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Conserved domains on  [gi|502661429|ref|WP_012897463|]
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MULTISPECIES: rhodanese-like domain-containing protein [Lactococcus]

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]; ...
 7-97 6.31e-36

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: 117.76  E-value: 6.31e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429   7 KIKSISPAEVSTELK-KGTQLIDVREAHEFQNGHIKGARNIPLSKLGEHV--LAKNKKYLLICQSGMRSKKAYKILNKAN 83
Cdd:COG0607    2 SVKEISPAELAELLEsEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLdeLPKDKPIVVYCASGGRSAQAAALLRRAG 81

                         90
                 ....*....|....*
gi 502661429  84 YD-VTNVNGGMRAWR 97
Cdd:COG0607   82 YTnVYNLAGGIEAWK 96
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 7-97 6.31e-36

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: 117.76  E-value: 6.31e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429   7 KIKSISPAEVSTELK-KGTQLIDVREAHEFQNGHIKGARNIPLSKLGEHV--LAKNKKYLLICQSGMRSKKAYKILNKAN 83
Cdd:COG0607    2 SVKEISPAELAELLEsEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLdeLPKDKPIVVYCASGGRSAQAAALLRRAG 81

                         90
                 ....*....|....*
gi 502661429  84 YD-VTNVNGGMRAWR 97
Cdd:COG0607   82 YTnVYNLAGGIEAWK 96
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 21-97 1.34e-29

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: 101.22  E-value: 1.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429  21 KKGTQLIDVREAHEFQNGHIKGARNIPLSKLGEHV----LAKNKKYLLICQSGMRSKKAYKILNKANY-DVTNVNGGMRA 95
Cdd:cd00158    8 DEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAalleLDKDKPIVVYCRSGNRSARAAKLLRKAGGtNVYNLEGGMLA 87


                 ..
gi 502661429  96 WR 97
Cdd:cd00158   88 WK 89
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
8-97 3.48e-22

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 88.53  E-value: 3.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429   8 IKSISPAEVSTELKKGTQLIDVREAHEFQNGHIKGARNIPLSKL----GEHVLAKNKKYLLICQSGMRSKKAYKILNKAN 83
Cdd:PRK08762   2 IREISPAEARARAAQGAVLIDVREAHERASGQAEGALRIPRGFLelriETHLPDRDREIVLICASGTRSAHAAATLRELG 81

                         90
                 ....*....|....*
gi 502661429  84 Y-DVTNVNGGMRAWR 97
Cdd:PRK08762  82 YtRVASVAGGFSAWK 96
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 21-96 1.01e-20

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: 78.68  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429   21 KKGTQLIDVREAHEFQNGHIKGARNIPLSKLGEHV------------LAKNKKYLLICQSGMRSKKAYKILNKANY-DVT 87
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPlpllelleklleLLKDKPIVVYCNSGNRAAAAAALLKALGYkNVY 82


                  ....*....
gi 502661429   88 NVNGGMRAW 96
Cdd:pfam00581  83 VLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 21-97 1.27e-19

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: 76.34  E-value: 1.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429    21 KKGTQLIDVREAHEFQNGHIKGARNIPLSKL----------------GEHVLAKNKKYLLICQSGMRSKKAYKILNKANY 84
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELldrrgeldilefeellKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81

                           90
                   ....*....|....
gi 502661429    85 -DVTNVNGGMRAWR 97
Cdd:smart00450  82 kNVYLLDGGYKEWS 95
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 22-97 2.15e-09

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: 52.60  E-value: 2.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429   22 KGTQLIDVREAHEFQNGHIKGARNIPL------------------------------SKLGEHV-----LAKNKKYLLIC 66
Cdd:TIGR03167   1 AFDPLIDVRSPAEFAEGHLPGAINLPLlndeeraevgtlykqvgpfaaiklglalvsPNLAAHVeqwraFADGPPQPLLY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 502661429   67 --QSGMRSKKAYKILNKANYDVTNVNGGMRAWR 97
Cdd:TIGR03167  81 cwRGGMRSGSLAWLLAQIGFRVPRLEGGYKAYR 113
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 7-97 6.31e-36

