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Conserved domains on  [gi|490580327|ref|WP_004445347|]
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MULTISPECIES: rhodanese-like domain-containing protein [Agrobacterium]

Protein Classification

rhodanese-like domain-containing protein( domain architecture ID 13)

rhodanese-like domain-containing protein may have sulfurtransferase activity if an active site cysteine is present

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 120-223 2.55e-36

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.


The actual alignment was detected with superfamily member cd01533:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 109  Bit Score: 127.58  E-value: 2.55e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 120 VRSEKNTPVVFARELKAWQEAGEDVVILDTRTLPEYEKEHVPGAIAVPGAELLLRFSDLVPSPKTRVVVSCAGLPRAILG 199
Cdd:cd01533    3 VEAVRHTPSVSADELAALQARGAPLVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGELAPDPRTPIVVNCAGRTRSIIG 82

                         90       100
                 ....*....|....*....|....
gi 490580327 200 AQTLIDAGVENDVSYLHDGTRGWT 223
Cdd:cd01533   83 AQSLINAGLPNPVAALRNGTQGWT 106
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 264-348 1.23e-19

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.


The actual alignment was detected with superfamily member cd01534:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 95  Bit Score: 82.52  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 264 IDRPTAETWLKDPSRTTYFLDVRTPEEFETSHLQGSISSEGGQLLGVAYRTIAVRGARVILVDDlLGARARVVAHWLKRR 343
Cdd:cd01534    1 IGAAELARWAAEGDRTVYRFDVRTPEEYEAGHLPGFRHTPGGQLVQETDHFAPVRGARIVLADD-DGVRADMTASWLAQM 79


                 ....*
gi 490580327 344 GFEIA 348
Cdd:cd01534   80 GWEVY 84
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 15-100 1.61e-15

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.


The actual alignment was detected with superfamily member cd01532:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 92  Bit Score: 71.36  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327  15 LRDGRELAVLDIRAAEDVGYASPLFVANLPVDRLEAEIDRFIPRPVVRTVLVDDGKGS--AKQAAERLAAKGWTDIHFLR 92
Cdd:cd01532    5 LLAREEIALIDVREEDPFAQSHPLWAANLPLSRLELDAWVRIPRRDTPIVVYGEGGGEdlAPRAARRLSELGYTDVALLE 84


                 ....*...
gi 490580327  93 GGIPAWIE 100
Cdd:cd01532   85 GGLQGWRA 92
 
Name Accession Description Interval E-value
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 120-223 2.55e-36

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: 127.58  E-value: 2.55e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 120 VRSEKNTPVVFARELKAWQEAGEDVVILDTRTLPEYEKEHVPGAIAVPGAELLLRFSDLVPSPKTRVVVSCAGLPRAILG 199
Cdd:cd01533    3 VEAVRHTPSVSADELAALQARGAPLVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGELAPDPRTPIVVNCAGRTRSIIG 82

                         90       100
                 ....*....|....*....|....
gi 490580327 200 AQTLIDAGVENDVSYLHDGTRGWT 223
Cdd:cd01533   83 AQSLINAGLPNPVAALRNGTQGWT 106
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 264-348 1.23e-19

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: 82.52  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 264 IDRPTAETWLKDPSRTTYFLDVRTPEEFETSHLQGSISSEGGQLLGVAYRTIAVRGARVILVDDlLGARARVVAHWLKRR 343
Cdd:cd01534    1 IGAAELARWAAEGDRTVYRFDVRTPEEYEAGHLPGFRHTPGGQLVQETDHFAPVRGARIVLADD-DGVRADMTASWLAQM 79


                 ....*
gi 490580327 344 GFEIA 348
Cdd:cd01534   80 GWEVY 84
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 131-232 1.88e-18

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: 79.63  E-value: 1.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 131 ARELKAWQEAgEDVVILDTRTLPEYEKEHVPGAIAVPGAELLLRFSDLvpSPKTRVVVSCAGLPRAILGAQTLIDAGVEN 210
Cdd:COG0607    8 PAELAELLES-EDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDEL--PKDKPIVVYCASGGRSAQAAALLRRAGYTN 84

                         90       100
                 ....*....|....*....|..
gi 490580327 211 dVSYLHDGTRGWTDDGFELETG 232
Cdd:COG0607   85 -VYNLAGGIEAWKAAGLPVEKG 105
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 15-100 1.61e-15

