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Conserved domains on  [gi|500581502|gb|EOQ40133|]
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hypothetical protein HMPREF1526_00831 [Butyricicoccus pullicaecorum 1.2]

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]; ...
 26-121 7.25e-35

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: 116.22  E-value: 7.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  26 SYQQITQEKAKEMMDTQEVIVLDVREQNEYDSGHIPGAVLLPVGTIDEDTAAavIPeKDSTVLVYCRSGNRSKTASSALA 105
Cdd:COG0607    2 SVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDE--LP-KDKPIVVYCASGGRSAQAAALLR 78

                         90
                 ....*....|....*..
gi 500581502 106 ELGYTNIYEF-GGINSW 121
Cdd:COG0607   79 RAGYTNVYNLaGGIEAW 95
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 26-121 7.25e-35

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: 116.22  E-value: 7.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  26 SYQQITQEKAKEMMDTQEVIVLDVREQNEYDSGHIPGAVLLPVGTIDEDTAAavIPeKDSTVLVYCRSGNRSKTASSALA 105
Cdd:COG0607    2 SVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDE--LP-KDKPIVVYCASGGRSAQAAALLR 78

                         90
                 ....*....|....*..
gi 500581502 106 ELGYTNIYEF-GGINSW 121
Cdd:COG0607   79 RAGYTNVYNLaGGIEAW 95
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 35-122 9.28e-34

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: 112.78  E-value: 9.28e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  35 AKEMMDTQEVIVLDVREQNEYDSGHIPGAVLLPVGTIDEDTAAAVIPeKDSTVLVYCRSGNRSKTASSALAELGYTNIYE 114
Cdd:cd00158    2 LKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELD-KDKPIVVYCRSGNRSARAAKLLRKAGGTNVYN 80


                 ....*....
gi 500581502 115 F-GGINSWP 122
Cdd:cd00158   81 LeGGMLAWK 89
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 39-121 1.20e-23

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: 87.15  E-value: 1.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502   39 MDTQEVIVLDVREQNEYDSGHIPGAVLLPVGTI-------DEDTAAAVIPEKDSTVLVYCRSGNRSKTASSALAELGYTN 111
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLslpplplLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|.
gi 500581502  112 IYEF-GGINSW 121
Cdd:pfam00581  81 VYVLdGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 42-121 9.14e-23

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: 85.20  E-value: 9.14e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502    42 QEVIVLDVREQNEYDSGHIPGAVLLPVGTIDEDTAAAVIPE-----------KDSTVLVYCRSGNRSKTASSALAELGYT 110
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEfeellkrlgldKDKPVVVYCRSGNRSAKAAWLLRELGFK 82

                           90
                   ....*....|..
gi 500581502   111 NIYEF-GGINSW 121
Cdd:smart00450  83 NVYLLdGGYKEW 94
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
26-121 1.09e-21

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 88.14  E-value: 1.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  26 SYQQITQEKAKEMMDtQEVIVLDVREQNEYDSGHIPGAVLLPVGTIDEDTAAAViPEKDSTVLVYCRSGNRSKTASSALA 105
Cdd:PRK08762   1 SIREISPAEARARAA-QGAVLIDVREAHERASGQAEGALRIPRGFLELRIETHL-PDRDREIVLICASGTRSAHAAATLR 78

                         90
                 ....*....|....*..
gi 500581502 106 ELGYTNIYEF-GGINSW 121
Cdd:PRK08762  79 ELGYTRVASVaGGFSAW 95
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 46-110 5.91e-07

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: 46.43  E-value: 5.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502   46 VLDVREQNEYDSGHIPGAVLLP---------VGTI--DEDTAAAV----------IPE----------KDSTVLVYC-RS 93
Cdd:TIGR03167   5 LIDVRSPAEFAEGHLPGAINLPllndeeraeVGTLykQVGPFAAIklglalvspnLAAhveqwrafadGPPQPLLYCwRG 84

                          90
                  ....*....|....*..
gi 500581502   94 GNRSKTASSALAELGYT 110
Cdd:TIGR03167  85 GMRSGSLAWLLAQIGFR 101
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 26-121 7.25e-35

