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Conserved domains on  [gi|388453369|ref|NP_001253767|]
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centrosomal protein of 41 kDa [Macaca mulatta]

Protein Classification

rhodanese-like domain-containing protein( domain architecture ID 10456811)

rhodanese-like domain-containing protein may have sulfurtransferase activity if an active site cysteine is present

CATH:  3.40.250.10
PubMed:  12151332|17454295
SCOP:  4000452

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 170-255 2.77e-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: 70.59  E-value: 2.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453369  170 DCPFLLLDVRDRDSYQQCHIVGAYSYPIATLSRTMNPYSNDILEYKN-AHGKIIILYDDDERLASQAATTMCERGFENLF 248
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLLElLKDKPIVVYCNSGNRAAAAAALLKALGYKNVY 82


                  ....*..
gi 388453369  249 MLSGGLK 255
Cdd:pfam00581  83 VLDGGFE 89
 
Name Accession Description Interval E-value
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 170-255 2.77e-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: 70.59  E-value: 2.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453369  170 DCPFLLLDVRDRDSYQQCHIVGAYSYPIATLSRTMNPYSNDILEYKN-AHGKIIILYDDDERLASQAATTMCERGFENLF 248
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLLElLKDKPIVVYCNSGNRAAAAAALLKALGYKNVY 82


                  ....*..
gi 388453369  249 MLSGGLK 255
Cdd:pfam00581  83 VLDGGFE 89
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 170-255 3.92e-15

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: 70.02  E-value: 3.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453369 170 DCPFLLLDVRDRDSYQQCHIVGAYSYPIATLSRtmnpysnDILEYKNAHGKIIILYDDDERLASQAATTMCERGFENLFM 249
Cdd:cd00158    8 DEDAVLLDVREPEEYAAGHIPGAINIPLSELEE-------RAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYN 80


                 ....*.
gi 388453369 250 LSGGLK 255
Cdd:cd00158   81 LEGGML 86
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 173-263 2.54e-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: 62.48  E-value: 2.54e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453369   173 FLLLDVRDRDSYQQCHIVGAYSYPIATLSRTMNPYSNDILEYKNA-----HGKIIILYDDDERLASQAATTMCERGFENL 247
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKrlgldKDKPVVVYCRSGNRSAKAAWLLRELGFKNV 84

                           90
                   ....*....|....*.
gi 388453369   248 FMLSGGLKVLAQKFPE 263
Cdd:smart00450  85 YLLDGGYKEWSAAGPP 100
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 172-255 3.92e-11

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: 59.21  E-value: 3.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453369 172 PFLLLDVRDRDSYQQCHIVGAYSYPIATLSRTMNPYSNDileyknahgKIIILYDDDERLASQAATTMCERGFENLFMLS 251
Cdd:COG0607   19 DAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKD---------KPIVVYCASGGRSAQAAALLRRAGYTNVYNLA 89


                 ....
gi 388453369 252 GGLK 255
Cdd:COG0607   90 GGIE 93
 
Name Accession Description Interval E-value
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 170-255 2.77e-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: 70.59  E-value: 2.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453369  170 DCPFLLLDVRDRDSYQQCHIVGAYSYPIATLSRTMNPYSNDILEYKN-AHGKIIILYDDDERLASQAATTMCERGFENLF 248
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLLElLKDKPIVVYCNSGNRAAAAAALLKALGYKNVY 82


                  ....*..
gi 388453369  249 MLSGGLK 255
Cdd:pfam00581  83 VLDGGFE 89
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 170-255 3.92e-15

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: 70.02  E-value: 3.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453369 170 DCPFLLLDVRDRDSYQQCHIVGAYSYPIATLSRtmnpysnDILEYKNAHGKIIILYDDDERLASQAATTMCERGFENLFM 249
Cdd:cd00158    8 DEDAVLLDVREPEEYAAGHIPGAINIPLSELEE-------RAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYN 80


                 ....*.
gi 388453369 250 LSGGLK 255
Cdd:cd00158   81 LEGGML 86
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 173-263 2.54e-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: 62.48  E-value: 2.54e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453369   173 FLLLDVRDRDSYQQCHIVGAYSYPIATLSRTMNPYSNDILEYKNA-----HGKIIILYDDDERLASQAATTMCERGFENL 247
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKrlgldKDKPVVVYCRSGNRSAKAAWLLRELGFKNV 84

                           90
                   ....*....|....*.
gi 388453369   248 FMLSGGLKVLAQKFPE 263
Cdd:smart00450  85 YLLDGGYKEWSAAGPP 100
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 172-255 3.92e-11

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: 59.21  E-value: 3.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453369 172 PFLLLDVRDRDSYQQCHIVGAYSYPIATLSRTMNPYSNDileyknahgKIIILYDDDERLASQAATTMCERGFENLFMLS 251
Cdd:COG0607   19 DAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKD---------KPIVVYCASGGRSAQAAALLRRAGYTNVYNLA 89


                 ....
gi 388453369 252 GGLK 255
Cdd:COG0607   90 GGIE 93
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 175-254 1.67e-06

Member of the Rhodanese Homology Domain superfamily. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. Only the second and most of the fourth repeats contain the putative catalytic Cys residue. This CD aligns the 1st , 2nd, 3rd, and 4th repeats.


Pssm-ID: 238787 [Multi-domain]  Cd Length: 96  Bit Score: 46.13  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453369 175 LLDVRDRDSYQQCHIVGAYSYPIATLsrtmnPYSNDILEYKNAHGKI--IILYDDDERLASQAATTMCERGFENLFMLSG 252
Cdd:cd01529   15 LLDVRAEDEYAAGHLPGKRSIPGAAL-----VLRSQELQALEAPGRAtrYVLTCDGSLLARFAAQELLALGGKPVALLDG 89


                 ..
gi 388453369 253 GL 254
Cdd:cd01529   90 GT 91
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 174-254 1.90e-04

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: 39.94  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453369 174 LLLDVRDRDSYQQC--HIVGAYSYPIATLSRTMNPYSNDileyknahgKIIILYDDDERLASQAATTMCERGFENLFMLS 251
Cdd:cd01444   18 VLLDVRDPASYAALpdHIPGAIHLDEDSLDDWLGDLDRD---------RPVVVYCYHGNSSAQLAQALREAGFTDVRSLA 88


                 ...
gi 388453369 252 GGL 254
Cdd:cd01444   89 GGF 91
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 175-254 8.29e-04

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


Pssm-ID: 238792 [Multi-domain]  Cd Length: 95  Bit Score: 38.22  E-value: 8.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453369 175 LLDVRDRDSYQQCHIVGAYSYPIATLSRTMNpysndilEYKNAHGKIIILYDDDERLASQAATTMCERGFEnLFMLSGGL 254
Cdd:cd01534   19 RFDVRTPEEYEAGHLPGFRHTPGGQLVQETD-------HFAPVRGARIVLADDDGVRADMTASWLAQMGWE-VYVLEGGL 90
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 173-255 9.44e-04

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: 9.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453369 173 FLLLDVRDRDSYQQCHIVGAYSYPiatlSRTMNPYSNDILEyknaHGKIIILYDDDE--RLASQAATTMCERGFENLFML 250
Cdd:cd01521   26 FVLVDVRSAEAYARGHVPGAINLP----HREICENATAKLD----KEKLFVVYCDGPgcNGATKAALKLAELGFPVKEMI 97


                 ....*
gi 388453369 251 sGGLK 255
Cdd:cd01521   98 -GGLD 101
 
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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