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Conserved domains on  [gi|319028455|ref|NP_001186943|]
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thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 3 [Danio rerio]

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 ...
 66-171 1.57e-43

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: 140.10  E-value: 1.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  66 VSYEQLKKLL-VSGSSVVIDVREPWELReYGNIQGSINVPLGQVNGALQLTPDEFKEKYGGDMPSKSQNIVFSCLAGVRS 144
Cdd:cd01519    1 YSFEEVKNLPnPHPNKVLIDVREPEELK-TGKIPGAINIPLSSLPDALALSEEEFEKKYGFPKPSKDKELIFYCKAGVRS 79

                         90       100
                 ....*....|....*....|....*..
gi 319028455 145 KHALEAAVSLGYTKVQHFPGGWQEWAE 171
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 ...
 66-171 1.57e-43

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: 140.10  E-value: 1.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  66 VSYEQLKKLL-VSGSSVVIDVREPWELReYGNIQGSINVPLGQVNGALQLTPDEFKEKYGGDMPSKSQNIVFSCLAGVRS 144
Cdd:cd01519    1 YSFEEVKNLPnPHPNKVLIDVREPEELK-TGKIPGAINIPLSSLPDALALSEEEFEKKYGFPKPSKDKELIFYCKAGVRS 79

                         90       100
                 ....*....|....*....|....*..
gi 319028455 145 KHALEAAVSLGYTKVQHFPGGWQEWAE 171
Cdd:cd01519   80 KAAAELARSLGYENVGNYPGSWLDWAA 106
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 65-174 1.10e-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: 86.95  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  65 DVSYEQLKKLLVSGSSVVIDVREPWElREYGNIQGSINVPLGQVNGALQLTPdefkekyggdmpsKSQNIVFSCLAGVRS 144
Cdd:COG0607    5 EISPAELAELLESEDAVLLDVREPEE-FAAGHIPGAINIPLGELAERLDELP-------------KDKPIVVYCASGGRS 70

                         90       100       110
                 ....*....|....*....|....*....|
gi 319028455 145 KHALEAAVSLGYTKVQHFPGGWQEWAEREL 174
Cdd:COG0607   71 AQAAALLRRAGYTNVYNLAGGIEAWKAAGL 100
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 81-171 5.48e-15

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: 67.10  E-value: 5.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455    81 VVIDVREPWELREyGNIQGSINVPLGQ-VNGALQLTPDEFKEKYGGDMPSKSQNIVFSCLAGVRSKHALEAAVSLGYTKV 159
Cdd:smart00450   6 VLLDVRSPEEYEG-GHIPGAVNIPLSElLDRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGFKNV 84

                           90
                   ....*....|..
gi 319028455   160 QHFPGGWQEWAE 171
Cdd:smart00450  85 YLLDGGYKEWSA 96
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 77-170 2.10e-14

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: 65.20  E-value: 2.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455   77 SGSSVVIDVREPWELrEYGNIQGSINVPLGqvngALQLTPDEFKEKYGGDMP-SKSQNIVFSCLAGVRSKHALEAAVSLG 155
Cdd:pfam00581   3 DGKVVLIDVRPPEEY-AKGHIPGAVNVPLS----SLSLPPLPLLELLEKLLElLKDKPIVVYCNSGNRAAAAAALLKALG 77

                          90
                  ....*....|....*
gi 319028455  156 YTKVQHFPGGWQEWA 170
Cdd:pfam00581  78 YKNVYVLDGGFEAWK 92
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
65-174 4.62e-11

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 60.03  E-value: 4.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  65 DVSYEQLKKLLVSGSsVVIDVREPWElREYGNIQGSINVPlgqvNGALQLTPDEFKekyggdmPSKSQNIVFSCLAGVRS 144
Cdd:PRK08762   4 EISPAEARARAAQGA-VLIDVREAHE-RASGQAEGALRIP----RGFLELRIETHL-------PDRDREIVLICASGTRS 70

