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Conserved domains on  [gi|446181408|ref|WP_000259263|]
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rhodanese-like domain-containing protein [Streptococcus pneumoniae]

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]; ...
 27-120 1.22e-24

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: 90.03  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408  27 AAKIVDNKEFEALIRTG--QLIDLRDPAEFHRKHILGARNIPSSQLKTSLAALRKDKPVLLY--ENQRAQRvtnAALYLK 102
Cdd:COG0607    2 SVKEISPAELAELLESEdaVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYcaSGGRSAQ---AAALLR 78

                         90
                 ....*....|....*...
gi 446181408 103 KQGFSEIYILSYGLDSWK 120
Cdd:COG0607   79 RAGYTNVYNLAGGIEAWK 96
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 27-120 1.22e-24

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: 90.03  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408  27 AAKIVDNKEFEALIRTG--QLIDLRDPAEFHRKHILGARNIPSSQLKTSLAALRKDKPVLLY--ENQRAQRvtnAALYLK 102
Cdd:COG0607    2 SVKEISPAELAELLESEdaVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYcaSGGRSAQ---AAALLR 78

                         90
                 ....*....|....*...
gi 446181408 103 KQGFSEIYILSYGLDSWK 120
Cdd:COG0607   79 RAGYTNVYNLAGGIEAWK 96
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 35-120 2.73e-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: 78.50  E-value: 2.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408  35 EFEALIRTG--QLIDLRDPAEFHRKHILGARNIPSSQLKT--SLAALRKDKPVLLYEnQRAQRVTNAALYLKKQGFSEIY 110
Cdd:cd00158    1 ELKELLDDEdaVLLDVREPEEYAAGHIPGAINIPLSELEEraALLELDKDKPIVVYC-RSGNRSARAAKLLRKAGGTNVY 79

                         90
                 ....*....|
gi 446181408 111 ILSYGLDSWK 120
Cdd:cd00158   80 NLEGGMLAWK 89
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 44-120 2.48e-15

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: 2.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408   44 QLIDLRDPAEFHRKHILGARNIPSS----------QLKTSLAALRKDKPVLLYENQRaQRVTNAALYLKKQGFSEIYILS 113
Cdd:pfam00581   7 VLIDVRPPEEYAKGHIPGAVNVPLSslslpplpllELLEKLLELLKDKPIVVYCNSG-NRAAAAAALLKALGYKNVYVLD 85


                  ....*..
gi 446181408  114 YGLDSWK 120
Cdd:pfam00581  86 GGFEAWK 92
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 44-120 4.21e-14

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: 63.25  E-value: 4.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408    44 QLIDLRDPAEFHRKHILGARNIPSSQLKTS--------------LAALRKDKPVLLY--ENQRAQRvtnAALYLKKQGFS 107
Cdd:smart00450   6 VLLDVRSPEEYEGGHIPGAVNIPLSELLDRrgeldilefeellkRLGLDKDKPVVVYcrSGNRSAK---AAWLLRELGFK 82

                           90
                   ....*....|...
gi 446181408   108 EIYILSYGLDSWK 120
Cdd:smart00450  83 NVYLLDGGYKEWS 95
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
45-119 5.53e-10

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 52.72  E-value: 5.53e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446181408  45 LIDLRDPAEFHRKHILGARNIPSSQLKTSLAALRKDKPVLL--YENQRAQrvtNAALYLKKQGFSEIYILSYGLDSW 119
Cdd:PRK00162  23 LVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVmcYHGNSSQ---GAAQYLLQQGFDVVYSIDGGFEAW 96
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 27-120 1.22e-24

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: 90.03  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408  27 AAKIVDNKEFEALIRTG--QLIDLRDPAEFHRKHILGARNIPSSQLKTSLAALRKDKPVLLY--ENQRAQRvtnAALYLK 102
Cdd:COG0607    2 SVKEISPAELAELLESEdaVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYcaSGGRSAQ---AAALLR 78

