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Conserved domains on  [gi|24646383|ref|NP_650227|]
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uncharacterized protein Dmel_CG12279 [Drosophila melanogaster]

Protein Classification

rhodanese-like domain-containing protein( domain architecture ID 10107410)

rhodanese-like domain-containing protein similar to Mus musculus thiosulfate sulfurtransferase (rhodanese)-like domain containing 3, Saccharomyces cerevisiae mitochondrial thiosulfate sulfurtransferase, and Drosophila melanogaster heat shock protein 67B2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 2-107 9.32e-45

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: 140.48  E-value: 9.32e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646383   2 ATYEEVKDIPN-HPEKYLFDVRNESELKeTGVLPASINIPLSELEKALNLPEEDFAQTYGRVKPAVDAVLIFSCKAGGRA 80
Cdd:cd01519   1 YSFEEVKNLPNpHPNKVLIDVREPEELK-TGKIPGAINIPLSSLPDALALSEEEFEKKYGFPKPSKDKELIFYCKAGVRS 79

                        90       100
                ....*....|....*....|....*..
gi 24646383  81 ARAANLASTLGFTNAKAYAGSWTEWQA 107
Cdd:cd01519  80 KAAAELARSLGYENVGNYPGSWLDWAA 106
 
Name Accession Description Interval E-value
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 2-107 9.32e-45

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: 140.48  E-value: 9.32e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646383   2 ATYEEVKDIPN-HPEKYLFDVRNESELKeTGVLPASINIPLSELEKALNLPEEDFAQTYGRVKPAVDAVLIFSCKAGGRA 80
Cdd:cd01519   1 YSFEEVKNLPNpHPNKVLIDVREPEELK-TGKIPGAINIPLSSLPDALALSEEEFEKKYGFPKPSKDKELIFYCKAGVRS 79

                        90       100
                ....*....|....*....|....*..
gi 24646383  81 ARAANLASTLGFTNAKAYAGSWTEWQA 107
Cdd:cd01519  80 KAAAELARSLGYENVGNYPGSWLDWAA 106
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 3-107 7.69e-11

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: 54.20  E-value: 7.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646383   3 TYEEVKDIPNHPEKYLFDVRNESELkETGVLPASINIPLSELEKALN-LPEedfaqtygrvkpavDAVLIFSCKAGGRAA 81
Cdd:COG0607   7 SPAELAELLESEDAVLLDVREPEEF-AAGHIPGAINIPLGELAERLDeLPK--------------DKPIVVYCASGGRSA 71

                        90       100
                ....*....|....*....|....*.
gi 24646383  82 RAANLASTLGFTNAKAYAGSWTEWQA 107
Cdd:COG0607  72 QAAALLRRAGYTNVYNLAGGIEAWKA 97
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 12-108 7.98e-10

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: 51.69  E-value: 7.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646383     12 NHPEKYLFDVRNESELKEtGVLPASINIPLSEL-EKALNLPEEDFAQTYGRVKPAVDAVLIFSCKAGGRAARAANLASTL 90
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEG-GHIPGAVNIPLSELlDRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLREL 79

                           90
                   ....*....|....*...
gi 24646383     91 GFTNAKAYAGSWTEWQAK 108
Cdd:smart00450  80 GFKNVYLLDGGYKEWSAA 97
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 18-106 9.64e-09

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: 48.63  E-value: 9.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646383    18 LFDVRNESELKEtGVLPASINIPLSELEkalnLPEEDFAQTYGRVKPAV-DAVLIFSCKAGGRAARAANLASTLGFTNAK 96
Cdd:pfam00581   8 LIDVRPPEEYAK-GHIPGAVNVPLSSLS----LPPLPLLELLEKLLELLkDKPIVVYCNSGNRAAAAAALLKALGYKNVY 82

