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Conserved domains on  [gi|544682424|ref|WP_021114438|]
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rhodanese-like domain-containing protein [Glaesserella parasuis]

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 ...
 148-235 5.96e-12

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 cd01448:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 122  Bit Score: 60.71  E-value: 5.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682424 148 ISPEWLYALMQGERpetyhnnqFMLFEVSWGSLEK--AKAY-TQHIVGAYHFDIDWVE-GEAPVY-DLADPQKIEQNLLQ 222
Cdd:cd01448    2 VSPDWLAEHLDDPD--------VRILDARWYLPDRdgRKEYlEGHIPGAVFFDLDEDLdDKSPGPhMLPSPEEFAELLGS 73

                         90
                 ....*....|...
gi 544682424 223 HGITKDKTIVLYS 235
Cdd:cd01448   74 LGISNDDTVVVYD 86
SseA super family cl34515
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 25-101 3.95e-10

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


The actual alignment was detected with superfamily member COG2897:

Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 58.26  E-value: 3.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682424  25 IDTTELLANLDNPDYVIIDSRNDSLYNGFKEKHASRGGHIKGAIQFrcNWFERIEAD-KFDSFAE------AKGISKQKT 97
Cdd:COG2897  140 ADADEVLAALGDPDAVLVDARSPERYRGEVEPIDPRAGHIPGAVNL--PWTDLLDEDgTFKSAEElralfaALGIDPDKP 217


                 ....
gi 544682424  98 LVIY 101
Cdd:COG2897  218 VITY 221
 
Name Accession Description Interval E-value
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 148-235 5.96e-12

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: 60.71  E-value: 5.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682424 148 ISPEWLYALMQGERpetyhnnqFMLFEVSWGSLEK--AKAY-TQHIVGAYHFDIDWVE-GEAPVY-DLADPQKIEQNLLQ 222
Cdd:cd01448    2 VSPDWLAEHLDDPD--------VRILDARWYLPDRdgRKEYlEGHIPGAVFFDLDEDLdDKSPGPhMLPSPEEFAELLGS 73

                         90
                 ....*....|...
gi 544682424 223 HGITKDKTIVLYS 235
Cdd:cd01448   74 LGISNDDTVVVYD 86
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 25-101 3.95e-10

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 58.26  E-value: 3.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682424  25 IDTTELLANLDNPDYVIIDSRNDSLYNGFKEKHASRGGHIKGAIQFrcNWFERIEAD-KFDSFAE------AKGISKQKT 97
Cdd:COG2897  140 ADADEVLAALGDPDAVLVDARSPERYRGEVEPIDPRAGHIPGAVNL--PWTDLLDEDgTFKSAEElralfaALGIDPDKP 217


                 ....
gi 544682424  98 LVIY 101
Cdd:COG2897  218 VITY 221
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 25-102 5.82e-10

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: 55.32  E-value: 5.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682424  25 IDTTELLANLDNPDYVIIDSRNDSLYNGFKEKHAsrGGHIKGAIQFRCNWFE---------RIEADKFDSFAEAKGISKQ 95
Cdd:cd01448    2 VSPDWLAEHLDDPDVRILDARWYLPDRDGRKEYL--EGHIPGAVFFDLDEDLddkspgphmLPSPEEFAELLGSLGISND 79


                 ....*..
gi 544682424  96 KTLVIYD 102
Cdd:cd01448   80 DTVVVYD 86
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 34-121 9.67e-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: 54.03  E-value: 9.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682424   34 LDNPDYVIIDSRNDSLYNGfkekhasrgGHIKGAIQFRCNWFERIEADKFDSFAEAKGISKQKTLVIYDSNPDELACISA 113
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAK---------GHIPGAVNVPLSSLSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAA 71


                  ....*...
gi 544682424  114 EFKAKGYK 121
Cdd:pfam00581  72 LLKALGYK 79
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 166-234 1.34e-09

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 56.72  E-value: 1.34e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544682424 166 HNNQFMLFEVSWGSLEKAKAYTQ-HIVGAYHFDI--DWVEGEAPV-YDLADPQKIEQNLLQHGITKDKTIVLY 234
Cdd:COG2897    6 DDPDVVILDVRWDLPDGRAAYEAgHIPGAVFLDLdtDLSDPRSPGrHPLPSPEAFAALLGALGISNDTTVVVY 78
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 35-102 1.98e-05