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: 116.22  E-value: 7.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  26 SYQQITQEKAKEMMDTQEVIVLDVREQNEYDSGHIPGAVLLPVGTIDEDTAAavIPeKDSTVLVYCRSGNRSKTASSALA 105
Cdd:COG0607    2 SVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDE--LP-KDKPIVVYCASGGRSAQAAALLR 78

                         90
                 ....*....|....*..
gi 500581502 106 ELGYTNIYEF-GGINSW 121
Cdd:COG0607   79 RAGYTNVYNLaGGIEAW 95
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 35-122 9.28e-34

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: 112.78  E-value: 9.28e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  35 AKEMMDTQEVIVLDVREQNEYDSGHIPGAVLLPVGTIDEDTAAAVIPeKDSTVLVYCRSGNRSKTASSALAELGYTNIYE 114
Cdd:cd00158    2 LKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELD-KDKPIVVYCRSGNRSARAAKLLRKAGGTNVYN 80


                 ....*....
gi 500581502 115 F-GGINSWP 122
Cdd:cd00158   81 LeGGMLAWK 89
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 39-121 1.20e-23

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: 87.15  E-value: 1.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502   39 MDTQEVIVLDVREQNEYDSGHIPGAVLLPVGTI-------DEDTAAAVIPEKDSTVLVYCRSGNRSKTASSALAELGYTN 111
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLslpplplLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|.
gi 500581502  112 IYEF-GGINSW 121
Cdd:pfam00581  81 VYVLdGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 42-121 9.14e-23

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: 85.20  E-value: 9.14e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502    42 QEVIVLDVREQNEYDSGHIPGAVLLPVGTIDEDTAAAVIPE-----------KDSTVLVYCRSGNRSKTASSALAELGYT 110
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEfeellkrlgldKDKPVVVYCRSGNRSAKAAWLLRELGFK 82

                           90
                   ....*....|..
gi 500581502   111 NIYEF-GGINSW 121
Cdd:smart00450  83 NVYLLdGGYKEW 94
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
26-121 1.09e-21

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 88.14  E-value: 1.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  26 SYQQITQEKAKEMMDtQEVIVLDVREQNEYDSGHIPGAVLLPVGTIDEDTAAAViPEKDSTVLVYCRSGNRSKTASSALA 105
Cdd:PRK08762   1 SIREISPAEARARAA-QGAVLIDVREAHERASGQAEGALRIPRGFLELRIETHL-PDRDREIVLICASGTRSAHAAATLR 78

                         90
                 ....*....|....*..
gi 500581502 106 ELGYTNIYEF-GGINSW 121
Cdd:PRK08762  79 ELGYTRVASVaGGFSAW 95
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 43-121 4.08e-18

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: 73.46  E-value: 4.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  43 EVIVLDVREQNEYDSGHIPGAVLLPVGTID----------EDTAAAVIPEKDSTVLVYCRSGNRSKTASSALAELGYTNI 112
Cdd:cd01519   15 NKVLIDVREPEELKTGKIPGAINIPLSSLPdalalseeefEKKYGFPKPSKDKELIFYCKAGVRSKAAAELARSLGYENV 94


                 ....*....
gi 500581502 113 YEFGGinSW 121
Cdd:cd01519   95 GNYPG--SW 101
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 30-121 7.90e-17

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 74.74  E-value: 7.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  30 ITQEKAKEMMDTQEVIVL-DVREQNEYDSGHIPGAVLLPVGTIDEDTAAAVIPEkDSTVLVYCRSGNRSKTASSALAELG 108
Cdd:PRK07878 289 ITPRELKEWLDSGKKIALiDVREPVEWDIVHIPGAQLIPKSEILSGEALAKLPQ-DRTIVLYCKTGVRSAEALAALKKAG 367

                         90
                 ....*....|....
gi 500581502 109 YTN-IYEFGGINSW 121
Cdd:PRK07878 368 FSDaVHLQGGVVAW 381
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
28-127 2.29e-16

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 73.62  E-value: 2.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  28 QQITQEKAKEMMDTQ--EVIVLDVREQNEYDSGHIPGAVLLPVGTIDEDTAAAVIPE--KDSTVLVYCRSGNRSKTASSA 103
Cdd:PRK07411 282 PEMTVTELKALLDSGadDFVLIDVRNPNEYEIARIPGSVLVPLPDIENGPGVEKVKEllNGHRLIAHCKMGGRSAKALGI 361