                          90
                  ....*....|
gi 24646383    97 AYAGSWTEWQ 106
Cdd:pfam00581  83 VLDGGFEAWK 92
PRK09629 PRK09629
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
 31-105 2.29e-04

bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional


Pssm-ID: 104071 [Multi-domain]  Cd Length: 610  Bit Score: 38.95  E-value: 2.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24646383   31 GVLPASINIPLSE-LEKALNLP-EEDFAQTYGRVKPAVDAVLIFSCKAGGRAARAANLASTLGFTNAKAYAGSWTEW 105
Cdd:PRK09629 185 GHIPGAVNFEWTAgMDKARNLRiRQDMPEILRDLGITPDKEVITHCQTHHRSGFTYLVAKALGYPRVKAYAGSWGEW 261
 
Name Accession Description Interval E-value
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 2-107 9.32e-45

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: 140.48  E-value: 9.32e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646383   2 ATYEEVKDIPN-HPEKYLFDVRNESELKeTGVLPASINIPLSELEKALNLPEEDFAQTYGRVKPAVDAVLIFSCKAGGRA 80
Cdd:cd01519   1 YSFEEVKNLPNpHPNKVLIDVREPEELK-TGKIPGAINIPLSSLPDALALSEEEFEKKYGFPKPSKDKELIFYCKAGVRS 79

                        90       100
                ....*....|....*....|....*..
gi 24646383  81 ARAANLASTLGFTNAKAYAGSWTEWQA 107
Cdd:cd01519  80 KAAAELARSLGYENVGNYPGSWLDWAA 106
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 3-107 7.69e-11

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: 54.20  E-value: 7.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646383   3 TYEEVKDIPNHPEKYLFDVRNESELkETGVLPASINIPLSELEKALN-LPEedfaqtygrvkpavDAVLIFSCKAGGRAA 81
Cdd:COG0607   7 SPAELAELLESEDAVLLDVREPEEF-AAGHIPGAINIPLGELAERLDeLPK--------------DKPIVVYCASGGRSA 71

                        90       100
                ....*....|....*....|....*.
gi 24646383  82 RAANLASTLGFTNAKAYAGSWTEWQA 107
Cdd:COG0607  72 QAAALLRRAGYTNVYNLAGGIEAWKA 97
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 12-108 7.98e-10

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: 51.69  E-value: 7.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646383     12 NHPEKYLFDVRNESELKEtGVLPASINIPLSEL-EKALNLPEEDFAQTYGRVKPAVDAVLIFSCKAGGRAARAANLASTL 90
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEG-GHIPGAVNIPLSELlDRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLREL 79

                           90
                   ....*....|....*...
gi 24646383     91 GFTNAKAYAGSWTEWQAK 108
Cdd:smart00450  80 GFKNVYLLDGGYKEWSAA 97
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 2-107 5.63e-09

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: 49.55  E-value: 5.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646383   2 ATYEEVKDIPNHPEKYLFDVRNESEL----------KETGVLPASINIPLSEL---EKALnLPEEDFAQTYGRVKPAVDA 68
Cdd:cd01449   1 VTAEEVLANLDSGDVQLVDARSPERFrgevpeprpgLRSGHIPGAVNIPWTSLldeDGTF-KSPEELRALFAALGITPDK 79

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 24646383  69 VLIFSCKAGGRAARAANLASTLGFTNAKAYAGSWTEWQA 107
Cdd:cd01449  80 PVIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEWGS 118
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 18-106 9.64e-09

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: 48.63  E-value: 9.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646383    18 LFDVRNESELKEtGVLPASINIPLSELEkalnLPEEDFAQTYGRVKPAV-DAVLIFSCKAGGRAARAANLASTLGFTNAK 96
Cdd:pfam00581   8 LIDVRPPEEYAK-GHIPGAVNVPLSSLS----LPPLPLLELLEKLLELLkDKPIVVYCNSGNRAAAAAALLKALGYKNVY 82

                          90
                  ....*....|
gi 24646383    97 AYAGSWTEWQ 106
Cdd:pfam00581  83 VLDGGFEAWK 92
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 6-106 1.26e-07

