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Conserved domains on  [gi|19115925|ref|NP_595013|]
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cation-binding HHE domain-containing protein [Schizosaccharomyces pombe]

Protein Classification

hemerythrin domain-containing protein( domain architecture ID 10485355)

hemerythrin domain-containing protein adopts a four alpha helix bundle fold and may bind cations

Gene Ontology:  GO:0043169

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5592 super family cl44265
Hemerythrin domain-containing protein [General function prediction only];
23-175 2.21e-15

Hemerythrin domain-containing protein [General function prediction only];


The actual alignment was detected with superfamily member COG5592:

Pssm-ID: 444331 [Multi-domain]  Cd Length: 151  Bit Score: 70.02  E-value: 2.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115925  23 MTRISDAIFKDHRKLQSDYQNIKSANDYDTATRWQNQFVWELARHSVGEEIVVYPKFEKYLGEEGKEMAEKdrhEHQLVK 102
Cdd:COG5592   1 MMNIQDLIRMDHQKVNTLFEEILQTNDPQKIQEYFGQLYKDLRAHAEAEEEVVYPAVRPFYGEEPTQELYD---EQAEMK 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115925 103 EMLYKFQSMKANQSNFIPALDELMESLQKHIDEEEQHDIPFLEKHLSEEESLHMASSFERTKKFVPTHSHPSA 175
Cdd:COG5592  78 QLLDEIKALDPSSPEFKDRIRQLKDLVGDHVRQEESTLFPAIRNNLSPEQQEQLATEFKAAKSKLQDQMAQAV 150
 
Name Accession Description Interval E-value
COG5592 COG5592
Hemerythrin domain-containing protein [General function prediction only];
23-175 2.21e-15

Hemerythrin domain-containing protein [General function prediction only];


Pssm-ID: 444331 [Multi-domain]  Cd Length: 151  Bit Score: 70.02  E-value: 2.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115925  23 MTRISDAIFKDHRKLQSDYQNIKSANDYDTATRWQNQFVWELARHSVGEEIVVYPKFEKYLGEEGKEMAEKdrhEHQLVK 102
Cdd:COG5592   1 MMNIQDLIRMDHQKVNTLFEEILQTNDPQKIQEYFGQLYKDLRAHAEAEEEVVYPAVRPFYGEEPTQELYD---EQAEMK 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115925 103 EMLYKFQSMKANQSNFIPALDELMESLQKHIDEEEQHDIPFLEKHLSEEESLHMASSFERTKKFVPTHSHPSA 175
Cdd:COG5592  78 QLLDEIKALDPSSPEFKDRIRQLKDLVGDHVRQEESTLFPAIRNNLSPEQQEQLATEFKAAKSKLQDQMAQAV 150
Hemerythrin pfam01814
Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to ...
 25-144 1.67e-09

Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor Swiss:P80255 binds Cadmium so as to protect the organizm from toxicity. However Hemerythrin is classically described as Oxygen-binding through two attached Fe2+ ions. And the bacterial Swiss:Q7WX96 is a regulator of response to NO, which suggests yet another set-up for its metal ligands. In Staphylococcus aureus P72360 has been noted to be important when the organizm switches to living in environments with low oxygen concentrations; perhaps this protein acts as an oxygen store or scavenger. This domain can bind oxygen (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043)


Pssm-ID: 396400 [Multi-domain]  Cd Length: 128  Bit Score: 53.77  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115925    25 RISDAIFKDHRKLQSDYQNIKSAND------YDTATRWQNQFVWELARHSVGEEIVVYPKFEKYLGeEGKEMAEKDRHEH 98
Cdd:pfam01814   1 TIIELLDAEHRRLRELLALLRALADalgdshLRKLAELLDELVDELEAHHAAEEELLFPALERRSP-GGEAPIEVLRKEH 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 19115925    99 QLVKEMLYKFQSMKANQSN---FIPALDELMESLQKHIDEEEQHDIPFL 144
Cdd:pfam01814  80 DEIRELLEELEALLKGAEPgaaFAELLEALAEWLREHIAKEEEVLFPLL 128
Hr-like cd12108
Hemerythrin-like domain; Hemerythrin (Hr) like domains have the same four alpha helix bundle ...
 63-138 7.66e-05

Hemerythrin-like domain; Hemerythrin (Hr) like domains have the same four alpha helix bundle and a similar, but slightly different active site structure than hemerythrin. They are non-heme diiron binding proteins mainly found in bacteria and eukaryotes. Like Hr, they may be involved in oxygen transport or like human FBXL5 (F-box and leucine-rich repeat protein 5), a member of this group, play a role in cellular iron homeostasis.


