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Conserved domains on  [gi|488943120|ref|WP_002854195|]
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MULTISPECIES: hemerythrin domain-containing protein [Campylobacter]

Protein Classification

hemerythrin domain-containing protein( domain architecture ID 81998)

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

CATH:  1.20.120.50
Gene Ontology:  GO:0046872
PubMed:  18081840
SCOP:  4000819

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Hemerythrin-like super family cl15774
Hemerythrin family; Hemerythrin (Hr) and related proteins are found in bacteria, archaea and ...
 8-127 5.05e-25

Hemerythrin family; Hemerythrin (Hr) and related proteins are found in bacteria, archaea and eukaryotes. They are non-heme diiron oxygen transport proteins. In addition to oxygen transport, members are involved in cadmium fixation and host anti-bacterial defense. They have the same "four alpha helix bundle" motif and similar active site structures. Some members, like Hr, form oligomers, the octameric form being most prevalent, while others are monomeric.


The actual alignment was detected with superfamily member TIGR02481:

Pssm-ID: 449588  Cd Length: 126  Bit Score: 92.01  E-value: 5.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943120    8 ISMNNDLLDHQHKELFEISKKLSLMNQCHVGTKELKIVLRELLIMINRHFSDEEAFMRKIEYPYINHHTRIHRK-IILEI 86
Cdd:TIGR02481   6 LSTGIEEIDAQHKELFELINELYDALSAGRGKDELKEILKELIDYTENHFADEERLMEAYGYPDLEEHKKEHEKfVKKIE 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 488943120   87 EEIIISEAKFVNIMTEKLNLVVQDFIFKHTAKEDSKIVKYY 127
Cdd:TIGR02481  86 ELQEAVAEGADESLAEELLDFLKDWLVNHILKEDKKYAPYL 126
 
Name Accession Description Interval E-value
hemeryth_dom TIGR02481
hemerythrin-like metal-binding domain; This model describes both members of the hemerythrin ...
 8-127 5.05e-25

hemerythrin-like metal-binding domain; This model describes both members of the hemerythrin (TIGR00058) family of marine invertebrates and a broader collection of bacterial and archaeal homologs. Many of the latter group are multidomain proteins with signal-transducing domains such as the GGDEF diguanylate cyclase domain (TIGR00254, pfam00990) and methyl-accepting chemotaxis protein signaling domain (pfam00015). Most hemerythrins are oxygen-carriers with a bound non-heme iron, but at least one example is a cadmium-binding protein, apparently with a role in sequestering toxic metals rather than in binding oxygen. Patterns of conserved residues suggest that all prokaryotic instances of this domain bind iron or another heavy metal, but the exact function is unknown. Not surprisingly, the prokaryote with the most instances of this domain is Magnetococcus sp. MC-1, a magnetotactic bacterium.


Pssm-ID: 274154  Cd Length: 126  Bit Score: 92.01  E-value: 5.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943120    8 ISMNNDLLDHQHKELFEISKKLSLMNQCHVGTKELKIVLRELLIMINRHFSDEEAFMRKIEYPYINHHTRIHRK-IILEI 86
Cdd:TIGR02481   6 LSTGIEEIDAQHKELFELINELYDALSAGRGKDELKEILKELIDYTENHFADEERLMEAYGYPDLEEHKKEHEKfVKKIE 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 488943120   87 EEIIISEAKFVNIMTEKLNLVVQDFIFKHTAKEDSKIVKYY 127
Cdd:TIGR02481  86 ELQEAVAEGADESLAEELLDFLKDWLVNHILKEDKKYAPYL 126
COG2703 COG2703
Hemerythrin [Signal transduction mechanisms];
9-130 7.07e-18

Hemerythrin [Signal transduction mechanisms];


Pssm-ID: 442023  Cd Length: 132  Bit Score: 73.89  E-value: 7.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943120   9 SMNNDLLDHQHKELFEISKKLSLMNQCHVGTKELKIVLRELLIMINRHFSDEEAFMRKIEYPYINHHTRIHRKIILEIEE 88
Cdd:COG2703    8 SVGIPEIDEQHKELFELINELYDALESGKGREELAELLDELLDYTEEHFAREEALMEEYGYPDLEEHKAEHRRFLEELEE 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488943120  89 IIISEAKFVNIMTEKLNLVVQDFIFKHTAKEDSKIVKYYEEK 130
Cdd:COG2703   88 LRERLEAGDLELARELLEFLKDWLVNHILKEDKKYARYLKKK 129
Hemerythrin cd12107
Hemerythrin; Hemerythrin (Hr) is a non-heme diiron oxygen transport protein found in four ...
 13-125 1.37e-15

Hemerythrin; Hemerythrin (Hr) is a non-heme diiron oxygen transport protein found in four marine invertebrate phyla including priapulida, brachiopoda, sipunculida, and annelida, as well as in protozoa. Myohemerythrin (Mhr), a hemerythrin homolog, is found in the muscle tissue of sipunculids as well as in polycheate and oligocheate annelids. In addition to oxygen transport, Mhr proteins are involved in cadmium fixation and host anti-bacterial defense. Hr and Mhr proteins have the same "four alpha helix bundle" motif and active site structure. Hr forms oligomers, the octameric form being most prevalent, while Mhr is monomeric.