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: 71.36  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327  15 LRDGRELAVLDIRAAEDVGYASPLFVANLPVDRLEAEIDRFIPRPVVRTVLVDDGKGS--AKQAAERLAAKGWTDIHFLR 92
Cdd:cd01532    5 LLAREEIALIDVREEDPFAQSHPLWAANLPLSRLELDAWVRIPRRDTPIVVYGEGGGEdlAPRAARRLSELGYTDVALLE 84


                 ....*...
gi 490580327  93 GGIPAWIE 100
Cdd:cd01532   85 GGLQGWRA 92
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
133-236 1.60e-11

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 65.03  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 133 ELKAWQEAGedVVILDTRTLPEYEKEHVPGAIAVPGAELLLRFSDLVPSPKTRVVVSCAGLPRAILGAQTLIDAGVEnDV 212
Cdd:PRK08762   9 EARARAAQG--AVLIDVREAHERASGQAEGALRIPRGFLELRIETHLPDRDREIVLICASGTRSAHAAATLRELGYT-RV 85

                         90       100
                 ....*....|....*....|....
gi 490580327 213 SYLHDGTRGWTDDGFELETGPSRT 236
Cdd:PRK08762  86 ASVAGGFSAWKDAGLPLERPRLLT 109
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 1-102 2.19e-10

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: 57.28  E-value: 2.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327   1 MSVFAVTKDRLIEWLRDGrELAVLDIRAAEDVGYASPLFVANLPVDRLEAEIDRfIP--RPVVrtvLVDDGKGSAKQAAE 78
Cdd:COG0607    1 ASVKEISPAELAELLESE-DAVLLDVREPEEFAAGHIPGAINIPLGELAERLDE-LPkdKPIV---VYCASGGRSAQAAA 75

                         90       100
                 ....*....|....*....|....
gi 490580327  79 RLAAKGWTDIHFLRGGIPAWIEGG 102
Cdd:COG0607   76 LLRRAGYTNVYNLAGGIEAWKAAG 99
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 141-222 7.46e-10

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 55.18  E-value: 7.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327  141 GEDVVILDTRTLPEYEKEHVPGAIAVPGAELLLRFSDLVPSPK--------TRVVVSCAGLPRAILGAQTLIDAGVENdV 212
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEkllellkdKPIVVYCNSGNRAAAAAALLKALGYKN-V 81

                          90
                  ....*....|
gi 490580327  213 SYLHDGTRGW 222
Cdd:pfam00581  82 YVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 141-228 1.08e-09

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: 55.16  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327   141 GEDVVILDTRTLPEYEKEHVPGAIAVP------------GAELLLRFSDLVPSPKTRVVVSCAGLPRAILGAQTLIDAGV 208
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPlselldrrgeldILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81

                           90       100
                   ....*....|....*....|
gi 490580327   209 ENdVSYLHDGTRGWTDDGFE 228
Cdd:smart00450  82 KN-VYLLDGGYKEWSAAGPP 100
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 264-351 1.88e-08

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: 51.89  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 264 IDRPTAETWLKDPSrtTYFLDVRTPEEFETSHLQGSISSEGGQLlgvAYRTIAV-RGARVILVDDlLGARARVVAHWLKR 342
Cdd:COG0607    6 ISPAELAELLESED--AVLLDVREPEEFAAGHIPGAINIPLGEL---AERLDELpKDKPIVVYCA-SGGRSAQAAALLRR 79


                 ....*....
gi 490580327 343 RGFEIALHL 351
Cdd:COG0607   80 AGYTNVYNL 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 17-98 1.64e-05

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: 42.86  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327   17 DGRELAVLDIRAAEDvgYAS---------PLFVANLPVDRLEAEIDRFIPRPVVRTVLV-DDGKGSAKQAAERLAAKGWT 86
Cdd:pfam00581   2 EDGKVVLIDVRPPEE--YAKghipgavnvPLSSLSLPPLPLLELLEKLLELLKDKPIVVyCNSGNRAAAAAALLKALGYK 79

                          90
                  ....*....|..
gi 490580327   87 DIHFLRGGIPAW 98
Cdd:pfam00581  80 NVYVLDGGFEAW 91
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 282-351 1.55e-03

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: 37.46  E-value: 1.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490580327  282 FLDVRTPEEFETSHLQGSI-------SSEGGQLLGVAYRTIA-VRGARVILVDDlLGARARVVAHWLKRRGFEIALHL 351
Cdd:pfam00581   8 LIDVRPPEEYAKGHIPGAVnvplsslSLPPLPLLELLEKLLElLKDKPIVVYCN-SGNRAAAAAALLKALGYKNVYVL 84
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
2-102 5.11e-03

