELGYTRVASVAGGFSAWKDAGLPLERPR 106
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
60-144 1.12e-10

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: 54.96  E-value: 1.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700  60 LDVRTNEEFAKSHVEEALNIPymfkTDEGRvinpDFLSQVasvcKKDEHLIVACNAGGRGSRACVDLLNEGYDhVANMGG 139
Cdd:cd01524  17 IDVRTPQEFEKGHIKGAINIP----LDELR----DRLNEL----PKDKEIIVYCAVGLRGYIAARILTQNGFK-VKNLDG 83

                ....*
gi 79558700 140 GYSAW 144
Cdd:cd01524  84 GYKTY 88
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
60-144 1.65e-09

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: 52.40  E-value: 1.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700  60 LDVRTNEEFAKSHVEEALNIPymfktdegrvinpdfLSQVASVCK------KDEHLIVACNAGGRGSRACVDLLNEGYDH 133
Cdd:cd01528  21 IDVREPEELEIAFLPGFLHLP---------------MSEIPERSKeldsdnPDKDIVVLCHHGGRSMQVAQWLLRQGFEN 85
                        90
                ....*....|.
gi 79558700 134 VANMGGGYSAW 144
Cdd:cd01528  86 VYNLQGGIDAW 96
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
59-139 3.72e-08

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 49.07  E-value: 3.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700   59 YLDVRTNEEFAKSHVEEALNIPYM-FKTDEGRVInPDflsqvasvckKDEHLIVACNAGGRGSRACVDLLNEGYDHVANM 137
Cdd:PRK10287  23 WIDVRVPEQYQQEHVQGAINIPLKeVKERIATAV-PD----------KNDTVKLYCNAGRQSGQAKEILSEMGYTHAENA 91

                 ..
gi 79558700  138 GG 139
Cdd:PRK10287  92 GG 93
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
60-146 6.05e-08

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: 48.26  E-value: 6.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700  60 LDVRTNEEFAKSHVEEALNIPYMFKTDEGRVINPDFLSQVasvcKKDEHLIVACNAGGrGSRACVDLLNE-GYDhVANMG 138
Cdd:cd01523  19 LDVRNESDYERWKIDGENNTPYFDPYFDFLEIEEDILDQL----PDDQEVTVICAKEG-SSQFVAELLAErGYD-VDYLA 92

                ....*...
gi 79558700 139 GGYSAWVD 146
Cdd:cd01523  93 GGMKAWSE 100
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
37-147 6.10e-08

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 51.03  E-value: 6.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700   37 TVEDVETVDV--YTAkgfLSTGHRYLDVRTNEEFAKSHVEEALNIPyMFKTDEGrvINPDFLSqvasvckKDEHLIVACN 114
Cdd:PRK05597 256 SGGFGEVLDVprVSA---LPDGVTLIDVREPSEFAAYSIPGAHNVP-LSAIREG--ANPPSVS-------AGDEVVVYCA 322
                         90       100       110
                 ....*....|....*....|....*....|...
gi 79558700  115 AGGRGSRACVDLLNEGYDHVANMGGGYSAWVDA 147
Cdd:PRK05597 323 AGVRSAQAVAILERAGYTGMSSLDGGIEGWLDS 355
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
58-156 8.48e-08

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: 48.09  E-value: 8.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700  58 RYLDVRTNEEFAK-SHVEEALNIPYmfKTDEGRVINPDFLSQVASVCKKDEHLIVACNAGGRGSRACVDLLNEGYDHVAN 136
Cdd:cd01522  17 VLVDVRTEAEWKFvGGVPDAVHVAW--QVYPDMEINPNFLAELEEKVGKDRPVLLLCRSGNRSIAAAEAAAQAGFTNVYN 94
                        90       100
                ....*....|....*....|
gi 79558700 137 mgggysawVDAGFAGDKPPE 156
Cdd:cd01522  95 --------VLEGFEGDLDAA 106
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
56-145 1.33e-07