Pssm-ID: 213982  Cd Length: 113  Bit Score: 67.38  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943120  13 DLLDHQHKELFEISKKLSLMNQCHVGTKELKIVLRELLIMINRHFSDEEAFMRKIEYPYINHHTRIHRKIILEIEEIIIS 92
Cdd:cd12107    1 PEIDEQHKELFELINRLYEAIAAGDGKEELAELLDELIDYTREHFATEEALMEEIGYPDLEEHKAEHRRFLEKLEELKAR 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488943120  93 EAKFVNIMTEKLNLVVQDFIFKHTAKEDSKIVK 125
Cdd:cd12107   81 LEAGDLELAEELLDFLKDWLVNHILGEDKKLAR 113
bact_hemeryth NF033749
bacteriohemerythrin; Bacteriohemerythrin, an O2-carrying protein that lacks a heme moiety, is ...
 9-81 2.39e-07

bacteriohemerythrin; Bacteriohemerythrin, an O2-carrying protein that lacks a heme moiety, is named based on its homology to eukaryotic proteins such as myohemerythrin.


Pssm-ID: 468167  Cd Length: 129  Bit Score: 46.34  E-value: 2.39e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488943120   9 SMNNDLLDHQHKELFEISKKL-SLMNQCHVGTKELKIVLRELLIMINRHFSDEEAFMRKIEYPYINHHTRIHRK 81
Cdd:NF033749   9 SVGIKEIDEQHKKLVDLINELhDAMKTGGKGREVLGKILDELIDYTVYHFATEEKLMEKYGYPDYEAHKAEHDK 82
PRK00808 PRK00808
bacteriohemerythrin;
13-120 6.70e-04

bacteriohemerythrin;


Pssm-ID: 179132  Cd Length: 150  Bit Score: 37.36  E-value: 6.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943120  13 DLLDHQHKELFEISKKLSLMNQC--HVGTKElkiVLRELLIMINRHFSDEEAFMRKIEYPYINHHTRIHRKIILEIEEII 90
Cdd:PRK00808  15 DVIDQQHKRIVDYINHLHDAQDSpdRLAVAE---VIDELIDYTLSHFAFEESLMEEAGYPFLVPHKRVHELFIKRVEEYR 91

                         90       100       110
                 ....*....|....*....|....*....|
gi 488943120  91 ISEAKFVNIMTEKLNLvVQDFIFKHTAKED 120
Cdd:PRK00808  92 ERFQAGEDVADELHGM-LSRWLFNHIRNDD 120
 
Name Accession Description Interval E-value
hemeryth_dom TIGR02481
hemerythrin-like metal-binding domain; This model describes both members of the hemerythrin ...
 8-127 5.05e-25

hemerythrin-like metal-binding domain; This model describes both members of the hemerythrin (TIGR00058) family of marine invertebrates and a broader collection of bacterial and archaeal homologs. Many of the latter group are multidomain proteins with signal-transducing domains such as the GGDEF diguanylate cyclase domain (TIGR00254, pfam00990) and methyl-accepting chemotaxis protein signaling domain (pfam00015). Most hemerythrins are oxygen-carriers with a bound non-heme iron, but at least one example is a cadmium-binding protein, apparently with a role in sequestering toxic metals rather than in binding oxygen. Patterns of conserved residues suggest that all prokaryotic instances of this domain bind iron or another heavy metal, but the exact function is unknown. Not surprisingly, the prokaryote with the most instances of this domain is Magnetococcus sp. MC-1, a magnetotactic bacterium.


Pssm-ID: 274154  Cd Length: 126  Bit Score: 92.01  E-value: 5.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943120    8 ISMNNDLLDHQHKELFEISKKLSLMNQCHVGTKELKIVLRELLIMINRHFSDEEAFMRKIEYPYINHHTRIHRK-IILEI 86
Cdd:TIGR02481   6 LSTGIEEIDAQHKELFELINELYDALSAGRGKDELKEILKELIDYTENHFADEERLMEAYGYPDLEEHKKEHEKfVKKIE 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 488943120   87 EEIIISEAKFVNIMTEKLNLVVQDFIFKHTAKEDSKIVKYY 127
Cdd:TIGR02481  86 ELQEAVAEGADESLAEELLDFLKDWLVNHILKEDKKYAPYL 126
COG2703 COG2703
Hemerythrin [Signal transduction mechanisms];
9-130 7.07e-18

Hemerythrin [Signal transduction mechanisms];