                         90       100
                 ....*....|....*....|....
gi 500581502 104 LAELGYTNIYEFGGINSWPYETES 127
Cdd:PRK07411 362 LKEAGIEGTNVKGGITAWSREVDP 385
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 29-121 5.15e-15

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: 65.36  E-value: 5.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  29 QITQEKAKEMMDT-QEVIVLDVREQNEY--DSGHIPGAVLLpvgtiDEDTAAAVIPE--KDSTVLVYCRSGNRSKTASSA 103
Cdd:cd01444    1 RISVDELAELLAAgEAPVLLDVRDPASYaaLPDHIPGAIHL-----DEDSLDDWLGDldRDRPVVVYCYHGNSSAQLAQA 75

                         90
                 ....*....|....*....
gi 500581502 104 LAELGYTNIYEF-GGINSW 121
Cdd:cd01444   76 LREAGFTDVRSLaGGFEAW 94
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 27-121 3.05e-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: 3.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  27 YQQITQEKAKEmmdtqevIVLDVREQNEYDSGHIPGAVLLPVGTIdEDTAAAVIP--------EKDSTVLVYCRSGNRSK 98
Cdd:cd01526   15 YKNILQAGKKH-------VLLDVRPKVHFEICRLPEAINIPLSEL-LSKAAELKSlqelpldnDKDSPIYVVCRRGNDSQ 86

                         90       100
                 ....*....|....*....|....*
gi 500581502  99 TASSALAELGYT-NIYEF-GGINSW 121
Cdd:cd01526   87 TAVRKLKELGLErFVRDIiGGLKAW 111
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 44-121 4.46e-14

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 66.82  E-value: 4.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  44 VIVLDVREQNEYDSGHIPGAVLLPVGTIDED-TAAAVIPEKDstVLVYCRSGNRSKTASSALAELGYTNIYEF-GGINSW 121
Cdd:PRK05597 275 VTLIDVREPSEFAAYSIPGAHNVPLSAIREGaNPPSVSAGDE--VVVYCAAGVRSAQAVAILERAGYTGMSSLdGGIEGW 352
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 30-113 1.58e-13

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: 61.96  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  30 ITQEKAKEMM-DTQEVIVLDVREQNEYDS-GHIPGAV-----LLPVGTIDEDTAAAV--IPEKDSTVLVYCRSGNRSKTA 100
Cdd:cd01522    1 LTPAEAWALLqADPQAVLVDVRTEAEWKFvGGVPDAVhvawqVYPDMEINPNFLAELeeKVGKDRPVLLLCRSGNRSIAA 80

                         90
                 ....*....|...
gi 500581502 101 SSALAELGYTNIY 113
Cdd:cd01522   81 AEAAAQAGFTNVY 93
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 29-121 1.68e-13

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: 61.64  E-value: 1.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  29 QITQEKAKEMMDTQ--EVIVLDVREQNEYDSGHIPGAVLLPVGTIDE--DTAAAVIPEKDstVLVYCRSGNRSKTASSAL 104
Cdd:cd01528    1 QISVAELAEWLADEreEPVLIDVREPEELEIAFLPGFLHLPMSEIPErsKELDSDNPDKD--IVVLCHHGGRSMQVAQWL 78

                         90
                 ....*....|....*...
gi 500581502 105 AELGYTNIYEF-GGINSW 121
Cdd:cd01528   79 LRQGFENVYNLqGGIDAW 96
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
27-127 2.80e-13

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 61.19  E-value: 2.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  27 YQQITQEKAKEMMDTQEVIVLDVREQNEYDSGHIPGAVLLpvgtiDEDTAAAVIPEKD--STVLVYCRSGNRSKTASSAL 104
Cdd:PRK00162   4 FECINVEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFHL-----TNDSLGAFMRQADfdTPVMVMCYHGNSSQGAAQYL 78

                         90       100
                 ....*....|....*....|....*...
gi 500581502 105 AELGYTNIYEF-GGINSW----PYETES 127
Cdd:PRK00162  79 LQQGFDVVYSIdGGFEAWrrtfPAEVAS 106
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 30-121 2.19e-12