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: 45.37  E-value: 1.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646383   6 EVKDIPNHPEKYLFDVRNESELKEtGVLPASINIPLSELEKALNLPEEDFAQTYgrvkpavdavlIFSCKAGGRAARAAN 85
Cdd:cd00158   1 ELKELLDDEDAVLLDVREPEEYAA-GHIPGAINIPLSELEERAALLELDKDKPI-----------VVYCRSGNRSARAAK 68

                        90       100
                ....*....|....*....|.
gi 24646383  86 LASTLGFTNAKAYAGSWTEWQ 106
Cdd:cd00158  69 LLRKAGGTNVYNLEGGMLAWK 89
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 1-105 2.20e-07

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 47.09  E-value: 2.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646383   1 MATYEEVKDIPNHPEKYLFDVRNESE---LKETGVL-----PASINIPLSEL--EKALNLPEEDFAQTYGRVKPAVDAVL 70
Cdd:COG2897 139 LADADEVLAALGDPDAVLVDARSPERyrgEVEPIDPraghiPGAVNLPWTDLldEDGTFKSAEELRALFAALGIDPDKPV 218

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 24646383  71 IFSCkaggraaraaN---LAST-------LGFTNAKAYAGSWTEW 105
Cdd:COG2897 219 ITYC----------GsgvRAAHtwlalelLGYPNVRLYDGSWSEW 253
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 15-49 1.02e-05

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: 40.71  E-value: 1.02e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 24646383  15 EKYLFDVRNESELkETGVLPASINIPLSELEKALN 49
Cdd:cd01524  13 GVTLIDVRTPQEF-EKGHIKGAINIPLDELRDRLN 46
PRK09629 PRK09629
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
 31-105 2.29e-04

bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional


Pssm-ID: 104071 [Multi-domain]  Cd Length: 610  Bit Score: 38.95  E-value: 2.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24646383   31 GVLPASINIPLSE-LEKALNLP-EEDFAQTYGRVKPAVDAVLIFSCKAGGRAARAANLASTLGFTNAKAYAGSWTEW 105
Cdd:PRK09629 185 GHIPGAVNFEWTAgMDKARNLRiRQDMPEILRDLGITPDKEVITHCQTHHRSGFTYLVAKALGYPRVKAYAGSWGEW 261
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 6-107 1.61e-03

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 36.39  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646383    6 EVKDIPnhPEKYLFDVRNESELKEtGVLPASINIPLSELEKALNLPeedfaqtygRVKPAVDAVLIfsCKAGGRAARAAN 85
Cdd:PRK05597 267 RVSALP--DGVTLIDVREPSEFAA-YSIPGAHNVPLSAIREGANPP---------SVSAGDEVVVY--CAAGVRSAQAVA 332

                         90       100
                 ....*....|....*....|..
gi 24646383   86 LASTLGFTNAKAYAGSWTEWQA 107
Cdd:PRK05597 333 ILERAGYTGMSSLDGGIEGWLD 354
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 14-95 2.88e-03

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: 34.61  E-value: 2.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646383  14 PEKYLFDVRNESELKETGVLPASINIPLSELekaLNL-PEEDF-AQTYGRVKPavDAVLIFSCKAGGRAARAANLASTLG 91
Cdd:cd01522  14 PQAVLVDVRTEAEWKFVGGVPDAVHVAWQVY---PDMeINPNFlAELEEKVGK--DRPVLLLCRSGNRSIAAAEAAAQAG 88


                ....
gi 24646383  92 FTNA 95
Cdd:cd01522  89 FTNV 92
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 5-45 3.88e-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: 34.21  E-value: 3.88e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24646383   5 EEVKDIPNHPEKYLF-DVRnESELKETGVLPASINIPLSELE 45
Cdd:cd01526  13 KDYKNILQAGKKHVLlDVR-PKVHFEICRLPEAINIPLSELL 53
 
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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