NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|163965371|ref|NP_001106676|]
View 

thiosulfate:glutathione sulfurtransferase isoform 3 [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
7-101 1.20e-36

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 cd01519:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 106  Bit Score: 120.07  E-value: 1.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   7 VSLPELRSLLA-SGRARLFDVRSREEAAAGTIPGALNIPVSELESALQMEPAAFQALYSAEKPKLEDEhLVFFCQMGKRG 85
Cdd:cd01519    1 YSFEEVKNLPNpHPNKVLIDVREPEELKTGKIPGAINIPLSSLPDALALSEEEFEKKYGFPKPSKDKE-LIFYCKAGVRS 79
                         90
                 ....*....|....*.
gi 163965371  86 LQATQLARSLGYTGYG 101
Cdd:cd01519   80 KAAAELARSLGYENVG 95
 
Name Accession Description Interval E-value
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
7-101 1.20e-36

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: 120.07  E-value: 1.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   7 VSLPELRSLLA-SGRARLFDVRSREEAAAGTIPGALNIPVSELESALQMEPAAFQALYSAEKPKLEDEhLVFFCQMGKRG 85
Cdd:cd01519    1 YSFEEVKNLPNpHPNKVLIDVREPEELKTGKIPGAINIPLSSLPDALALSEEEFEKKYGFPKPSKDKE-LIFYCKAGVRS 79
                         90
                 ....*....|....*.
gi 163965371  86 LQATQLARSLGYTGYG 101
Cdd:cd01519   80 KAAAELARSLGYENVG 95
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
2-108 1.63e-21

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: 81.55  E-value: 1.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   2 AGAPTVSLPELRSLLASGRARLFDVRSREEAAAGTIPGALNIPVSELESALqmepaafqalysAEKPKleDEHLVFFCQM 81
Cdd:COG0607    1 ASVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERL------------DELPK--DKPIVVYCAS 66
                         90       100
                 ....*....|....*....|....*..
gi 163965371  82 GKRGLQATQLARSLGYTgygEVWLLAG 108
Cdd:COG0607   67 GGRSAQAAALLRRAGYT---NVYNLAG 90
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
16-108 7.65e-19

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: 74.44  E-value: 7.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   16 LASGRARLFDVRSREEAAAGTIPGALNIPVSElesaLQMEPAAFQALYSAEKPKLEDEHLVFFCQMGKRGLQATQLARSL 95
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSS----LSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKAL 76
                          90
                  ....*....|...
gi 163965371   96 GYTgygEVWLLAG 108
Cdd:pfam00581  77 GYK---NVYVLDG 86
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
19-108 6.73e-17

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 69.80  E-value: 6.73e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371    19 GRARLFDVRSREEAAAGTIPGALNIPVSELESALQMEPAAFQALYSAEKPKLEDEHLVFFCQMGKRGLQATQLARSLGYT 98
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGFK 82
                           90
                   ....*....|
gi 163965371    99 gygEVWLLAG 108
Cdd:smart00450  83 ---NVYLLDG 89
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
5-108 8.49e-14

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 65.42  E-value: 8.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   5 PTVSLPELRSLLASGrARLFDVRSREEAAAGTIPGALNIPVSELEsalqMEPAafqalysAEKPKLeDEHLVFFCQMGKR 84
Cdd:PRK08762   3 REISPAEARARAAQG-AVLIDVREAHERASGQAEGALRIPRGFLE----LRIE-------THLPDR-DREIVLICASGTR 69
                         90       100
                 ....*....|....*....|....
gi 163965371  85 GLQAtqlARSLGYTGYGEVWLLAG 108
Cdd:PRK08762  70 SAHA---AATLRELGYTRVASVAG 90
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
23-45 2.47e-03

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: 35.65  E-value: 2.47e-03
                          10        20
                  ....*....|....*....|...
gi 163965371   23 LFDVRSREEAAAGTIPGALNIPV 45
Cdd:TIGR03167   5 LIDVRSPAEFAEGHLPGAINLPL 27
 
Name Accession Description Interval E-value
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
7-101 1.20e-36