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: 117.76  E-value: 6.31e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429   7 KIKSISPAEVSTELK-KGTQLIDVREAHEFQNGHIKGARNIPLSKLGEHV--LAKNKKYLLICQSGMRSKKAYKILNKAN 83
Cdd:COG0607    2 SVKEISPAELAELLEsEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLdeLPKDKPIVVYCASGGRSAQAAALLRRAG 81

                         90
                 ....*....|....*
gi 502661429  84 YD-VTNVNGGMRAWR 97
Cdd:COG0607   82 YTnVYNLAGGIEAWK 96
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 21-97 1.34e-29

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: 101.22  E-value: 1.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429  21 KKGTQLIDVREAHEFQNGHIKGARNIPLSKLGEHV----LAKNKKYLLICQSGMRSKKAYKILNKANY-DVTNVNGGMRA 95
Cdd:cd00158    8 DEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAalleLDKDKPIVVYCRSGNRSARAAKLLRKAGGtNVYNLEGGMLA 87


                 ..
gi 502661429  96 WR 97
Cdd:cd00158   88 WK 89
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 11-96 4.16e-23

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: 84.63  E-value: 4.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429  11 ISPAEVSTELKKGTQLIDVREAHEFQNGHIKGARNIPLSKLGEHV--LAKNKKYLLICQSGMRSKKAYKILNKANYDVTN 88
Cdd:cd01524    1 VQWHELDNYRADGVTLIDVRTPQEFEKGHIKGAINIPLDELRDRLneLPKDKEIIVYCAVGLRGYIAARILTQNGFKVKN 80


                 ....*...
gi 502661429  89 VNGGMRAW 96
Cdd:cd01524   81 LDGGYKTY 88
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
8-97 3.48e-22

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 88.53  E-value: 3.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429   8 IKSISPAEVSTELKKGTQLIDVREAHEFQNGHIKGARNIPLSKL----GEHVLAKNKKYLLICQSGMRSKKAYKILNKAN 83
Cdd:PRK08762   2 IREISPAEARARAAQGAVLIDVREAHERASGQAEGALRIPRGFLelriETHLPDRDREIVLICASGTRSAHAAATLRELG 81

                         90
                 ....*....|....*
gi 502661429  84 Y-DVTNVNGGMRAWR 97
Cdd:PRK08762  82 YtRVASVAGGFSAWK 96
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 21-96 1.01e-20

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: 78.68  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429   21 KKGTQLIDVREAHEFQNGHIKGARNIPLSKLGEHV------------LAKNKKYLLICQSGMRSKKAYKILNKANY-DVT 87
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPlpllelleklleLLKDKPIVVYCNSGNRAAAAAALLKALGYkNVY 82


                  ....*....
gi 502661429   88 NVNGGMRAW 96
Cdd:pfam00581  83 VLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 21-97 1.27e-19

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: 76.34  E-value: 1.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429    21 KKGTQLIDVREAHEFQNGHIKGARNIPLSKL----------------GEHVLAKNKKYLLICQSGMRSKKAYKILNKANY 84
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELldrrgeldilefeellKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81

                           90
                   ....*....|....
gi 502661429    85 -DVTNVNGGMRAWR 97
Cdd:smart00450  82 kNVYLLDGGYKEWS 95
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 18-97 1.02e-15

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 70.67  E-value: 1.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429  18 TELKKGTQLIDVREAHEFQNGHIKGARNIPLSK-LGEHV---LAKNKKYLLICQSGMRSKKAYKILNKANY-DVTNVNGG 92
Cdd:PRK05597 269 SALPDGVTLIDVREPSEFAAYSIPGAHNVPLSAiREGANppsVSAGDEVVVYCAAGVRSAQAVAILERAGYtGMSSLDGG 348


                 ....*
gi 502661429  93 MRAWR 97
Cdd:PRK05597 349 IEGWL 353
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 8-97 4.26e-15