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 38.45  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327   2 SVFAVTKDRLIEWLRDGreLAVLDIRAAEDvgYASPLFVANLPVDR--LEAEIDRFIP---RPVVrtVLVDDGKGSAkQA 76
Cdd:PRK08762   1 SIREISPAEARARAAQG--AVLIDVREAHE--RASGQAEGALRIPRgfLELRIETHLPdrdREIV--LICASGTRSA-HA 73

                         90       100
                 ....*....|....*....|....*.
gi 490580327  77 AERLAAKGWTDIHFLRGGIPAWIEGG 102
Cdd:PRK08762  74 AATLRELGYTRVASVAGGFSAWKDAG 99
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 282-353 5.43e-03

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: 35.90  E-value: 5.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327   282 FLDVRTPEEFETSHLQGSI-------SSEGGQLLGVAYRTIAVR-----GARVILVDDlLGARARVVAHWLKRRGFEIAL 349
Cdd:smart00450   7 LLDVRSPEEYEGGHIPGAVniplselLDRRGELDILEFEELLKRlgldkDKPVVVYCR-SGNRSAKAAWLLRELGFKNVY 85


                   ....
gi 490580327   350 HLHD 353
Cdd:smart00450  86 LLDG 89
 
Name Accession Description Interval E-value
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 120-223 2.55e-36

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: 127.58  E-value: 2.55e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 120 VRSEKNTPVVFARELKAWQEAGEDVVILDTRTLPEYEKEHVPGAIAVPGAELLLRFSDLVPSPKTRVVVSCAGLPRAILG 199
Cdd:cd01533    3 VEAVRHTPSVSADELAALQARGAPLVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGELAPDPRTPIVVNCAGRTRSIIG 82

                         90       100
                 ....*....|....*....|....
gi 490580327 200 AQTLIDAGVENDVSYLHDGTRGWT 223
Cdd:cd01533   83 AQSLINAGLPNPVAALRNGTQGWT 106
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 264-348 1.23e-19

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: 82.52  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 264 IDRPTAETWLKDPSRTTYFLDVRTPEEFETSHLQGSISSEGGQLLGVAYRTIAVRGARVILVDDlLGARARVVAHWLKRR 343
Cdd:cd01534    1 IGAAELARWAAEGDRTVYRFDVRTPEEYEAGHLPGFRHTPGGQLVQETDHFAPVRGARIVLADD-DGVRADMTASWLAQM 79


                 ....*
gi 490580327 344 GFEIA 348
Cdd:cd01534   80 GWEVY 84
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 131-232 1.88e-18

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: 79.63  E-value: 1.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 131 ARELKAWQEAgEDVVILDTRTLPEYEKEHVPGAIAVPGAELLLRFSDLvpSPKTRVVVSCAGLPRAILGAQTLIDAGVEN 210
Cdd:COG0607    8 PAELAELLES-EDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDEL--PKDKPIVVYCASGGRSAQAAALLRRAGYTN 84

                         90       100
                 ....*....|....*....|..
gi 490580327 211 dVSYLHDGTRGWTDDGFELETG 232
Cdd:COG0607   85 -VYNLAGGIEAWKAAGLPVEKG 105
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 133-222 8.68e-16

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: 71.95  E-value: 8.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 133 ELKAWQEaGEDVVILDTRTLPEYEKEHVPGAIAVPGAELLLRFSDLVPSPKTRVVVSCAGLPRAILGAQTLIDAGVENdV 212
Cdd:cd00158    1 ELKELLD-DEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTN-V 78

                         90
                 ....*....|
gi 490580327 213 SYLHDGTRGW 222
Cdd:cd00158   79 YNLEGGMLAW 88
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 15-100 1.61e-15

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: 71.36  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327  15 LRDGRELAVLDIRAAEDVGYASPLFVANLPVDRLEAEIDRFIPRPVVRTVLVDDGKGS--AKQAAERLAAKGWTDIHFLR 92
Cdd:cd01532    5 LLAREEIALIDVREEDPFAQSHPLWAANLPLSRLELDAWVRIPRRDTPIVVYGEGGGEdlAPRAARRLSELGYTDVALLE 84


                 ....*...
gi 490580327  93 GGIPAWIE 100
Cdd:cd01532   85 GGLQGWRA 92
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 134-223 1.42e-13

