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Conserved domains on  [gi|616781967|gb|KAF77013|]
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hypothetical protein W673_02083 [Staphylococcus aureus VET0462R]

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]; ...
1-102 1.63e-36

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: 119.30  E-value: 1.63e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   1 MKSITTDELKtKLLESKPVQIVDVRTDEETAMGYIPNAKLIPMDTIPDNLDVFNKNETYYIVCAGGVRSAKVVDYLEANG 80
Cdd:COG0607    3 VKEISPAELA-ELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAG 81
                         90       100
                 ....*....|....*....|...
gi 616781967  81 IDAV-NVEGGMHAWGDEGLEIKS 102
Cdd:COG0607   82 YTNVyNLAGGIEAWKAAGLPVEK 104
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
1-102 1.63e-36

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: 119.30  E-value: 1.63e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   1 MKSITTDELKtKLLESKPVQIVDVRTDEETAMGYIPNAKLIPMDTIPDNLDVFNKNETYYIVCAGGVRSAKVVDYLEANG 80
Cdd:COG0607    3 VKEISPAELA-ELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAG 81
                         90       100
                 ....*....|....*....|...
gi 616781967  81 IDAV-NVEGGMHAWGDEGLEIKS 102
Cdd:COG0607   82 YTNVyNLAGGIEAWKAAGLPVEK 104
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
8-93 6.56e-26

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: 91.98  E-value: 6.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   8 ELKtKLLESKPVQIVDVRTDEETAMGYIPNAKLIPMDTIPDN--LDVFNKNETYYIVCAGGVRSAKVVDYLEANG-IDAV 84
Cdd:cd00158    1 ELK-ELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERaaLLELDKDKPIVVYCRSGNRSARAAKLLRKAGgTNVY 79

                 ....*....
gi 616781967  85 NVEGGMHAW 93
Cdd:cd00158   80 NLEGGMLAW 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
14-93 1.61e-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: 63.27  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   14 LESKPVQIVDVRTDEETAMGYIPNAKLIP----------MDTIPDNLDVFNKNETYYIVCAGGVRSAKVVDYLEANGI-D 82
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPlsslslpplpLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYkN 80
                          90
                  ....*....|.
gi 616781967   83 AVNVEGGMHAW 93
Cdd:pfam00581  81 VYVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
15-99 6.34e-14

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: 61.71  E-value: 6.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967    15 ESKPVQIVDVRTDEETAMGYIPNAKLIPMDTIPDNLDVF--------------NKNETYYIVCAGGVRSAKVVDYLEANG 80
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELdilefeellkrlglDKDKPVVVYCRSGNRSAKAAWLLRELG 80
                           90       100
                   ....*....|....*....|
gi 616781967    81 IDAV-NVEGGMHAWGDEGLE 99
Cdd:smart00450  81 FKNVyLLDGGYKEWSAAGPP 100
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
1-100 1.72e-13

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 64.26  E-value: 1.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   1 MKSITTDELKTKLLESkpVQIVDVRTDEETAMGYIPNAKLIPM--------DTIPDnldvfnKNETYYIVCAGGVRSAKV 72
Cdd:PRK08762   2 IREISPAEARARAAQG--AVLIDVREAHERASGQAEGALRIPRgflelrieTHLPD------RDREIVLICASGTRSAHA 73
                         90       100
                 ....*....|....*....|....*....
gi 616781967  73 VDYLEANGI-DAVNVEGGMHAWGDEGLEI 100
Cdd:PRK08762  74 AATLRELGYtRVASVAGGFSAWKDAGLPL 102
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
1-102 1.63e-36

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: 119.30  E-value: 1.63e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   1 MKSITTDELKtKLLESKPVQIVDVRTDEETAMGYIPNAKLIPMDTIPDNLDVFNKNETYYIVCAGGVRSAKVVDYLEANG 80
Cdd:COG0607    3 VKEISPAELA-ELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAG 81
                         90       100
                 ....*....|....*....|...
gi 616781967  81 IDAV-NVEGGMHAWGDEGLEIKS 102
Cdd:COG0607   82 YTNVyNLAGGIEAWKAAGLPVEK 104
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
8-93 6.56e-26

