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Conserved domains on  [gi|145360051|ref|NP_565426|]
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Rhodanese/Cell cycle control phosphatase superfamily protein [Arabidopsis thaliana]

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 ...
 24-150 1.12e-44

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 PLN02160:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 136  Bit Score: 143.30  E-value: 1.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  24 TTSMSEPKVITIDVNQAQKLLDSGYTFLDVRTVEEFKKGHVDSENVFNVPYWLYTPQGQEINPNFLKHVSSLCNQTDHLI 103
Cdd:PLN02160   6 SSSTKAEEVVSVDVSQAKTLLQSGHQYLDVRTQDEFRRGHCEAAKIVNIPYMLNTPQGRVKNQEFLEQVSSLLNPADDIL 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 145360051 104 LGCKSGVRSLHATKFLVSSGFKTVRNMDGGYIAWVNKRFPVKVEHKE 150
Cdd:PLN02160  86 VGCQSGARSLKATTELVAAGYKKVRNKGGGYLAWVDHSFPINQEEEE 132
 
Name Accession Description Interval E-value
PLN02160 PLN02160
thiosulfate sulfurtransferase
 24-150 1.12e-44

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 143.30  E-value: 1.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  24 TTSMSEPKVITIDVNQAQKLLDSGYTFLDVRTVEEFKKGHVDSENVFNVPYWLYTPQGQEINPNFLKHVSSLCNQTDHLI 103
Cdd:PLN02160   6 SSSTKAEEVVSVDVSQAKTLLQSGHQYLDVRTQDEFRRGHCEAAKIVNIPYMLNTPQGRVKNQEFLEQVSSLLNPADDIL 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 145360051 104 LGCKSGVRSLHATKFLVSSGFKTVRNMDGGYIAWVNKRFPVKVEHKE 150
Cdd:PLN02160  86 VGCQSGARSLKATTELVAAGYKKVRNKGGGYLAWVDHSFPINQEEEE 132
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 45-143 1.82e-21

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: 82.89  E-value: 1.82e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051    45 DSGYTFLDVRTVEEFKKGHVDSENVFNVPYWLYTPQGQEINPNFLKHVSSLCNQTDHLILGCKSGVRSLHATKFLVSSGF 124
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81

                           90
                   ....*....|....*....
gi 145360051   125 KTVRNMDGGYIAWVNKRFP 143
Cdd:smart00450  82 KNVYLLDGGYKEWSAAGPP 100
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 34-145 1.89e-21

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: 83.09  E-value: 1.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  34 TIDVNQAQKLLDS-GYTFLDVRTVEEFKKGHVdsENVFNVPYwlytpqgqeinPNFLKHVSSLcNQTDHLILGCKSGVRS 112
Cdd:COG0607    5 EISPAELAELLESeDAVLLDVREPEEFAAGHI--PGAINIPL-----------GELAERLDEL-PKDKPIVVYCASGGRS 70

                         90       100       110
                 ....*....|....*....|....*....|...
gi 145360051 113 LHATKFLVSSGFKTVRNMDGGYIAWVNKRFPVK 145
Cdd:COG0607   71 AQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVE 103
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 40-138 3.41e-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.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 76.95  E-value: 3.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  40 AQKLLDSGYTFLDVRTVEEFKKGHVdsENVFNVPYwlytpqgqeinPNFLKHVSSL-CNQTDHLILGCKSGVRSLHATKF 118
Cdd:cd00158    3 KELLDDEDAVLLDVREPEEYAAGHI--PGAINIPL-----------SELEERAALLeLDKDKPIVVYCRSGNRSARAAKL 69

                         90       100
                 ....*....|....*....|
gi 145360051 119 LVSSGFKTVRNMDGGYIAWV 138
Cdd:cd00158   70 LRKAGGTNVYNLEGGMLAWK 89
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 45-138 6.68e-17