Pssm-ID: 213983 [Multi-domain]  Cd Length: 130  Bit Score: 40.88  E-value: 7.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115925  63 ELARHSVGEEIVVYPKFEKYLGEEgkEMAEKDRHEHQLVKEMLYKFQSM--------KANQSNFIPALDELMESLQKHID 134
Cdd:cd12108  45 ELHHHHTAEEELLFPALRERVPLA--AVLDALEAEHAEIDELLARLEALlpallagdAEDAEELAAALEALRTALREHLD 122


                ....
gi 19115925 135 EEEQ 138
Cdd:cd12108 123 EEEE 126
 
Name Accession Description Interval E-value
COG5592 COG5592
Hemerythrin domain-containing protein [General function prediction only];
23-175 2.21e-15

Hemerythrin domain-containing protein [General function prediction only];


Pssm-ID: 444331 [Multi-domain]  Cd Length: 151  Bit Score: 70.02  E-value: 2.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115925  23 MTRISDAIFKDHRKLQSDYQNIKSANDYDTATRWQNQFVWELARHSVGEEIVVYPKFEKYLGEEGKEMAEKdrhEHQLVK 102
Cdd:COG5592   1 MMNIQDLIRMDHQKVNTLFEEILQTNDPQKIQEYFGQLYKDLRAHAEAEEEVVYPAVRPFYGEEPTQELYD---EQAEMK 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115925 103 EMLYKFQSMKANQSNFIPALDELMESLQKHIDEEEQHDIPFLEKHLSEEESLHMASSFERTKKFVPTHSHPSA 175
Cdd:COG5592  78 QLLDEIKALDPSSPEFKDRIRQLKDLVGDHVRQEESTLFPAIRNNLSPEQQEQLATEFKAAKSKLQDQMAQAV 150
Hemerythrin pfam01814
Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to ...
 25-144 1.67e-09

Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor Swiss:P80255 binds Cadmium so as to protect the organizm from toxicity. However Hemerythrin is classically described as Oxygen-binding through two attached Fe2+ ions. And the bacterial Swiss:Q7WX96 is a regulator of response to NO, which suggests yet another set-up for its metal ligands. In Staphylococcus aureus P72360 has been noted to be important when the organizm switches to living in environments with low oxygen concentrations; perhaps this protein acts as an oxygen store or scavenger. This domain can bind oxygen (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043)


Pssm-ID: 396400 [Multi-domain]  Cd Length: 128  Bit Score: 53.77  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115925    25 RISDAIFKDHRKLQSDYQNIKSAND------YDTATRWQNQFVWELARHSVGEEIVVYPKFEKYLGeEGKEMAEKDRHEH 98
Cdd:pfam01814   1 TIIELLDAEHRRLRELLALLRALADalgdshLRKLAELLDELVDELEAHHAAEEELLFPALERRSP-GGEAPIEVLRKEH 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 19115925    99 QLVKEMLYKFQSMKANQSN---FIPALDELMESLQKHIDEEEQHDIPFL 144
Cdd:pfam01814  80 DEIRELLEELEALLKGAEPgaaFAELLEALAEWLREHIAKEEEVLFPLL 128
COG3945 COG3945
Hemerythrin domain [General function prediction only];
71-162 2.35e-07

Hemerythrin domain [General function prediction only];


Pssm-ID: 443145 [Multi-domain]  Cd Length: 180  Bit Score: 48.86  E-value: 2.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115925  71 EEIVVYPKFEKYLGEEGKEMAEKdRHEH----QLVKEMLYKFQSMKANQSN----FIPALDELMESLQKHIDEEEQHDIP 142
Cdd:COG3945  58 EEDILFPRLEERGGEAAGPIAVL-LAEHeqgrQLTRELEEALEAYLAGDVVardeLAAALRAYIALLRQHIAKEENVLFP 136

                        90       100
                ....*....|....*....|
gi 19115925 143 FLEKHLSEEESLHMASSFER 162
Cdd:COG3945 137 LAERLLSDEDWEELGEAFEE 156
Hr-like cd12108
Hemerythrin-like domain; Hemerythrin (Hr) like domains have the same four alpha helix bundle ...
 63-138 7.66e-05

Hemerythrin-like domain; Hemerythrin (Hr) like domains have the same four alpha helix bundle and a similar, but slightly different active site structure than hemerythrin. They are non-heme diiron binding proteins mainly found in bacteria and eukaryotes. Like Hr, they may be involved in oxygen transport or like human FBXL5 (F-box and leucine-rich repeat protein 5), a member of this group, play a role in cellular iron homeostasis.


Pssm-ID: 213983 [Multi-domain]  Cd Length: 130  Bit Score: 40.88  E-value: 7.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115925  63 ELARHSVGEEIVVYPKFEKYLGEEgkEMAEKDRHEHQLVKEMLYKFQSM--------KANQSNFIPALDELMESLQKHID 134
Cdd:cd12108  45 ELHHHHTAEEELLFPALRERVPLA--AVLDALEAEHAEIDELLARLEALlpallagdAEDAEELAAALEALRTALREHLD 122


                ....
gi 19115925 135 EEEQ 138
Cdd:cd12108 123 EEEE 126
 
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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