                         90       100       110
                 ....*....|....*....|....*....|
gi 319028455 145 KHALEAAVSLGYTKVQHFPGGWQEWAEREL 174
Cdd:PRK08762  71 AHAAATLRELGYTRVASVAGGFSAWKDAGL 100
 
Name Accession Description Interval E-value
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 66-171 1.57e-43

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: 140.10  E-value: 1.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  66 VSYEQLKKLL-VSGSSVVIDVREPWELReYGNIQGSINVPLGQVNGALQLTPDEFKEKYGGDMPSKSQNIVFSCLAGVRS 144
Cdd:cd01519    1 YSFEEVKNLPnPHPNKVLIDVREPEELK-TGKIPGAINIPLSSLPDALALSEEEFEKKYGFPKPSKDKELIFYCKAGVRS 79

                         90       100
                 ....*....|....*....|....*..
gi 319028455 145 KHALEAAVSLGYTKVQHFPGGWQEWAE 171
Cdd:cd01519   80 KAAAELARSLGYENVGNYPGSWLDWAA 106
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 65-174 1.10e-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: 86.95  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  65 DVSYEQLKKLLVSGSSVVIDVREPWElREYGNIQGSINVPLGQVNGALQLTPdefkekyggdmpsKSQNIVFSCLAGVRS 144
Cdd:COG0607    5 EISPAELAELLESEDAVLLDVREPEE-FAAGHIPGAINIPLGELAERLDELP-------------KDKPIVVYCASGGRS 70

                         90       100       110
                 ....*....|....*....|....*....|
gi 319028455 145 KHALEAAVSLGYTKVQHFPGGWQEWAEREL 174
Cdd:COG0607   71 AQAAALLRRAGYTNVYNLAGGIEAWKAAGL 100
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 70-170 3.55e-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: 77.34  E-value: 3.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  70 QLKKLLVSGSSVVIDVREPWELREyGNIQGSINVPLgqvngalqltpDEFKEKYGGDMPSKSQNIVFSCLAGVRSKHALE 149
Cdd:cd00158    1 ELKELLDDEDAVLLDVREPEEYAA-GHIPGAINIPL-----------SELEERAALLELDKDKPIVVYCRSGNRSARAAK 68

                         90       100
                 ....*....|....*....|.
gi 319028455 150 AAVSLGYTKVQHFPGGWQEWA 170
Cdd:cd00158   69 LLRKAGGTNVYNLEGGMLAWK 89
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 54-170 2.00e-17

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 77.14  E-value: 2.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  54 RNFSSSSQPSVDVSYEQLKKLLVSGSSVVIDVR---------EPWELReYGNIQGSINVPLGQV---NGALqLTPDEFKE 121
Cdd:COG2897  128 GDFTARPDPELLADADEVLAALGDPDAVLVDARsperyrgevEPIDPR-AGHIPGAVNLPWTDLldeDGTF-KSAEELRA 205

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 319028455 122 KYGGDMPSKSQNIVFSCLAGVRSKHALEAAVSLGYTKVQHFPGGWQEWA 170
Cdd:COG2897  206 LFAALGIDPDKPVITYCGSGVRAAHTWLALELLGYPNVRLYDGSWSEWG 254
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 66-170 1.77e-15

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: 68.81  E-value: 1.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  66 VSYEQLKKLLVSGSSVVIDVR----------EPWELREYGNIQGSINVPLGQV---NGALqLTPDEFKEKYG--GDMPSK 130
Cdd:cd01449    1 VTAEEVLANLDSGDVQLVDARsperfrgevpEPRPGLRSGHIPGAVNIPWTSLldeDGTF-KSPEELRALFAalGITPDK 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 319028455 131 SqnIVFSCLAGVRSKHALEAAVSLGYTKVQHFPGGWQEWA 170
Cdd:cd01449   80 P--VIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEWG 117
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 81-171 5.48e-15