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: 70.98  E-value: 6.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051   45 DSGYTFLDVRTVEEFKKGHVdsENVFNVPYWLYTPQGQEINPNFLKHVSSLCNqtDHLILGCKSGVRSLHATKFLVSSGF 124
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHI--PGAVNVPLSSLSLPPLPLLELLEKLLELLKD--KPIVVYCNSGNRAAAAAALLKALGY 78

                          90
                  ....*....|....
gi 145360051  125 KTVRNMDGGYIAWV 138
Cdd:pfam00581  79 KNVYVLDGGFEAWK 92
 
Name Accession Description Interval E-value
PLN02160 PLN02160
thiosulfate sulfurtransferase
 24-150 1.12e-44

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 143.30  E-value: 1.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  24 TTSMSEPKVITIDVNQAQKLLDSGYTFLDVRTVEEFKKGHVDSENVFNVPYWLYTPQGQEINPNFLKHVSSLCNQTDHLI 103
Cdd:PLN02160   6 SSSTKAEEVVSVDVSQAKTLLQSGHQYLDVRTQDEFRRGHCEAAKIVNIPYMLNTPQGRVKNQEFLEQVSSLLNPADDIL 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 145360051 104 LGCKSGVRSLHATKFLVSSGFKTVRNMDGGYIAWVNKRFPVKVEHKE 150
Cdd:PLN02160  86 VGCQSGARSLKATTELVAAGYKKVRNKGGGYLAWVDHSFPINQEEEE 132
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 45-143 1.82e-21

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: 82.89  E-value: 1.82e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051    45 DSGYTFLDVRTVEEFKKGHVDSENVFNVPYWLYTPQGQEINPNFLKHVSSLCNQTDHLILGCKSGVRSLHATKFLVSSGF 124
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81

                           90
                   ....*....|....*....
gi 145360051   125 KTVRNMDGGYIAWVNKRFP 143
Cdd:smart00450  82 KNVYLLDGGYKEWSAAGPP 100
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 34-145 1.89e-21

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: 83.09  E-value: 1.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  34 TIDVNQAQKLLDS-GYTFLDVRTVEEFKKGHVdsENVFNVPYwlytpqgqeinPNFLKHVSSLcNQTDHLILGCKSGVRS 112
Cdd:COG0607    5 EISPAELAELLESeDAVLLDVREPEEFAAGHI--PGAINIPL-----------GELAERLDEL-PKDKPIVVYCASGGRS 70

                         90       100       110
                 ....*....|....*....|....*....|...
gi 145360051 113 LHATKFLVSSGFKTVRNMDGGYIAWVNKRFPVK 145
Cdd:COG0607   71 AQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVE 103
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 40-138 3.41e-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.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 76.95  E-value: 3.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  40 AQKLLDSGYTFLDVRTVEEFKKGHVdsENVFNVPYwlytpqgqeinPNFLKHVSSL-CNQTDHLILGCKSGVRSLHATKF 118
Cdd:cd00158    3 KELLDDEDAVLLDVREPEEYAAGHI--PGAINIPL-----------SELEERAALLeLDKDKPIVVYCRSGNRSARAAKL 69

                         90       100
                 ....*....|....*....|
gi 145360051 119 LVSSGFKTVRNMDGGYIAWV 138
Cdd:cd00158   70 LRKAGGTNVYNLEGGMLAWK 89
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 45-138 6.68e-17

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: 70.98  E-value: 6.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051   45 DSGYTFLDVRTVEEFKKGHVdsENVFNVPYWLYTPQGQEINPNFLKHVSSLCNqtDHLILGCKSGVRSLHATKFLVSSGF 124
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHI--PGAVNVPLSSLSLPPLPLLELLEKLLELLKD--KPIVVYCNSGNRAAAAAALLKALGY 78

                          90
                  ....*....|....
gi 145360051  125 KTVRNMDGGYIAWV 138
Cdd:pfam00581  79 KNVYVLDGGFEAWK 92
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
35-146 4.66e-13

