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Conserved domains on  [gi|1002239233|ref|XP_015623850|]
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rhodanese-like domain-containing protein 11, chloroplastic [Oryza sativa Japonica Group]

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]; ...
 87-225 4.33e-17

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: 75.00  E-value: 4.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239233  87 KIKTLTPREAGYTFKLTDKVLLDVRPSNERQKAWVKGSTWIPVFDVDTSFDlggagkkftnyvmggwwsgsstmtvnknf 166
Cdd:COG0607     2 SVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLD----------------------------- 52

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002239233 167 vqqveeKFSKDTDIIVVCQKGLRSLAACEQLYGAGFQNLFWVQGGLEAAEEEDFEREGP 225
Cdd:COG0607    53 ------ELPKDKPIVVYCASGGRSAQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVEKG 105
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 87-225 4.33e-17

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: 75.00  E-value: 4.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239233  87 KIKTLTPREAGYTFKLTDKVLLDVRPSNERQKAWVKGSTWIPVFDVDTSFDlggagkkftnyvmggwwsgsstmtvnknf 166
Cdd:COG0607     2 SVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLD----------------------------- 52

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002239233 167 vqqveeKFSKDTDIIVVCQKGLRSLAACEQLYGAGFQNLFWVQGGLEAAEEEDFEREGP 225
Cdd:COG0607    53 ------ELPKDKPIVVYCASGGRSAQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVEKG 105
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 106-214 8.81e-14

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: 65.78  E-value: 8.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239233 106 VLLDVRPSNERQKAWVKGSTWIPVFDVDTsfdlggagkkftnyvmggwwsgsstmtvnknfvQQVEEKFSKDTDIIVVCQ 185
Cdd:cd00158    12 VLLDVREPEEYAAGHIPGAINIPLSELEE---------------------------------RAALLELDKDKPIVVYCR 58

                          90       100
                  ....*....|....*....|....*....
gi 1002239233 186 KGLRSLAACEQLYGAGFQNLFWVQGGLEA 214
Cdd:cd00158    59 SGNRSARAAKLLRKAGGTNVYNLEGGMLA 87
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 104-221 1.53e-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: 54.39  E-value: 1.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239233  104 DKVLLDVRPSNERQKAWVKGSTWIPVFDVDTSFDLGGAGKkftnyvmggwwsgsstmtvnkNFVQQVEEKFSKDTDIIVV 183
Cdd:smart00450   4 KVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILE---------------------FEELLKRLGLDKDKPVVVY 62

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1002239233  184 CQKGLRSLAACEQLYGAGFQNLFWVQGGLEAAEEEDFE 221
Cdd:smart00450  63 CRSGNRSAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 106-214 1.25e-07

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: 48.63  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239233 106 VLLDVRPSNERQKAWVKGSTWIPVfdvdtsfdlggagkkftnyvmggwwsgSSTMTVNKNFVQQVEE--KFSKDTDIIVV 183
Cdd:pfam00581   7 VLIDVRPPEEYAKGHIPGAVNVPL---------------------------SSLSLPPLPLLELLEKllELLKDKPIVVY 59

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1002239233 184 CQKGLRSLAACEQLYGAGFQNLFWVQGGLEA 214
Cdd:pfam00581  60 CNSGNRAAAAAALLKALGYKNVYVLDGGFEA 90
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
88-226 6.80e-07

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 50.01  E-value: 6.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239233  88 IKTLTPREAgYTFKLTDKVLLDVRPSNERQKAWVKGSTWIPvfdvdtsfdlggagkkftnyvmggwwsgsstmtvnKNFV 167
Cdd:PRK08762    2 IREISPAEA-RARAAQGAVLIDVREAHERASGQAEGALRIP-----------------------------------RGFL 45

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002239233 168 Q-QVEEKF-SKDTDIIVVCQKGLRSLAACEQLYGAGFQNLFWVQGGLEAAEEEDFEREGPQ 226
Cdd:PRK08762   46 ElRIETHLpDRDREIVLICASGTRSAHAAATLRELGYTRVASVAGGFSAWKDAGLPLERPR 106
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 87-225 4.33e-17

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: 75.00  E-value: 4.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239233  87 KIKTLTPREAGYTFKLTDKVLLDVRPSNERQKAWVKGSTWIPVFDVDTSFDlggagkkftnyvmggwwsgsstmtvnknf 166
Cdd:COG0607     2 SVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLD----------------------------- 52

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002239233 167 vqqveeKFSKDTDIIVVCQKGLRSLAACEQLYGAGFQNLFWVQGGLEAAEEEDFEREGP 225
Cdd:COG0607    53 ------ELPKDKPIVVYCASGGRSAQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVEKG 105
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 106-214 8.81e-14