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: 67.10  E-value: 5.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455    81 VVIDVREPWELREyGNIQGSINVPLGQ-VNGALQLTPDEFKEKYGGDMPSKSQNIVFSCLAGVRSKHALEAAVSLGYTKV 159
Cdd:smart00450   6 VLLDVRSPEEYEG-GHIPGAVNIPLSElLDRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGFKNV 84

                           90
                   ....*....|..
gi 319028455   160 QHFPGGWQEWAE 171
Cdd:smart00450  85 YLLDGGYKEWSA 96
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 77-170 2.10e-14

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: 65.20  E-value: 2.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455   77 SGSSVVIDVREPWELrEYGNIQGSINVPLGqvngALQLTPDEFKEKYGGDMP-SKSQNIVFSCLAGVRSKHALEAAVSLG 155
Cdd:pfam00581   3 DGKVVLIDVRPPEEY-AKGHIPGAVNVPLS----SLSLPPLPLLELLEKLLElLKDKPIVVYCNSGNRAAAAAALLKALG 77

                          90
                  ....*....|....*
gi 319028455  156 YTKVQHFPGGWQEWA 170
Cdd:pfam00581  78 YKNVYVLDGGFEAWK 92
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 66-171 1.32e-12

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: 60.90  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  66 VSYEQLKKLLVSGSSVVIDVREPWELREYGNIQGSINVPLGQVNGALQLTPDEFKEKYGGDMPsksqnIVFSCLAGVRSK 145
Cdd:cd01447    1 LSPEDARALLGSPGVLLVDVRDPRELERTGMIPGAFHAPRGMLEFWADPDSPYHKPAFAEDKP-----FVFYCASGWRSA 75

                         90       100
                 ....*....|....*....|....*.
gi 319028455 146 HALEAAVSLGYTKVQHFPGGWQEWAE 171
Cdd:cd01447   76 LAGKTLQDMGLKPVYNIEGGFKDWKE 101
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
65-174 4.62e-11

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 60.03  E-value: 4.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  65 DVSYEQLKKLLVSGSsVVIDVREPWElREYGNIQGSINVPlgqvNGALQLTPDEFKekyggdmPSKSQNIVFSCLAGVRS 144
Cdd:PRK08762   4 EISPAEARARAAQGA-VLIDVREAHE-RASGQAEGALRIP----RGFLELRIETHL-------PDRDREIVLICASGTRS 70

                         90       100       110
                 ....*....|....*....|....*....|
gi 319028455 145 KHALEAAVSLGYTKVQHFPGGWQEWAEREL 174
Cdd:PRK08762  71 AHAAATLRELGYTRVASVAGGFSAWKDAGL 100
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 65-170 1.40e-10

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: 55.48  E-value: 1.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  65 DVSYEQLKKLLVSGSS--VVIDVREPWELrEYGNIQGSINVPLGQVngalQLTPDEFKEKyggdmpSKSQNIVFSCLAGV 142
Cdd:cd01528    1 QISVAELAEWLADEREepVLIDVREPEEL-EIAFLPGFLHLPMSEI----PERSKELDSD------NPDKDIVVLCHHGG 69

                         90       100
                 ....*....|....*....|....*...
gi 319028455 143 RSKHALEAAVSLGYTKVQHFPGGWQEWA 170
Cdd:cd01528   70 RSMQVAQWLLRQGFENVYNLQGGIDAWS 97
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 75-171 1.36e-09

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 56.03  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  75 LVSGSSVvIDVREPWELREYgNIQGSINVPLGQVNGALqlTPDEFkekyggdmpSKSQNIVFSCLAGVRSKHALEAAVSL 154
Cdd:PRK05597 271 LPDGVTL-IDVREPSEFAAY-SIPGAHNVPLSAIREGA--NPPSV---------SAGDEVVVYCAAGVRSAQAVAILERA 337

                         90
                 ....*....|....*..
gi 319028455 155 GYTKVQHFPGGWQEWAE 171
Cdd:PRK05597 338 GYTGMSSLDGGIEGWLD 354
PLN02723 PLN02723
3-mercaptopyruvate sulfurtransferase
 50-172 1.44e-08