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 65.03  E-value: 4.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  35 IDVNQAQKLLDSGYTFLDVRTVEEFKKGHVdsenvfnvPYWLYTPQGQ-EINPNflkhvSSLCNQTDHLILGCKSGVRSL 113
Cdd:PRK08762   5 ISPAEARARAAQGAVLIDVREAHERASGQA--------EGALRIPRGFlELRIE-----THLPDRDREIVLICASGTRSA 71

                         90       100       110
                 ....*....|....*....|....*....|...
gi 145360051 114 HATKFLVSSGFKTVRNMDGGYIAWVNKRFPVKV 146
Cdd:PRK08762  72 HAAATLRELGYTRVASVAGGFSAWKDAGLPLER 104
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 50-134 2.74e-11

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: 56.95  E-value: 2.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  50 FLDVRTVEEFKK-GHV-DSENVfnvpYWLYTPqGQEINPNFLKHVSSLCNQTDHLILGCKSGVRSLHATKFLVSSGFKTV 127
Cdd:cd01522   18 LVDVRTEAEWKFvGGVpDAVHV----AWQVYP-DMEINPNFLAELEEKVGKDRPVLLLCRSGNRSIAAAEAAAQAGFTNV 92


                 ....*..
gi 145360051 128 RNMDGGY 134
Cdd:cd01522   93 YNVLEGF 99
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 35-137 4.00e-11

Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as a polysulfide binding and transferase domain in anaerobic gram-negative bacteria, functioning in oxidative phosphorylation with polysulfide-sulfur as a terminal electron acceptor. The active site contains the same conserved cysteine that is the catalytic residue in other Rhodanese Homology Domain proteins.


Pssm-ID: 238724 [Multi-domain]  Cd Length: 103  Bit Score: 56.28  E-value: 4.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  35 IDVNQAQKLL-DSGYTFLDVRTVEEFK-KGHVdsENVFNVP-----YWLyTPQGQEINPNFlkhvsslcNQTDHLILGCK 107
Cdd:cd01447    1 LSPEDARALLgSPGVLLVDVRDPRELErTGMI--PGAFHAPrgmleFWA-DPDSPYHKPAF--------AEDKPFVFYCA 69

                         90       100       110
                 ....*....|....*....|....*....|
gi 145360051 108 SGVRSLHATKFLVSSGFKTVRNMDGGYIAW 137
Cdd:cd01447   70 SGWRSALAGKTLQDMGLKPVYNIEGGFKDW 99
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 35-139 5.24e-09

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: 51.09  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  35 IDVNQAQKLLDSG-YTFLDVRTVEEF-----------KKGHVdsENVFNVPY-WLYTPQGQEINPNFLKHV--SSLCNQT 99
Cdd:cd01449    1 VTAEEVLANLDSGdVQLVDARSPERFrgevpeprpglRSGHI--PGAVNIPWtSLLDEDGTFKSPEELRALfaALGITPD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 145360051 100 DHLILGCKSGVRSLHaTKF-LVSSGFKTVRNMDGGYIAWVN 139
Cdd:cd01449   79 KPVIVYCGSGVTACV-LLLaLELLGYKNVRLYDGSWSEWGS 118
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 34-137 6.08e-09

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: 50.47  E-value: 6.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  34 TIDVNQAQKLLDSG---YTFLDVRTVEEFKKGHvdSENVFNVPYWLYTPQGQEINPNflkhvsslcNQTDHLILGCKSGV 110
Cdd:cd01528    1 QISVAELAEWLADEreePVLIDVREPEELEIAF--LPGFLHLPMSEIPERSKELDSD---------NPDKDIVVLCHHGG 69

                         90       100
                 ....*....|....*....|....*..
gi 145360051 111 RSLHATKFLVSSGFKTVRNMDGGYIAW 137
Cdd:cd01528   70 RSMQVAQWLLRQGFENVYNLQGGIDAW 96
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 47-134 1.40e-08

