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Conserved domains on  [gi|74191856|dbj|BAE32878|]
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unnamed protein product [Mus musculus]

Protein Classification

rhodanese-like domain-containing protein( domain architecture ID 10107410)

rhodanese-like domain-containing protein similar to Mus musculus thiosulfate sulfurtransferase (rhodanese)-like domain containing 3, Saccharomyces cerevisiae mitochondrial thiosulfate sulfurtransferase, and Drosophila melanogaster heat shock protein 67B2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 42-147 3.66e-45

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: 143.56  E-value: 3.66e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856  42 VTYRELKSLLN-SKDIMLIDVRNTLEiLEQGKIPGSINIPLDEVGEALQMNPVDFKEKYCQVKPSKSDRLVFSCLAGVRS 120
Cdd:cd01519   1 YSFEEVKNLPNpHPNKVLIDVREPEE-LKTGKIPGAINIPLSSLPDALALSEEEFEKKYGFPKPSKDKELIFYCKAGVRS 79

                        90       100
                ....*....|....*....|....*..
gi 74191856 121 KKAMDTAISLGFNSAQHYAGGWKEWVT 147
Cdd:cd01519  80 KAAAELARSLGYENVGNYPGSWLDWAA 106
 
Name Accession Description Interval E-value
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 42-147 3.66e-45

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: 143.56  E-value: 3.66e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856  42 VTYRELKSLLN-SKDIMLIDVRNTLEiLEQGKIPGSINIPLDEVGEALQMNPVDFKEKYCQVKPSKSDRLVFSCLAGVRS 120
Cdd:cd01519   1 YSFEEVKNLPNpHPNKVLIDVREPEE-LKTGKIPGAINIPLSSLPDALALSEEEFEKKYGFPKPSKDKELIFYCKAGVRS 79

                        90       100
                ....*....|....*....|....*..
gi 74191856 121 KKAMDTAISLGFNSAQHYAGGWKEWVT 147
Cdd:cd01519  80 KAAAELARSLGYENVGNYPGSWLDWAA 106
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 37-145 4.11e-22

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: 84.63  E-value: 4.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856  37 STPKGVTYRELKSLLNSKDIMLIDVRNTLEIlEQGKIPGSINIPLDEVGEalQMNPVDfkekycqvkpsKSDRLVFSCLA 116
Cdd:COG0607   1 ASVKEISPAELAELLESEDAVLLDVREPEEF-AAGHIPGAINIPLGELAE--RLDELP-----------KDKPIVVYCAS 66

                        90       100
                ....*....|....*....|....*....
gi 74191856 117 GVRSKKAMDTAISLGFNSAQHYAGGWKEW 145
Cdd:COG0607  67 GGRSAQAAALLRRAGYTNVYNLAGGIEAW 95
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 52-145 1.53e-18

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: 75.57  E-value: 1.53e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856     52 NSKDIMLIDVRNTLEIlEQGKIPGSINIPLDE-VGEALQMNPVDFKEKYCQVKPSKSDRLVFSCLAGVRSKKAMDTAISL 130
Cdd:smart00450   1 NDEKVVLLDVRSPEEY-EGGHIPGAVNIPLSElLDRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLREL 79

                           90
                   ....*....|....*
gi 74191856    131 GFNSAQHYAGGWKEW 145
Cdd:smart00450  80 GFKNVYLLDGGYKEW 94
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 51-146 3.99e-15

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: 66.35  E-value: 3.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856    51 LNSKDIMLIDVRNTLEiLEQGKIPGSINIPLDEvgeaLQMNPVDFKEKY-CQVKPSKSDRLVFSCLAGVRSKKAMDTAIS 129
Cdd:pfam00581   1 LEDGKVVLIDVRPPEE-YAKGHIPGAVNVPLSS----LSLPPLPLLELLeKLLELLKDKPIVVYCNSGNRAAAAAALLKA 75

                          90
                  ....*....|....*..
gi 74191856   130 LGFNSAQHYAGGWKEWV 146
Cdd:pfam00581  76 LGYKNVYVLDGGFEAWK 92
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 42-146 2.35e-12