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: 65.77  E-value: 1.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 134 LKAWQEAGEDVV-ILDTRTLPEYEKEHVPGAIAVPGAELLLRFSDL----VPSPKTRVVVSCAGLPRAILGAQTLIDAGV 208
Cdd:cd01529    2 LADWLGEHEPGTaLLDVRAEDEYAAGHLPGKRSIPGAALVLRSQELqaleAPGRATRYVLTCDGSLLARFAAQELLALGG 81

                         90
                 ....*....|....*
gi 490580327 209 EnDVSYLHDGTRGWT 223
Cdd:cd01529   82 K-PVALLDGGTSAWV 95
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
133-236 1.60e-11

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 65.03  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 133 ELKAWQEAGedVVILDTRTLPEYEKEHVPGAIAVPGAELLLRFSDLVPSPKTRVVVSCAGLPRAILGAQTLIDAGVEnDV 212
Cdd:PRK08762   9 EARARAAQG--AVLIDVREAHERASGQAEGALRIPRGFLELRIETHLPDRDREIVLICASGTRSAHAAATLRELGYT-RV 85

                         90       100
                 ....*....|....*....|....
gi 490580327 213 SYLHDGTRGWTDDGFELETGPSRT 236
Cdd:PRK08762  86 ASVAGGFSAWKDAGLPLERPRLLT 109
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 1-102 2.19e-10

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: 57.28  E-value: 2.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327   1 MSVFAVTKDRLIEWLRDGrELAVLDIRAAEDVGYASPLFVANLPVDRLEAEIDRfIP--RPVVrtvLVDDGKGSAKQAAE 78
Cdd:COG0607    1 ASVKEISPAELAELLESE-DAVLLDVREPEEFAAGHIPGAINIPLGELAERLDE-LPkdKPIV---VYCASGGRSAQAAA 75

                         90       100
                 ....*....|....*....|....
gi 490580327  79 RLAAKGWTDIHFLRGGIPAWIEGG 102
Cdd:COG0607   76 LLRRAGYTNVYNLAGGIEAWKAAG 99
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 141-222 7.46e-10

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 55.18  E-value: 7.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327  141 GEDVVILDTRTLPEYEKEHVPGAIAVPGAELLLRFSDLVPSPK--------TRVVVSCAGLPRAILGAQTLIDAGVENdV 212
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEkllellkdKPIVVYCNSGNRAAAAAALLKALGYKN-V 81

                          90
                  ....*....|
gi 490580327  213 SYLHDGTRGW 222
Cdd:pfam00581  82 YVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 141-228 1.08e-09

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: 55.16  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327   141 GEDVVILDTRTLPEYEKEHVPGAIAVP------------GAELLLRFSDLVPSPKTRVVVSCAGLPRAILGAQTLIDAGV 208
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPlselldrrgeldILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81

                           90       100
                   ....*....|....*....|
gi 490580327   209 ENdVSYLHDGTRGWTDDGFE 228
Cdd:smart00450  82 KN-VYLLDGGYKEWSAAGPP 100
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 19-98 1.10e-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: 54.99  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327  19 RELAVLDIRAAED-----VGYASPLFVANLPVDRLEAEIDRfIPRPVVRTVLVDDGKGSAKQAAERLAAKGWTDIHFLRG 93
Cdd:cd01529   11 PGTALLDVRAEDEyaaghLPGKRSIPGAALVLRSQELQALE-APGRATRYVLTCDGSLLARFAAQELLALGGKPVALLDG 89


                 ....*
gi 490580327  94 GIPAW 98
Cdd:cd01529   90 GTSAW 94
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 134-308 1.59e-09

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 57.88  E-value: 1.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 134 LKAWQEAgEDVVILDTRTLP-----EYEKEHVPGAIAVPgaeLLLRFSD-------LVPSPK--------------TRVV 187
Cdd:COG2897    1 LAAHLDD-PDVVILDVRWDLpdgraAYEAGHIPGAVFLD---LDTDLSDprspgrhPLPSPEafaallgalgisndTTVV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 188 V-SCAGLPRAILGAQTLIDAGVEnDVSYLHDGTRGWTDDGFELETG-PSRTYSHVSAnakeiaearlkafsRDDDLLFID 265
Cdd:COG2897   77 VyDDGGGLFAARAWWLLRYAGHE-DVRVLDGGLAAWKAAGLPLETGpPTPAPGDFTA--------------RPDPELLAD 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490580327 266 RPTAETWLKDPSRTtyFLDVRTPEEF--ETS-------HLQGSISSEGGQLL 308
Cdd:COG2897  142 ADEVLAALGDPDAV--LVDARSPERYrgEVEpidpragHIPGAVNLPWTDLL 191
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 11-98 5.63e-09