                         90
                 ....*....|....*...
gi 446181408 103 KQGFSEIYILSYGLDSWK 120
Cdd:COG0607   79 RAGYTNVYNLAGGIEAWK 96
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 35-120 2.73e-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: 78.50  E-value: 2.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408  35 EFEALIRTG--QLIDLRDPAEFHRKHILGARNIPSSQLKT--SLAALRKDKPVLLYEnQRAQRVTNAALYLKKQGFSEIY 110
Cdd:cd00158    1 ELKELLDDEdaVLLDVREPEEYAAGHIPGAINIPLSELEEraALLELDKDKPIVVYC-RSGNRSARAAKLLRKAGGTNVY 79

                         90
                 ....*....|
gi 446181408 111 ILSYGLDSWK 120
Cdd:cd00158   80 NLEGGMLAWK 89
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 44-120 2.48e-15

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: 2.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408   44 QLIDLRDPAEFHRKHILGARNIPSS----------QLKTSLAALRKDKPVLLYENQRaQRVTNAALYLKKQGFSEIYILS 113
Cdd:pfam00581   7 VLIDVRPPEEYAKGHIPGAVNVPLSslslpplpllELLEKLLELLKDKPIVVYCNSG-NRAAAAAALLKALGYKNVYVLD 85


                  ....*..
gi 446181408  114 YGLDSWK 120
Cdd:pfam00581  86 GGFEAWK 92
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 44-120 4.21e-14

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: 63.25  E-value: 4.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408    44 QLIDLRDPAEFHRKHILGARNIPSSQLKTS--------------LAALRKDKPVLLY--ENQRAQRvtnAALYLKKQGFS 107
Cdd:smart00450   6 VLLDVRSPEEYEGGHIPGAVNIPLSELLDRrgeldilefeellkRLGLDKDKPVVVYcrSGNRSAK---AAWLLRELGFK 82

                           90
                   ....*....|...
gi 446181408   108 EIYILSYGLDSWK 120
Cdd:smart00450  83 NVYLLDGGYKEWS 95
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 38-120 1.85e-12

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: 58.65  E-value: 1.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408  38 ALIRTGQ-LIDLRDPAEFHRKHILGARNIPSSQL-KTSLAALRKDkpVLLYENQRAQRVTNAALYLKKQGFSEIYILSYG 115
Cdd:cd01527   11 ELLAQGAvLVDIREPDEYLRERIPGARLVPLSQLeSEGLPLVGAN--AIIFHCRSGMRTQQNAERLAAISAGEAYVLEGG 88


                 ....*
gi 446181408 116 LDSWK 120
Cdd:cd01527   89 LDAWK 93
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
45-119 5.53e-10

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 52.72  E-value: 5.53e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446181408  45 LIDLRDPAEFHRKHILGARNIPSSQLKTSLAALRKDKPVLL--YENQRAQrvtNAALYLKKQGFSEIYILSYGLDSW 119
Cdd:PRK00162  23 LVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVmcYHGNSSQ---GAAQYLLQQGFDVVYSIDGGFEAW 96
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 35-120 1.44e-09

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: 51.11  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408  35 EFEALIRTG-QLIDLRDPAEFHRKHILGARNIPSSQLKTSLAALRKDKPVLLYeNQRAQRVTNAALYLKKQGFsEIYILS 113
Cdd:cd01524    5 ELDNYRADGvTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKEIIVY-CAVGLRGYIAARILTQNGF-KVKNLD 82


                 ....*..
gi 446181408 114 YGLDSWK 120
Cdd:cd01524   83 GGYKTYS 89
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 26-119 3.19e-09

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 53.34  E-value: 3.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408  26 RAAKIVDNKEFEALIRTGQLIDLRDPAEFHRKHILGARNIPSSQLKTSLAALRKDKP--VLLYeNQRAQRVTNAALYLKK 103
Cdd:PRK05597 258 GFGEVLDVPRVSALPDGVTLIDVREPSEFAAYSIPGAHNVPLSAIREGANPPSVSAGdeVVVY-CAAGVRSAQAVAILER 336