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: 64.81  E-value: 4.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429   8 IKSISPAEVSTELKKGTQLIDVREAHEFQNGHIKGARNIPLSKLGEHVLAKNKKYLLI--CQSGMRSKKAYKILNK-ANY 84
Cdd:cd01527    1 LTTISPNDACELLAQGAVLVDIREPDEYLRERIPGARLVPLSQLESEGLPLVGANAIIfhCRSGMRTQQNAERLAAiSAG 80

                         90
                 ....*....|...
gi 502661429  85 DVTNVNGGMRAWR 97
Cdd:cd01527   81 EAYVLEGGLDAWK 93
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 11-100 1.36e-14

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: 63.87  E-value: 1.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429  11 ISPAEVSTELKKGTQ--LIDVREAHEFQNGHIKGARNIPLSKL----GEHVLA--------KNKKYLLICQSGMRSKKAY 76
Cdd:cd01526   10 VSVKDYKNILQAGKKhvLLDVRPKVHFEICRLPEAINIPLSELlskaAELKSLqelpldndKDSPIYVVCRRGNDSQTAV 89

                         90       100
                 ....*....|....*....|....*.
gi 502661429  77 KILNKANY--DVTNVNGGMRAWRGKI 100
Cdd:cd01526   90 RKLKELGLerFVRDIIGGLKAWADKV 115
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 10-96 1.44e-14

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 67.43  E-value: 1.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429  10 SISPAEVSTELKKGT--QLIDVREAHEFQNGHIKGARNIPLSKL--GEHV--LAKNKKYLLICQSGMRSKKAYKILNKAN 83
Cdd:PRK07878 288 TITPRELKEWLDSGKkiALIDVREPVEWDIVHIPGAQLIPKSEIlsGEALakLPQDRTIVLYCKTGVRSAEALAALKKAG 367

                         90
                 ....*....|....
gi 502661429  84 Y-DVTNVNGGMRAW 96
Cdd:PRK07878 368 FsDAVHLQGGVVAW 381
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 26-96 9.10e-14

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: 61.52  E-value: 9.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429  26 LIDVREAHEFQNGHIKGARNIPLSKL---------------GEHVLAKNKKYLLICQSGMRSKKAYKILNKANY-DVTNV 89
Cdd:cd01519   18 LIDVREPEELKTGKIPGAINIPLSSLpdalalseeefekkyGFPKPSKDKELIFYCKAGVRSKAAAELARSLGYeNVGNY 97


                 ....*..
gi 502661429  90 NGGMRAW 96
Cdd:cd01519   98 PGSWLDW 104
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
7-96 8.75e-13

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 62.44  E-value: 8.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429   7 KIKSISPAEVSTELKKGTQ---LIDVREAHEFQNGHIKGARNIPLSKL--GEHV-----LAKNKKYLLICQSGMRSKKAY 76
Cdd:PRK07411 280 EIPEMTVTELKALLDSGADdfvLIDVRNPNEYEIARIPGSVLVPLPDIenGPGVekvkeLLNGHRLIAHCKMGGRSAKAL 359

                         90       100
                 ....*....|....*....|
gi 502661429  77 KILNKANYDVTNVNGGMRAW 96
Cdd:PRK07411 360 GILKEAGIEGTNVKGGITAW 379
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 11-100 1.52e-12

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: 58.17  E-value: 1.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429  11 ISPAEVSTELKKG---TQLIDVREAHEFQNGHIKGARNIPLSKLGEHV-----LAKNKKYLLICQSGMRSKKAYKILNKA 82
Cdd:cd01528    2 ISVAELAEWLADEreePVLIDVREPEELEIAFLPGFLHLPMSEIPERSkeldsDNPDKDIVVLCHHGGRSMQVAQWLLRQ 81

                         90
                 ....*....|....*....
gi 502661429  83 NYD-VTNVNGGMRAWRGKI 100
Cdd:cd01528   82 GFEnVYNLQGGIDAWSLEV 100
PLN02160 PLN02160
thiosulfate sulfurtransferase
 6-98 2.17e-10