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: 91.98  E-value: 6.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   8 ELKtKLLESKPVQIVDVRTDEETAMGYIPNAKLIPMDTIPDN--LDVFNKNETYYIVCAGGVRSAKVVDYLEANG-IDAV 84
Cdd:cd00158    1 ELK-ELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERaaLLELDKDKPIVVYCRSGNRSARAAKLLRKAGgTNVY 79

                 ....*....
gi 616781967  85 NVEGGMHAW 93
Cdd:cd00158   80 NLEGGMLAW 88
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
4-93 3.26e-15

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: 65.11  E-value: 3.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   4 ITTDELKTKLLESKP-VQIVDVRTDEETAMGYIPNAKLIPMDTIP---DNLDVFNKNETYYIVCAGGVRSAKVVDYLEAN 79
Cdd:cd01528    2 ISVAELAEWLADEREePVLIDVREPEELEIAFLPGFLHLPMSEIPersKELDSDNPDKDIVVLCHHGGRSMQVAQWLLRQ 81
                         90
                 ....*....|....*
gi 616781967  80 GIDAV-NVEGGMHAW 93
Cdd:cd01528   82 GFENVyNLQGGIDAW 96
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
14-93 1.61e-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: 63.27  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   14 LESKPVQIVDVRTDEETAMGYIPNAKLIP----------MDTIPDNLDVFNKNETYYIVCAGGVRSAKVVDYLEANGI-D 82
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPlsslslpplpLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYkN 80
                          90
                  ....*....|.
gi 616781967   83 AVNVEGGMHAW 93
Cdd:pfam00581  81 VYVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
15-99 6.34e-14

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: 61.71  E-value: 6.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967    15 ESKPVQIVDVRTDEETAMGYIPNAKLIPMDTIPDNLDVF--------------NKNETYYIVCAGGVRSAKVVDYLEANG 80
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELdilefeellkrlglDKDKPVVVYCRSGNRSAKAAWLLRELG 80
                           90       100
                   ....*....|....*....|
gi 616781967    81 IDAV-NVEGGMHAWGDEGLE 99
Cdd:smart00450  81 FKNVyLLDGGYKEWSAAGPP 100
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
1-100 1.72e-13

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 64.26  E-value: 1.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   1 MKSITTDELKTKLLESkpVQIVDVRTDEETAMGYIPNAKLIPM--------DTIPDnldvfnKNETYYIVCAGGVRSAKV 72
Cdd:PRK08762   2 IREISPAEARARAAQG--AVLIDVREAHERASGQAEGALRIPRgflelrieTHLPD------RDREIVLICASGTRSAHA 73
                         90       100
                 ....*....|....*....|....*....
gi 616781967  73 VDYLEANGI-DAVNVEGGMHAWGDEGLEI 100
Cdd:PRK08762  74 AATLRELGYtRVASVAGGFSAWKDAGLPL 102
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
19-95 1.85e-13

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 64.12  E-value: 1.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967  19 VQIVDVRTDEETAMGYIPNAKLIPMDTI-----PDNLDVfnkNETYYIVCAGGVRSAKVVDYLEANGI-DAVNVEGGMHA 92
Cdd:PRK05597 275 VTLIDVREPSEFAAYSIPGAHNVPLSAIreganPPSVSA---GDEVVVYCAAGVRSAQAVAILERAGYtGMSSLDGGIEG 351

                 ...
gi 616781967  93 WGD 95
Cdd:PRK05597 352 WLD 354
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
3-96 3.48e-13

