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Conserved domains on  [gi|2502538751|ref|WP_281869196|]
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MULTISPECIES: rhodanese-like domain-containing protein [Brevibacillus]

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]; ...
 9-109 3.89e-17

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


:

Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 70.77  E-value: 3.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751   9 QEIKQLLEKGTPILfLDVRDEAKFQTGSVEskfaDTRNVPYvhmlaqgdKLLDEETERAVKERQIITVCTTGNKAQKAAA 88
Cdd:COG0607     9 AELAELLESEDAVL-LDVREPEEFAAGHIP----GAINIPL--------GELAERLDELPKDKPIVVYCASGGRSAQAAA 75

                          90       100
                  ....*....|....*....|..
gi 2502538751  89 LLREHGYE-AKALLGGLTAWKD 109
Cdd:COG0607    76 LLRRAGYTnVYNLAGGIEAWKA 97
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 9-109 3.89e-17

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 70.77  E-value: 3.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751   9 QEIKQLLEKGTPILfLDVRDEAKFQTGSVEskfaDTRNVPYvhmlaqgdKLLDEETERAVKERQIITVCTTGNKAQKAAA 88
Cdd:COG0607     9 AELAELLESEDAVL-LDVREPEEFAAGHIP----GAINIPL--------GELAERLDELPKDKPIVVYCASGGRSAQAAA 75

                          90       100
                  ....*....|....*....|..
gi 2502538751  89 LLREHGYE-AKALLGGLTAWKD 109
Cdd:COG0607    76 LLRRAGYTnVYNLAGGIEAWKA 97
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 9-112 1.25e-14

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: 64.64  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751   9 QEIKQLLEKGTPILFLDVRDEAKFQTGSVEskfaDTRNVPYVHMLAQGDKLLDEETERAV--KERQIITVCTTGNKAQKA 86
Cdd:cd01526    13 KDYKNILQAGKKHVLLDVRPKVHFEICRLP----EAINIPLSELLSKAAELKSLQELPLDndKDSPIYVVCRRGNDSQTA 88

                          90       100
                  ....*....|....*....|....*...
gi 2502538751  87 AALLREHGYEAKA--LLGGLTAWKDDED 112
Cdd:cd01526    89 VRKLKELGLERFVrdIIGGLKAWADKVD 116
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 21-113 3.38e-12

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: 57.85  E-value: 3.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751   21 ILFLDVRDEAKFQTGSVESkfadTRNVPY---VHMLAQGDKLLDEETERAV---KERQIITVCTTGNKAQKAAALLREHG 94
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPG----AVNIPLselLDRRGELDILEFEELLKRLgldKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 2502538751   95 YE-AKALLGGLTAWKDDEDE 113
Cdd:smart00450  81 FKnVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 15-108 4.93e-12

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: 57.11  E-value: 4.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751  15 LEKGTPILfLDVRDEAKFQTGSVESkfAdtRNVPYVHMLAQGDKLLD--EETERAVKERQIITVCTTGNKAQKAAALLRE 92
Cdd:pfam00581   1 LEDGKVVL-IDVRPPEEYAKGHIPG--A--VNVPLSSLSLPPLPLLEllEKLLELLKDKPIVVYCNSGNRAAAAAALLKA 75

                          90
                  ....*....|....*..
gi 2502538751  93 HGY-EAKALLGGLTAWK 108
Cdd:pfam00581  76 LGYkNVYVLDGGFEAWK 92
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
7-112 1.11e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 51.27  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751   7 TKQEIKQLLEKGTP-ILFLDVRDEAKFQT----GSVESKFADTRNVPYVhmlaqgdklldEETERAVKERQIITVCTTGN 81
Cdd:PRK07411  285 TVTELKALLDSGADdFVLIDVRNPNEYEIaripGSVLVPLPDIENGPGV-----------EKVKELLNGHRLIAHCKMGG 353

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2502538751  82 KAQKAAALLREHGYEAKALLGGLTAWKDDED 112
Cdd:PRK07411  354 RSAKALGILKEAGIEGTNVKGGITAWSREVD 384
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 9-109 3.89e-17

