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Conserved domains on  [gi|1238810666|gb|ASW22296|]
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hemerythrin [Proneomeniidae sp. Proneo3]

Protein Classification

Hemerythrin family protein( domain architecture ID 10015447)

Hemerythrin family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Hemerythrin TIGR00058
hemerythrin family non-heme iron protein; This family includes oxygen carrier proteins of ...
 5-120 1.88e-56

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: 170.71  E-value: 1.88e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238810666   5 IPEPYVWDESFKVFYELLDEEHKGLFKGIFDVAKAPSdAGALDHLKKVVEKHFSDEEGMMTAANYPDIGPHKQAHVEFVA 84
Cdd:TIGR00058   1 IPEPYVWDESFKVFYDNLDEEHKTLFNGIFALAADNS-ATALKELIDVTVLHFLDEEAMMIAANYSDYDEHKKAHDDFLA 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1238810666  85 KLKGLTTPVSNDTIHFAKDWLVNHIKGTDFKYKGKL 120
Cdd:TIGR00058  80 VLRGLKAPVPQDDLLYAKDWLVNHIKTTDFKYKGKL 115
 
Name Accession Description Interval E-value
Hemerythrin TIGR00058
hemerythrin family non-heme iron protein; This family includes oxygen carrier proteins of ...
 5-120 1.88e-56

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: 170.71  E-value: 1.88e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238810666   5 IPEPYVWDESFKVFYELLDEEHKGLFKGIFDVAKAPSdAGALDHLKKVVEKHFSDEEGMMTAANYPDIGPHKQAHVEFVA 84
Cdd:TIGR00058   1 IPEPYVWDESFKVFYDNLDEEHKTLFNGIFALAADNS-ATALKELIDVTVLHFLDEEAMMIAANYSDYDEHKKAHDDFLA 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1238810666  85 KLKGLTTPVSNDTIHFAKDWLVNHIKGTDFKYKGKL 120
Cdd:TIGR00058  80 VLRGLKAPVPQDDLLYAKDWLVNHIKTTDFKYKGKL 115
Hemerythrin cd12107
Hemerythrin; Hemerythrin (Hr) is a non-heme diiron oxygen transport protein found in four ...
 20-118 2.10e-25

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: 92.03  E-value: 2.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238810666  20 ELLDEEHKGLFKGIFDVAKAPSD-------AGALDHLKKVVEKHFSDEEGMMTAANYPDIGPHKQAHVEFVAKLKGL--- 89
Cdd:cd12107     1 PEIDEQHKELFELINRLYEAIAAgdgkeelAELLDELIDYTREHFATEEALMEEIGYPDLEEHKAEHRRFLEKLEELkar 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1238810666  90 ----TTPVSNDTIHFAKDWLVNHIKGTDFKYKG 118
Cdd:cd12107    81 leagDLELAEELLDFLKDWLVNHILGEDKKLAR 113
bact_hemeryth NF033749
bacteriohemerythrin; Bacteriohemerythrin, an O2-carrying protein that lacks a heme moiety, is ...
 10-116 4.43e-25

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: 91.79  E-value: 4.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238810666  10 VWDESFKVFYELLDEEHKGLFKGI---FDVAKAPSDA-----GALDHLKKVVEKHFSDEEGMMTAANYPDIGPHKQAHVE 81
Cdd:NF033749    3 TWSDELSVGIKEIDEQHKKLVDLInelHDAMKTGGKGrevlgKILDELIDYTVYHFATEEKLMEKYGYPDYEAHKAEHDK 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1238810666  82 FVAKLKGL-------TTPVSNDTIHFAKDWLVNHIKGTDFKY 116
Cdd:NF033749   83 LVAKVLDLqkkfeagEATLSIELLNFLKDWLVNHILGTDKKY 124
COG2703 COG2703
Hemerythrin [Signal transduction mechanisms];
10-117 7.41e-24

Hemerythrin [Signal transduction mechanisms];


Pssm-ID: 442023  Cd Length: 132  Bit Score: 88.53  E-value: 7.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238810666  10 VWDESFKVFYELLDEEHKGLFK---GIFDVAKAPSD----AGALDHLKKVVEKHFSDEEGMMTAANYPDIGPHKQAHVEF 82
Cdd:COG2703     2 EWSDELSVGIPEIDEQHKELFElinELYDALESGKGreelAELLDELLDYTEEHFAREEALMEEYGYPDLEEHKAEHRRF 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1238810666  83 VAKLKGL-------TTPVSNDTIHFAKDWLVNHIKGTDFKYK 117
Cdd:COG2703    82 LEELEELrerleagDLELARELLEFLKDWLVNHILKEDKKYA 123
Hemerythrin pfam01814
Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to ...
 17-120 1.55e-10

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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043)