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 63.19  E-value: 2.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856   42 VTYRELKSLLNS-KDIMLIDVRNTLEiLEQGKIPGSINIPLDEV--GEALQMNPVDfkekycqvkpsksDRLVFSCLAGV 118
Cdd:PRK07878 289 ITPRELKEWLDSgKKIALIDVREPVE-WDIVHIPGAQLIPKSEIlsGEALAKLPQD-------------RTIVLYCKTGV 354

                         90       100
                 ....*....|....*....|....*...
gi 74191856  119 RSKKAMDTAISLGFNSAQHYAGGWKEWV 146
Cdd:PRK07878 355 RSAEALAALKKAGFSDAVHLQGGVVAWA 382
 
Name Accession Description Interval E-value
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 42-147 3.66e-45

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: 143.56  E-value: 3.66e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856  42 VTYRELKSLLN-SKDIMLIDVRNTLEiLEQGKIPGSINIPLDEVGEALQMNPVDFKEKYCQVKPSKSDRLVFSCLAGVRS 120
Cdd:cd01519   1 YSFEEVKNLPNpHPNKVLIDVREPEE-LKTGKIPGAINIPLSSLPDALALSEEEFEKKYGFPKPSKDKELIFYCKAGVRS 79

                        90       100
                ....*....|....*....|....*..
gi 74191856 121 KKAMDTAISLGFNSAQHYAGGWKEWVT 147
Cdd:cd01519  80 KAAAELARSLGYENVGNYPGSWLDWAA 106
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 37-145 4.11e-22

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: 84.63  E-value: 4.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856  37 STPKGVTYRELKSLLNSKDIMLIDVRNTLEIlEQGKIPGSINIPLDEVGEalQMNPVDfkekycqvkpsKSDRLVFSCLA 116
Cdd:COG0607   1 ASVKEISPAELAELLESEDAVLLDVREPEEF-AAGHIPGAINIPLGELAE--RLDELP-----------KDKPIVVYCAS 66

                        90       100
                ....*....|....*....|....*....
gi 74191856 117 GVRSKKAMDTAISLGFNSAQHYAGGWKEW 145
Cdd:COG0607  67 GGRSAQAAALLRRAGYTNVYNLAGGIEAW 95
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 46-146 3.15e-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: 3.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856  46 ELKSLLNSKDIMLIDVRNTLEIlEQGKIPGSINIPLDEvgealqmnpvdFKEKYCQVKPSKSDRLVFSCLAGVRSKKAMD 125
Cdd:cd00158   1 ELKELLDDEDAVLLDVREPEEY-AAGHIPGAINIPLSE-----------LEERAALLELDKDKPIVVYCRSGNRSARAAK 68

                        90       100
                ....*....|....*....|.
gi 74191856 126 TAISLGFNSAQHYAGGWKEWV 146
Cdd:cd00158  69 LLRKAGGTNVYNLEGGMLAWK 89
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 52-145 1.53e-18

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: 75.57  E-value: 1.53e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856     52 NSKDIMLIDVRNTLEIlEQGKIPGSINIPLDE-VGEALQMNPVDFKEKYCQVKPSKSDRLVFSCLAGVRSKKAMDTAISL 130
Cdd:smart00450   1 NDEKVVLLDVRSPEEY-EGGHIPGAVNIPLSElLDRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLREL 79

                           90
                   ....*....|....*
gi 74191856    131 GFNSAQHYAGGWKEW 145
Cdd:smart00450  80 GFKNVYLLDGGYKEW 94
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 51-146 3.99e-15

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: 66.35  E-value: 3.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856    51 LNSKDIMLIDVRNTLEiLEQGKIPGSINIPLDEvgeaLQMNPVDFKEKY-CQVKPSKSDRLVFSCLAGVRSKKAMDTAIS 129
Cdd:pfam00581   1 LEDGKVVLIDVRPPEE-YAKGHIPGAVNVPLSS----LSLPPLPLLELLeKLLELLKDKPIVVYCNSGNRAAAAAALLKA 75