3-mercaptopyruvate sulfurtransferase


Pssm-ID: 178324 [Multi-domain]  Cd Length: 320  Bit Score: 52.88  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  50 SVSLRNFSSSSQPSVDVSYEQLKKLLVSGSSVVIDVR----------EPWELREYGNIQGSINVPLGQVNGALQ--LTPD 117
Cdd:PLN02723 176 TVSPITFQTKFQPHLVWTLEQVKKNIEDKTYQHIDARskarfdgaapEPRKGIRSGHIPGSKCVPFPQMLDSSQtlLPAE 255

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 319028455 118 EFKEKYGGDMPSKSQNIVFSCLAGVRSKHALEAAVSLGYTKVQHFPGGWQEWAER 172
Cdd:PLN02723 256 ELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEWGAL 310
PLN02160 PLN02160
thiosulfate sulfurtransferase
 54-169 7.03e-08

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 48.93  E-value: 7.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  54 RNFSSSSQP----SVDVSyeQLKKLLVSGSSVvIDVREPWELR-------EYGNIQGSINVPLGQVNGalqltpDEFKEK 122
Cdd:PLN02160   3 QSISSSTKAeevvSVDVS--QAKTLLQSGHQY-LDVRTQDEFRrghceaaKIVNIPYMLNTPQGRVKN------QEFLEQ 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 319028455 123 YGgDMPSKSQNIVFSCLAGVRSKHALEAAVSLGYTKVQHFPGGWQEW 169
Cdd:PLN02160  74 VS-SLLNPADDILVGCQSGARSLKATTELVAAGYKKVRNKGGGYLAW 119
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 70-172 2.92e-07

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 49.32  E-value: 2.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  70 QLKKLLVSGSSV-VIDVREPWELrEYGNIQGSINVPLGQVNGALQLtpdefkekygGDMPSKSQnIVFSCLAGVRSKHAL 148
Cdd:PRK07878 293 ELKEWLDSGKKIaLIDVREPVEW-DIVHIPGAQLIPKSEILSGEAL----------AKLPQDRT-IVLYCKTGVRSAEAL 360

                         90       100
                 ....*....|....*....|....
gi 319028455 149 EAAVSLGYTKVQHFPGGWQEWAER 172
Cdd:PRK07878 361 AALKKAGFSDAVHLQGGVVAWAKQ 384
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 81-165 1.02e-06

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.


Pssm-ID: 238782 [Multi-domain]  Cd Length: 90  Bit Score: 44.95  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  81 VVIDVREPWELrEYGNIQGSINVPLgqvngalqltpDEFKEKYgGDMPsKSQNIVFSCLAGVRSKHALEAAVSLGYtKVQ 160
Cdd:cd01524   15 TLIDVRTPQEF-EKGHIKGAINIPL-----------DELRDRL-NELP-KDKEIIVYCAVGLRGYIAARILTQNGF-KVK 79


                 ....*
gi 319028455 161 HFPGG 165
Cdd:cd01524   80 NLDGG 84
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 78-161 1.66e-06

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: 45.01  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  78 GSSVVIDVREPWELREYGNIQGSINVPLgQVNGALQLTP---DEFKEKYGGDMPsksqnIVFSCLAGVRSKHALEAAVSL 154
Cdd:cd01522   14 PQAVLVDVRTEAEWKFVGGVPDAVHVAW-QVYPDMEINPnflAELEEKVGKDRP-----VLLLCRSGNRSIAAAEAAAQA 87


                 ....*..
gi 319028455 155 GYTKVQH 161
Cdd:cd01522   88 GFTNVYN 94
sseA PRK11493
3-mercaptopyruvate sulfurtransferase; Provisional
 74-172 1.72e-06