Pssm-ID: 396400 [Multi-domain]  Cd Length: 128  Bit Score: 54.54  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238810666  17 VFYELLDEEHKGLFKGIFDVAKAPSDAG---------ALDHLKKVVEKHFSDEEGMM-------TAANYPDIGPHKQAHV 80
Cdd:pfam01814   1 TIIELLDAEHRRLRELLALLRALADALGdshlrklaeLLDELVDELEAHHAAEEELLfpalerrSPGGEAPIEVLRKEHD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1238810666  81 EFVAKLKGLTTPVSN--------DTIHFAKDWLVNHIKGTDFKYKGKL 120
Cdd:pfam01814  81 EIRELLEELEALLKGaepgaafaELLEALAEWLREHIAKEEEVLFPLL 128
PRK00808 PRK00808
bacteriohemerythrin;
8-116 4.04e-09

bacteriohemerythrin;


Pssm-ID: 179132  Cd Length: 150  Bit Score: 51.22  E-value: 4.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238810666   8 PYVWDESFKVFYELLDEEHKGLFKGI--FDVAKAPSDAGA----LDHLKKVVEKHFSDEEGMMTAANYPDIGPHKQAHVE 81
Cdd:PRK00808    3 LLVWQSDLNTGIDVIDQQHKRIVDYInhLHDAQDSPDRLAvaevIDELIDYTLSHFAFEESLMEEAGYPFLVPHKRVHEL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1238810666  82 FVAKLKGLTT------PVSNDTIHFAKDWLVNHIKGTDFKY 116
Cdd:PRK00808   83 FIKRVEEYRErfqageDVADELHGMLSRWLFNHIRNDDAAY 123
 
Name Accession Description Interval E-value
Hemerythrin TIGR00058
hemerythrin family non-heme iron protein; This family includes oxygen carrier proteins of ...
 5-120 1.88e-56

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: 170.71  E-value: 1.88e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238810666   5 IPEPYVWDESFKVFYELLDEEHKGLFKGIFDVAKAPSdAGALDHLKKVVEKHFSDEEGMMTAANYPDIGPHKQAHVEFVA 84
Cdd:TIGR00058   1 IPEPYVWDESFKVFYDNLDEEHKTLFNGIFALAADNS-ATALKELIDVTVLHFLDEEAMMIAANYSDYDEHKKAHDDFLA 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1238810666  85 KLKGLTTPVSNDTIHFAKDWLVNHIKGTDFKYKGKL 120
Cdd:TIGR00058  80 VLRGLKAPVPQDDLLYAKDWLVNHIKTTDFKYKGKL 115
hemeryth_dom TIGR02481
hemerythrin-like metal-binding domain; This model describes both members of the hemerythrin ...
 10-120 4.20e-29

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: 102.03  E-value: 4.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238810666  10 VWDESFKVFYELLDEEHKGLFKGIFDVAKAPSDAGALDHLKKV-------VEKHFSDEEGMMTAANYPDIGPHKQAHVEF 82
Cdd:TIGR02481   1 KWDDSLSTGIEEIDAQHKELFELINELYDALSAGRGKDELKEIlkelidyTENHFADEERLMEAYGYPDLEEHKKEHEKF 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1238810666  83 VAKLKGLTTP--------VSNDTIHFAKDWLVNHIKGTDFKYKGKL 120
Cdd:TIGR02481  81 VKKIEELQEAvaegadesLAEELLDFLKDWLVNHILKEDKKYAPYL 126
Hemerythrin cd12107
Hemerythrin; Hemerythrin (Hr) is a non-heme diiron oxygen transport protein found in four ...
 20-118 2.10e-25

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: 92.03  E-value: 2.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238810666  20 ELLDEEHKGLFKGIFDVAKAPSD-------AGALDHLKKVVEKHFSDEEGMMTAANYPDIGPHKQAHVEFVAKLKGL--- 89
Cdd:cd12107     1 PEIDEQHKELFELINRLYEAIAAgdgkeelAELLDELIDYTREHFATEEALMEEIGYPDLEEHKAEHRRFLEKLEELkar 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1238810666  90 ----TTPVSNDTIHFAKDWLVNHIKGTDFKYKG 118
Cdd:cd12107    81 leagDLELAEELLDFLKDWLVNHILGEDKKLAR 113
bact_hemeryth NF033749
bacteriohemerythrin; Bacteriohemerythrin, an O2-carrying protein that lacks a heme moiety, is ...
 10-116 4.43e-25

