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Conserved domains on  [gi|2172123877|ref|WP_233272525|]
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MULTISPECIES: heme-binding protein [Rhodococcus]

Protein Classification

GlcG/HbpS family heme-binding protein( domain architecture ID 10007034)

heme-binding protein may degrade heme, sequester iron, and may protect from iron-mediated oxidative stress; similar to Salmonella enterica corrinoid adenosyltransferase PduO that converts cob(I)alamin to adenosylcobalamin (adenosylcob(III)alamin), the cofactor for propanediol dehydratase

CATH:  3.30.450.150
Gene Ontology:  GO:0020037
PubMed:  19244623|8606183
SCOP:  4003947

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GlcG COG3193
Heme-binding protein HbpS, GlcG/HbpS family [Signal transduction mechanisms];
1-128 1.60e-24

Heme-binding protein HbpS, GlcG/HbpS family [Signal transduction mechanisms];


:

Pssm-ID: 442426  Cd Length: 135  Bit Score: 91.37  E-value: 1.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172123877   1 MATAESAIRAALEMAESDGVGICVAIVDDRGHDLMVVR-DKAIWFTAGAARAKAATAALLGMPTSSFAELAGEYPDLSPl 79
Cdd:COG3193     7 LEDARKIAAAALAKARELGVPVAIAVVDAGGNLLAFLRmDGAPLGSIDIAIGKAYTAAAFGRPTGELEERAQPGPPLLG- 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2172123877  80 IQSQVREPMTTLPGGVPLTVDGEVVGGIGVSGATPEQDAQYAHVGAEIF 128
Cdd:COG3193    86 LNTSNGPGLVPFGGGVPIKVDGEVIGAIGVSGGTSEQDEAIAQAGLAAL 134
 
Name Accession Description Interval E-value
GlcG COG3193
Heme-binding protein HbpS, GlcG/HbpS family [Signal transduction mechanisms];
1-128 1.60e-24

Heme-binding protein HbpS, GlcG/HbpS family [Signal transduction mechanisms];


Pssm-ID: 442426  Cd Length: 135  Bit Score: 91.37  E-value: 1.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172123877   1 MATAESAIRAALEMAESDGVGICVAIVDDRGHDLMVVR-DKAIWFTAGAARAKAATAALLGMPTSSFAELAGEYPDLSPl 79
Cdd:COG3193     7 LEDARKIAAAALAKARELGVPVAIAVVDAGGNLLAFLRmDGAPLGSIDIAIGKAYTAAAFGRPTGELEERAQPGPPLLG- 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2172123877  80 IQSQVREPMTTLPGGVPLTVDGEVVGGIGVSGATPEQDAQYAHVGAEIF 128
Cdd:COG3193    86 LNTSNGPGLVPFGGGVPIKVDGEVIGAIGVSGGTSEQDEAIAQAGLAAL 134
HbpS-like pfam03928
Haem degrading protein HbpS-like; This entry includes haem degrading protein HbpS from ...
2-121 2.42e-20

Haem degrading protein HbpS-like; This entry includes haem degrading protein HbpS from Streptomyces reticuli (swiss:Q9RIM2) and and GlcG from Escherichia coli. HbpS is up-regulated in response to haemin- and peroxide-based oxidative stress. It interacts with the SenS/SenR two-component signal transduction system. Iron binds to surface-exposed lysine residues of an octomeric assembly of the protein. The structure of GlcG is composed of an alpha-beta(2)-alpha(3)-beta(2)-alpha fold, similar to the Roadblock/LC7 domain.


Pssm-ID: 461095 [Multi-domain]  Cd Length: 116  Bit Score: 79.85  E-value: 2.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172123877   2 ATAESAIRAALEMAESDGVGICVAIVDDRGHDLMVVR-DKAIWFTAGAARAKAATAALLGMPTSSFAELAGEYPDLSPLI 80
Cdd:pfam03928   4 EDAWELGAAAVAKARELGVPVAIAVVDAGGHLLFFARmDGASLDSIDIARRKAYTAARFGRSTSALGERAGPGDAPEYAP 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2172123877  81 qsqvrepmttLPGGVPLTVDGEVVGGIGVSGATPEQDAQYA 121
Cdd:pfam03928  84 ----------FGGGVPIRVDGVVVGAIGVSGGTGEEDHAVA 114
PRK09732 PRK09732
hypothetical protein; Provisional
4-130 4.08e-09