3-mercaptopyruvate sulfurtransferase; Provisional


Pssm-ID: 236917 [Multi-domain]  Cd Length: 281  Bit Score: 46.62  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  74 LLVS--GSSVVIDVR----------EPWELREYGNIQGSINVPLGQV--NGALQlTPDEFKEKYGGDMPSKSQNIVFSCL 139
Cdd:PRK11493 161 LLASheKTAQIVDARpaarfnaevdEPRPGLRRGHIPGALNVPWTELvrEGELK-TTDELDAIFFGRGVSFDRPIIASCG 239

                         90       100       110
                 ....*....|....*....|....*....|...
gi 319028455 140 AGVRSKHALEAAVSLGYTKVQHFPGGWQEWAER 172
Cdd:PRK11493 240 SGVTAAVVVLALATLDVPNVKLYDGAWSEWGAR 272
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 66-171 9.12e-06

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: 42.78  E-value: 9.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  66 VSYEQLKKLLVSGSS------VVIDVREPweLREYGNIQGSINVPlgqvngaLQLTPDEFKEKYGGDMPSKSQNIVFSCL 139
Cdd:cd01443    4 ISPEELVALLENSDSnagkdfVVVDLRRD--DYEGGHIKGSINLP-------AQSCYQTLPQVYALFSLAGVKLAIFYCG 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 319028455 140 -------AGVRSKHALEAAVSLGYTKVQHFPGGWQEWAE 171
Cdd:cd01443   75 ssqgrgpRAARWFADYLRKVGESLPKSYILTGGIKAWYH 113
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 69-165 2.92e-05

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 43.33  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  69 EQLKKLLVSGSSVVIDVREPWE--LREYGNIQGSINVPLGQVNGalqltPDEFKEKYGgdmPSKSQNIVFSCLAGVRSKH 146
Cdd:PRK05600 276 TSLIDATLNGSATLLDVREPHEvlLKDLPEGGASLKLPLSAITD-----DADILHALS---PIDGDNVVVYCASGIRSAD 347

                         90       100
                 ....*....|....*....|
gi 319028455 147 ALEAAVSLGYTKVQH-FPGG 165
Cdd:PRK05600 348 FIEKYSHLGHELTLHnLPGG 367
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 83-164 1.81e-04

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 39.06  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  83 IDVREPWELREYgNIQGSINVPLgqvngalqltpDEFKEKYGGDMPSKSQNIVFSCLAGVRSKHALEAAVSLGYTKVQHF 162
Cdd:PRK10287  24 IDVRVPEQYQQE-HVQGAINIPL-----------KEVKERIATAVPDKNDTVKLYCNAGRQSGQAKEILSEMGYTHAENA 91


                 ..
gi 319028455 163 PG 164
Cdd:PRK10287  92 GG 93
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 66-171 2.22e-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: 39.21  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  66 VSYEQLKKLLVSGSS-VVIDVREPWELrEYGNIQGSINVPLGQVngaLQLTPDEFKEKYGGDMPSKSQNIVFSCLAGVRS 144
Cdd:cd01526   10 VSVKDYKNILQAGKKhVLLDVRPKVHF-EICRLPEAINIPLSEL---LSKAAELKSLQELPLDNDKDSPIYVVCRRGNDS 85

                         90       100
                 ....*....|....*....|....*...
gi 319028455 145 KHALEAAVSLGYT-KVQHFPGGWQEWAE 171
Cdd:cd01526   86 QTAVRKLKELGLErFVRDIIGGLKAWAD 113
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 66-171 2.04e-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: 36.08  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319028455  66 VSYEQLKKLLVSGSS-VVIDVREPWELREygniqgsinvPLGQVNGALQLTPDEFKEkYGGDMPsKSQNIVFSCLAGVRS 144
Cdd:cd01444    2 ISVDELAELLAAGEApVLLDVRDPASYAA----------LPDHIPGAIHLDEDSLDD-WLGDLD-RDRPVVVYCYHGNSS 69

                         90       100
                 ....*....|....*....|....*..
gi 319028455 145 KHALEAAVSLGYTKVQHFPGGWQEWAE 171
Cdd:cd01444   70 AQLAQALREAGFTDVRSLAGGFEAWRR 96
 
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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