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Conserved domains on  [gi|503110436|ref|WP_013345178|]
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rhodanese-like domain-containing protein [Ferrimonas balearica]

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]; ...
 36-140 2.42e-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: 84.63  E-value: 2.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503110436  36 EINYMSLAQAEQRLGHPGVRFYDVNVLEIWADGYIPGAIHFFVDNWKDLLPE-DKGTEMIFYCANRlcNASEIAAHAVKA 114
Cdd:COG0607    2 SVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDElPKDKPIVVYCASG--GRSAQAAALLRR 79

                         90       100
                 ....*....|....*....|....*.
gi 503110436 115 MGYTNVSQMPDGIFGWKMSGRAVEKP 140
Cdd:COG0607   80 AGYTNVYNLAGGIEAWKAAGLPVEKG 105
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 36-140 2.42e-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: 84.63  E-value: 2.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503110436  36 EINYMSLAQAEQRLGHPGVRFYDVNVLEIWADGYIPGAIHFFVDNWKDLLPE-DKGTEMIFYCANRlcNASEIAAHAVKA 114
Cdd:COG0607    2 SVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDElPKDKPIVVYCASG--GRSAQAAALLRR 79

                         90       100
                 ....*....|....*....|....*.
gi 503110436 115 MGYTNVSQMPDGIFGWKMSGRAVEKP 140
Cdd:COG0607   80 AGYTNVYNLAGGIEAWKAAGLPVEKG 105
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 44-131 1.55e-13

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: 61.93  E-value: 1.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503110436  44 QAEQRLGHPGVRFYDVNVLEIWADGYIPGAIHFFVDNWKD---LLPEDKGTEMIFYCANrlCNASEIAAHAVKAMGYTNV 120
Cdd:cd00158    1 ELKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEEraaLLELDKDKPIVVYCRS--GNRSARAAKLLRKAGGTNV 78

                         90
                 ....*....|.
gi 503110436 121 SQMPDGIFGWK 131
Cdd:cd00158   79 YNLEGGMLAWK 89
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
36-140 5.13e-13

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 64.65  E-value: 5.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503110436  36 EINYMSLAQAEQRLGHpGVRFYDVNVLEIWADGYIPGAIHffVD-NWKDLLPE----DKGTEMIFYCA--NRlcnaSEIA 108
Cdd:PRK08762   1 SIREISPAEARARAAQ-GAVLIDVREAHERASGQAEGALR--IPrGFLELRIEthlpDRDREIVLICAsgTR----SAHA 73

                         90       100       110
                 ....*....|....*....|....*....|..
gi 503110436 109 AHAVKAMGYTNVSQMPDGIFGWKMSGRAVEKP 140
Cdd:PRK08762  74 AATLRELGYTRVASVAGGFSAWKDAGLPLERP 105
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 65-131 2.91e-10

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: 53.26  E-value: 2.91e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503110436   65 WADGYIPGAIHF-----------FVDNWKDLLPEDKGTEMIFYCANRlcNASEIAAHAVKAMGYTNVSQMPDGIFGWK 131
Cdd:pfam00581  17 YAKGHIPGAVNVplsslslpplpLLELLEKLLELLKDKPIVVYCNSG--NRAAAAAALLKALGYKNVYVLDGGFEAWK 92
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 50-136 2.31e-06

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: 43.22  E-value: 2.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503110436    50 GHPGVRFYDVNVLEIWADGYIPGAIHFFVDNWKDLLPE---------------DKGTEMIFYC--ANRlcnaSEIAAHAV 112
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGEldilefeellkrlglDKDKPVVVYCrsGNR----SAKAAWLL 76

                           90       100
                   ....*....|....*....|....
gi 503110436   113 KAMGYTNVSQMPDGIFGWKMSGRA 136
Cdd:smart00450  77 RELGFKNVYLLDGGYKEWSAAGPP 100
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 36-140 2.42e-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: 84.63  E-value: 2.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503110436  36 EINYMSLAQAEQRLGHPGVRFYDVNVLEIWADGYIPGAIHFFVDNWKDLLPE-DKGTEMIFYCANRlcNASEIAAHAVKA 114
Cdd:COG0607    2 SVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDElPKDKPIVVYCASG--GRSAQAAALLRR 79

                         90       100
                 ....*....|....*....|....*.
gi 503110436 115 MGYTNVSQMPDGIFGWKMSGRAVEKP 140
Cdd:COG0607   80 AGYTNVYNLAGGIEAWKAAGLPVEKG 105
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 44-131 1.55e-13

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: 61.93  E-value: 1.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503110436  44 QAEQRLGHPGVRFYDVNVLEIWADGYIPGAIHFFVDNWKD---LLPEDKGTEMIFYCANrlCNASEIAAHAVKAMGYTNV 120
Cdd:cd00158    1 ELKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEEraaLLELDKDKPIVVYCRS--GNRSARAAKLLRKAGGTNV 78

                         90
                 ....*....|.
gi 503110436 121 SQMPDGIFGWK 131
Cdd:cd00158   79 YNLEGGMLAWK 89
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
36-140 5.13e-13