hypothetical protein; Provisional


Pssm-ID: 170072  Cd Length: 134  Bit Score: 51.31  E-value: 4.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172123877   4 AESAIRAALEMAESDGVGICVAIVDDRGHDLMVVR-DKAIWFTAGAARAKAATAALLGMPTSSFAELAGEypDLSPLIQS 82
Cdd:PRK09732   12 ASAIIAAGQEEAQKNNWSVSIAVADDGGHLLALSRmDDCAPIAAYISQEKARTAALGRRETKGYEEMVNN--GRTAFVTA 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2172123877  83 QVrepMTTLPGGVPLTVDGEVVGGIGVSGATPEQDAQYAHVGAEIFVR 130
Cdd:PRK09732   90 PL---LTSLEGGVPVVVDGQIIGAVGVSGLTGAQDAQVAKAAAAVLAK 134
 
Name Accession Description Interval E-value
GlcG COG3193
Heme-binding protein HbpS, GlcG/HbpS family [Signal transduction mechanisms];
1-128 1.60e-24

Heme-binding protein HbpS, GlcG/HbpS family [Signal transduction mechanisms];


Pssm-ID: 442426  Cd Length: 135  Bit Score: 91.37  E-value: 1.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172123877   1 MATAESAIRAALEMAESDGVGICVAIVDDRGHDLMVVR-DKAIWFTAGAARAKAATAALLGMPTSSFAELAGEYPDLSPl 79
Cdd:COG3193     7 LEDARKIAAAALAKARELGVPVAIAVVDAGGNLLAFLRmDGAPLGSIDIAIGKAYTAAAFGRPTGELEERAQPGPPLLG- 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2172123877  80 IQSQVREPMTTLPGGVPLTVDGEVVGGIGVSGATPEQDAQYAHVGAEIF 128
Cdd:COG3193    86 LNTSNGPGLVPFGGGVPIKVDGEVIGAIGVSGGTSEQDEAIAQAGLAAL 134
HbpS-like pfam03928
Haem degrading protein HbpS-like; This entry includes haem degrading protein HbpS from ...
2-121 2.42e-20

Haem degrading protein HbpS-like; This entry includes haem degrading protein HbpS from Streptomyces reticuli (swiss:Q9RIM2) and and GlcG from Escherichia coli. HbpS is up-regulated in response to haemin- and peroxide-based oxidative stress. It interacts with the SenS/SenR two-component signal transduction system. Iron binds to surface-exposed lysine residues of an octomeric assembly of the protein. The structure of GlcG is composed of an alpha-beta(2)-alpha(3)-beta(2)-alpha fold, similar to the Roadblock/LC7 domain.


Pssm-ID: 461095 [Multi-domain]  Cd Length: 116  Bit Score: 79.85  E-value: 2.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172123877   2 ATAESAIRAALEMAESDGVGICVAIVDDRGHDLMVVR-DKAIWFTAGAARAKAATAALLGMPTSSFAELAGEYPDLSPLI 80
Cdd:pfam03928   4 EDAWELGAAAVAKARELGVPVAIAVVDAGGHLLFFARmDGASLDSIDIARRKAYTAARFGRSTSALGERAGPGDAPEYAP 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2172123877  81 qsqvrepmttLPGGVPLTVDGEVVGGIGVSGATPEQDAQYA 121
Cdd:pfam03928  84 ----------FGGGVPIRVDGVVVGAIGVSGGTGEEDHAVA 114
PRK09732 PRK09732
hypothetical protein; Provisional
4-130 4.08e-09

hypothetical protein; Provisional


Pssm-ID: 170072  Cd Length: 134  Bit Score: 51.31  E-value: 4.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172123877   4 AESAIRAALEMAESDGVGICVAIVDDRGHDLMVVR-DKAIWFTAGAARAKAATAALLGMPTSSFAELAGEypDLSPLIQS 82
Cdd:PRK09732   12 ASAIIAAGQEEAQKNNWSVSIAVADDGGHLLALSRmDDCAPIAAYISQEKARTAALGRRETKGYEEMVNN--GRTAFVTA 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2172123877  83 QVrepMTTLPGGVPLTVDGEVVGGIGVSGATPEQDAQYAHVGAEIFVR 130
Cdd:PRK09732   90 PL---LTSLEGGVPVVVDGQIIGAVGVSGLTGAQDAQVAKAAAAVLAK 134
 
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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