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: 65.78  E-value: 8.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239233 106 VLLDVRPSNERQKAWVKGSTWIPVFDVDTsfdlggagkkftnyvmggwwsgsstmtvnknfvQQVEEKFSKDTDIIVVCQ 185
Cdd:cd00158    12 VLLDVREPEEYAAGHIPGAINIPLSELEE---------------------------------RAALLELDKDKPIVVYCR 58

                          90       100
                  ....*....|....*....|....*....
gi 1002239233 186 KGLRSLAACEQLYGAGFQNLFWVQGGLEA 214
Cdd:cd00158    59 SGNRSARAAKLLRKAGGTNVYNLEGGMLA 87
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 104-221 1.53e-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: 54.39  E-value: 1.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239233  104 DKVLLDVRPSNERQKAWVKGSTWIPVFDVDTSFDLGGAGKkftnyvmggwwsgsstmtvnkNFVQQVEEKFSKDTDIIVV 183
Cdd:smart00450   4 KVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILE---------------------FEELLKRLGLDKDKPVVVY 62

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1002239233  184 CQKGLRSLAACEQLYGAGFQNLFWVQGGLEAAEEEDFE 221
Cdd:smart00450  63 CRSGNRSAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 106-214 1.25e-07

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: 48.63  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239233 106 VLLDVRPSNERQKAWVKGSTWIPVfdvdtsfdlggagkkftnyvmggwwsgSSTMTVNKNFVQQVEE--KFSKDTDIIVV 183
Cdd:pfam00581   7 VLIDVRPPEEYAKGHIPGAVNVPL---------------------------SSLSLPPLPLLELLEKllELLKDKPIVVY 59

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1002239233 184 CQKGLRSLAACEQLYGAGFQNLFWVQGGLEA 214
Cdd:pfam00581  60 CNSGNRAAAAAALLKALGYKNVYVLDGGFEA 90
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 159-224 4.20e-07

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: 47.71  E-value: 4.20e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002239233 159 TMTVNKNFVQQVEEKFSKDTDIIVVCQKGLRSLAACEQLYGAGFQNLFWVQGGLEAAEEEDFEREG 224
Cdd:cd01522    46 DMEINPNFLAELEEKVGKDRPVLLLCRSGNRSIAAAEAAAQAGFTNVYNVLEGFEGDLDAAGHRGG 111
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
88-226 6.80e-07

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 50.01  E-value: 6.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239233  88 IKTLTPREAgYTFKLTDKVLLDVRPSNERQKAWVKGSTWIPvfdvdtsfdlggagkkftnyvmggwwsgsstmtvnKNFV 167
Cdd:PRK08762    2 IREISPAEA-RARAAQGAVLIDVREAHERASGQAEGALRIP-----------------------------------RGFL 45

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002239233 168 Q-QVEEKF-SKDTDIIVVCQKGLRSLAACEQLYGAGFQNLFWVQGGLEAAEEEDFEREGPQ 226
Cdd:PRK08762   46 ElRIETHLpDRDREIVLICASGTRSAHAAATLRELGYTRVASVAGGFSAWKDAGLPLERPR 106
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 106-214 1.84e-05

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: 42.77  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002239233 106 VLLDVRPSNERQKAWVKGSTWIPVFDVDTsfdlggagkkftnyvmggwWSGSSTmtvnknfvqqveeKFSKDTDIIVVCQ 185
Cdd:cd01528    19 VLIDVREPEELEIAFLPGFLHLPMSEIPE-------------------RSKELD-------------SDNPDKDIVVLCH 66

                          90       100
                  ....*....|....*....|....*....
gi 1002239233 186 KGLRSLAACEQLYGAGFQNLFWVQGGLEA 214
Cdd:cd01528    67 HGGRSMQVAQWLLRQGFENVYNLQGGIDA 95
PLN02160 PLN02160
thiosulfate sulfurtransferase
 163-211 7.99e-05

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 41.61  E-value: 7.99e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002239233 163 NKNFVQQVEEKFSKDTDIIVVCQKGLRSLAACEQLYGAGFQNLFWVQGG 211
Cdd:PLN02160   67 NQEFLEQVSSLLNPADDILVGCQSGARSLKATTELVAAGYKKVRNKGGG 115
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 167-214 2.05e-03

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: 36.86  E-value: 2.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1002239233 167 VQQVEEKFSKDTDIIVVCQKGLRSLAACEQLYGAGFQNLFWVQGGLEA 214
Cdd:cd01444    46 LDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAGFTDVRSLAGGFEA 93
 
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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