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 70.77  E-value: 3.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751   9 QEIKQLLEKGTPILfLDVRDEAKFQTGSVEskfaDTRNVPYvhmlaqgdKLLDEETERAVKERQIITVCTTGNKAQKAAA 88
Cdd:COG0607     9 AELAELLESEDAVL-LDVREPEEFAAGHIP----GAINIPL--------GELAERLDELPKDKPIVVYCASGGRSAQAAA 75

                          90       100
                  ....*....|....*....|..
gi 2502538751  89 LLREHGYE-AKALLGGLTAWKD 109
Cdd:COG0607    76 LLRRAGYTnVYNLAGGIEAWKA 97
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 9-112 1.25e-14

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: 64.64  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751   9 QEIKQLLEKGTPILFLDVRDEAKFQTGSVEskfaDTRNVPYVHMLAQGDKLLDEETERAV--KERQIITVCTTGNKAQKA 86
Cdd:cd01526    13 KDYKNILQAGKKHVLLDVRPKVHFEICRLP----EAINIPLSELLSKAAELKSLQELPLDndKDSPIYVVCRRGNDSQTA 88

                          90       100
                  ....*....|....*....|....*...
gi 2502538751  87 AALLREHGYEAKA--LLGGLTAWKDDED 112
Cdd:cd01526    89 VRKLKELGLERFVrdIIGGLKAWADKVD 116
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 10-108 1.06e-13

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: 61.16  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751  10 EIKQLLEKGTPILfLDVRDEAKFQTGSVESkfadTRNVPyVHMLAQGDKLLDEEteravKERQIITVCTTGNKAQKAAAL 89
Cdd:cd00158     1 ELKELLDDEDAVL-LDVREPEEYAAGHIPG----AINIP-LSELEERAALLELD-----KDKPIVVYCRSGNRSARAAKL 69

                          90       100
                  ....*....|....*....|
gi 2502538751  90 LREHGY-EAKALLGGLTAWK 108
Cdd:cd00158    70 LRKAGGtNVYNLEGGMLAWK 89
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 21-113 3.38e-12

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: 57.85  E-value: 3.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751   21 ILFLDVRDEAKFQTGSVESkfadTRNVPY---VHMLAQGDKLLDEETERAV---KERQIITVCTTGNKAQKAAALLREHG 94
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPG----AVNIPLselLDRRGELDILEFEELLKRLgldKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 2502538751   95 YE-AKALLGGLTAWKDDEDE 113
Cdd:smart00450  81 FKnVYLLDGGYKEWSAAGPP 100
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 9-109 4.88e-12

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: 57.27  E-value: 4.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751   9 QEIKQLLEKGTPILFLDVRDEAKFQtgsveskfADTRNVPyvhmlaqGDKLLDEET-----ERAVKERQIITVCTTGNKA 83
Cdd:cd01444     5 DELAELLAAGEAPVLLDVRDPASYA--------ALPDHIP-------GAIHLDEDSlddwlGDLDRDRPVVVYCYHGNSS 69

                          90       100
                  ....*....|....*....|....*..
gi 2502538751  84 QKAAALLREHGY-EAKALLGGLTAWKD 109
Cdd:cd01444    70 AQLAQALREAGFtDVRSLAGGFEAWRR 96
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 15-108 4.93e-12

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: 57.11  E-value: 4.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751  15 LEKGTPILfLDVRDEAKFQTGSVESkfAdtRNVPYVHMLAQGDKLLD--EETERAVKERQIITVCTTGNKAQKAAALLRE 92
Cdd:pfam00581   1 LEDGKVVL-IDVRPPEEYAKGHIPG--A--VNVPLSSLSLPPLPLLEllEKLLELLKDKPIVVYCNSGNRAAAAAALLKA 75

                          90
                  ....*....|....*..
gi 2502538751  93 HGY-EAKALLGGLTAWK 108
Cdd:pfam00581  76 LGYkNVYVLDGGFEAWK 92
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 7-109 2.24e-11