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: 42.45  E-value: 1.98e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544682424    35 DNPDYVIIDSRNDSLYNgfkekhasrGGHIKGAIQFRCNWFER----IEADKFDSFAEAKGISKQKTLVIYD 102
Cdd:smart00450   1 NDEKVVLLDVRSPEEYE---------GGHIPGAVNIPLSELLDrrgeLDILEFEELLKRLGLDKDKPVVVYC 63
sseA PRK11493
3-mercaptopyruvate sulfurtransferase; Provisional
 30-103 1.26e-03

3-mercaptopyruvate sulfurtransferase; Provisional


Pssm-ID: 236917 [Multi-domain]  Cd Length: 281  Bit Score: 39.31  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682424  30 LLANLDNPDYVIIDSRNDSLYNGFKEKHAS-RGGHIKGAIQFRcnwferIEA------------DKFDSFAEAK---GIS 93
Cdd:PRK11493  12 LAEHIDDPEIQIIDARMAPPGQEDRDVAAEyRAGHIPGAVFFD------IEAlsdhtsplphmmPRPETFAVAMrelGVN 85

                         90
                 ....*....|
gi 544682424  94 KQKTLVIYDS 103
Cdd:PRK11493  86 QDKHLVVYDE 95
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 189-234 9.58e-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: 34.74  E-value: 9.58e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 544682424   189 HIVGAYHFDIDWVEGEAPVYDladPQKIEQNLLQHGITKDKTIVLY 234
Cdd:smart00450  20 HIPGAVNIPLSELLDRRGELD---ILEFEELLKRLGLDKDKPVVVY 62
 
Name Accession Description Interval E-value
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 148-235 5.96e-12

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: 60.71  E-value: 5.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682424 148 ISPEWLYALMQGERpetyhnnqFMLFEVSWGSLEK--AKAY-TQHIVGAYHFDIDWVE-GEAPVY-DLADPQKIEQNLLQ 222
Cdd:cd01448    2 VSPDWLAEHLDDPD--------VRILDARWYLPDRdgRKEYlEGHIPGAVFFDLDEDLdDKSPGPhMLPSPEEFAELLGS 73

                         90
                 ....*....|...
gi 544682424 223 HGITKDKTIVLYS 235
Cdd:cd01448   74 LGISNDDTVVVYD 86
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 25-101 3.95e-10

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 58.26  E-value: 3.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682424  25 IDTTELLANLDNPDYVIIDSRNDSLYNGFKEKHASRGGHIKGAIQFrcNWFERIEAD-KFDSFAE------AKGISKQKT 97
Cdd:COG2897  140 ADADEVLAALGDPDAVLVDARSPERYRGEVEPIDPRAGHIPGAVNL--PWTDLLDEDgTFKSAEElralfaALGIDPDKP 217


                 ....
gi 544682424  98 LVIY 101
Cdd:COG2897  218 VITY 221
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 25-102 5.82e-10

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: 55.32  E-value: 5.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682424  25 IDTTELLANLDNPDYVIIDSRNDSLYNGFKEKHAsrGGHIKGAIQFRCNWFE---------RIEADKFDSFAEAKGISKQ 95
Cdd:cd01448    2 VSPDWLAEHLDDPDVRILDARWYLPDRDGRKEYL--EGHIPGAVFFDLDEDLddkspgphmLPSPEEFAELLGSLGISND 79


                 ....*..
gi 544682424  96 KTLVIYD 102
Cdd:cd01448   80 DTVVVYD 86
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 34-121 9.67e-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: 54.03  E-value: 9.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682424   34 LDNPDYVIIDSRNDSLYNGfkekhasrgGHIKGAIQFRCNWFERIEADKFDSFAEAKGISKQKTLVIYDSNPDELACISA 113
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAK---------GHIPGAVNVPLSSLSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAA 71


                  ....*...
gi 544682424  114 EFKAKGYK 121
Cdd:pfam00581  72 LLKALGYK 79
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 166-234 1.34e-09

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 56.72  E-value: 1.34e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544682424 166 HNNQFMLFEVSWGSLEKAKAYTQ-HIVGAYHFDI--DWVEGEAPV-YDLADPQKIEQNLLQHGITKDKTIVLY 234
Cdd:COG2897    6 DDPDVVILDVRWDLPDGRAAYEAgHIPGAVFLDLdtDLSDPRSPGrHPLPSPEAFAALLGALGISNDTTVVVY 78
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 30-110 7.08e-09