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: 52.69  E-value: 5.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327  11 LIEWLrDGRELAVLDIRAAEDVGYASPLFVANLPVDRLEAEIDRFIPRPVVRTVLVDDGKGSAKQAAERLAAKGWTDIHF 90
Cdd:cd00158    2 LKELL-DDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYN 80


                 ....*...
gi 490580327  91 LRGGIPAW 98
Cdd:cd00158   81 LEGGMLAW 88
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 268-345 8.98e-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: 52.29  E-value: 8.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 268 TAETWLKDPSRTTYFLDVRTPEEFETSHLQGSISSEGGQL-LGVAYRTIA---VRGARVILVDDlLGARARVVAHWLKRR 343
Cdd:cd01529    1 LLADWLGEHEPGTALLDVRAEDEYAAGHLPGKRSIPGAALvLRSQELQALeapGRATRYVLTCD-GSLLARFAAQELLAL 79


                 ..
gi 490580327 344 GF 345
Cdd:cd01529   80 GG 81
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 264-351 1.88e-08

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: 51.89  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 264 IDRPTAETWLKDPSrtTYFLDVRTPEEFETSHLQGSISSEGGQLlgvAYRTIAV-RGARVILVDDlLGARARVVAHWLKR 342
Cdd:COG0607    6 ISPAELAELLESED--AVLLDVREPEEFAAGHIPGAINIPLGEL---AERLDELpKDKPIVVYCA-SGGRSAQAAALLRR 79


                 ....*....
gi 490580327 343 RGFEIALHL 351
Cdd:COG0607   80 AGYTNVYNL 88
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 136-229 3.33e-08

Member of the Rhodanese Homology Domain superfamily. This CD includes the putative rhodanese-like protein, Psp2, of Yersinia pestis biovar Medievalis and other similar uncharacterized proteins.


Pssm-ID: 238779 [Multi-domain]  Cd Length: 110  Bit Score: 51.20  E-value: 3.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 136 AWQEAGEDVVILDTRTLPEYEKEHVPGAIAVPGAELLLRFSDLVPSPKTrVVVSCAGlPRAILGAQTLID-AGVENDVSY 214
Cdd:cd01521   18 ALKNGKPDFVLVDVRSAEAYARGHVPGAINLPHREICENATAKLDKEKL-FVVYCDG-PGCNGATKAALKlAELGFPVKE 95

                         90
                 ....*....|....*
gi 490580327 215 LHDGTRGWTDDGFEL 229
Cdd:cd01521   96 MIGGLDWWKREGYAT 110
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 133-224 2.35e-07

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: 48.41  E-value: 2.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 133 ELKAWQEAGEDVVILDTRTLPEYEK--EHVPGAIAVPgaelLLRFSDLVPS-PKTR-VVVSCAGLPRAILGAQTLIDAGV 208
Cdd:cd01444    6 ELAELLAAGEAPVLLDVRDPASYAAlpDHIPGAIHLD----EDSLDDWLGDlDRDRpVVVYCYHGNSSAQLAQALREAGF 81

                         90
                 ....*....|....*.
gi 490580327 209 EnDVSYLHDGTRGWTD 224
Cdd:cd01444   82 T-DVRSLAGGFEAWRR 96
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 268-346 2.78e-07

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 48.06  E-value: 2.78e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490580327 268 TAETWLKDPSrtTYFLDVRTPEEFETSHLQGSISSEGGQLLGVAYRTIAVRGARVILVDDlLGARARVVAHWLKRRGFE 346
Cdd:cd00158    1 ELKELLDDED--AVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCR-SGNRSARAAKLLRKAGGT 76
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 64-190 4.83e-07

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 50.56  E-value: 4.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327  64 VLVDDGKGSAkqAAeRLAakgWT-------DIHFLRGGIPAWIEGG--VEALPTfDIPGVPFVQKVRSEkntPVVFAREL 134
Cdd:COG2897   76 VVYDDGGGLF--AA-RAW---WLlryagheDVRVLDGGLAAWKAAGlpLETGPP-TPAPGDFTARPDPE---LLADADEV 145

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490580327 135 KAWQEAGeDVVILDTRTLPEY--EKE-------HVPGAIAVPGAELL-----------LR--FSDLVPSPKTRVVVSC 190
Cdd:COG2897  146 LAALGDP-DAVLVDARSPERYrgEVEpidpragHIPGAVNLPWTDLLdedgtfksaeeLRalFAALGIDPDKPVITYC 222
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 5-98 6.48e-07