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: 55.58  E-value: 2.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751   7 TKQEIKQLLEKGTPILFLDVRDEAKFQTGSVESKFADTRNVPYVHMLAQGDKLLDEeterAVKERQIITVCTTGNKAQKA 86
Cdd:cd01523     2 DPEDLYARLLAGQPLFILDVRNESDYERWKIDGENNTPYFDPYFDFLEIEEDILDQ----LPDDQEVTVICAKEGSSQFV 77

                          90       100
                  ....*....|....*....|...
gi 2502538751  87 AALLREHGYEAKALLGGLTAWKD 109
Cdd:cd01523    78 AELLAERGYDVDYLAGGMKAWSE 100
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
7-112 1.11e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 51.27  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751   7 TKQEIKQLLEKGTP-ILFLDVRDEAKFQT----GSVESKFADTRNVPYVhmlaqgdklldEETERAVKERQIITVCTTGN 81
Cdd:PRK07411  285 TVTELKALLDSGADdFVLIDVRNPNEYEIaripGSVLVPLPDIENGPGV-----------EKVKELLNGHRLIAHCKMGG 353

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2502538751  82 KAQKAAALLREHGYEAKALLGGLTAWKDDED 112
Cdd:PRK07411  354 RSAKALGILKEAGIEGTNVKGGITAWSREVD 384
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
10-110 1.44e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 50.78  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751  10 EIKQLLEKGtpILFLDVRDEAKFQTGSVESKFAdtrnvpyvhmLAQGDKLLDEETERAVKERQIITVCTTGNKAQKAAAL 89
Cdd:PRK08762    9 EARARAAQG--AVLIDVREAHERASGQAEGALR----------IPRGFLELRIETHLPDRDREIVLICASGTRSAHAAAT 76

                          90       100
                  ....*....|....*....|..
gi 2502538751  90 LREHGYE-AKALLGGLTAWKDD 110
Cdd:PRK08762   77 LRELGYTrVASVAGGFSAWKDA 98
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 7-107 1.06e-07

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 48.55  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751   7 TKQEIKQLLEKGTPILFLDVRDEAKFqtgsveskfaDTRNVPYVHMLAQGDKLLDEETERAVKERQIITVCTTGNKAQKA 86
Cdd:PRK07878  290 TPRELKEWLDSGKKIALIDVREPVEW----------DIVHIPGAQLIPKSEILSGEALAKLPQDRTIVLYCKTGVRSAEA 359

                          90       100
                  ....*....|....*....|..
gi 2502538751  87 AALLREHGY-EAKALLGGLTAW 107
Cdd:PRK07878  360 LAALKKAGFsDAVHLQGGVVAW 381
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 10-111 4.42e-07

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: 44.65  E-value: 4.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751  10 EIKQLLEKGTP-ILFLDVRDEAKFQTGSVESkfadTRNVPyvhmlaqGDKLLDEETERAVKERQIITVC--TTGNKAQKA 86
Cdd:cd01521    14 DVAIALKNGKPdFVLVDVRSAEAYARGHVPG----AINLP-------HREICENATAKLDKEKLFVVYCdgPGCNGATKA 82

                          90       100
                  ....*....|....*....|....*
gi 2502538751  87 AALLREHGYEAKALLGGLTAWKDDE 111
Cdd:cd01521    83 ALKLAELGFPVKEMIGGLDWWKREG 107
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 10-108 1.42e-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: 43.02  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751  10 EIKQLLEKGTpiLFLDVRDEAKFQTGSVESKFadtrNVPyvhmlaqgdklLDEETERAV---KERQIITVCTTGNKAQKA 86
Cdd:cd01524     5 ELDNYRADGV--TLIDVRTPQEFEKGHIKGAI----NIP-----------LDELRDRLNelpKDKEIIVYCAVGLRGYIA 67

