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Conserved domains on  [gi|17508157|ref|NP_492023|]
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FErroChelatase-Like [Caenorhabditis elegans]

Protein Classification

ferrochelatase( domain architecture ID 1004157)

ferrochelatase catalyzes the insertion of the ferrous form of iron into protoporphyrin IX in the heme synthesis pathway

CATH:  3.40.50.1400
EC:  4.98.1.1
Gene Ontology:  GO:0004325|GO:0006783
PubMed:  7592569
SCOP:  4000838

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
hemH super family cl30481
ferrochelatase; Human ferrochelatase, found at the mitochondrial inner membrane inner surface, ...
26-313 4.27e-10

ferrochelatase; Human ferrochelatase, found at the mitochondrial inner membrane inner surface, was shown in an active recombinant form to be a homodimer. This contrasts to an earlier finding by gel filtration that overexpressed E. coli ferrochelatase runs as a monomer. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


The actual alignment was detected with superfamily member TIGR00109:

Pssm-ID: 272909 [Multi-domain]  Cd Length: 322  Bit Score: 60.16  E-value: 4.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508157    26 RSPQTEIILLHAGQPWNEFHAKEFLKNQSAQSMRLRMPN-----FVHTLIANgkLKNENLKGCIAAYKNVPSL----ESQ 96
Cdd:TIGR00109   2 KRKKTGVLLMNLGGPDKLEEVERFLKQLFADPRIIDISRakwrkPLAKMILP--LRSPKIAKNYEAIGGGSPLlqitEQQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508157    97 VDRLGKKIeesldtvvPEHGPFKVSRLFQFDEVSFEDQLKEIKSHRSQHYIFMPLYPHFSAIDSETLLVKSAKIIeqtss 176
Cdd:TIGR00109  80 AHALEKRL--------PNEIDFKVYIAMRYGEPFTEEAVKELLKDGVERAVVLPLYPHFSSSTTGSSFNELAEAL----- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508157   177 plvqgnKNITSSRIeqnsdysyDVSAIWRWNNHPILADYWSSKIKEVL---PKLDGVV--FAA---PRKFTCNYGPVFAS 248
Cdd:TIGR00109 147 ------KKLRSLRP--------TISVIESWYDNPKYIKALADSIKETLasfPEPDNAVllFSAhglPQSYVDEGDPYPAE 212
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17508157   249 CERT----MNQLGDLIPWRLGFYSSwdsfdLPSMQGVASQVQK-IRKTSESG--KVAVVPITDVIETFNTLY 313
Cdd:TIGR00109 213 CEATtrliAEKLGFPNEYRLTWQSR-----VGPEPWLGPYTEElLEKLGEQGvqHIVVVPIGFTADHLETLY 279
 
Name Accession Description Interval E-value
hemH TIGR00109
ferrochelatase; Human ferrochelatase, found at the mitochondrial inner membrane inner surface, ...
26-313 4.27e-10

ferrochelatase; Human ferrochelatase, found at the mitochondrial inner membrane inner surface, was shown in an active recombinant form to be a homodimer. This contrasts to an earlier finding by gel filtration that overexpressed E. coli ferrochelatase runs as a monomer. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 272909 [Multi-domain]  Cd Length: 322  Bit Score: 60.16  E-value: 4.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508157    26 RSPQTEIILLHAGQPWNEFHAKEFLKNQSAQSMRLRMPN-----FVHTLIANgkLKNENLKGCIAAYKNVPSL----ESQ 96
Cdd:TIGR00109   2 KRKKTGVLLMNLGGPDKLEEVERFLKQLFADPRIIDISRakwrkPLAKMILP--LRSPKIAKNYEAIGGGSPLlqitEQQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508157    97 VDRLGKKIeesldtvvPEHGPFKVSRLFQFDEVSFEDQLKEIKSHRSQHYIFMPLYPHFSAIDSETLLVKSAKIIeqtss 176
Cdd:TIGR00109  80 AHALEKRL--------PNEIDFKVYIAMRYGEPFTEEAVKELLKDGVERAVVLPLYPHFSSSTTGSSFNELAEAL----- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508157   177 plvqgnKNITSSRIeqnsdysyDVSAIWRWNNHPILADYWSSKIKEVL---PKLDGVV--FAA---PRKFTCNYGPVFAS 248
Cdd:TIGR00109 147 ------KKLRSLRP--------TISVIESWYDNPKYIKALADSIKETLasfPEPDNAVllFSAhglPQSYVDEGDPYPAE 212
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17508157   249 CERT----MNQLGDLIPWRLGFYSSwdsfdLPSMQGVASQVQK-IRKTSESG--KVAVVPITDVIETFNTLY 313
Cdd:TIGR00109 213 CEATtrliAEKLGFPNEYRLTWQSR-----VGPEPWLGPYTEElLEKLGEQGvqHIVVVPIGFTADHLETLY 279
 
Name Accession Description Interval E-value
hemH TIGR00109
ferrochelatase; Human ferrochelatase, found at the mitochondrial inner membrane inner surface, ...
26-313 4.27e-10

ferrochelatase; Human ferrochelatase, found at the mitochondrial inner membrane inner surface, was shown in an active recombinant form to be a homodimer. This contrasts to an earlier finding by gel filtration that overexpressed E. coli ferrochelatase runs as a monomer. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 272909 [Multi-domain]  Cd Length: 322  Bit Score: 60.16  E-value: 4.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508157    26 RSPQTEIILLHAGQPWNEFHAKEFLKNQSAQSMRLRMPN-----FVHTLIANgkLKNENLKGCIAAYKNVPSL----ESQ 96
Cdd:TIGR00109   2 KRKKTGVLLMNLGGPDKLEEVERFLKQLFADPRIIDISRakwrkPLAKMILP--LRSPKIAKNYEAIGGGSPLlqitEQQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508157    97 VDRLGKKIeesldtvvPEHGPFKVSRLFQFDEVSFEDQLKEIKSHRSQHYIFMPLYPHFSAIDSETLLVKSAKIIeqtss 176
Cdd:TIGR00109  80 AHALEKRL--------PNEIDFKVYIAMRYGEPFTEEAVKELLKDGVERAVVLPLYPHFSSSTTGSSFNELAEAL----- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508157   177 plvqgnKNITSSRIeqnsdysyDVSAIWRWNNHPILADYWSSKIKEVL---PKLDGVV--FAA---PRKFTCNYGPVFAS 248
Cdd:TIGR00109 147 ------KKLRSLRP--------TISVIESWYDNPKYIKALADSIKETLasfPEPDNAVllFSAhglPQSYVDEGDPYPAE 212
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17508157   249 CERT----MNQLGDLIPWRLGFYSSwdsfdLPSMQGVASQVQK-IRKTSESG--KVAVVPITDVIETFNTLY 313
Cdd:TIGR00109 213 CEATtrliAEKLGFPNEYRLTWQSR-----VGPEPWLGPYTEElLEKLGEQGvqHIVVVPIGFTADHLETLY 279
 
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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