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: 59.18  E-value: 2.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  30 ITQEKAKEMMDTQEVIVLDVREQNEYD-----------SGHIPGAVLLPVGT-IDEDTA-----------AAVIPEKDST 86
Cdd:cd01449    1 VTAEEVLANLDSGDVQLVDARSPERFRgevpeprpglrSGHIPGAVNIPWTSlLDEDGTfkspeelralfAALGITPDKP 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 500581502  87 VLVYCRSGNRSKTASSALAELGYTNIYEFGGinSW 121
Cdd:cd01449   81 VIVYCGSGVTACVLLLALELLGYKNVRLYDG--SW 113
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 30-112 2.43e-12

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 61.34  E-value: 2.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  30 ITQEKAKEMMDTQEVIVLDVREQNEYD---------SGHIPGAVLLPVGT-IDEDTA-----------AAVIPEKDSTVL 88
Cdd:COG2897  140 ADADEVLAALGDPDAVLVDARSPERYRgevepidprAGHIPGAVNLPWTDlLDEDGTfksaeelralfAALGIDPDKPVI 219

                         90       100
                 ....*....|....*....|....
gi 500581502  89 VYCRSGNRSKTASSALAELGYTNI 112
Cdd:COG2897  220 TYCGSGVRAAHTWLALELLGYPNV 243
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 47-118 3.07e-12

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 58.32  E-value: 3.07e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500581502  47 LDVREQNEYDSGHIPGAVLLPVGTIDEDTAAAViPEKDSTVLVYCRSGNRSKTASSALAELGYTNIYEFGGI 118
Cdd:PRK10287  24 IDVRVPEQYQQEHVQGAINIPLKEVKERIATAV-PDKNDTVKLYCNAGRQSGQAKEILSEMGYTHAENAGGL 94
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 30-121 1.07e-11

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: 57.05  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  30 ITQEKAKEMMDTQEVIVLDVREQNEYD-SGHIPGAVLLPVGT----IDEDTA-AAVIPEKDSTVLVYCRSGNRSKTASSA 103
Cdd:cd01447    1 LSPEDARALLGSPGVLLVDVRDPRELErTGMIPGAFHAPRGMlefwADPDSPyHKPAFAEDKPFVFYCASGWRSALAGKT 80

                         90
                 ....*....|....*....
gi 500581502 104 LAELGYTNIYEF-GGINSW 121
Cdd:cd01447   81 LQDMGLKPVYNIeGGFKDW 99
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 39-110 1.42e-11

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: 56.12  E-value: 1.42e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500581502  39 MDTQEVIVLDVREQNEYDSGHIPGAVLLPVGTIDEDTAAavIPeKDSTVLVYCRSGNRSKTASSALAELGYT 110
Cdd:cd01524    9 YRADGVTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNE--LP-KDKEIIVYCAVGLRGYIAARILTQNGFK 77
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 42-121 1.80e-11

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: 56.59  E-value: 1.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  42 QEVIVLDVREQNEYDSGHIPGAVLLPVGTIDEDTAAAVIPEKdsTVLVYCRS--GNRSKTASSALAELGYTNIYEFGGIN 119
Cdd:cd01521   24 PDFVLVDVRSAEAYARGHVPGAINLPHREICENATAKLDKEK--LFVVYCDGpgCNGATKAALKLAELGFPVKEMIGGLD 101


                 ..
gi 500581502 120 SW 121
Cdd:cd01521  102 WW 103
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 33-118 4.24e-11

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: 55.28  E-value: 4.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  33 EKAKEMMDTQEVIVLDVREQNEYDSGHIPGAVLLPVGTIDEDTAAAV---IPEKDSTVLVYCRSGNRSKTASSALAELGY 109
Cdd:cd01518    7 AEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDenlDLLKGKKVLMYCTGGIRCEKASAYLKERGF 86

                         90
                 ....*....|
gi 500581502 110 TNIYEF-GGI 118
Cdd:cd01518   87 KNVYQLkGGI 96
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 35-121 1.05e-09

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: 51.73  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  35 AKEMMDTQEVIVLDVREQNEYDSGHIPGAVLLPVG------TIDEDTAAAVIPeKDSTVLVYCRSGNRSKTASSALAELG 108
Cdd:cd01523    7 YARLLAGQPLFILDVRNESDYERWKIDGENNTPYFdpyfdfLEIEEDILDQLP-DDQEVTVICAKEGSSQFVAELLAERG 85