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: 47.29  E-value: 1.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700  56 GHRYLDVRTNEEFAKSHVEEALNIP---YMFKTDEgrvinpdflSQVASVCKKDEHLIVACNAGGRGSRACVDLLNEGYD 132
Cdd:cd01529  12 GTALLDVRAEDEYAAGHLPGKRSIPgaaLVLRSQE---------LQALEAPGRATRYVLTCDGSLLARFAAQELLALGGK 82
                        90
                ....*....|...
gi 79558700 133 HVANMGGGYSAWV 145
Cdd:cd01529  83 PVALLDGGTSAWV 95
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
53-146 5.61e-07

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: 45.72  E-value: 5.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700  53 LSTGHR--YL-DVRTNEEFAKSHVEEALNIPymFKTDEGRV-INPDFLSQVASVCK--KDEHLIVACNAGGRGSRACVDL 126
Cdd:cd01519   9 LPNPHPnkVLiDVREPEELKTGKIPGAINIP--LSSLPDALaLSEEEFEKKYGFPKpsKDKELIFYCKAGVRSKAAAELA 86
                        90       100
                ....*....|....*....|
gi 79558700 127 LNEGYDHVANMGGGYSAWVD 146
Cdd:cd01519  87 RSLGYENVGNYPGSWLDWAA 106
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
60-144 2.58e-06

tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a selenophosphate-dependent tRNA 2-selenouridine synthase, essential for modification of some tRNAs to replace a sulfur atom with selenium. This enzyme works with SelD, the selenium donor protein, which also acts in selenocysteine incorporation. Although the members of this protein family show a fairly deep split, sequences from both sides of the split are supported by co-occurence with, and often proximity to, the selD gene. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274463 [Multi-domain]  Cd Length: 311  Bit Score: 46.05  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700    60 LDVRTNEEFAKSHVEEALNIPYMfkTDEGRVI------------------------NPDFLSQVASVCKKDEHLIVACNA 115
Cdd:TIGR03167   6 IDVRSPAEFAEGHLPGAINLPLL--NDEERAEvgtlykqvgpfaaiklglalvspnLAAHVEQWRAFADGPPQPLLYCWR 83
                          90       100       110
                  ....*....|....*....|....*....|
gi 79558700   116 GGRGSRACVDLLNE-GYDhVANMGGGYSAW 144
Cdd:TIGR03167  84 GGMRSGSLAWLLAQiGFR-VPRLEGGYKAY 112
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
60-148 3.11e-05

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: 40.87  E-value: 3.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700  60 LDVRTNEEF-AKSHVEEALNIPY-M--FKTD-EGRVINPDFlsqvasvcKKDEHLIVACNAGGRGSRACVDLLNEGYDHV 134
Cdd:cd01447  18 VDVRDPRELeRTGMIPGAFHAPRgMleFWADpDSPYHKPAF--------AEDKPFVFYCASGWRSALAGKTLQDMGLKPV 89
                        90
                ....*....|....
gi 79558700 135 ANMGGGYSAWVDAG 148
Cdd:cd01447  90 YNIEGGFKDWKEAG 103
SelU COG2603
tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal ...
60-144 7.57e-05

tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal structure and biogenesis]; tRNA 2-selenouridine synthase SelU, contains rhodanese domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442015 [Multi-domain]  Cd Length: 341  Bit Score: 41.68  E-value: 7.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700  60 LDVRTNEEFAKSHVEEALNIPYMfkTDEGRVI-----------------------N-PDFLSQVASVCKKDEHLIVACNA 115
Cdd:COG2603  20 IDVRSPVEFAEGHIPGAINLPLL--DDEERAEvgtcykqqgpfaaiklghalvsgKlAAHREEAWAFAPKHPRPLVYCWR 97
                        90       100       110
                ....*....|....*....|....*....|
gi 79558700 116 GGRGSRACVDLLNE-GYDhVANMGGGYSAW 144
Cdd:COG2603  98 GGLRSGSVAQWLREaGID-VPRLEGGYKAY 126
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
60-150 3.95e-04

Member of the Rhodanese Homology Domain superfamily. This CD includes the putative rhodanese-like protein, Psp2, of Yersinia pestis biovar Medievalis and other similar uncharacterized proteins.