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: 49.19  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  47 GYTFLDVRTVEEFKKGHVdsENVFNVPYwlytpqgQEINpnflKHVSSLcnQTDHLIL-GCKSGVRSLHATKFLVSSGFK 125
Cdd:cd01524   13 GVTLIDVRTPQEFEKGHI--KGAINIPL-------DELR----DRLNEL--PKDKEIIvYCAVGLRGYIAARILTQNGFK 77


                 ....*....
gi 145360051 126 tVRNMDGGY 134
Cdd:cd01524   78 -VKNLDGGY 85
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 21-137 2.58e-08

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 51.41  E-value: 2.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  21 PRTTTSMSEPKVITIDVNQAQKL--LDSGYTFLDVRTVEEFKKGHVdsENVFNVPYwlytpqgQEINPNflkHVSSLCNQ 98
Cdd:PRK05597 246 VRGSTPVHGISGGFGEVLDVPRVsaLPDGVTLIDVREPSEFAAYSI--PGAHNVPL-------SAIREG---ANPPSVSA 313

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 145360051  99 TDHLILGCKSGVRSLHATKFLVSSGFKTVRNMDGGYIAW 137
Cdd:PRK05597 314 GDEVVVYCAAGVRSAQAVAILERAGYTGMSSLDGGIEGW 352
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 52-138 3.52e-08

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: 48.81  E-value: 3.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  52 DVRTVEEFKKGHVdsENVFNVPYWLYtPQGQEINP-------NFLKHVSSlcnqtDHLILGCKSGVRSLHATKFLVSSGF 124
Cdd:cd01519   20 DVREPEELKTGKI--PGAINIPLSSL-PDALALSEeefekkyGFPKPSKD-----KELIFYCKAGVRSKAAAELARSLGY 91

                         90
                 ....*....|....
gi 145360051 125 KTVRNMDGGYIAWV 138
Cdd:cd01519   92 ENVGNYPGSWLDWA 105
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 34-140 1.25e-06

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 46.62  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  34 TIDVNQAQKLLDSGYTF--LDVRTVEEFKKGHVDSENVFnvpywlytPQGqEINPNflKHVSSLcNQTDHLILGCKSGVR 111
Cdd:PRK07878 288 TITPRELKEWLDSGKKIalIDVREPVEWDIVHIPGAQLI--------PKS-EILSG--EALAKL-PQDRTIVLYCKTGVR 355

                         90       100
                 ....*....|....*....|....*....
gi 145360051 112 SLHATKFLVSSGFKTVRNMDGGYIAWVNK 140
Cdd:PRK07878 356 SAEALAALKKAGFSDAVHLQGGVVAWAKQ 384
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
27-148 4.45e-06

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 43.09  E-value: 4.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  27 MSEPKviTIDVNQAQKLLDSGYTFL-DVRTVEEFKKGHvdsenvfnvpywlyTPQGQEINPNFLkhvSSLCNQTDH---L 102
Cdd:PRK00162   1 MDQFE--CINVEQAHQKLQEGGAVLvDIRDPQSFAMGH--------------APGAFHLTNDSL---GAFMRQADFdtpV 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 145360051 103 ILGCKSGVRSLHATKFLVSSGFKTVRNMDGGYIAWvNKRFPVKVEH 148
Cdd:PRK00162  62 MVMCYHGNSSQGAAQYLLQQGFDVVYSIDGGFEAW-RRTFPAEVAS 106
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 37-139 8.65e-06

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: 42.28  E-value: 8.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  37 VNQAQKLLDSGYTFLDVRTVEEFKKGHVdsenvfnvPYWLYTPQGQEINPNFLKHVSSLCNQTDHLILGCKSGVRSLHAT 116
Cdd:cd01529    2 LADWLGEHEPGTALLDVRAEDEYAAGHL--------PGKRSIPGAALVLRSQELQALEAPGRATRYVLTCDGSLLARFAA 73