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: 120.07  E-value: 1.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   7 VSLPELRSLLA-SGRARLFDVRSREEAAAGTIPGALNIPVSELESALQMEPAAFQALYSAEKPKLEDEhLVFFCQMGKRG 85
Cdd:cd01519    1 YSFEEVKNLPNpHPNKVLIDVREPEELKTGKIPGAINIPLSSLPDALALSEEEFEKKYGFPKPSKDKE-LIFYCKAGVRS 79
                         90
                 ....*....|....*.
gi 163965371  86 LQATQLARSLGYTGYG 101
Cdd:cd01519   80 KAAAELARSLGYENVG 95
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
2-108 1.63e-21

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: 81.55  E-value: 1.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   2 AGAPTVSLPELRSLLASGRARLFDVRSREEAAAGTIPGALNIPVSELESALqmepaafqalysAEKPKleDEHLVFFCQM 81
Cdd:COG0607    1 ASVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERL------------DELPK--DKPIVVYCAS 66
                         90       100
                 ....*....|....*....|....*..
gi 163965371  82 GKRGLQATQLARSLGYTgygEVWLLAG 108
Cdd:COG0607   67 GGRSAQAAALLRRAGYT---NVYNLAG 90
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
11-108 3.26e-20

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 77.73  E-value: 3.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371  11 ELRSLLASGRARLFDVRSREEAAAGTIPGALNIPVSELESALQMepaafqalysAEKPKleDEHLVFFCQMGKRGLQATQ 90
Cdd:cd00158    1 ELKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAAL----------LELDK--DKPIVVYCRSGNRSARAAK 68
                         90
                 ....*....|....*...
gi 163965371  91 LARSLGYTgygEVWLLAG 108
Cdd:cd00158   69 LLRKAGGT---NVYNLEG 83
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
16-108 7.65e-19

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: 74.44  E-value: 7.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   16 LASGRARLFDVRSREEAAAGTIPGALNIPVSElesaLQMEPAAFQALYSAEKPKLEDEHLVFFCQMGKRGLQATQLARSL 95
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSS----LSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKAL 76
                          90
                  ....*....|...
gi 163965371   96 GYTgygEVWLLAG 108
Cdd:pfam00581  77 GYK---NVYVLDG 86
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
19-108 6.73e-17

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 69.80  E-value: 6.73e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371    19 GRARLFDVRSREEAAAGTIPGALNIPVSELESALQMEPAAFQALYSAEKPKLEDEHLVFFCQMGKRGLQATQLARSLGYT 98
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGFK 82
                           90
                   ....*....|
gi 163965371    99 gygEVWLLAG 108
Cdd:smart00450  83 ---NVYLLDG 89
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
5-108 8.49e-14

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 65.42  E-value: 8.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   5 PTVSLPELRSLLASGrARLFDVRSREEAAAGTIPGALNIPVSELEsalqMEPAafqalysAEKPKLeDEHLVFFCQMGKR 84
Cdd:PRK08762   3 REISPAEARARAAQG-AVLIDVREAHERASGQAEGALRIPRGFLE----LRIE-------THLPDR-DREIVLICASGTR 69
                         90       100
                 ....*....|....*....|....
gi 163965371  85 GLQAtqlARSLGYTGYGEVWLLAG 108
Cdd:PRK08762  70 SAHA---AATLRELGYTRVASVAG 90
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
6-108 1.13e-11

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: 56.25  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   6 TVSLPELRSLLASGRAR--LFDVRSREEAAAGTIPGALNIPVSELesalqmepaafqALYSAEKP-KLEDEHLVFFCQMG 82
Cdd:cd01528    1 QISVAELAEWLADEREEpvLIDVREPEELEIAFLPGFLHLPMSEI------------PERSKELDsDNPDKDIVVLCHHG 68
                         90       100
                 ....*....|....*....|....*.
gi 163965371  83 KRGLQATQLARSlgyTGYGEVWLLAG 108
Cdd:cd01528   69 GRSMQVAQWLLR---QGFENVYNLQG 91
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
11-98 3.88e-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: 51.88  E-value: 3.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371  11 ELRSLLASGRArLFDVRSREEAAAGTIPGALNIPVSELESALqmepaafqalysAEKPKleDEHLVFFCQMGKRGLQATQ 90
Cdd:cd01524    5 ELDNYRADGVT-LIDVRTPQEFEKGHIKGAINIPLDELRDRL------------NELPK--DKEIIVYCAVGLRGYIAAR 69