Pssm-ID: 238779 [Multi-domain]  Cd Length: 110  Bit Score: 38.10  E-value: 3.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700  60 LDVRTNEEFAKSHVEEALNIPymfktdeGRVINPDFLSQVasvcKKDEHLIV-----ACNAggrGSRACVDLLNEGYDhV 134
Cdd:cd01521  29 VDVRSAEAYARGHVPGAINLP-------HREICENATAKL----DKEKLFVVycdgpGCNG---ATKAALKLAELGFP-V 93
                        90
                ....*....|....*.
gi 79558700 135 ANMGGGYSAWVDAGFA 150
Cdd:cd01521  94 KEMIGGLDWWKREGYA 109
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
52-144 6.81e-04

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 39.04  E-value: 6.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700   52 FLSTGHRYLDVRTNEEFAKSHVEEALNIPYMfkTDEGRV---------------------INPDF----LSQVASVCKKD 106
Cdd:PRK11784  11 LFLNDTPLIDVRSPIEFAEGHIPGAINLPLL--NDEERAevgtcykqqgqfaaialghalVAGNIaahrEEAWADFPRAN 88
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 79558700  107 EHLIVACNAGGRGSRACVDLLNE-GYDhVANMGGGYSAW 144
Cdd:PRK11784  89 PRGLLYCWRGGLRSGSVQQWLKEaGID-VPRLEGGYKAY 126
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
57-146 2.77e-03

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: 36.13  E-value: 2.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700  57 HRYLDVRTNEEFAKSHVEEALNIP--------YMFKTDEGRVINPDFLSQVASVCKKdehlivacnagGRGSRACVDLLN 128
Cdd:cd01526  25 HVLLDVRPKVHFEICRLPEAINIPlsellskaAELKSLQELPLDNDKDSPIYVVCRR-----------GNDSQTAVRKLK 93
                        90       100
                ....*....|....*....|
gi 79558700 129 E-GYDH-VANMGGGYSAWVD 146
Cdd:cd01526  94 ElGLERfVRDIIGGLKAWAD 113
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
60-144 3.62e-03

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: 35.31  E-value: 3.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700  60 LDVRTNEEFAKS--HveealnIPYMFKTDEGRVinPDFLSQVAsvckKDEHLIVACnAGGRGSRACVDLLNE-GYDHVAN 136
Cdd:cd01444  20 LDVRDPASYAALpdH------IPGAIHLDEDSL--DDWLGDLD----RDRPVVVYC-YHGNSSAQLAQALREaGFTDVRS 86

                ....*...
gi 79558700 137 MGGGYSAW 144
Cdd:cd01444  87 LAGGFEAW 94
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
61-144 4.79e-03

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 35.00  E-value: 4.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700   61 DVRTNEEFAKSHVEEAlnipymFKTDEGRVinPDFLSQVasvcKKDEHLIVACNAGGRGSRACVDLLNEGYDHVANMGGG 140
Cdd:PRK00162  25 DIRDPQSFAMGHAPGA------FHLTNDSL--GAFMRQA----DFDTPVMVMCYHGNSSQGAAQYLLQQGFDVVYSIDGG 92

                 ....
gi 79558700  141 YSAW 144
Cdd:PRK00162  93 FEAW 96
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
60-144 5.59e-03

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: 34.39  E-value: 5.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700  60 LDVRTNEEFAKSHVEEALNIPymfktdegrvINPDFLSQVASVCKKDEHLIVACNAGGRG--SRACVDLLNEGYDHVANM 137
Cdd:cd01532  14 IDVREEDPFAQSHPLWAANLP----------LSRLELDAWVRIPRRDTPIVVYGEGGGEDlaPRAARRLSELGYTDVALL 83

                ....*..
gi 79558700 138 GGGYSAW 144
Cdd:cd01532  84 EGGLQGW 90
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
60-148 8.15e-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: 34.52  E-value: 8.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79558700  60 LDVRTN-------EEFAKSHVEEALNIPY---MFKTDEGRVINPDfLSQVASVCKK-----DEHLIVACNAGGRGS-RAC 123
Cdd:cd01448  19 LDARWYlpdrdgrKEYLEGHIPGAVFFDLdedLDDKSPGPHMLPS-PEEFAELLGSlgisnDDTVVVYDDGGGFFAaRAW 97
                        90       100
                ....*....|....*....|....*
gi 79558700 124 VDLLNEGYDHVANMGGGYSAWVDAG 148
Cdd:cd01448  98 WTLRYFGHENVRVLDGGLQAWKAEG 122
 
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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