                         90
                 ....*....|...
gi 500581502 109 YTNIYEFGGINSW 121
Cdd:cd01523   86 YDVDYLAGGMKAW 98
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 43-109 1.17e-09

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 54.45  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  43 EVIVLDVREQNEYDSGHIPGAVLLP---------VGTI------DE-----------------DTAAAVIPEKDSTVLVY 90
Cdd:PRK11784  15 DTPLIDVRSPIEFAEGHIPGAINLPllndeeraeVGTCykqqgqFAaialghalvagniaahrEEAWADFPRANPRGLLY 94

                         90       100
                 ....*....|....*....|
gi 500581502  91 C-RSGNRSKTASSALAELGY 109
Cdd:PRK11784  95 CwRGGLRSGSVQQWLKEAGI 114
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 28-121 1.57e-09

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: 51.33  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  28 QQITQEKAKEMMDTQEVIVlDVREQNEYDSGHIPGAVLLPVGTIDEDTAAAVipeKDSTVLVYCRSGNRSKTASSALAEL 107
Cdd:cd01527    2 TTISPNDACELLAQGAVLV-DIREPDEYLRERIPGARLVPLSQLESEGLPLV---GANAIIFHCRSGMRTQQNAERLAAI 77

                         90
                 ....*....|....*
gi 500581502 108 GYTNIYEF-GGINSW 121
Cdd:cd01527   78 SAGEAYVLeGGLDAW 92
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 38-121 3.99e-09

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: 50.18  E-value: 3.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  38 MMDTQEVIVLDVREQNEYDSGHIPGAVLLPVGTIDEDtAAAVIPEKDSTVLVYCRSGNR--SKTASSALAELGYTNIYEF 115
Cdd:cd01532    5 LLAREEIALIDVREEDPFAQSHPLWAANLPLSRLELD-AWVRIPRRDTPIVVYGEGGGEdlAPRAARRLSELGYTDVALL 83


                 ....*..
gi 500581502 116 -GGINSW 121
Cdd:cd01532   84 eGGLQGW 90
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 46-121 5.27e-09

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: 49.98  E-value: 5.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  46 VLDVREQNEYDSGHIPGAVLLPVGTIDEDTA---AAVIPEKDSTVLVYCRSGNRSKTASSALAELGYTNIYEF-GGINSW 121
Cdd:cd01529   15 LLDVRAEDEYAAGHLPGKRSIPGAALVLRSQelqALEAPGRATRYVLTCDGSLLARFAAQELLALGGKPVALLdGGTSAW 94
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 30-121 5.94e-09

Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the 1st repeat, which does not contain the catalytically active Cys residue. The role of the 1st repeat is uncertain, but it is believed to be involved in protein interaction.


Pssm-ID: 238725 [Multi-domain]  Cd Length: 122  Bit Score: 50.31  E-value: 5.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  30 ITQEKAKEMMDTQEVIVLDVRE-------QNEYDSGHIPGAVLLPVGTI--DEDTAAAVIPE--------------KDST 86
Cdd:cd01448    2 VSPDWLAEHLDDPDVRILDARWylpdrdgRKEYLEGHIPGAVFFDLDEDldDKSPGPHMLPSpeefaellgslgisNDDT 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 500581502  87 VLVYCRSGNRSktASSA---LAELGYTNIYEF-GGINSW 121
Cdd:cd01448   82 VVVYDDGGGFF--AARAwwtLRYFGHENVRVLdGGLQAW 118
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
36-118 9.34e-09

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 51.77  E-value: 9.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  36 KEMMDTQEVIVLDVREQNEYDSGHIPGAVLLPVGT-------IDEDTAaaviPEKDSTVLVYCRSGNRSKTASSALAELG 108
Cdd:PRK00142 120 NELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETfrefppwVEENLD----PLKDKKVVMYCTGGIRCEKASAWMKHEG 195

                         90
                 ....*....|.
gi 500581502 109 YTNIYEF-GGI 118
Cdd:PRK00142 196 FKEVYQLeGGI 206
RHOD_YbbB cd01520
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ...
 43-121 1.45e-07