                 ....*...
gi 163965371  91 LARSLGYT 98
Cdd:cd01524   70 ILTQNGFK 77
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
4-99 2.30e-08

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 49.79  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   4 APTVSLPELRSLLASGRARLFDVRSREE---------AAAGTIPGALNIPVSEL--ESALQMEPAAFQALYSAEKPKLeD 72
Cdd:COG2897  137 ELLADADEVLAALGDPDAVLVDARSPERyrgevepidPRAGHIPGAVNLPWTDLldEDGTFKSAEELRALFAALGIDP-D 215
                         90       100
                 ....*....|....*....|....*..
gi 163965371  73 EHLVFFCQMGKRGLQATQLARSLGYTG 99
Cdd:COG2897  216 KPVITYCGSGVRAAHTWLALELLGYPN 242
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
7-108 3.59e-08

Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as a polysulfide binding and transferase domain in anaerobic gram-negative bacteria, functioning in oxidative phosphorylation with polysulfide-sulfur as a terminal electron acceptor. The active site contains the same conserved cysteine that is the catalytic residue in other Rhodanese Homology Domain proteins.


Pssm-ID: 238724 [Multi-domain]  Cd Length: 103  Bit Score: 47.42  E-value: 3.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   7 VSLPELRSLLASGRARLFDVRS-REEAAAGTIPGALNIPVSELESALQMEPAAFQALYSAEKPkledehLVFFCQMGKRG 85
Cdd:cd01447    1 LSPEDARALLGSPGVLLVDVRDpRELERTGMIPGAFHAPRGMLEFWADPDSPYHKPAFAEDKP------FVFYCASGWRS 74
                         90       100       110
                 ....*....|....*....|....*....|
gi 163965371  86 LQATQLARSLGYT-------GYGEvWLLAG 108
Cdd:cd01447   75 ALAGKTLQDMGLKpvyniegGFKD-WKEAG 103
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
7-108 4.69e-08

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: 47.24  E-value: 4.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   7 VSLPELRSLLASGRARLFDVRSREE-----------AAAGTIPGALNIPVSE-LESALQMEPAA-FQALYSAEKPKLEDE 73
Cdd:cd01449    1 VTAEEVLANLDSGDVQLVDARSPERfrgevpeprpgLRSGHIPGAVNIPWTSlLDEDGTFKSPEeLRALFAALGITPDKP 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 163965371  74 hLVFFCQMGKRglqATQLARSLGYTGYGEVWLLAG 108
Cdd:cd01449   81 -VIVYCGSGVT---ACVLLLALELLGYKNVRLYDG 111
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
1-99 4.88e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 49.35  E-value: 4.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   1 MAGAPTVSLPELRSLLASGRAR--LFDVRSREEAAAGTIPGALNIPVSELESALQMEPAafqalysaeKPKLEDEHLVFF 78
Cdd:PRK07411 278 KAEIPEMTVTELKALLDSGADDfvLIDVRNPNEYEIARIPGSVLVPLPDIENGPGVEKV---------KELLNGHRLIAH 348
                         90       100
                 ....*....|....*....|.
gi 163965371  79 CQMGKRGLQATQLARSLGYTG 99
Cdd:PRK07411 349 CKMGGRSAKALGILKEAGIEG 369
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
21-99 3.11e-07