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 54.80  E-value: 7.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682424  30 LLANLDNPDYVIIDSRNDsLYNGFKEKHAsrgGHIKGAIQFrcNWFERI------------EADKFDSFAEAKGISKQKT 97
Cdd:COG2897    1 LAAHLDDPDVVILDVRWD-LPDGRAAYEA---GHIPGAVFL--DLDTDLsdprspgrhplpSPEAFAALLGALGISNDTT 74

                         90
                 ....*....|...
gi 544682424  98 LVIYDSNPDELAC 110
Cdd:COG2897   75 VVVYDDGGGLFAA 87
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 25-101 1.96e-07

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: 48.40  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682424  25 IDTTELLANLDNPDYVIIDSRNDSLYNGFKE--KHASRGGHIKGAIqfrcNWF---------ERIEADKFDSFAEAKGIS 93
Cdd:cd01449    1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPepRPGLRSGHIPGAV----NIPwtslldedgTFKSPEELRALFAALGIT 76


                 ....*...
gi 544682424  94 KQKTLVIY 101
Cdd:cd01449   77 PDKPVIVY 84
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 22-138 4.21e-07

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: 47.27  E-value: 4.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682424  22 IKKIDTTELLANLDNPDYVIIDSRNDSLYngfkekhasRGGHIKGAIQfrcnwferIEADKFDSFAEAkgISKQKTLVIY 101
Cdd:COG0607    3 VKEISPAELAELLESEDAVLLDVREPEEF---------AAGHIPGAIN--------IPLGELAERLDE--LPKDKPIVVY 63

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 544682424 102 DSNPD--ELACisAEFKAKGYK-VRTFSD-FISYANAGYPL 138
Cdd:COG0607   64 CASGGrsAQAA--ALLRRAGYTnVYNLAGgIEAWKAAGLPV 102
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 29-121 5.25e-06

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: 43.44  E-value: 5.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682424  29 ELLANLDNPDYVIIDSRNDSLYngfkekhasRGGHIKGAIQfrcnwferIEADKFDSFAEAKGISKQKTLVIYDSNpDEL 108
Cdd:cd00158    1 ELKELLDDEDAVLLDVREPEEY---------AAGHIPGAIN--------IPLSELEERAALLELDKDKPIVVYCRS-GNR 62

                         90
                 ....*....|....
gi 544682424 109 ACISAEF-KAKGYK 121
Cdd:cd00158   63 SARAAKLlRKAGGT 76
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 35-102 1.98e-05

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: 42.45  E-value: 1.98e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544682424    35 DNPDYVIIDSRNDSLYNgfkekhasrGGHIKGAIQFRCNWFER----IEADKFDSFAEAKGISKQKTLVIYD 102
Cdd:smart00450   1 NDEKVVLLDVRSPEEYE---------GGHIPGAVNIPLSELLDrrgeLDILEFEELLKRLGLDKDKPVVVYC 63
sseA PRK11493
3-mercaptopyruvate sulfurtransferase; Provisional
 30-103 1.26e-03

3-mercaptopyruvate sulfurtransferase; Provisional


Pssm-ID: 236917 [Multi-domain]  Cd Length: 281  Bit Score: 39.31  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544682424  30 LLANLDNPDYVIIDSRNDSLYNGFKEKHAS-RGGHIKGAIQFRcnwferIEA------------DKFDSFAEAK---GIS 93
Cdd:PRK11493  12 LAEHIDDPEIQIIDARMAPPGQEDRDVAAEyRAGHIPGAVFFD------IEAlsdhtsplphmmPRPETFAVAMrelGVN 85

                         90
                 ....*....|
gi 544682424  94 KQKTLVIYDS 103
Cdd:PRK11493  86 QDKHLVVYDE 95
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 189-234 9.58e-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: 34.74  E-value: 9.58e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 544682424   189 HIVGAYHFDIDWVEGEAPVYDladPQKIEQNLLQHGITKDKTIVLY 234
Cdd:smart00450  20 HIPGAVNIPLSELLDRRGELD---ILEFEELLKRLGLDKDKPVVVY 62
 
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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