Pssm-ID: 442023  Cd Length: 132  Bit Score: 73.89  E-value: 7.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943120   9 SMNNDLLDHQHKELFEISKKLSLMNQCHVGTKELKIVLRELLIMINRHFSDEEAFMRKIEYPYINHHTRIHRKIILEIEE 88
Cdd:COG2703    8 SVGIPEIDEQHKELFELINELYDALESGKGREELAELLDELLDYTEEHFAREEALMEEYGYPDLEEHKAEHRRFLEELEE 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488943120  89 IIISEAKFVNIMTEKLNLVVQDFIFKHTAKEDSKIVKYYEEK 130
Cdd:COG2703   88 LRERLEAGDLELARELLEFLKDWLVNHILKEDKKYARYLKKK 129
Hemerythrin cd12107
Hemerythrin; Hemerythrin (Hr) is a non-heme diiron oxygen transport protein found in four ...
 13-125 1.37e-15

Hemerythrin; Hemerythrin (Hr) is a non-heme diiron oxygen transport protein found in four marine invertebrate phyla including priapulida, brachiopoda, sipunculida, and annelida, as well as in protozoa. Myohemerythrin (Mhr), a hemerythrin homolog, is found in the muscle tissue of sipunculids as well as in polycheate and oligocheate annelids. In addition to oxygen transport, Mhr proteins are involved in cadmium fixation and host anti-bacterial defense. Hr and Mhr proteins have the same "four alpha helix bundle" motif and active site structure. Hr forms oligomers, the octameric form being most prevalent, while Mhr is monomeric.


Pssm-ID: 213982  Cd Length: 113  Bit Score: 67.38  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943120  13 DLLDHQHKELFEISKKLSLMNQCHVGTKELKIVLRELLIMINRHFSDEEAFMRKIEYPYINHHTRIHRKIILEIEEIIIS 92
Cdd:cd12107    1 PEIDEQHKELFELINRLYEAIAAGDGKEELAELLDELIDYTREHFATEEALMEEIGYPDLEEHKAEHRRFLEKLEELKAR 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488943120  93 EAKFVNIMTEKLNLVVQDFIFKHTAKEDSKIVK 125
Cdd:cd12107   81 LEAGDLELAEELLDFLKDWLVNHILGEDKKLAR 113
bact_hemeryth NF033749
bacteriohemerythrin; Bacteriohemerythrin, an O2-carrying protein that lacks a heme moiety, is ...
 9-81 2.39e-07

bacteriohemerythrin; Bacteriohemerythrin, an O2-carrying protein that lacks a heme moiety, is named based on its homology to eukaryotic proteins such as myohemerythrin.


Pssm-ID: 468167  Cd Length: 129  Bit Score: 46.34  E-value: 2.39e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488943120   9 SMNNDLLDHQHKELFEISKKL-SLMNQCHVGTKELKIVLRELLIMINRHFSDEEAFMRKIEYPYINHHTRIHRK 81
Cdd:NF033749   9 SVGIKEIDEQHKKLVDLINELhDAMKTGGKGREVLGKILDELIDYTVYHFATEEKLMEKYGYPDYEAHKAEHDK 82
PRK00808 PRK00808
bacteriohemerythrin;
13-120 6.70e-04

bacteriohemerythrin;


Pssm-ID: 179132  Cd Length: 150  Bit Score: 37.36  E-value: 6.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943120  13 DLLDHQHKELFEISKKLSLMNQC--HVGTKElkiVLRELLIMINRHFSDEEAFMRKIEYPYINHHTRIHRKIILEIEEII 90
Cdd:PRK00808  15 DVIDQQHKRIVDYINHLHDAQDSpdRLAVAE---VIDELIDYTLSHFAFEESLMEEAGYPFLVPHKRVHELFIKRVEEYR 91

                         90       100       110
                 ....*....|....*....|....*....|
gi 488943120  91 ISEAKFVNIMTEKLNLvVQDFIFKHTAKED 120
Cdd:PRK00808  92 ERFQAGEDVADELHGM-LSRWLFNHIRNDD 120
Hemerythrin TIGR00058
hemerythrin family non-heme iron protein; This family includes oxygen carrier proteins of ...
 12-81 2.79e-03

hemerythrin family non-heme iron protein; This family includes oxygen carrier proteins of various oligomeric states from the vascular fluid (hemerythrin) and muscle (myohemerythrin) of some marine invertebrates. Each unit binds 2 non-heme Fe using 5 H, one E and one D. One member of this family,from the sandworm Nereis diversicolor, is an unusual (non-metallothionein) cadmium-binding protein. Homologous proteins, excluded from this narrowly defined family, are found in archaea and bacteria (see pfam01814).


Pssm-ID: 129168  Cd Length: 115  Bit Score: 35.12  E-value: 2.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943120   12 NDLLDHQHKELFEiskklSLMNQCHVGTKElkiVLRELLIMINRHFSDEEAFMRKIEYPYINHHTRIHRK 81
Cdd:TIGR00058  15 YDNLDEEHKTLFN-----GIFALAADNSAT---ALKELIDVTVLHFLDEEAMMIAANYSDYDEHKKAHDD 76
 
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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