                          90
                  ....*....|....*..
gi 74191856   130 LGFNSAQHYAGGWKEWV 146
Cdd:pfam00581  76 LGYKNVYVLDGGFEAWK 92
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 42-146 2.35e-12

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 63.19  E-value: 2.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856   42 VTYRELKSLLNS-KDIMLIDVRNTLEiLEQGKIPGSINIPLDEV--GEALQMNPVDfkekycqvkpsksDRLVFSCLAGV 118
Cdd:PRK07878 289 ITPRELKEWLDSgKKIALIDVREPVE-WDIVHIPGAQLIPKSEIlsGEALAKLPQD-------------RTIVLYCKTGV 354

                         90       100
                 ....*....|....*....|....*...
gi 74191856  119 RSKKAMDTAISLGFNSAQHYAGGWKEWV 146
Cdd:PRK07878 355 RSAEALAALKKAGFSDAVHLQGGVVAWA 382
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 42-145 1.59e-10

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: 54.74  E-value: 1.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856  42 VTYRELKSLLNSKDIMLIDVRNTLEILEQGKIPGSINIPLDEVgEALqmnpVDFKEKYCQVKPSKSDRLVFSCLAGVRSK 121
Cdd:cd01447   1 LSPEDARALLGSPGVLLVDVRDPRELERTGMIPGAFHAPRGML-EFW----ADPDSPYHKPAFAEDKPFVFYCASGWRSA 75

                        90       100
                ....*....|....*....|....
gi 74191856 122 KAMDTAISLGFNSAQHYAGGWKEW 145
Cdd:cd01447  76 LAGKTLQDMGLKPVYNIEGGFKDW 99
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 42-145 9.33e-10

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 55.18  E-value: 9.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856  42 VTYRELKSLLNSKDIMLIDVRN------TLEILEQ--GKIPGSINIP----LDEVGealQMNPVD-FKEKYCQVKPSKSD 108
Cdd:COG2897 140 ADADEVLAALGDPDAVLVDARSperyrgEVEPIDPraGHIPGAVNLPwtdlLDEDG---TFKSAEeLRALFAALGIDPDK 216

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 74191856 109 RLVFSCLAGVRSkkAMDTAI--SLGFNSAQHYAGGWKEW 145
Cdd:COG2897 217 PVITYCGSGVRA--AHTWLAleLLGYPNVRLYDGSWSEW 253
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 42-145 1.32e-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: 52.64  E-value: 1.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856  42 VTYRELKSLLNSKDIMLIDVRN----------TLEILEQGKIPGSINIPL-DEVGEALQMNPVD-FKEKYCQVKPSKSDR 109
Cdd:cd01449   1 VTAEEVLANLDSGDVQLVDARSperfrgevpePRPGLRSGHIPGAVNIPWtSLLDEDGTFKSPEeLRALFAALGITPDKP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 74191856 110 LVFSCLAGVRSkkamdtAIS------LGFNSAQHYAGGWKEW 145
Cdd:cd01449  81 VIVYCGSGVTA------CVLllalelLGYKNVRLYDGSWSEW 116
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 58-145 1.72e-09

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: 51.88  E-value: 1.72e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856  58 LIDVRNTLEiLEQGKIPGSINIPLDEVGEALQMNPVDfKE--KYCQVkpsksdrlvfsclaGVRSKKAMDTAISLGFNsA 135
Cdd:cd01524  16 LIDVRTPQE-FEKGHIKGAINIPLDELRDRLNELPKD-KEiiVYCAV--------------GLRGYIAARILTQNGFK-V 78

                        90
                ....*....|
gi 74191856 136 QHYAGGWKEW 145
Cdd:cd01524  79 KNLDGGYKTY 88
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 46-145 1.04e-08

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: 50.09  E-value: 1.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856  46 ELKSLLNSKD--IMLIDVRNTLEiLEQGKIPGSINIPLDEVGEalqmnpvdfkekYCQVKPSKS--DRLVFSCLAGVRSK 121
Cdd:cd01528   6 ELAEWLADEReePVLIDVREPEE-LEIAFLPGFLHLPMSEIPE------------RSKELDSDNpdKDIVVLCHHGGRSM 72