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 63.57  E-value: 3.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   3 SITTDELKTKLLESKPVQIVDVRTDEETAMGYIPNAKLIPMDTIP--DNLDVFNKNETYYIVCAGGVRSAKVVDYLEANG 80
Cdd:PRK07878 288 TITPRELKEWLDSGKKIALIDVREPVEWDIVHIPGAQLIPKSEILsgEALAKLPQDRTIVLYCKTGVRSAEALAALKKAG 367
                         90
                 ....*....|....*..
gi 616781967  81 I-DAVNVEGGMHAWGDE 96
Cdd:PRK07878 368 FsDAVHLQGGVVAWAKQ 384
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
4-97 1.20e-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: 55.90  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   4 ITTDELKtKLLESKPVQIVDVR-TDEETAMGYIPNAKLIPMDTI--------PDNLDVFNKNETYYIVCAGGVRSAKVVD 74
Cdd:cd01447    1 LSPEDAR-ALLGSPGVLLVDVRdPRELERTGMIPGAFHAPRGMLefwadpdsPYHKPAFAEDKPFVFYCASGWRSALAGK 79
                         90       100
                 ....*....|....*....|....
gi 616781967  75 YLEANGIDAV-NVEGGMHAWGDEG 97
Cdd:cd01447   80 TLQDMGLKPVyNIEGGFKDWKEAG 103
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
19-89 2.02e-11

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: 54.96  E-value: 2.02e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616781967  19 VQIVDVRTDEETAMGYIPNAKLIPMDTIPDNLDVFNKNETYYIVCAGGVRSAKVVDYLEANGIDAVNVEGG 89
Cdd:cd01524   14 VTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGFKVKNLDGG 84
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
1-96 2.42e-11

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 58.21  E-value: 2.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   1 MKSITTDELKtKLLES--KPVQIVDVRTDEETAMGYIPNAKLIPMDTIpDNLDVFNK-----NETYYIV-CAGGVRSAKV 72
Cdd:PRK07411 281 IPEMTVTELK-ALLDSgaDDFVLIDVRNPNEYEIARIPGSVLVPLPDI-ENGPGVEKvkellNGHRLIAhCKMGGRSAKA 358
                         90       100
                 ....*....|....*....|....
gi 616781967  73 VDYLEANGIDAVNVEGGMHAWGDE 96
Cdd:PRK07411 359 LGILKEAGIEGTNVKGGITAWSRE 382
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
4-95 9.77e-10

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: 50.96  E-value: 9.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   4 ITTDELKTKLLESKPVQIVDVRTDEETAMGYIPNAKLIPMDTIPDN--------LDVFNKNETYYIVCAGGVRSAKVVDY 75
Cdd:cd01523    1 LDPEDLYARLLAGQPLFILDVRNESDYERWKIDGENNTPYFDPYFDfleieediLDQLPDDQEVTVICAKEGSSQFVAEL 80
                         90       100
                 ....*....|....*....|
gi 616781967  76 LEANGIDAVNVEGGMHAWGD 95
Cdd:cd01523   81 LAERGYDVDYLAGGMKAWSE 100
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
4-96 1.15e-09

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: 51.54  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   4 ITTDELKTKLLESKPVQIVDVRTDEETAMGYIPNAKLIPMDTIPDN----------LDVFNKNETYYIVCAGGVRSAKVV 73
Cdd:cd01526   10 VSVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSKaaelkslqelPLDNDKDSPIYVVCRRGNDSQTAV 89
                         90       100
                 ....*....|....*....|....*
gi 616781967  74 DYLEANGIDA--VNVEGGMHAWGDE 96
Cdd:cd01526   90 RKLKELGLERfvRDIIGGLKAWADK 114
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
4-93 3.48e-09