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: 46.87  E-value: 6.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327   5 AVTKDRLIEWLRDGRELAVLDIRAAEDvgYASP-------LFVANLPVDRLEAEIDRfiPRPVVrtVLVDDGKgSAKQAA 77
Cdd:cd01444    1 RISVDELAELLAAGEAPVLLDVRDPAS--YAALpdhipgaIHLDEDSLDDWLGDLDR--DRPVV--VYCYHGN-SSAQLA 73

                         90       100
                 ....*....|....*....|.
gi 490580327  78 ERLAAKGWTDIHFLRGGIPAW 98
Cdd:cd01444   74 QALREAGFTDVRSLAGGFEAW 94
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 131-224 2.82e-06

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: 45.56  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 131 ARELKAWQEAGEDVVILDTRTLPEYEKEHVPGAIAVPG----AELLLRFSDLVPSPKT--RVVVSCAGLPRAILGAQTLI 204
Cdd:cd01523    3 PEDLYARLLAGQPLFILDVRNESDYERWKIDGENNTPYfdpyFDFLEIEEDILDQLPDdqEVTVICAKEGSSQFVAELLA 82

                         90       100
                 ....*....|....*....|
gi 490580327 205 DAGVenDVSYLHDGTRGWTD 224
Cdd:cd01523   83 ERGY--DVDYLAGGMKAWSE 100
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 141-191 3.16e-06

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: 44.95  E-value: 3.16e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490580327 141 GEDVVILDTRTLPEYEKEHVPGAIAVPGAELLLRFSDLvPSPKTrVVVSCA 191
Cdd:cd01524   11 ADGVTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNEL-PKDKE-IIVYCA 59
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 131-209 1.26e-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: 43.23  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 131 ARELKAWQEAGE-DVVILDTRTLPEYEKEHVPGAIAVPGAELLLRFSDLVPSPKTRVVVSCAGLPRAILGAQTLIDAGVE 209
Cdd:cd01534    3 AAELARWAAEGDrTVYRFDVRTPEEYEAGHLPGFRHTPGGQLVQETDHFAPVRGARIVLADDDGVRADMTASWLAQMGWE 82
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 17-98 1.64e-05

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: 42.86  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327   17 DGRELAVLDIRAAEDvgYAS---------PLFVANLPVDRLEAEIDRFIPRPVVRTVLV-DDGKGSAKQAAERLAAKGWT 86
Cdd:pfam00581   2 EDGKVVLIDVRPPEE--YAKghipgavnvPLSSLSLPPLPLLELLEKLLELLKDKPIVVyCNSGNRAAAAAALLKALGYK 79

                          90
                  ....*....|..
gi 490580327   87 DIHFLRGGIPAW 98
Cdd:pfam00581  80 NVYVLDGGFEAW 91
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 104-224 5.88e-05

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 44.48  E-value: 5.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 104 EALPTFDIPGVPFVQKVRSEKNTPVVFARE---LKAWQEAGEDVVILDTRTLPEYEKEHVPGAIAVPGAELLlrfSDLVP 180
Cdd:PRK05597 232 EYIPVVGNPAVLERVRGSTPVHGISGGFGEvldVPRVSALPDGVTLIDVREPSEFAAYSIPGAHNVPLSAIR---EGANP 308

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 490580327 181 ---SPKTRVVVSCAGLPRAILGAQTLIDAGVENDVSyLHDGTRGWTD 224
Cdd:PRK05597 309 psvSAGDEVVVYCAAGVRSAQAVAILERAGYTGMSS-LDGGIEGWLD 354
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 131-172 5.97e-05

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 44.70  E-value: 5.97e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 490580327 131 ARELKAWQEAGEDVVILDTRTLPEYEKEHVPGAIAVPGAELL 172
Cdd:PRK07878 291 PRELKEWLDSGKKIALIDVREPVEWDIVHIPGAQLIPKSEIL 332
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 6-100 9.77e-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: 40.91  E-value: 9.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327   6 VTKDRLIEWLRDG-RELAVLDIRAAEDvgYAS---PLFVaNLPVDRLEAEIDRFIPRPVVRTVLVDDGKGSAKQAAERLA 81
Cdd:cd01534    1 IGAAELARWAAEGdRTVYRFDVRTPEE--YEAghlPGFR-HTPGGQLVQETDHFAPVRGARIVLADDDGVRADMTASWLA 77