                        90       100
                ....*....|....*....|....
gi 74191856 122 KAMDTAISLGFNSAQHYAGGWKEW 145
Cdd:cd01528  73 QVAQWLLRQGFENVYNLQGGIDAW 96
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
33-145 1.55e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 52.43  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856   33 QAFCSTPKG-------------VTYRELKSLLNS--KDIMLIDVRNTLEiLEQGKIPGSINIPLDEV--GEALQmnpvdf 95
Cdd:PRK07411 262 EQFCGIPQAkaaeaaqkaeipeMTVTELKALLDSgaDDFVLIDVRNPNE-YEIARIPGSVLVPLPDIenGPGVE------ 334

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 74191856   96 kekycQVKP-SKSDRLVFSCLAGVRSKKAMDTAISLGFnSAQHYAGGWKEW 145
Cdd:PRK07411 335 -----KVKElLNGHRLIAHCKMGGRSAKALGILKEAGI-EGTNVKGGITAW 379
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 55-145 3.00e-06

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 45.63  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856   55 DIMLIDVRNTLEILEqGKIPGSINIPLDEVGEALQMNPVDfkekycqvkpsKSDRLVFSCLAGVRSKKAMDTAISLGFNS 134
Cdd:PRK05597 274 GVTLIDVREPSEFAA-YSIPGAHNVPLSAIREGANPPSVS-----------AGDEVVVYCAAGVRSAQAVAILERAGYTG 341

                         90
                 ....*....|.
gi 74191856  135 AQHYAGGWKEW 145
Cdd:PRK05597 342 MSSLDGGIEGW 352
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 59-144 8.37e-06

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 42.52  E-value: 8.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856   59 IDVRnTLEILEQGKIPGSINIPLDEVgealqmnpvdfKEKYCQVKPSKSDRLVFSCLAGVRSKKAMDTAISLGFNSAQHy 138
Cdd:PRK10287  24 IDVR-VPEQYQQEHVQGAINIPLKEV-----------KERIATAVPDKNDTVKLYCNAGRQSGQAKEILSEMGYTHAEN- 90


                 ....*.
gi 74191856  139 AGGWKE 144
Cdd:PRK10287  91 AGGLKD 96
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 39-147 2.30e-05

Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included in this CD are eukaryotic arsenate resistance proteins such as Saccharomyces cerevisiae Acr2p and similar proteins. Cdc25 phosphatases activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. The Cdc25 and Acr2p RHOD domains have the signature motif (H/YCxxxxxR).


Pssm-ID: 238720 [Multi-domain]  Cd Length: 113  Bit Score: 41.24  E-value: 2.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856  39 PKGVTYRELKSLLNS------KDIMLIDVRNTleILEQGKIPGSINIPLDEVGEALqmnpvdfKEKYCQVKPSKSDRLVF 112
Cdd:cd01443   1 LKYISPEELVALLENsdsnagKDFVVVDLRRD--DYEGGHIKGSINLPAQSCYQTL-------PQVYALFSLAGVKLAIF 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 74191856 113 SC-LAGVRSKKAM----DTAISLGFNSAQHYA--GGWKEWVT 147
Cdd:cd01443  72 YCgSSQGRGPRAArwfaDYLRKVGESLPKSYIltGGIKAWYH 113
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 42-145 2.83e-05

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: 41.14  E-value: 2.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856  42 VTYRELKSLL-NSKDIMLIDVRNTLEIlEQGKIPGSINIPLDEVgeaLQMNPVDFKEKYCQVKPSKSDRLVFSCLAGVRS 120
Cdd:cd01526  10 VSVKDYKNILqAGKKHVLLDVRPKVHF-EICRLPEAINIPLSEL---LSKAAELKSLQELPLDNDKDSPIYVVCRRGNDS 85