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 53.55  E-value: 2.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429   6 KKIKSISPAEVSTELKKGTQLIDVREAHEFQNGHIKGAR--NIPLSKLGEHVLAKNKKYL-------------LI-CQSG 69
Cdd:PLN02160  12 EEVVSVDVSQAKTLLQSGHQYLDVRTQDEFRRGHCEAAKivNIPYMLNTPQGRVKNQEFLeqvssllnpaddiLVgCQSG 91

                         90       100       110
                 ....*....|....*....|....*....|
gi 502661429  70 MRSKKAYKILNKANY-DVTNVNGGMRAWRG 98
Cdd:PLN02160  92 ARSLKATTELVAAGYkKVRNKGGGYLAWVD 121
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 22-97 1.19e-09

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 53.29  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429  22 KGTQLIDVREAHEFQNGHIKGARNIPL------------------------------SKLGEHVLA-------KNKKYLL 64
Cdd:PRK11784  14 NDTPLIDVRSPIEFAEGHIPGAINLPLlndeeraevgtcykqqgqfaaialghalvaGNIAAHREEawadfprANPRGLL 93

                         90       100       110
                 ....*....|....*....|....*....|....
gi 502661429  65 IC-QSGMRSKKAYKILNKANYDVTNVNGGMRAWR 97
Cdd:PRK11784  94 YCwRGGLRSGSVQQWLKEAGIDVPRLEGGYKAYR 127
RHOD_YbbB cd01520
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ...
 20-98 1.21e-09

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: 51.53  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429  20 LKKGTQLIDVREAHEFQNGHIKGARNIPL-------------------------------------SKLGEHVLAKNKKY 62
Cdd:cd01520   10 RKADGPLIDVRSPKEFFEGHLPGAINLPLlddeeralvgtlykqqgreaaielglelvsgklkrilNEAWEARLERDPKL 89

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 502661429  63 LLIC-QSGMRSKKAYKILNKANYDVTNVNGGMRAWRG 98
Cdd:cd01520   90 LIYCaRGGMRSQSLAWLLESLGIDVPLLEGGYKAYRK 126
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 22-97 2.15e-09

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: 52.60  E-value: 2.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429   22 KGTQLIDVREAHEFQNGHIKGARNIPL------------------------------SKLGEHV-----LAKNKKYLLIC 66
Cdd:TIGR03167   1 AFDPLIDVRSPAEFAEGHLPGAINLPLlndeeraevgtlykqvgpfaaiklglalvsPNLAAHVeqwraFADGPPQPLLY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 502661429   67 --QSGMRSKKAYKILNKANYDVTNVNGGMRAWR 97
Cdd:TIGR03167  81 cwRGGMRSGSLAWLLAQIGFRVPRLEGGYKAYR 113
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 11-97 4.70e-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: 4.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429  11 ISPAEVSTELKKGT--QLIDVREAHEFQN--GHIKGARNIPLSKLGEHV--LAKNKKYLLICQSGMRSKKAYKILNKANY 84
Cdd:cd01444    2 ISVDELAELLAAGEapVLLDVRDPASYAAlpDHIPGAIHLDEDSLDDWLgdLDRDRPVVVYCYHGNSSAQLAQALREAGF 81

                         90
                 ....*....|....
gi 502661429  85 -DVTNVNGGMRAWR 97
Cdd:cd01444   82 tDVRSLAGGFEAWR 95
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 11-96 1.92e-08

Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with rhodanese-like domains found N-terminal of the metallo-beta-lactamase domain.