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: 49.57  E-value: 3.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   4 ITTDELKTKLLESKPVQIVDVRTDEETAM--GYIPNAKLIPMDTIPDNLDVFNKNETYYIVCAGGVRSAKVVDYL-EANG 80
Cdd:cd01444    2 ISVDELAELLAAGEAPVLLDVRDPASYAAlpDHIPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALrEAGF 81
                         90
                 ....*....|...
gi 616781967  81 IDAVNVEGGMHAW 93
Cdd:cd01444   82 TDVRSLAGGFEAW 94
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
5-93 1.70e-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: 48.03  E-value: 1.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   5 TTDELKTKLLESKPVQIVDVRTDEETAMGYIPNAKLIPMDTIPDNLD---------------VFNKNETYYivCAGGVRS 69
Cdd:cd01519    2 SFEEVKNLPNPHPNKVLIDVREPEELKTGKIPGAINIPLSSLPDALAlseeefekkygfpkpSKDKELIFY--CKAGVRS 79
                         90       100
                 ....*....|....*....|....*
gi 616781967  70 AKVVDYLEANGI-DAVNVEGGMHAW 93
Cdd:cd01519   80 KAAAELARSLGYeNVGNYPGSWLDW 104
4RHOD_Repeat_4 cd01535
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative ...
13-102 7.50e-06

Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 4th repeat which, in general, contains the putative catalytic Cys residue.


Pssm-ID: 238793 [Multi-domain]  Cd Length: 145  Bit Score: 41.72  E-value: 7.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967  13 LLESKPVQIVDVRTDEETAMGYIPNAKLIPMDTIPDNLDVFNKNETYYIVCAGGVRSAKVVDYLEANGIDAVNV-EGGMH 91
Cdd:cd01535    6 LGEGGQTAVVDVTASANYVKRHIPGAWWVLRAQLAQALEKLPAAERYVLTCGSSLLARFAAADLAALTVKPVFVlEGGTA 85
                         90
                 ....*....|.
gi 616781967  92 AWGDEGLEIKS 102
Cdd:cd01535   86 AWIAAGLPVES 96
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
1-98 1.04e-05

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, and similar uncharacterized putative rhodanese-related sulfurtransferases.


Pssm-ID: 238785 [Multi-domain]  Cd Length: 99  Bit Score: 40.55  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   1 MKSITTDELKTKLleSKPVQIVDVRTDEETAMGYIPNAKLIPMDTI-PDNLDVFNKNETYYiVCAGGVRSAKVVDYLEA- 78
Cdd:cd01527    1 LTTISPNDACELL--AQGAVLVDIREPDEYLRERIPGARLVPLSQLeSEGLPLVGANAIIF-HCRSGMRTQQNAERLAAi 77
                         90       100
                 ....*....|....*....|
gi 616781967  79 NGIDAVNVEGGMHAWGDEGL 98
Cdd:cd01527   78 SAGEAYVLEGGLDAWKAAGL 97
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
13-93 1.63e-05

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 40.39  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967  13 LLESKPVQIVDVRTDEETAMGYIPNAKLIPMDTIPDNLDVFNKNETYYIVCAGGVRSAKVVDYLEANGIDAV-NVEGGMH 91
Cdd:PRK00162  15 KLQEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQQGFDVVySIDGGFE 94

                 ..
gi 616781967  92 AW 93
Cdd:PRK00162  95 AW 96
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
19-99 8.05e-05

Member of the Rhodanese Homology Domain superfamily. This CD includes the putative rhodanese-like protein, Psp2, of Yersinia pestis biovar Medievalis and other similar uncharacterized proteins.


Pssm-ID: 238779 [Multi-domain]  Cd Length: 110  Bit Score: 38.49  E-value: 8.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967  19 VQIVDVRTDEETAMGYIPNAKLIPMDTIP-DNLDVFNKNETYYIVCAGGV--RSAKVVDYLEANGIDAVNVEGGMHAWGD 95
Cdd:cd01521   26 FVLVDVRSAEAYARGHVPGAINLPHREICeNATAKLDKEKLFVVYCDGPGcnGATKAALKLAELGFPVKEMIGGLDWWKR 105

                 ....
gi 616781967  96 EGLE 99
Cdd:cd01521  106 EGYA 109
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
12-96 8.85e-05

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 39.45  E-value: 8.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967  12 KLLESKPVQIVDVRTDEETAMGYIPNAKLIPMDT-------IPDNLDVF-NKN-ETYyivCAGGVRSAKVVDYLEANGID 82
Cdd:PRK00142 121 ELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETfrefppwVEENLDPLkDKKvVMY---CTGGIRCEKASAWMKHEGFK 197
                         90
                 ....*....|....*
gi 616781967  83 AVN-VEGGMHAWGDE 96
Cdd:PRK00142 198 EVYqLEGGIITYGED 212
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
12-94 1.26e-04

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins.