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 46.79  E-value: 3.11e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163965371  21 ARLFDVRSREEAAAGTIPGALNIPVSELESALQmePAAFQAlysaekpkleDEHLVFFCQMGKRGLQATQLARSLGYTG 99
Cdd:PRK05597 275 VTLIDVREPSEFAAYSIPGAHNVPLSAIREGAN--PPSVSA----------GDEVVVYCAAGVRSAQAVAILERAGYTG 341
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
7-98 6.57e-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: 44.22  E-value: 6.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   7 VSLPELRSLLASGRARLF-DVRSREEAAAGTIPGALNIPVSELESalqmepAAFQALYSAEKPKLEDEHLVFF--CQMGK 83
Cdd:cd01526   10 VSVKDYKNILQAGKKHVLlDVRPKVHFEICRLPEAINIPLSELLS------KAAELKSLQELPLDNDKDSPIYvvCRRGN 83
                         90
                 ....*....|....*
gi 163965371  84 RGLQATQLARSLGYT 98
Cdd:cd01526   84 DSQTAVRKLKELGLE 98
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
15-98 6.98e-07

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: 44.24  E-value: 6.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371  15 LLASGRARLFDVRSREE-AAAGTIPGALNIpvsELESALQMEP-AAFQALYSAEKPKleDEHLVFFCQMGKRGLQATQLA 92
Cdd:cd01522   10 LQADPQAVLVDVRTEAEwKFVGGVPDAVHV---AWQVYPDMEInPNFLAELEEKVGK--DRPVLLLCRSGNRSIAAAEAA 84

                 ....*.
gi 163965371  93 RSLGYT 98
Cdd:cd01522   85 AQAGFT 90
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
5-108 2.11e-06

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: 42.47  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   5 PTVSLPELRSLLASGrARLFDVRSREEAAAGTIPGALNIPVSELESalqmepaafQALysaekPKLEDEHLVFFCQMGKR 84
Cdd:cd01527    2 TTISPNDACELLAQG-AVLVDIREPDEYLRERIPGARLVPLSQLES---------EGL-----PLVGANAIIFHCRSGMR 66
                         90       100
                 ....*....|....*....|....
gi 163965371  85 GLQATQLarsLGYTGYGEVWLLAG 108
Cdd:cd01527   67 TQQNAER---LAAISAGEAYVLEG 87
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
7-108 7.89e-06

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: 41.09  E-value: 7.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   7 VSLPELRSLLASGR-ARLFDVRSREEAAA--GTIPGAlnIPVSELEsalqmePAAFQALYSAEKPkledehLVFFCQmgk 83
Cdd:cd01444    2 ISVDELAELLAAGEaPVLLDVRDPASYAAlpDHIPGA--IHLDEDS------LDDWLGDLDRDRP------VVVYCY--- 64
                         90       100
                 ....*....|....*....|....*
gi 163965371  84 RGLQATQLARSLGYTGYGEVWLLAG 108
Cdd:cd01444   65 HGNSSAQLAQALREAGFTDVRSLAG 89
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
2-98 9.25e-05

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 39.69  E-value: 9.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   2 AGAPTVSLPELRSLLASGRA-RLFDVRSREEAAAGTIPGALNIPVSELESAlqmepaafQALysAEKPklEDEHLVFFCQ 80
Cdd:PRK07878 284 AAGSTITPRELKEWLDSGKKiALIDVREPVEWDIVHIPGAQLIPKSEILSG--------EAL--AKLP--QDRTIVLYCK 351
                         90
                 ....*....|....*...
gi 163965371  81 MGKRGLQATQLARSLGYT 98
Cdd:PRK07878 352 TGVRSAEALAALKKAGFS 369
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
16-58 2.33e-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: 37.33  E-value: 2.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 163965371  16 LASGRAR--LFDVRSREEAAAGTIPGALNIPVSEL-ESALQMEPAA 58
Cdd:cd01521   19 LKNGKPDfvLVDVRSAEAYARGHVPGAINLPHREIcENATAKLDKE 64
SelU COG2603
tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal ...
23-45 3.04e-04

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: 38.21  E-value: 3.04e-04
                         10        20
                 ....*....|....*....|...
gi 163965371  23 LFDVRSREEAAAGTIPGALNIPV 45
Cdd:COG2603   19 LIDVRSPVEFAEGHIPGAINLPL 41
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
5-48 3.63e-04