                         90
                 ....*....|....*....
gi 490580327  82 AKGWtDIHFLRGGIPAWIE 100
Cdd:cd01534   78 QMGW-EVYVLEGGLAAALA 95
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 272-346 1.24e-04

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: 40.84  E-value: 1.24e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490580327 272 WLKDPSRTTYFLDVRTPEEFETSHLQGSISSEGGQLLGVAYRTIAVRGARVILVDDLLGARARVVAHWLKRRGFE 346
Cdd:cd01528   10 WLADEREEPVLIDVREPEELEIAFLPGFLHLPMSEIPERSKELDSDNPDKDIVVLCHHGGRSMQVAQWLLRQGFE 84
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 147-210 4.76e-04

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 39.06  E-value: 4.76e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490580327 147 LDTRTLPEYEKEHVPGAIAVPGAELLLRFSDLVPSPKTRVVVSCAGLPRAILGAQTLIDAGVEN 210
Cdd:PRK10287  24 IDVRVPEQYQQEHVQGAINIPLKEVKERIATAVPDKNDTVKLYCNAGRQSGQAKEILSEMGYTH 87
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 132-214 4.96e-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: 39.18  E-value: 4.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 132 RELKAWQEAGEDVVILDTRTLPEYEKEHVPGAIAVP-----------GAELLLRFSDLVPSPKTRVVVSCAGLPRAILGA 200
Cdd:cd01519    4 EEVKNLPNPHPNKVLIDVREPEELKTGKIPGAINIPlsslpdalalsEEEFEKKYGFPKPSKDKELIFYCKAGVRSKAAA 83

                         90
                 ....*....|....
gi 490580327 201 QTLIDAGVENDVSY 214
Cdd:cd01519   84 ELARSLGYENVGNY 97
4RHOD_Repeat_4 cd01535
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative ...
 134-235 6.24e-04

Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 4th repeat which, in general, contains the putative catalytic Cys residue.


Pssm-ID: 238793 [Multi-domain]  Cd Length: 145  Bit Score: 39.80  E-value: 6.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 134 LKAWQEAGEDVVILDTRTLPEYEKEHVPGAIAVPGAELLLRFSDLVPSPKTRVVVSCAGLPR-AILGAQTLIDAgvenDV 212
Cdd:cd01535    2 LAAWLGEGGQTAVVDVTASANYVKRHIPGAWWVLRAQLAQALEKLPAAERYVLTCGSSLLARfAAADLAALTVK----PV 77

                         90       100
                 ....*....|....*....|...
gi 490580327 213 SYLHDGTRGWTDDGFELETGPSR 235
Cdd:cd01535   78 FVLEGGTAAWIAAGLPVESGETR 100
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 131-222 7.15e-04

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: 38.53  E-value: 7.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 131 ARELKAW-QEAGEDVVILDTRTLPEYEKEHVPGAIAVPGAELLLRFSDLV-PSPKTRVVVSCAGLPRAILGAQTLIDAGV 208
Cdd:cd01528    4 VAELAEWlADEREEPVLIDVREPEELEIAFLPGFLHLPMSEIPERSKELDsDNPDKDIVVLCHHGGRSMQVAQWLLRQGF 83

                         90
                 ....*....|....
gi 490580327 209 ENdVSYLHDGTRGW 222
Cdd:cd01528   84 EN-VYNLQGGIDAW 96
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 6-100 1.13e-03

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: 37.86  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327   6 VTKDRLIEWLRDGRELAVLDIRAAEDVG-------YASPLFVanLPVDRLEAEIDRFIPRPVVRTVLVDDGKGSAKQ-AA 77
Cdd:cd01523    1 LDPEDLYARLLAGQPLFILDVRNESDYErwkidgeNNTPYFD--PYFDFLEIEEDILDQLPDDQEVTVICAKEGSSQfVA 78

                         90       100
                 ....*....|....*....|...
gi 490580327  78 ERLAAKGWtDIHFLRGGIPAWIE 100
Cdd:cd01523   79 ELLAERGY-DVDYLAGGMKAWSE 100
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 126-198 1.13e-03

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: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 126 TPVVFARELKawqEAGEDVVILDTRTLPEYEKEHVPGAIAVPGAELLLR--------FSDLVPSPKTRVVVScAGLPRAI 197
Cdd:cd01446    3 DCAWLAALLR---EGGERLLLLDCRPFLEYSSSHIRGAVNVCCPTILRRrlqggkilLQQLLSCPEDRDRLR-RGESLAV 78