Pssm-ID: 238776 [Multi-domain]  Cd Length: 101  Bit Score: 37.56  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967  12 KLLESKPVQIVDVRTDEETAMGYIPNAKLIPMDT-------IPDNLDVFnKNETYYIVCAGGVRSAKVVDYLEANGIDAV 84
Cdd:cd01518   11 ELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTfrefpfwLDENLDLL-KGKKVLMYCTGGIRCEKASAYLKERGFKNV 89
                         90
                 ....*....|.
gi 616781967  85 N-VEGGMHAWG 94
Cdd:cd01518   90 YqLKGGILKYL 100
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
9-93 3.03e-04

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: 36.88  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   9 LKTKLLESKPVQ-IVDVRTDEETAMGYIPNAKLIPMDTIP------DNLDVFNKNETYYIVCAGGVRSAKVVDYLEANGI 81
Cdd:cd01529    2 LADWLGEHEPGTaLLDVRAEDEYAAGHLPGKRSIPGAALVlrsqelQALEAPGRATRYVLTCDGSLLARFAAQELLALGG 81
                         90
                 ....*....|...
gi 616781967  82 DAVNV-EGGMHAW 93
Cdd:cd01529   82 KPVALlDGGTSAW 94
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
1-93 4.44e-04

Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain superfamily. Included in this CD is the Saccharomyces cerevisiae arsenate reductase protein, Acr2p, and other yeast and plant homologs.


Pssm-ID: 238789 [Multi-domain]  Cd Length: 113  Bit Score: 36.62  E-value: 4.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   1 MKSITTDELKTKLLES-KPVQIVDVRtDEETAMGYIPNAKLIPMDTIPDNLD------VFNKNETYYIVCAGG-VR---- 68
Cdd:cd01531    1 VSYISPAQLKGWIRNGrPPFQVVDVR-DEDYAGGHIKGSWHYPSTRFKAQLNqlvqllSGSKKDTVVFHCALSqVRgpsa 79
                         90       100       110
                 ....*....|....*....|....*....|.
gi 616781967  69 SAKVVDYLEaNGIDAVN------VEGGMHAW 93
Cdd:cd01531   80 ARKFLRYLD-EEDLETSkfevyvLHGGFNAW 109
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
4-93 1.87e-03

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: 34.75  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967   4 ITTDELKTKLLES-KPVQIVDVRTDEETAMGYIPNAKLIPMDTIPDNLDVFNKNETYYIVCAG--GVRSAKVVDYLEANG 80
Cdd:cd01534    1 IGAAELARWAAEGdRTVYRFDVRTPEEYEAGHLPGFRHTPGGQLVQETDHFAPVRGARIVLADddGVRADMTASWLAQMG 80
                         90
                 ....*....|...
gi 616781967  81 IDAVNVEGGMHAW 93
Cdd:cd01534   81 WEVYVLEGGLAAA 93
PRK05320 PRK05320
rhodanese superfamily protein; Provisional
15-89 2.30e-03

rhodanese superfamily protein; Provisional


Pssm-ID: 235405 [Multi-domain]  Cd Length: 257  Bit Score: 35.39  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616781967  15 ESKPVQIVDVRTDEETAMGYIPNAKLIPMDT---IPDNLDVfNKNE----TYYIVCAGGVRSAKVVDYLEANGIDAV-NV 86
Cdd:PRK05320 128 AGRPVVMLDTRNAFEVDVGTFDGALDYRIDKfteFPEALAA-HRADlagkTVVSFCTGGIRCEKAAIHMQEVGIDNVyQL 206

                 ...
gi 616781967  87 EGG 89
Cdd:PRK05320 207 EGG 209
 
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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