                        90       100
                ....*....|....*....|....*.
gi 74191856 121 KKAMDTAISLGFNS-AQHYAGGWKEW 145
Cdd:cd01526  86 QTAVRKLKELGLERfVRDIIGGLKAW 111
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
42-145 3.26e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 42.69  E-value: 3.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856   42 VTYRELKSLLNSKdIMLIDVRNTLEIlEQGKIPGSINIPLDEvgeaLQMNPVdfkekycQVKPSKSDRLVFSCLAGVRSK 121
Cdd:PRK08762   5 ISPAEARARAAQG-AVLIDVREAHER-ASGQAEGALRIPRGF----LELRIE-------THLPDRDREIVLICASGTRSA 71

                         90       100
                 ....*....|....*....|....
gi 74191856  122 KAMDTAISLGFNSAQHYAGGWKEW 145
Cdd:PRK08762  72 HAAATLRELGYTRVASVAGGFSAW 95
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 57-143 6.25e-05

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: 40.39  E-value: 6.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856  57 MLIDVRNTLEILEQGKIPGSINIPLDeVGEALQMNPvDFKEKyCQVKPSKSDRLVFSCLAGVRSKKAMDTAISLGF---- 132
Cdd:cd01522  17 VLVDVRTEAEWKFVGGVPDAVHVAWQ-VYPDMEINP-NFLAE-LEEKVGKDRPVLLLCRSGNRSIAAAEAAAQAGFtnvy 93

                        90       100
                ....*....|....*....|...
gi 74191856 133 ----------NSAQHY--AGGWK 143
Cdd:cd01522  94 nvlegfegdlDAAGHRggVNGWR 116
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 37-83 7.01e-04

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 38.66  E-value: 7.01e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 74191856   37 STPKGVTYRELKSllnsKDIMLIDVRNTLEiLEQGKIPGSINIPL--DE 83
Cdd:PRK11784   1 MRPDAQDFRALFL----NDTPLIDVRSPIE-FAEGHIPGAINLPLlnDE 44
sseA PRK11493
3-mercaptopyruvate sulfurtransferase; Provisional
 68-145 7.33e-04

3-mercaptopyruvate sulfurtransferase; Provisional


Pssm-ID: 236917 [Multi-domain]  Cd Length: 281  Bit Score: 38.54  E-value: 7.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74191856   68 LEQGKIPGSINIPLDEVGEALQMNPVD-FKEKYCQVKPSKSDRLVFSCLAGVRSKKAMDTAISLGFNSAQHYAGGWKEW 145
Cdd:PRK11493 191 LRRGHIPGALNVPWTELVREGELKTTDeLDAIFFGRGVSFDRPIIASCGSGVTAAVVVLALATLDVPNVKLYDGAWSEW 269
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 47-83 3.21e-03

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 36.69  E-value: 3.21e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 74191856  47 LKSLLNSKDIMLIDVRNTLEIL----EQGKIPGSINIPLDE 83
Cdd:COG2897   1 LAAHLDDPDVVILDVRWDLPDGraayEAGHIPGAVFLDLDT 41
RHOD_YbbB cd01520
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ...
 43-81 3.81e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP /GTP binding proteins including E. coli YbbB.


Pssm-ID: 238778 [Multi-domain]  Cd Length: 128  Bit Score: 35.35  E-value: 3.81e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 74191856  43 TYRELKSLLNSKDImLIDVRNTLEiLEQGKIPGSINIPL 81
Cdd:cd01520   2 TAEDLLALRKADGP-LIDVRSPKE-FFEGHLPGAINLPL 38
PRK01415 PRK01415
hypothetical protein; Validated
 45-141 4.93e-03

hypothetical protein; Validated


Pssm-ID: 167229 [Multi-domain]  Cd Length: 247  Bit Score: 36.08  E-value: 4.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74191856   45 RELKSLLNSKDIMLIDVRNTLEIlEQGKIPGSINiPLDEVgealqmnpvdFKEKYCQVKPS----KSDRLVFSCLAGVRS 120
Cdd:PRK01415 117 KDWDEFITKQDVIVIDTRNDYEV-EVGTFKSAIN-PNTKT----------FKQFPAWVQQNqellKGKKIAMVCTGGIRC 184

                         90       100
                 ....*....|....*....|.
gi 74191856  121 KKAMDTAISLGFNSAQHYAGG 141
Cdd:PRK01415 185 EKSTSLLKSIGYDEVYHLKGG 205
 
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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