                         90
                 ....*....|....*.
gi 446181408 104 QGFSEIYILSYGLDSW 119
Cdd:PRK05597 337 AGYTGMSSLDGGIEGW 352
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 34-126 6.64e-09

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 52.40  E-value: 6.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408  34 KEFEALIRTGQ---LIDLRDPAEFHRKHILGARNIPSSQLK--TSLAALRKDKPVLLYeNQRAQRVTNAALYLKKQGFSE 108
Cdd:PRK07878 292 RELKEWLDSGKkiaLIDVREPVEWDIVHIPGAQLIPKSEILsgEALAKLPQDRTIVLY-CKTGVRSAEALAALKKAGFSD 370

                         90
                 ....*....|....*...
gi 446181408 109 IYILSYGLDSWKGKVKTS 126
Cdd:PRK07878 371 AVHLQGGVVAWAKQVDPS 388
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 35-120 8.38e-09

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: 49.18  E-value: 8.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408  35 EFEALIRTG---QLIDLRDPAEFHRK--HILGARNIPSSQLKTSLAALRKDKPVLLY---ENQRAQrvtnAALYLKKQGF 106
Cdd:cd01444    6 ELAELLAAGeapVLLDVRDPASYAALpdHIPGAIHLDEDSLDDWLGDLDRDRPVVVYcyhGNSSAQ----LAQALREAGF 81

                         90
                 ....*....|....
gi 446181408 107 SEIYILSYGLDSWK 120
Cdd:cd01444   82 TDVRSLAGGFEAWR 95
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 31-120 2.26e-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: 48.19  E-value: 2.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408  31 VDNKEFEALIRTGQ--LIDLRDPAEFHRK-HILGARNIPSSQLKTSLA--------ALRKDKPVLLYeNQRAQRVTNAAL 99
Cdd:cd01447    1 LSPEDARALLGSPGvlLVDVRDPRELERTgMIPGAFHAPRGMLEFWADpdspyhkpAFAEDKPFVFY-CASGWRSALAGK 79

                         90       100
                 ....*....|....*....|.
gi 446181408 100 YLKKQGFSEIYILSYGLDSWK 120
Cdd:cd01447   80 TLQDMGLKPVYNIEGGFKDWK 100
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 44-123 8.00e-08

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: 47.00  E-value: 8.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408  44 QLIDLRDPAEFHRKHILGARNIPSSQLKT---SLAALRKDKPVLLYeNQRAQRVTNAALYLKKQGFSEIYILSYGLDSWK 120
Cdd:cd01528   19 VLIDVREPEELEIAFLPGFLHLPMSEIPErskELDSDNPDKDIVVL-CHHGGRSMQVAQWLLRQGFENVYNLQGGIDAWS 97


                 ...
gi 446181408 121 GKV 123
Cdd:cd01528   98 LEV 100
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 44-120 2.04e-07

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: 45.81  E-value: 2.04e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446181408  44 QLIDLRDPAEFHRKHILGARNIPSSQL-KTSLAALRKDKPVLLY-ENQRAQRVTNAALYLKKQGFsEIYILSYGLDSWK 120
Cdd:cd01521   27 VLVDVRSAEAYARGHVPGAINLPHREIcENATAKLDKEKLFVVYcDGPGCNGATKAALKLAELGF-PVKEMIGGLDWWK 104
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 34-123 2.39e-06

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: 43.45  E-value: 2.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408  34 KEFEALIRTGQ---LIDLRDPAEFHRKHILGARNIPSSQLKTSLAALRKDKPVLLYENQRAQ-----RVTN----AALYL 101
Cdd:cd01526   13 KDYKNILQAGKkhvLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKSLQELPLDNDKDSPiyvvcRRGNdsqtAVRKL 92

                         90       100
                 ....*....|....*....|...
gi 446181408 102 KKQGFS-EIYILSYGLDSWKGKV 123
Cdd:cd01526   93 KELGLErFVRDIIGGLKAWADKV 115
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 41-119 8.15e-06

Member of the Rhodanese Homology Domain superfamily. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. Only the second and most of the fourth repeats contain the putative catalytic Cys residue. This CD aligns the 1st , 2nd, 3rd, and 4th repeats.