                         90       100
                 ....*....|....*....|...
gi 145360051 117 KFLVSSGFKTVRNMDGGYIAWVN 139
Cdd:cd01529   74 QELLALGGKPVALLDGGTSAWVA 96
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
35-137 9.39e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 44.34  E-value: 9.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  35 IDVNQAQKLLDSG---YTFLDVRTVEEFKkghvdsenVFNVPYWLYTPQGQEINPNFLKHVSSLCNQTdHLILGCKSGVR 111
Cdd:PRK07411 284 MTVTELKALLDSGaddFVLIDVRNPNEYE--------IARIPGSVLVPLPDIENGPGVEKVKELLNGH-RLIAHCKMGGR 354

                         90       100
                 ....*....|....*....|....*.
gi 145360051 112 SLHATKFLVSSGFKTVrNMDGGYIAW 137
Cdd:PRK07411 355 SAKALGILKEAGIEGT-NVKGGITAW 379
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 35-137 1.02e-04

Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 3rd repeat which does not contain the putative catalytic Cys residue.


Pssm-ID: 238792 [Multi-domain]  Cd Length: 95  Bit Score: 38.99  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  35 IDVNQAQKLLDSGYT---FLDVRTVEEFKKGHvdsenvfnVPYWLYTPQGQeinpnflkhvssLCNQTDH--------LI 103
Cdd:cd01534    1 IGAAELARWAAEGDRtvyRFDVRTPEEYEAGH--------LPGFRHTPGGQ------------LVQETDHfapvrgarIV 60

                         90       100       110
                 ....*....|....*....|....*....|....
gi 145360051 104 LGCKSGVRSLHATKFLVSSGFKtVRNMDGGYIAW 137
Cdd:cd01534   61 LADDDGVRADMTASWLAQMGWE-VYVLEGGLAAA 93
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 35-143 1.17e-04

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 39.60  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  35 IDVNQAQKLLDSG--YTFLDVRTVEEFKKGHVdsENVFNVPYW-LYTPQGqEINPNFLKHVSSlcNQTDHLILGCKSGVR 111
Cdd:cd01526   10 VSVKDYKNILQAGkkHVLLDVRPKVHFEICRL--PEAINIPLSeLLSKAA-ELKSLQELPLDN--DKDSPIYVVCRRGND 84

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 145360051 112 SLHATKFLVSSGFK-TVRNMDGGYIAW---VNKRFP 143
Cdd:cd01526   85 SQTAVRKLKELGLErFVRDIIGGLKAWadkVDPTFP 120
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 29-139 3.52e-04

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: 3.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  29 EPKVITIDVNQAQKLldsgyTFLDVRTVEEFKKGHVDSENV--FNVPYWlytpqgqeinpNFLKHVSSLCNQ--TDHLIL 104
Cdd:cd01523    2 DPEDLYARLLAGQPL-----FILDVRNESDYERWKIDGENNtpYFDPYF-----------DFLEIEEDILDQlpDDQEVT 65

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 145360051 105 G-CKSGVRSLHATKFLVSSGFkTVRNMDGGYIAWVN 139
Cdd:cd01523   66 ViCAKEGSSQFVAELLAERGY-DVDYLAGGMKAWSE 100
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 33-139 9.44e-03

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 35.15  E-value: 9.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145360051  33 ITIDVNQAQKLLDSG-YTFLDVRTVEEF---------KKGHVDseNVFNVPY-WLYTPQGQEINPNFLKHV--SSLCNQT 99
Cdd:COG2897  138 LLADADEVLAALGDPdAVLVDARSPERYrgevepidpRAGHIP--GAVNLPWtDLLDEDGTFKSAEELRALfaALGIDPD 215

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 145360051 100 DHLILGCKSGVRSLHATKFLVSSGFKTVRNMDGGYIAWVN 139
Cdd:COG2897  216 KPVITYCGSGVRAAHTWLALELLGYPNVRLYDGSWSEWGS 255
 
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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