                 .
gi 490580327 198 L 198
Cdd:cd01446   79 V 79
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 282-351 1.55e-03

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: 37.46  E-value: 1.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490580327  282 FLDVRTPEEFETSHLQGSI-------SSEGGQLLGVAYRTIA-VRGARVILVDDlLGARARVVAHWLKRRGFEIALHL 351
Cdd:pfam00581   8 LIDVRPPEEYAKGHIPGAVnvplsslSLPPLPLLELLEKLLElLKDKPIVVYCN-SGNRAAAAAALLKALGYKNVYVL 84
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 131-222 1.96e-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: 37.78  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 131 ARELKAW-QEAGEDVVILDTRTlPEYEKEHVPGAIAVPGAELLLRFSDLV----PSPKTRVVVSCAGL----PRAILGAQ 201
Cdd:cd01531    6 PAQLKGWiRNGRPPFQVVDVRD-EDYAGGHIKGSWHYPSTRFKAQLNQLVqllsGSKKDTVVFHCALSqvrgPSAARKFL 84

                         90       100
                 ....*....|....*....|....*
gi 490580327 202 TLIDAGVEND----VSYLHDGTRGW 222
Cdd:cd01531   85 RYLDEEDLETskfeVYVLHGGFNAW 109
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 129-190 2.10e-03

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: 37.61  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327 129 VFARELKAWQEAGeDVVILDTRTLPEYEKE-----------HVPGAIAVP-------------GAELLLRFSDLVPSPKT 184
Cdd:cd01449    1 VTAEEVLANLDSG-DVQLVDARSPERFRGEvpeprpglrsgHIPGAVNIPwtslldedgtfksPEELRALFAALGITPDK 79


                 ....*.
gi 490580327 185 RVVVSC 190
Cdd:cd01449   80 PVIVYC 85
4RHOD_Repeat_4 cd01535
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative ...
 11-120 3.92e-03

Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 4th repeat which, in general, contains the putative catalytic Cys residue.


Pssm-ID: 238793 [Multi-domain]  Cd Length: 145  Bit Score: 37.49  E-value: 3.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327  11 LIEWLRDGRELAVLDIRAAEDvgYASplfvANLP------VDRLEAEIDRfIPrPVVRTVLVDDGKGSAKQAAERLAAKG 84
Cdd:cd01535    2 LAAWLGEGGQTAVVDVTASAN--YVK----RHIPgawwvlRAQLAQALEK-LP-AAERYVLTCGSSLLARFAAADLAALT 73

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490580327  85 WTDIHFLRGGIPAWIEGGveaLPTFDIPGVPFVQKV 120
Cdd:cd01535   74 VKPVFVLEGGTAAWIAAG---LPVESGETRLASPRI 106
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
2-102 5.11e-03

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 38.45  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327   2 SVFAVTKDRLIEWLRDGreLAVLDIRAAEDvgYASPLFVANLPVDR--LEAEIDRFIP---RPVVrtVLVDDGKGSAkQA 76
Cdd:PRK08762   1 SIREISPAEARARAAQG--AVLIDVREAHE--RASGQAEGALRIPRgfLELRIETHLPdrdREIV--LICASGTRSA-HA 73

                         90       100
                 ....*....|....*....|....*.
gi 490580327  77 AERLAAKGWTDIHFLRGGIPAWIEGG 102
Cdd:PRK08762  74 AATLRELGYTRVASVAGGFSAWKDAG 99
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 282-353 5.43e-03

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: 35.90  E-value: 5.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580327   282 FLDVRTPEEFETSHLQGSI-------SSEGGQLLGVAYRTIAVR-----GARVILVDDlLGARARVVAHWLKRRGFEIAL 349
Cdd:smart00450   7 LLDVRSPEEYEGGHIPGAVniplselLDRRGELDILEFEELLKRlgldkDKPVVVYCR-SGNRSAKAAWLLRELGFKNVY 85


                   ....
gi 490580327   350 HLHD 353
Cdd:smart00450  86 LLDG 89
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
113-167 9.60e-03

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 37.79  E-value: 9.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490580327 113 GVPFVQKVRSEK--NTPVVFARELKAWQEAG-EDVVILDTRTLPEYEKEHVPGAIAVP 167
Cdd:PRK07411 266 GIPQAKAAEAAQkaEIPEMTVTELKALLDSGaDDFVLIDVRNPNEYEIARIPGSVLVP 323
 
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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