Pssm-ID: 238781 [Multi-domain]  Cd Length: 100  Bit Score: 47.87  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429  11 ISPAEVSTELKKGTQL--IDVREAHEFQNGHIKGARNIPLSKLGEHVLA----------KNKKYLLICQSGMRSKKAYKI 78
Cdd:cd01523    1 LDPEDLYARLLAGQPLfiLDVRNESDYERWKIDGENNTPYFDPYFDFLEieedildqlpDDQEVTVICAKEGSSQFVAEL 80

                         90
                 ....*....|....*...
gi 502661429  79 LNKANYDVTNVNGGMRAW 96
Cdd:cd01523   81 LAERGYDVDYLAGGMKAW 98
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 27-102 5.83e-08

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 46.38  E-value: 5.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429  27 IDVREAHEFQNGHIKGARNIPLSKLGEH----VLAKNKKYLLICQSGMRSKKAYKILNKANY-DVTNVNGGMRAWRGKIK 101
Cdd:PRK10287  24 IDVRVPEQYQQEHVQGAINIPLKEVKERiataVPDKNDTVKLYCNAGRQSGQAKEILSEMGYtHAENAGGLKDIAMPKVK 103


                 .
gi 502661429 102 K 102
Cdd:PRK10287 104 G 104
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
1-97 1.96e-07

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 45.40  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429   1 MFEFfkkiKSISPAEVSTELK-KGTQLIDVREAHEFQNGHIKGARNIPLSKLGEHVLAKN--KKYLLICQSGMRSKKA-- 75
Cdd:PRK00162   1 MDQF----ECINVEQAHQKLQeGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADfdTPVMVMCYHGNSSQGAaq 76

                         90       100
                 ....*....|....*....|..
gi 502661429  76 YkILNKANYDVTNVNGGMRAWR 97
Cdd:PRK00162  77 Y-LLQQGFDVVYSIDGGFEAWR 97
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 11-97 2.03e-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: 45.42  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429  11 ISPAEVSTELKKGTQ---LIDVREAHEFQNGHIKGARNIPLSKLGEHVLA---KNKKYLLICQS---GMRSKKAYKiLNK 81
Cdd:cd01521   10 TDCWDVAIALKNGKPdfvLVDVRSAEAYARGHVPGAINLPHREICENATAkldKEKLFVVYCDGpgcNGATKAALK-LAE 88

                         90
                 ....*....|....*.
gi 502661429  82 ANYDVTNVNGGMRAWR 97
Cdd:cd01521   89 LGFPVKEMIGGLDWWK 104
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 19-97 2.47e-07

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


Pssm-ID: 238787 [Multi-domain]  Cd Length: 96  Bit Score: 44.59  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429  19 ELKKGTQLIDVREAHEFQNGHIKGARNIP--------LSKLGEHVLAKNKKYLLICQSGMRSKKAYKILNKANY-DVTNV 89
Cdd:cd01529    8 EHEPGTALLDVRAEDEYAAGHLPGKRSIPgaalvlrsQELQALEAPGRATRYVLTCDGSLLARFAAQELLALGGkPVALL 87


                 ....*...
gi 502661429  90 NGGMRAWR 97
Cdd:cd01529   88 DGGTSAWV 95
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 26-92 7.67e-05

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: 38.46  E-value: 7.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429  26 LIDVR--EAHEFQnGHIKGARNIP-------------LSKLGEHVlAKNKKYLLICQSGMRSKKAYKILNKANY-DVTNV 89
Cdd:cd01522   18 LVDVRteAEWKFV-GGVPDAVHVAwqvypdmeinpnfLAELEEKV-GKDRPVLLLCRSGNRSIAAAEAAAQAGFtNVYNV 95


                 ...
gi 502661429  90 NGG 92
Cdd:cd01522   96 LEG 98
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 10-51 8.65e-05

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 38.80  E-value: 8.65e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 502661429  10 SISPAEVSTELKKGTQ---LIDVREAHEFQNGHIKGARNIPLSKL 51
Cdd:cd01446    1 TIDCAWLAALLREGGErllLLDCRPFLEYSSSHIRGAVNVCCPTI 45
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 22-72 8.66e-05

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: 38.38  E-value: 8.66e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502661429  22 KGTQLIDVREAHEFQ-----------NGHIKGARNIPLSKL-----------------GEHVLAKNKKYLLICQSGMRS 72
Cdd:cd01449   13 GDVQLVDARSPERFRgevpeprpglrSGHIPGAVNIPWTSLldedgtfkspeelralfAALGITPDKPVIVYCGSGVTA 91
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 8-59 1.20e-04

Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They 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. Cdc25A phosphatase functions to regulate S phase entry and Cdc25B is required for G2/M phase transition of the cell cycle. The Cdc25 domain binds oxyanions at the catalytic site and has the signature motif (H/YCxxxxxR).