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: 46.90  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  43 EVIVLDVREQNEYDSGHIPGAVLLP---------VGTI--DEDTAAAVI---------------------PEKDSTVLVY 90
Cdd:cd01520   13 DGPLIDVRSPKEFFEGHLPGAINLPllddeeralVGTLykQQGREAAIElglelvsgklkrilneawearLERDPKLLIY 92

                         90       100       110
                 ....*....|....*....|....*....|..
gi 500581502  91 C-RSGNRSKTASSALAELGYTNIYEFGGINSW 121
Cdd:cd01520   93 CaRGGMRSQSLAWLLESLGIDVPLLEGGYKAY 124
SelU COG2603
tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal ...
 42-109 3.20e-07

tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal structure and biogenesis]; tRNA 2-selenouridine synthase SelU, contains rhodanese domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442015 [Multi-domain]  Cd Length: 341  Bit Score: 47.46  E-value: 3.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  42 QEVIVLDVREQNEYDSGHIPGAVLLP---------VGTI--DEDTAAAV----------IPE----------KDSTVLVY 90
Cdd:COG2603   15 DDDPLIDVRSPVEFAEGHIPGAINLPllddeeraeVGTCykQQGPFAAIklghalvsgkLAAhreeawafapKHPRPLVY 94

                         90       100
                 ....*....|....*....|
gi 500581502  91 C-RSGNRSKTASSALAELGY 109
Cdd:COG2603   95 CwRGGLRSGSVAQWLREAGI 114
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 46-110 5.91e-07

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: 46.43  E-value: 5.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502   46 VLDVREQNEYDSGHIPGAVLLP---------VGTI--DEDTAAAV----------IPE----------KDSTVLVYC-RS 93
Cdd:TIGR03167   5 LIDVRSPAEFAEGHLPGAINLPllndeeraeVGTLykQVGPFAAIklglalvspnLAAhveqwrafadGPPQPLLYCwRG 84

                          90
                  ....*....|....*..
gi 500581502   94 GNRSKTASSALAELGYT 110
Cdd:TIGR03167  85 GMRSGSLAWLLAQIGFR 101
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 44-109 6.93e-07

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: 44.38  E-value: 6.93e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500581502  44 VIVLDVREQNEYDSGHIPGAVLLPVGTIDEDTAAAViPEKDSTVLVYCRSGNRSKTASSALAELGY 109
Cdd:cd01534   17 VYRFDVRTPEEYEAGHLPGFRHTPGGQLVQETDHFA-PVRGARIVLADDDGVRADMTASWLAQMGW 81
PLN02160 PLN02160
thiosulfate sulfurtransferase
 47-117 1.84e-06

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 43.92  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  47 LDVREQNEYDSGH--------IPGAVLLPVGTID-----EDTAAAVIPEKDstVLVYCRSGNRSKTASSALAELGYTNIY 113
Cdd:PLN02160  33 LDVRTQDEFRRGHceaakivnIPYMLNTPQGRVKnqeflEQVSSLLNPADD--ILVGCQSGARSLKATTELVAAGYKKVR 110


                 ....
gi 500581502 114 EFGG 117
Cdd:PLN02160 111 NKGG 114
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 36-90 4.13e-06

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 44.01  E-value: 4.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  36 KEMMDTQEVIVLDVREQ-----NEYDSGHIPGAVLLPvgtIDEDTAAAVIPE--------------------KDSTVLVY 90
Cdd:COG2897    2 AAHLDDPDVVILDVRWDlpdgrAAYEAGHIPGAVFLD---LDTDLSDPRSPGrhplpspeafaallgalgisNDTTVVVY 78
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 27-121 7.98e-05

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: 39.31  E-value: 7.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  27 YQQITQEKAKEMMDTQ------EVIVLDVREqNEYDSGHIPGAVLLPVGTIDE---DTAAAVIPEKDSTVLVYC-RSGNR 96
Cdd:cd01443    1 LKYISPEELVALLENSdsnagkDFVVVDLRR-DDYEGGHIKGSINLPAQSCYQtlpQVYALFSLAGVKLAIFYCgSSQGR 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 500581502  97 -SKTA---SSALAELGYTNIYEF---GGINSW 121
Cdd:cd01443   80 gPRAArwfADYLRKVGESLPKSYiltGGIKAW 111
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 30-111 8.96e-05

Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 2nd repeat which does contain the putative catalytic Cys residue.