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: 37.05  E-value: 3.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 163965371   5 PTVSLPELRSLLASGR-ARLFDVRSREEAAAGTIPGALNIPVSEL 48
Cdd:cd01533   10 PSVSADELAALQARGApLVVLDGRRFDEYRKMTIPGSVSCPGAEL 54
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
7-44 3.78e-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: 36.68  E-value: 3.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 163965371   7 VSLPELRSLLASGRARL--FDVRSREEAAAGTIPGALNIP 44
Cdd:cd01534    1 IGAAELARWAAEGDRTVyrFDVRTPEEYEAGHLPGFRHTP 40
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
20-108 4.39e-04

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: 36.62  E-value: 4.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371  20 RARLFDVRsREEAAAGTIPGALNIPVselESALQMEPAAFQALYSAEKPKledehLVFFC----QMGKRGLQATQLA-RS 94
Cdd:cd01443   23 DFVVVDLR-RDDYEGGHIKGSINLPA---QSCYQTLPQVYALFSLAGVKL-----AIFYCgssqGRGPRAARWFADYlRK 93
                         90
                 ....*....|....
gi 163965371  95 LGYTgYGEVWLLAG 108
Cdd:cd01443   94 VGES-LPKSYILTG 106
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
7-108 4.70e-04

Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain superfamily. Included in this CD is the Saccharomyces cerevisiae arsenate reductase protein, Acr2p, and other yeast and plant homologs.


Pssm-ID: 238789 [Multi-domain]  Cd Length: 113  Bit Score: 36.62  E-value: 4.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   7 VSLPELRSLLASGRAR--LFDVRsREEAAAGTIPGALNIPVSELESALqmePAAFQALYSAEKpkledEHLVFFCQMGK- 83
Cdd:cd01531    4 ISPAQLKGWIRNGRPPfqVVDVR-DEDYAGGHIKGSWHYPSTRFKAQL---NQLVQLLSGSKK-----DTVVFHCALSQv 74
                         90       100       110
                 ....*....|....*....|....*....|
gi 163965371  84 RGLQAT-QLARSLG----YTGYGEVWLLAG 108
Cdd:cd01531   75 RGPSAArKFLRYLDeedlETSKFEVYVLHG 104
RHOD_YbbB cd01520
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ...
23-45 1.52e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP /GTP binding proteins including E. coli YbbB.


Pssm-ID: 238778 [Multi-domain]  Cd Length: 128  Bit Score: 35.35  E-value: 1.52e-03
                         10        20
                 ....*....|....*....|...
gi 163965371  23 LFDVRSREEAAAGTIPGALNIPV 45
Cdd:cd01520   16 LIDVRSPKEFFEGHLPGAINLPL 38
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
23-45 2.47e-03

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: 35.65  E-value: 2.47e-03
                          10        20
                  ....*....|....*....|...
gi 163965371   23 LFDVRSREEAAAGTIPGALNIPV 45
Cdd:TIGR03167   5 LIDVRSPAEFAEGHLPGAINLPL 27
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
23-45 3.44e-03

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 35.19  E-value: 3.44e-03
                         10        20
                 ....*....|....*....|...
gi 163965371  23 LFDVRSREEAAAGTIPGALNIPV 45
Cdd:PRK11784  18 LIDVRSPIEFAEGHIPGAINLPL 40
PRK05320 PRK05320
rhodanese superfamily protein; Provisional
4-84 8.17e-03

rhodanese superfamily protein; Provisional


Pssm-ID: 235405 [Multi-domain]  Cd Length: 257  Bit Score: 34.23  E-value: 8.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163965371   4 APTVSLPELRSLLASG---RAR---LFDVRSREEAAAGTIPGALNIPV---SELESALQmepaafqalysAEKPKLEDEH 74
Cdd:PRK05320 109 APSVDAATLKRWLDQGhddAGRpvvMLDTRNAFEVDVGTFDGALDYRIdkfTEFPEALA-----------AHRADLAGKT 177
                         90
                 ....*....|
gi 163965371  75 LVFFCQMGKR 84
Cdd:PRK05320 178 VVSFCTGGIR 187
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH