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Conserved domains on  [gi|15238192|ref|NP_196072|]
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3-oxoacyl-acyl-carrier synthase-like protein (Protein of unknown function DUF455) [Arabidopsis thaliana]

Protein Classification

ferritin-like domain-containing protein( domain architecture ID 10515402)

ferritin-like domain-containing protein similar to diiron-carboxylate proteins that catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF455 pfam04305
Protein of unknown function (DUF455);
15-282 2.07e-127

Protein of unknown function (DUF455);


:

Pssm-ID: 461256  Cd Length: 247  Bit Score: 362.61  E-value: 2.07e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192    15 NTSDPHEKARLGDSIAVKWLQGAIAEPYDPTVDFPVPDRPARLpvKLVSPSLMPKLGRAGSLQSRQAIVHSLAHTESWAI 94
Cdd:pfam04305   1 LTADPEEKVALTRAAAAAWRAGRLSEIPDAPPPPDRPGRPERP--ELVPPRDVPKRRKLGTLEGRAALLHALAHIELNAI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192    95 DLSWDIIARFgkqEKMPRDFFTDFVRVAQDEGRHFTLLAARLEEIGSSYGALPAHDGLWDSATATSHDLLARLAIEHCVH 174
Cdd:pfam04305  79 DLAWDAIARF---AGLPREFYDDWLKVADDEARHFSLLRERLEELGSEYGDLPAHNGLWEAAEKTAHDLLARLALVPRVL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192   175 EARGLDVLPTTISRFRNGGDNETADLLEkVVYPEEITHCAAGVKWFKYLCERskdpeftisskesddSNEEIINKFHSVV 254
Cdd:pfam04305 156 EARGLDVTPGTIAKLRAAGDEESAAILE-IILRDEIGHVAAGNRWFRYLCEQ---------------RGLDPVATFRELV 219
                         250       260
                  ....*....|....*....|....*...
gi 15238192   255 REHFRGPLKPPFNAEARKAAGFGPQWYE 282
Cdd:pfam04305 220 RRYFRGALKGPFNEEARLKAGFTEEEYE 247
 
Name Accession Description Interval E-value
DUF455 pfam04305
Protein of unknown function (DUF455);
15-282 2.07e-127

Protein of unknown function (DUF455);


Pssm-ID: 461256  Cd Length: 247  Bit Score: 362.61  E-value: 2.07e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192    15 NTSDPHEKARLGDSIAVKWLQGAIAEPYDPTVDFPVPDRPARLpvKLVSPSLMPKLGRAGSLQSRQAIVHSLAHTESWAI 94
Cdd:pfam04305   1 LTADPEEKVALTRAAAAAWRAGRLSEIPDAPPPPDRPGRPERP--ELVPPRDVPKRRKLGTLEGRAALLHALAHIELNAI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192    95 DLSWDIIARFgkqEKMPRDFFTDFVRVAQDEGRHFTLLAARLEEIGSSYGALPAHDGLWDSATATSHDLLARLAIEHCVH 174
Cdd:pfam04305  79 DLAWDAIARF---AGLPREFYDDWLKVADDEARHFSLLRERLEELGSEYGDLPAHNGLWEAAEKTAHDLLARLALVPRVL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192   175 EARGLDVLPTTISRFRNGGDNETADLLEkVVYPEEITHCAAGVKWFKYLCERskdpeftisskesddSNEEIINKFHSVV 254
Cdd:pfam04305 156 EARGLDVTPGTIAKLRAAGDEESAAILE-IILRDEIGHVAAGNRWFRYLCEQ---------------RGLDPVATFRELV 219
                         250       260
                  ....*....|....*....|....*...
gi 15238192   255 REHFRGPLKPPFNAEARKAAGFGPQWYE 282
Cdd:pfam04305 220 RRYFRGALKGPFNEEARLKAGFTEEEYE 247
COG2833 COG2833
Uncharacterized protein, contains ferritin-like DUF455 domain [Function unknown];
5-285 1.77e-98

Uncharacterized protein, contains ferritin-like DUF455 domain [Function unknown];


Pssm-ID: 442081  Cd Length: 265  Bit Score: 289.77  E-value: 1.77e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192   5 TLIESAIRILNTSDPHEKARLGDSIAVKWLQGAIAEPYDPTVDFPvPDRPARlPVK--LVSPSLMPKLgRAGSLQSRQAI 82
Cdd:COG2833   2 TLREAALAVLLTADPAEKLALTRALAAAWRAGRLALDPDPGPAAP-PDRPGR-PARpeLVPPRDVPRR-SLGTPEGRAAL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192  83 VHSLAHTESWAIDLSWDIIARFGKqekMPRDFFTDFVRVAQDEGRHFTLLAARLEEIGSSYGALPAHDGLWDSATATSHD 162
Cdd:COG2833  79 LHAIAHIEFNAINLALDAVLRFPG---MPRAFYDDWLRVAAEEARHFRLLRERLAELGYDYGDFPAHDGLWEMAEKTAHD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192 163 LLARLAIEHCVHEARGLDVLPTTISRFRNGGDNETADLLEkVVYPEEITHCAAGVKWFKYLCE-RSKDPEFTisskesdd 241
Cdd:COG2833 156 LLARMALVPRVLEARGLDVTPGMIEKLRAAGDEEAAAILD-IILRDEIGHVAIGNRWFRYLCEqRGLDPEET-------- 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15238192 242 sneeiinkFHSVVREHFRGPLKPPFNAEARKAAGFGPQWYEPLA 285
Cdd:COG2833 227 --------YRELLRRYFPGRLKGPFNREARRAAGFSEDELDPLA 262
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
81-220 4.06e-16

Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).


Pssm-ID: 153097  Cd Length: 130  Bit Score: 73.30  E-value: 4.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192  81 AIVHSLAHTESWAIDLSWDIIARFGkqekmPRDFFTDFVRVAQDEGRHFTLLAARLEEIGSSYGALPAHDGLWDSATATS 160
Cdd:cd00657   1 RLLNDALAGEYAAIIAYGQLAARAP-----DPDLKDELLEIADEERRHADALAERLRELGGTPPLPPAHLLAAYALPKTS 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192 161 HDLLARLAIEhCVHEARGLDVLPTTISRFRnggDNETADLLEKvVYPEEITHCAAGVKWF 220
Cdd:cd00657  76 DDPAEALRAA-LEVEARAIAAYRELIEQAD---DPELRRLLER-ILADEQRHAAWFRKLL 130
 
Name Accession Description Interval E-value
DUF455 pfam04305
Protein of unknown function (DUF455);
15-282 2.07e-127

Protein of unknown function (DUF455);


Pssm-ID: 461256  Cd Length: 247  Bit Score: 362.61  E-value: 2.07e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192    15 NTSDPHEKARLGDSIAVKWLQGAIAEPYDPTVDFPVPDRPARLpvKLVSPSLMPKLGRAGSLQSRQAIVHSLAHTESWAI 94
Cdd:pfam04305   1 LTADPEEKVALTRAAAAAWRAGRLSEIPDAPPPPDRPGRPERP--ELVPPRDVPKRRKLGTLEGRAALLHALAHIELNAI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192    95 DLSWDIIARFgkqEKMPRDFFTDFVRVAQDEGRHFTLLAARLEEIGSSYGALPAHDGLWDSATATSHDLLARLAIEHCVH 174
Cdd:pfam04305  79 DLAWDAIARF---AGLPREFYDDWLKVADDEARHFSLLRERLEELGSEYGDLPAHNGLWEAAEKTAHDLLARLALVPRVL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192   175 EARGLDVLPTTISRFRNGGDNETADLLEkVVYPEEITHCAAGVKWFKYLCERskdpeftisskesddSNEEIINKFHSVV 254
Cdd:pfam04305 156 EARGLDVTPGTIAKLRAAGDEESAAILE-IILRDEIGHVAAGNRWFRYLCEQ---------------RGLDPVATFRELV 219
                         250       260
                  ....*....|....*....|....*...
gi 15238192   255 REHFRGPLKPPFNAEARKAAGFGPQWYE 282
Cdd:pfam04305 220 RRYFRGALKGPFNEEARLKAGFTEEEYE 247
COG2833 COG2833
Uncharacterized protein, contains ferritin-like DUF455 domain [Function unknown];
5-285 1.77e-98

Uncharacterized protein, contains ferritin-like DUF455 domain [Function unknown];


Pssm-ID: 442081  Cd Length: 265  Bit Score: 289.77  E-value: 1.77e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192   5 TLIESAIRILNTSDPHEKARLGDSIAVKWLQGAIAEPYDPTVDFPvPDRPARlPVK--LVSPSLMPKLgRAGSLQSRQAI 82
Cdd:COG2833   2 TLREAALAVLLTADPAEKLALTRALAAAWRAGRLALDPDPGPAAP-PDRPGR-PARpeLVPPRDVPRR-SLGTPEGRAAL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192  83 VHSLAHTESWAIDLSWDIIARFGKqekMPRDFFTDFVRVAQDEGRHFTLLAARLEEIGSSYGALPAHDGLWDSATATSHD 162
Cdd:COG2833  79 LHAIAHIEFNAINLALDAVLRFPG---MPRAFYDDWLRVAAEEARHFRLLRERLAELGYDYGDFPAHDGLWEMAEKTAHD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192 163 LLARLAIEHCVHEARGLDVLPTTISRFRNGGDNETADLLEkVVYPEEITHCAAGVKWFKYLCE-RSKDPEFTisskesdd 241
Cdd:COG2833 156 LLARMALVPRVLEARGLDVTPGMIEKLRAAGDEEAAAILD-IILRDEIGHVAIGNRWFRYLCEqRGLDPEET-------- 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15238192 242 sneeiinkFHSVVREHFRGPLKPPFNAEARKAAGFGPQWYEPLA 285
Cdd:COG2833 227 --------YRELLRRYFPGRLKGPFNREARRAAGFSEDELDPLA 262
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
81-220 4.06e-16

Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).


Pssm-ID: 153097  Cd Length: 130  Bit Score: 73.30  E-value: 4.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192  81 AIVHSLAHTESWAIDLSWDIIARFGkqekmPRDFFTDFVRVAQDEGRHFTLLAARLEEIGSSYGALPAHDGLWDSATATS 160
Cdd:cd00657   1 RLLNDALAGEYAAIIAYGQLAARAP-----DPDLKDELLEIADEERRHADALAERLRELGGTPPLPPAHLLAAYALPKTS 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238192 161 HDLLARLAIEhCVHEARGLDVLPTTISRFRnggDNETADLLEKvVYPEEITHCAAGVKWF 220
Cdd:cd00657  76 DDPAEALRAA-LEVEARAIAAYRELIEQAD---DPELRRLLER-ILADEQRHAAWFRKLL 130
 
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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