Pssm-ID: 238791 [Multi-domain]  Cd Length: 109  Bit Score: 38.98  E-value: 8.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  30 ITQEKAKEMMDTQE-VIVLDVREQNEYDSGHIPGAVLLPVGTIDEDTAAAViPEKDSTVLVYCRSGNRSKTASSALAELG 108
Cdd:cd01533   12 VSADELAALQARGApLVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGELA-PDPRTPIVVNCAGRTRSIIGAQSLINAG 90


                 ...
gi 500581502 109 YTN 111
Cdd:cd01533   91 LPN 93
PRK05320 PRK05320
rhodanese superfamily protein; Provisional
 40-118 1.70e-04

rhodanese superfamily protein; Provisional


Pssm-ID: 235405 [Multi-domain]  Cd Length: 257  Bit Score: 39.62  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  40 DTQEVIVLDVREQNEYDSGHIPGAVLLPVGTIDEdTAAAVIPEKD----STVLVYCRSGNRSKTASSALAELGYTNIYEF 115
Cdd:PRK05320 128 AGRPVVMLDTRNAFEVDVGTFDGALDYRIDKFTE-FPEALAAHRAdlagKTVVSFCTGGIRCEKAAIHMQEVGIDNVYQL 206


                 ....
gi 500581502 116 -GGI 118
Cdd:PRK05320 207 eGGI 210
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 26-121 5.35e-04

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


Pssm-ID: 238789 [Multi-domain]  Cd Length: 113  Bit Score: 37.01  E-value: 5.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  26 SYQQITQEKAKEMMDTQEVIVLDVREQNeYDSGHIPGAVLLPVGTIDEDTAA---AVIPEKDSTVLVYCR-SGNRSKTAS 101
Cdd:cd01531    2 SYISPAQLKGWIRNGRPPFQVVDVRDED-YAGGHIKGSWHYPSTRFKAQLNQlvqLLSGSKKDTVVFHCAlSQVRGPSAA 80

                         90       100
                 ....*....|....*....|
gi 500581502 102 SALAELGYTNIYEFGGINSW 121
Cdd:cd01531   81 RKFLRYLDEEDLETSKFEVY 100
COG3453 COG3453
Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family ...
 66-112 5.74e-04

Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family [General function prediction only];


Pssm-ID: 442676 [Multi-domain]  Cd Length: 125  Bit Score: 37.12  E-value: 5.74e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 500581502  66 LPV--GTIDEDTAAA---VIPEKDSTVLVYCRSGNRSkTASSALAELGYTNI 112
Cdd:COG3453   62 IPVtgGAITDEDVEAfaaALAAAPGPVLAHCRSGTRS-SALWALYQAGKGGM 112
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 27-91 3.50e-03

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: 34.89  E-value: 3.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500581502  27 YQQITQEKAKEMMD------TQEVIVLDVREQNEYDSGHIPGAVLLPvgtiDEDTAAAVIPEKDS-------TVLV-YC 91
Cdd:cd01530    1 LKRISPETLARLLQgkydnfFDKYIIIDCRFPYEYNGGHIKGAVNLS----TKDELEEFFLDKPGvaskkkrRVLIfHC 75
PRK01415 PRK01415
hypothetical protein; Validated
 37-127 4.33e-03

hypothetical protein; Validated


Pssm-ID: 167229 [Multi-domain]  Cd Length: 247  Bit Score: 35.30  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500581502  37 EMMDTQEVIVLDVREQNEYDSGHIPGAVLLPVGTIDEDTA-----AAVIpeKDSTVLVYCRSGNRSKTASSALAELGYTN 111
Cdd:PRK01415 121 EFITKQDVIVIDTRNDYEVEVGTFKSAINPNTKTFKQFPAwvqqnQELL--KGKKIAMVCTGGIRCEKSTSLLKSIGYDE 198

                         90
                 ....*....|....*..
gi 500581502 112 IYEF-GGINSWPYETES 127
Cdd:PRK01415 199 VYHLkGGILQYLEDTQN 215
 
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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