Pssm-ID: 238787 [Multi-domain]  Cd Length: 96  Bit Score: 41.51  E-value: 8.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408  41 RTGQLIDLRDPAEFHRKHILGARNIP------SSQLKTSLAALRKDKPVLLYENQRAqRVTNAALYLKKQGFSEIYILSY 114
Cdd:cd01529   11 PGTALLDVRAEDEYAAGHLPGKRSIPgaalvlRSQELQALEAPGRATRYVLTCDGSL-LARFAAQELLALGGKPVALLDG 89


                 ....*
gi 446181408 115 GLDSW 119
Cdd:cd01529   90 GTSAW 94
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 29-120 9.42e-06

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: 41.63  E-value: 9.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408  29 KIVDNKEFEALIRTG----QLIDLRDpAEFHRKHILGARNIPSSQLKTSLAALRKDKP------VLLYENQRAQRVTNAA 98
Cdd:cd01531    2 SYISPAQLKGWIRNGrppfQVVDVRD-EDYAGGHIKGSWHYPSTRFKAQLNQLVQLLSgskkdtVVFHCALSQVRGPSAA 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 446181408  99 L----YLK----KQGFSEIYILSYGLDSWK 120
Cdd:cd01531   81 RkflrYLDeedlETSKFEVYVLHGGFNAWE 110
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 45-120 1.70e-05

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: 40.55  E-value: 1.70e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446181408  45 LIDLRDPAEFHRKHILGARNIPSSQLKTSLAAL--RKDKPVLLYENQRAQRVT-NAALYLKKQGFSEIYILSYGLDSWK 120
Cdd:cd01532   13 LIDVREEDPFAQSHPLWAANLPLSRLELDAWVRipRRDTPIVVYGEGGGEDLApRAARRLSELGYTDVALLEGGLQGWR 91
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 41-119 3.09e-05

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: 39.76  E-value: 3.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446181408  41 RTGQLIDLRDPAEFHRKHILGARNIPSSQL--KTSLAALRKDKPVLLYENQRAqRVTNAALYLKKQGFsEIYILSYGLDS 118
Cdd:cd01534   15 RTVYRFDVRTPEEYEAGHLPGFRHTPGGQLvqETDHFAPVRGARIVLADDDGV-RADMTASWLAQMGW-EVYVLEGGLAA 92


                 .
gi 446181408 119 W 119
Cdd:cd01534   93 A 93
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 46-92 4.22e-05

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 39.83  E-value: 4.22e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 446181408  46 IDLRDPAEFHRKHILGARNIPSSQLKTSLAALRKDK--PVLLYENQRAQ 92
Cdd:PRK10287  24 IDVRVPEQYQQEHVQGAINIPLKEVKERIATAVPDKndTVKLYCNAGRQ 72
RHOD_YbbB cd01520
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ...
 35-66 5.25e-04

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: 37.27  E-value: 5.25e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 446181408  35 EFEALIRT-GQLIDLRDPAEFHRKHILGARNIP 66
Cdd:cd01520    5 DLLALRKAdGPLIDVRSPKEFFEGHLPGAINLP 37
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 35-66 6.88e-04

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 37.89  E-value: 6.88e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 446181408  35 EFEAL-IRTGQLIDLRDPAEFHRKHILGARNIP 66
Cdd:PRK11784   7 DFRALfLNDTPLIDVRSPIEFAEGHIPGAINLP 39
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 45-109 7.79e-04

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: 36.48  E-value: 7.79e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446181408  45 LIDLRDPAEFHRKHILGARNIPSSQLKTSLA----ALRK---------DKPVLLYeNQRAQRVTNAALYLKKQGFSEI 109
Cdd:cd01519   18 LIDVREPEELKTGKIPGAINIPLSSLPDALAlseeEFEKkygfpkpskDKELIFY-CKAGVRSKAAAELARSLGYENV 94
 
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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