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Conserved domains on  [gi|488390499|ref|WP_002459884|]
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MULTISPECIES: hydrogen peroxide-dependent heme synthase [Staphylococcus]

Protein Classification

heme-binding protein( domain architecture ID 10013905)

uncharacterized heme-binding protein similar to Bacillus subtilis putative heme-dependent peroxidase YwfI and Listeria monocytogenenes chlorite dismutase-like protein HemQ

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK12276 PRK12276
putative heme peroxidase; Provisional
1-249 1.31e-175

putative heme peroxidase; Provisional


:

Pssm-ID: 237033  Cd Length: 248  Bit Score: 482.53  E-value: 1.31e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499   1 MSEAAETLDGWYSLHLFYAIDWTTFRLVPEDDRHAMVQELQQFLADKANARASHTGDQALYNITGQKADLLLWVLRPEMK 80
Cdd:PRK12276   1 MSEAAITLDGWYCLHDFRSIDWAAWKTLSSDEREAAVDEFLAFLEKWEEVEAAKQGSHAIYSIVGQKADLMLMILRPTME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499  81 ELNIIENELNKCRISDFLIPTYSYVSVIELGNYLAGkSDEDPYENPHIKARLYPELPHSEYICFYPMDKRRNETYNWYML 160
Cdd:PRK12276  81 ELNEIENELNKTRLADYLIPAYSYVSVVELSNYLAS-SDEDPYQNPHVKARLYPELPKSKYICFYPMDKRRQGGDNWYML 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499 161 PMEDRKELMYNHGKIGRKYAGKIKQFITGSVGFDDFEWGVTLFSDDVLQFKKIVYEMRFDETTARYGEFGSFYIGHILEL 240
Cdd:PRK12276 160 PMEERQKLMYSHGMIGRKYAGKVKQIITGSVGFDDWEWGVTLFADDPLQFKKIVYEMRFDEVSARYGEFGSFFVGNILPA 239

                 ....*....
gi 488390499 241 DQLDSFFAI 249
Cdd:PRK12276 240 EELLQFLHI 248
 
Name Accession Description Interval E-value
PRK12276 PRK12276
putative heme peroxidase; Provisional
1-249 1.31e-175

putative heme peroxidase; Provisional


Pssm-ID: 237033  Cd Length: 248  Bit Score: 482.53  E-value: 1.31e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499   1 MSEAAETLDGWYSLHLFYAIDWTTFRLVPEDDRHAMVQELQQFLADKANARASHTGDQALYNITGQKADLLLWVLRPEMK 80
Cdd:PRK12276   1 MSEAAITLDGWYCLHDFRSIDWAAWKTLSSDEREAAVDEFLAFLEKWEEVEAAKQGSHAIYSIVGQKADLMLMILRPTME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499  81 ELNIIENELNKCRISDFLIPTYSYVSVIELGNYLAGkSDEDPYENPHIKARLYPELPHSEYICFYPMDKRRNETYNWYML 160
Cdd:PRK12276  81 ELNEIENELNKTRLADYLIPAYSYVSVVELSNYLAS-SDEDPYQNPHVKARLYPELPKSKYICFYPMDKRRQGGDNWYML 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499 161 PMEDRKELMYNHGKIGRKYAGKIKQFITGSVGFDDFEWGVTLFSDDVLQFKKIVYEMRFDETTARYGEFGSFYIGHILEL 240
Cdd:PRK12276 160 PMEERQKLMYSHGMIGRKYAGKVKQIITGSVGFDDWEWGVTLFADDPLQFKKIVYEMRFDEVSARYGEFGSFFVGNILPA 239

                 ....*....
gi 488390499 241 DQLDSFFAI 249
Cdd:PRK12276 240 EELLQFLHI 248
HemQ COG3253
Coproheme decarboxylase/chlorite dismutase [Coenzyme transport and metabolism, Inorganic ion ...
1-247 6.03e-101