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: 91.79  E-value: 4.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238810666  10 VWDESFKVFYELLDEEHKGLFKGI---FDVAKAPSDA-----GALDHLKKVVEKHFSDEEGMMTAANYPDIGPHKQAHVE 81
Cdd:NF033749    3 TWSDELSVGIKEIDEQHKKLVDLInelHDAMKTGGKGrevlgKILDELIDYTVYHFATEEKLMEKYGYPDYEAHKAEHDK 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1238810666  82 FVAKLKGL-------TTPVSNDTIHFAKDWLVNHIKGTDFKY 116
Cdd:NF033749   83 LVAKVLDLqkkfeagEATLSIELLNFLKDWLVNHILGTDKKY 124
COG2703 COG2703
Hemerythrin [Signal transduction mechanisms];
10-117 7.41e-24

Hemerythrin [Signal transduction mechanisms];


Pssm-ID: 442023  Cd Length: 132  Bit Score: 88.53  E-value: 7.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238810666  10 VWDESFKVFYELLDEEHKGLFK---GIFDVAKAPSD----AGALDHLKKVVEKHFSDEEGMMTAANYPDIGPHKQAHVEF 82
Cdd:COG2703     2 EWSDELSVGIPEIDEQHKELFElinELYDALESGKGreelAELLDELLDYTEEHFAREEALMEEYGYPDLEEHKAEHRRF 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1238810666  83 VAKLKGL-------TTPVSNDTIHFAKDWLVNHIKGTDFKYK 117
Cdd:COG2703    82 LEELEELrerleagDLELARELLEFLKDWLVNHILKEDKKYA 123
Hemerythrin-like cd00522
Hemerythrin family; Hemerythrin (Hr) and related proteins are found in bacteria, archaea and ...
 20-118 8.26e-15

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.


Pssm-ID: 213981  Cd Length: 103  Bit Score: 65.01  E-value: 8.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238810666  20 ELLDEEHKGLFKGIFDVAKAPSDAGALDHLKKVVEKHFSDEEGMMTAANY----PDIGPHKQAHVEFVAKLKGLTTPVSN 95
Cdd:cd00522     1 DVFDDEHWRLFQLVFLYCDKLSKAQSLYATFKEFK*HFQIENEYMIGLLQqrsqTIYNVHSDNHLSF*LSLFEKGLKQLK 80

                          90       100
                  ....*....|....*....|...
gi 1238810666  96 DTIHFAKDWLVNHIKGTDFKYKG 118
Cdd:cd00522    81 ERLEAFTRWLVNHIKSEDFEYKG 103
Hemerythrin pfam01814
Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to ...
 17-120 1.55e-10

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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043)


Pssm-ID: 396400 [Multi-domain]  Cd Length: 128  Bit Score: 54.54  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238810666  17 VFYELLDEEHKGLFKGIFDVAKAPSDAG---------ALDHLKKVVEKHFSDEEGMM-------TAANYPDIGPHKQAHV 80
Cdd:pfam01814   1 TIIELLDAEHRRLRELLALLRALADALGdshlrklaeLLDELVDELEAHHAAEEELLfpalerrSPGGEAPIEVLRKEHD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1238810666  81 EFVAKLKGLTTPVSN--------DTIHFAKDWLVNHIKGTDFKYKGKL 120
Cdd:pfam01814  81 EIRELLEELEALLKGaepgaafaELLEALAEWLREHIAKEEEVLFPLL 128
PRK00808 PRK00808
bacteriohemerythrin;
8-116 4.04e-09

bacteriohemerythrin;


Pssm-ID: 179132  Cd Length: 150  Bit Score: 51.22  E-value: 4.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238810666   8 PYVWDESFKVFYELLDEEHKGLFKGI--FDVAKAPSDAGA----LDHLKKVVEKHFSDEEGMMTAANYPDIGPHKQAHVE 81
Cdd:PRK00808    3 LLVWQSDLNTGIDVIDQQHKRIVDYInhLHDAQDSPDRLAvaevIDELIDYTLSHFAFEESLMEEAGYPFLVPHKRVHEL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1238810666  82 FVAKLKGLTT------PVSNDTIHFAKDWLVNHIKGTDFKY 116
Cdd:PRK00808   83 FIKRVEEYRErfqageDVADELHGMLSRWLFNHIRNDDAAY 123
PRK01917 PRK01917
cation-binding hemerythrin HHE family protein; Provisional
 36-113 5.04e-03

cation-binding hemerythrin HHE family protein; Provisional


Pssm-ID: 179353  Cd Length: 139  Bit Score: 34.38  E-value: 5.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238810666  36 VAKAPSDA--GALDHLKKVVEKHFSDEEGMMTAANYPDIGPHKQAHVEFVAKLKGLTTPVSNDTIHF--------AKDWL 105
Cdd:PRK01917   31 VARADDADflQALDAWIDHTRHHFAQEERWMEATKFGPRHCHRAEHDEVLAVAADVREKVARDGDFElgrrlvaeLPEWF 110


                  ....*...
gi 1238810666 106 VNHIKGTD 113
Cdd:PRK01917  111 DQHVRTMD 118
 
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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