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 64.65  E-value: 5.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503110436  36 EINYMSLAQAEQRLGHpGVRFYDVNVLEIWADGYIPGAIHffVD-NWKDLLPE----DKGTEMIFYCA--NRlcnaSEIA 108
Cdd:PRK08762   1 SIREISPAEARARAAQ-GAVLIDVREAHERASGQAEGALR--IPrGFLELRIEthlpDRDREIVLICAsgTR----SAHA 73

                         90       100       110
                 ....*....|....*....|....*....|..
gi 503110436 109 AHAVKAMGYTNVSQMPDGIFGWKMSGRAVEKP 140
Cdd:PRK08762  74 AATLRELGYTRVASVAGGFSAWKDAGLPLERP 105
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 65-131 2.91e-10

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: 53.26  E-value: 2.91e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503110436   65 WADGYIPGAIHF-----------FVDNWKDLLPEDKGTEMIFYCANRlcNASEIAAHAVKAMGYTNVSQMPDGIFGWK 131
Cdd:pfam00581  17 YAKGHIPGAVNVplsslslpplpLLELLEKLLELLKDKPIVVYCNSG--NRAAAAAALLKALGYKNVYVLDGGFEAWK 92
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 50-137 4.21e-08

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: 48.12  E-value: 4.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503110436  50 GHPGVRFYDVNVLEIWADGYIPGAIH-----FFVDNWKDLlpeDKGTEMIFYCANRLCNASEIAAHAVKAMGYtNVSQMP 124
Cdd:cd01521   22 GKPDFVLVDVRSAEAYARGHVPGAINlphreICENATAKL---DKEKLFVVYCDGPGCNGATKAALKLAELGF-PVKEMI 97

                         90
                 ....*....|...
gi 503110436 125 DGIFGWKMSGRAV 137
Cdd:cd01521   98 GGLDWWKREGYAT 110
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 40-134 3.36e-07

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: 45.49  E-value: 3.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503110436  40 MSLAQAEQRLGHPGVRFYDV-NVLEIWADGYIPGAIH-------FFVD----NWKDLLPEDKgtEMIFYCANRLcnASEI 107
Cdd:cd01447    1 LSPEDARALLGSPGVLLVDVrDPRELERTGMIPGAFHaprgmleFWADpdspYHKPAFAEDK--PFVFYCASGW--RSAL 76

                         90       100
                 ....*....|....*....|....*..
gi 503110436 108 AAHAVKAMGYTNVSQMPDGIFGWKMSG 134
Cdd:cd01447   77 AGKTLQDMGLKPVYNIEGGFKDWKEAG 103
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 50-136 2.31e-06

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: 43.22  E-value: 2.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503110436    50 GHPGVRFYDVNVLEIWADGYIPGAIHFFVDNWKDLLPE---------------DKGTEMIFYC--ANRlcnaSEIAAHAV 112
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGEldilefeellkrlglDKDKPVVVYCrsGNR----SAKAAWLL 76

                           90       100
                   ....*....|....*....|....
gi 503110436   113 KAMGYTNVSQMPDGIFGWKMSGRA 136
Cdd:smart00450  77 RELGFKNVYLLDGGYKEWSAAGPP 100
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 42-130 3.07e-05

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: 40.35  E-value: 3.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503110436  42 LAQAEQRLGHPGVRFYDVNVLEIWADGYIPGAIHFFVDNW-------KDLLPEDKGTEMIFYCANRLcnASEIAAHAVKA 114
Cdd:cd01529    1 LLADWLGEHEPGTALLDVRAEDEYAAGHLPGKRSIPGAALvlrsqelQALEAPGRATRYVLTCDGSL--LARFAAQELLA 78

                         90
                 ....*....|....*.
gi 503110436 115 MGYTNVSQMPDGIFGW 130
Cdd:cd01529   79 LGGKPVALLDGGTSAW 94
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 52-130 1.24e-04

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 40.63  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503110436  52 PGVRFYDVNVLEIWADGYIPGAIHFFVDNWK-DLLPE--DKGTEMIFYCANRLCNASEIAAhaVKAMGYTNVSQMPDGIF 128
Cdd:PRK05597 273 DGVTLIDVREPSEFAAYSIPGAHNVPLSAIReGANPPsvSAGDEVVVYCAAGVRSAQAVAI--LERAGYTGMSSLDGGIE 350


                 ..
gi 503110436 129 GW 130
Cdd:PRK05597 351 GW 352
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 40-132 2.06e-04

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: 38.01  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503110436  40 MSLAQAEQRLGHPG-VRFYDVNVLEIWAD--GYIPGAIHFFVDNWKDLLPE-DKGTEMIFYCANRlcNASEIAAHAVKAM 115
Cdd:cd01444    2 ISVDELAELLAAGEaPVLLDVRDPASYAAlpDHIPGAIHLDEDSLDDWLGDlDRDRPVVVYCYHG--NSSAQLAQALREA 79

                         90
                 ....*....|....*..
gi 503110436 116 GYTNVSQMPDGIFGWKM 132
Cdd:cd01444   80 GFTDVRSLAGGFEAWRR 96
 
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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