Coproheme decarboxylase/chlorite dismutase [Coenzyme transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 442484  Cd Length: 231  Bit Score: 293.27  E-value: 6.03e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499   1 MSEAAeTLDGWYSLHLFYAIdWTTFRLVPEDDRHAMVQELQQFLADKANArashTGDQALYNITGQK--ADLLLWVLRPE 78
Cdd:COG3253    1 MSEAP-TEEGWYTLHSFFKV-WPAWRRLPDEEREEAAAEFEELLEELEAE----GGLRGLYDVSGLRadADLMFWHHAPT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499  79 MKELNIIENELNKCRISDFLIPTYSYVSVIELGNYLAgksdeDPYENPHIKARlypELPHSEYICFYPMDKRRNetynWY 158
Cdd:COG3253   75 LEDLQAAEREFRRTALGRYLEPTWSYVSVTRPSEYNK-----DSHLPAFLAGR---ELPPRKYVCVYPFVKSRE----WY 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499 159 MLPMEDRKELMYNHGKIGRKYAGKIKQFITGSVGFDDFEWGVTLFSDDVLQFKKIVYEMRFDETTARYGEFGSFYIGHIL 238
Cdd:COG3253  143 LLPFEERREMMAEHGMIGRKYAGKVRQNTTGSFGLDDYEWGVALEADDLHDFVDLVYELRFDEARAHVREFGPFYTGRRL 222

                 ....*....
gi 488390499 239 ELDQLDSFF 247
Cdd:COG3253  223 DPEELLAVL 231
Chlor_dismutase pfam06778
Chlorite dismutase; This family contains chlorite dismutase enzymes of bacterial and archaeal ...
33-238 8.55e-87

Chlorite dismutase; This family contains chlorite dismutase enzymes of bacterial and archaeal origin. This enzyme catalyzes the disproportionation of chlorite into chloride and oxygen. Note that many family members are hypothetical proteins.


Pssm-ID: 429114  Cd Length: 191  Bit Score: 255.91  E-value: 8.55e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499   33 RHAMVQELQQFLADKANArashtGDQALYNITGQK--ADLLLWVLRPEMKELNIIENELNKCRISDFLIPTYSYVSVIEL 110
Cdd:pfam06778   1 REAAAEEFEALLEEAAEG-----GLRGVYSVLGLRadADLMFWHHRPTLEDLQAAERRFRRTALGGYLEPVYSYVSVHEP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499  111 GNYLAGksdedpyENPHIKARLYPELPHSEYICFYPMDKRRNetynWYMLPMEDRKELMYNHGKIGRKYaGKIKQFITGS 190
Cdd:pfam06778  76 SEYVDG-------NKSHVPAFLYPELPPRKYVCVYPMVKSRE----WYLLPFEERREMMAEHGMIGRKY-PKVRQNTTGS 143
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 488390499  191 VGFDDFEWGVTLFSDDVLQFKKIVYEMRFDETTARYGEFGSFYIGHIL 238
Cdd:pfam06778 144 FGLDDYEWGVAFEADDLLDFKDLVYELRFDEASAHVREEGPFYTGRRL 191
 
Name Accession Description Interval E-value
PRK12276 PRK12276
putative heme peroxidase; Provisional
1-249 1.31e-175

putative heme peroxidase; Provisional


Pssm-ID: 237033  Cd Length: 248  Bit Score: 482.53  E-value: 1.31e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499   1 MSEAAETLDGWYSLHLFYAIDWTTFRLVPEDDRHAMVQELQQFLADKANARASHTGDQALYNITGQKADLLLWVLRPEMK 80
Cdd:PRK12276   1 MSEAAITLDGWYCLHDFRSIDWAAWKTLSSDEREAAVDEFLAFLEKWEEVEAAKQGSHAIYSIVGQKADLMLMILRPTME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499  81 ELNIIENELNKCRISDFLIPTYSYVSVIELGNYLAGkSDEDPYENPHIKARLYPELPHSEYICFYPMDKRRNETYNWYML 160
Cdd:PRK12276  81 ELNEIENELNKTRLADYLIPAYSYVSVVELSNYLAS-SDEDPYQNPHVKARLYPELPKSKYICFYPMDKRRQGGDNWYML 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499 161 PMEDRKELMYNHGKIGRKYAGKIKQFITGSVGFDDFEWGVTLFSDDVLQFKKIVYEMRFDETTARYGEFGSFYIGHILEL 240
Cdd:PRK12276 160 PMEERQKLMYSHGMIGRKYAGKVKQIITGSVGFDDWEWGVTLFADDPLQFKKIVYEMRFDEVSARYGEFGSFFVGNILPA 239

                 ....*....
gi 488390499 241 DQLDSFFAI 249
Cdd:PRK12276 240 EELLQFLHI 248
HemQ COG3253
Coproheme decarboxylase/chlorite dismutase [Coenzyme transport and metabolism, Inorganic ion ...
1-247 6.03e-101