Pssm-ID: 238788 [Multi-domain]  Cd Length: 121  Bit Score: 37.97  E-value: 1.20e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502661429   8 IKSISPaEVSTELKKGT--------QLIDVREAHEFQNGHIKGARNIPL-SKLGEHVLAKN 59
Cdd:cd01530    1 LKRISP-ETLARLLQGKydnffdkyIIIDCRFPYEYNGGHIKGAVNLSTkDELEEFFLDKP 60
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 21-51 1.87e-04

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 38.62  E-value: 1.87e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 502661429  21 KKGTQLIDVREAHEFQ---------NGHIKGARNIPLSKL 51
Cdd:COG2897  151 DPDAVLVDARSPERYRgevepidprAGHIPGAVNLPWTDL 190
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 26-98 2.37e-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: 37.06  E-value: 2.37e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502661429  26 LIDVREAHEFQNGHIKGARNIPLSKL----GEHVLAKNKKYLLICQSGMRSKKAYKILNKANYDVTNVNGGMRAWRG 98
Cdd:cd01534   19 RFDVRTPEEYEAGHLPGFRHTPGGQLvqetDHFAPVRGARIVLADDDGVRADMTASWLAQMGWEVYVLEGGLAAALA 95
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 9-92 4.92e-04

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins.


Pssm-ID: 238776 [Multi-domain]  Cd Length: 101  Bit Score: 36.02  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429   9 KSISPAEVSTEL-KKGTQLIDVREAHEFQNGHIKGARNIPL-------SKLGEHV-LAKNKKYLLICQSGMRSKKAY-KI 78
Cdd:cd01518    2 TYLSPAEWNELLeDPEVVLLDVRNDYEYDIGHFKGAVNPDVdtfrefpFWLDENLdLLKGKKVLMYCTGGIRCEKASaYL 81

                         90
                 ....*....|....
gi 502661429  79 LNKANYDVTNVNGG 92
Cdd:cd01518   82 KERGFKNVYQLKGG 95
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 9-48 1.08e-03

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: 35.46  E-value: 1.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 502661429   9 KSISPAEVSTELKKGT-------QLIDVREAhEFQNGHIKGARNIPL 48
Cdd:cd01443    2 KYISPEELVALLENSDsnagkdfVVVDLRRD-DYEGGHIKGSINLPA 47
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 26-97 1.45e-03

Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 1st repeat which does not contain the putative catalytic Cys residue.


Pssm-ID: 238790 [Multi-domain]  Cd Length: 92  Bit Score: 34.77  E-value: 1.45e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502661429  26 LIDVREAHEFQNGHIKGARNIPLSKLGEHVLAK-NKKYLLIC------QSGMRSKKAYKILNKANYDVTNVNGGMRAWR 97
Cdd:cd01532   13 LIDVREEDPFAQSHPLWAANLPLSRLELDAWVRiPRRDTPIVvygeggGEDLAPRAARRLSELGYTDVALLEGGLQGWR 91
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 8-96 1.75e-03

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: 35.08  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502661429   8 IKSISPAEVSTELKKGT---QLIDVREAhEFQNGHIKGARNIP----LSKLGEHV--LAKNKKYLLI--C-QSGMRSKKA 75
Cdd:cd01531    1 VSYISPAQLKGWIRNGRppfQVVDVRDE-DYAGGHIKGSWHYPstrfKAQLNQLVqlLSGSKKDTVVfhCaLSQVRGPSA 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 502661429  76 YK---------ILNKANYDVTNVNGGMRAW 96
Cdd:cd01531   80 ARkflryldeeDLETSKFEVYVLHGGFNAW 109
 
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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