                          90       100
                  ....*....|....*....|..
gi 2502538751  87 AALLREHGYEAKALLGGLTAWK 108
Cdd:cd01524    68 ARILTQNGFKVKNLDGGYKTYS 89
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 22-95 6.68e-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: 39.23  E-value: 6.68e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2502538751  22 LFLDVRDEA--KFQTGSveskfADTRNVP---YVHMlAQGDKLLDEETERAVKERQIITVCTTGNKAQKAAALLREHGY 95
Cdd:cd01522    17 VLVDVRTEAewKFVGGV-----PDAVHVAwqvYPDM-EINPNFLAELEEKVGKDRPVLLLCRSGNRSIAAAEAAAQAGF 89
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
9-107 6.92e-05

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 38.85  E-value: 6.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751   9 QEIKQLLEKGTPILfLDVRDEAKFQTGSVESKFADTrNVPYVHMLAQGDKlldeeteravkERQIITVCTTGNKAQKAAA 88
Cdd:PRK00162   10 EQAHQKLQEGGAVL-VDIRDPQSFAMGHAPGAFHLT-NDSLGAFMRQADF-----------DTPVMVMCYHGNSSQGAAQ 76

                          90       100
                  ....*....|....*....|
gi 2502538751  89 LLREHGYEA-KALLGGLTAW 107
Cdd:PRK00162   77 YLLQQGFDVvYSIDGGFEAW 96
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 24-107 1.86e-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: 37.66  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751  24 LDVRDEAKFQTGSVESKfadtRNVPYVHMLAQGDKLldEETERAVKERQIITVCTTGNKAQKAAALLREHGYEAKALL-G 102
Cdd:cd01529    16 LDVRAEDEYAAGHLPGK----RSIPGAALVLRSQEL--QALEAPGRATRYVLTCDGSLLARFAAQELLALGGKPVALLdG 89


                  ....*
gi 2502538751 103 GLTAW 107
Cdd:cd01529    90 GTSAW 94
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 7-108 2.67e-03

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: 34.77  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751   7 TKQEIKQLLEKGTpiLFLDVRDEAKFqtgsVESKFADTRNVPyvhmLAQgdklLDEETERAVKERQIITVCTTGNKAQKA 86
Cdd:cd01527     5 SPNDACELLAQGA--VLVDIREPDEY----LRERIPGARLVP----LSQ----LESEGLPLVGANAIIFHCRSGMRTQQN 70

                          90       100
                  ....*....|....*....|...
gi 2502538751  87 AALLRE-HGYEAKALLGGLTAWK 108
Cdd:cd01527    71 AERLAAiSAGEAYVLEGGLDAWK 93
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 9-96 2.79e-03

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: 34.48  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751   9 QEIKQLLEkGTPILFLDVRDEAKFQTGsvesKFADTRNVPYVHMLAQGDKLldEETERAVKERQIITVCTTGNKAQKAAA 88
Cdd:cd01518     7 AEWNELLE-DPEVVLLDVRNDYEYDIG----HFKGAVNPDVDTFREFPFWL--DENLDLLKGKKVLMYCTGGIRCEKASA 79


                  ....*...
gi 2502538751  89 LLREHGYE 96
Cdd:cd01518    80 YLKERGFK 87
PRK01415 PRK01415
hypothetical protein; Validated
 21-110 5.53e-03

hypothetical protein; Validated


Pssm-ID: 167229 [Multi-domain]  Cd Length: 247  Bit Score: 34.92  E-value: 5.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538751  21 ILFLDVRDEAKFQTGSVESKFAdtrnvPYVHMLAQGDKLLdEETERAVKERQIITVCTTGNKAQKAAALLREHGY-EAKA 99
Cdd:PRK01415  128 VIVIDTRNDYEVEVGTFKSAIN-----PNTKTFKQFPAWV-QQNQELLKGKKIAMVCTGGIRCEKSTSLLKSIGYdEVYH 201

                          90
                  ....*....|.
gi 2502538751 100 LLGGLTAWKDD 110
Cdd:PRK01415  202 LKGGILQYLED 212
 
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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