Coproheme decarboxylase/chlorite dismutase [Coenzyme transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 442484  Cd Length: 231  Bit Score: 293.27  E-value: 6.03e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499   1 MSEAAeTLDGWYSLHLFYAIdWTTFRLVPEDDRHAMVQELQQFLADKANArashTGDQALYNITGQK--ADLLLWVLRPE 78
Cdd:COG3253    1 MSEAP-TEEGWYTLHSFFKV-WPAWRRLPDEEREEAAAEFEELLEELEAE----GGLRGLYDVSGLRadADLMFWHHAPT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499  79 MKELNIIENELNKCRISDFLIPTYSYVSVIELGNYLAgksdeDPYENPHIKARlypELPHSEYICFYPMDKRRNetynWY 158
Cdd:COG3253   75 LEDLQAAEREFRRTALGRYLEPTWSYVSVTRPSEYNK-----DSHLPAFLAGR---ELPPRKYVCVYPFVKSRE----WY 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499 159 MLPMEDRKELMYNHGKIGRKYAGKIKQFITGSVGFDDFEWGVTLFSDDVLQFKKIVYEMRFDETTARYGEFGSFYIGHIL 238
Cdd:COG3253  143 LLPFEERREMMAEHGMIGRKYAGKVRQNTTGSFGLDDYEWGVALEADDLHDFVDLVYELRFDEARAHVREFGPFYTGRRL 222

                 ....*....
gi 488390499 239 ELDQLDSFF 247
Cdd:COG3253  223 DPEELLAVL 231
PRK09565 PRK09565
heme-binding protein;
1-248 8.05e-87

heme-binding protein;


Pssm-ID: 236571 [Multi-domain]  Cd Length: 533  Bit Score: 267.45  E-value: 8.05e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499   1 MSEAAETLDGWYSLHLFYAIDWTTFRLVPEDDRHAMVQELQQFLADKANARASHTGDQALYNITGQKADLLLWVLRPEMK 80
Cdd:PRK09565   3 RREPPQTEEGWYVLHDFRSIDWDAWRDAPERVRDRAIEEGIDYLQAHEAVEDAEEGDSAVFSVLGHKADLLILHLRPTLA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499  81 ELNIIENELNKCRISDFLIPTYSYVSVIELGNYLA-------GKSDEDPYENPHIKARLYPELPHSEYICFYPMDKRRNE 153
Cdd:PRK09565  83 DLDRAERRFEQTALAAFTEQADSYVSVTEASGYTEksreyfeGEVDDDSGLARYIESRLHPEIPDAEFVSFYPMSKRRGP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499 154 TYNWYMLPMEDRKELMYNHGKIGRKYAGKIKQFITGSVGFDDFEWGVTLFSDDVLQFKKIVYEMRFDETTARYGEFGSFY 233
Cdd:PRK09565 163 EHNWYDLPFDERAEHMSSHGDIGRQYAGKVTQIIAGSIGFDDWEWGVTLFADDPTDIKELLYEMRFDPSSSKFAEFGRFY 242
                        250
                 ....*....|....*
gi 488390499 234 IGHILELDQLDSFFA 248
Cdd:PRK09565 243 VGRRFPPSDLGAFLA 257
Chlor_dismutase pfam06778
Chlorite dismutase; This family contains chlorite dismutase enzymes of bacterial and archaeal ...
33-238 8.55e-87

Chlorite dismutase; This family contains chlorite dismutase enzymes of bacterial and archaeal origin. This enzyme catalyzes the disproportionation of chlorite into chloride and oxygen. Note that many family members are hypothetical proteins.


Pssm-ID: 429114  Cd Length: 191  Bit Score: 255.91  E-value: 8.55e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499   33 RHAMVQELQQFLADKANArashtGDQALYNITGQK--ADLLLWVLRPEMKELNIIENELNKCRISDFLIPTYSYVSVIEL 110
Cdd:pfam06778   1 REAAAEEFEALLEEAAEG-----GLRGVYSVLGLRadADLMFWHHRPTLEDLQAAERRFRRTALGGYLEPVYSYVSVHEP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390499  111 GNYLAGksdedpyENPHIKARLYPELPHSEYICFYPMDKRRNetynWYMLPMEDRKELMYNHGKIGRKYaGKIKQFITGS 190
Cdd:pfam06778  76 SEYVDG-------NKSHVPAFLYPELPPRKYVCVYPMVKSRE----WYLLPFEERREMMAEHGMIGRKY-PKVRQNTTGS 143
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 488390499  191 VGFDDFEWGVTLFSDDVLQFKKIVYEMRFDETTARYGEFGSFYIGHIL 238
Cdd:pfam06778 144 FGLDDYEWGVAFEADDLLDFKDLVYELRFDEASAHVREEGPFYTGRRL 191
 
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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