NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15596870|ref|NP_250364|]
View 

bacteriohemerythrin [Pseudomonas aeruginosa PAO1]

Protein Classification

bacteriohemerythrin( domain architecture ID 10792071)

bacteriohemerythrin is an oxygen-binding protein that may be involved in a storage mechanism or for delivery to oxygen-requiring enzymes

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK00808 PRK00808
bacteriohemerythrin;
1-150 1.75e-92

bacteriohemerythrin;


:

Pssm-ID: 179132  Cd Length: 150  Bit Score: 264.62  E-value: 1.75e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870    1 MAHLVWQDDLNTGIQVIDNQHKRIVEMINHLHDAQQGKEHAAIAEVIEELVDYTLSHFAFEETLMEDAGYQFSRAHKKIH 80
Cdd:PRK00808   1 MALLVWQSDLNTGIDVIDQQHKRIVDYINHLHDAQDSPDRLAVAEVIDELIDYTLSHFAFEESLMEEAGYPFLVPHKRVH 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870   81 ELFIRRVSEYRVRFQAGEDVGDELKGLLSRWLFNHIRNDDAGYVDAVRHSMSELVKDKSEGGWLSRSMKR 150
Cdd:PRK00808  81 ELFIKRVEEYRERFQAGEDVADELHGMLSRWLFNHIRNDDAAYVDAVKANMDGISREKEGGGWLARTLKR 150
 
Name Accession Description Interval E-value
PRK00808 PRK00808
bacteriohemerythrin;
1-150 1.75e-92

bacteriohemerythrin;


Pssm-ID: 179132  Cd Length: 150  Bit Score: 264.62  E-value: 1.75e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870    1 MAHLVWQDDLNTGIQVIDNQHKRIVEMINHLHDAQQGKEHAAIAEVIEELVDYTLSHFAFEETLMEDAGYQFSRAHKKIH 80
Cdd:PRK00808   1 MALLVWQSDLNTGIDVIDQQHKRIVDYINHLHDAQDSPDRLAVAEVIDELIDYTLSHFAFEESLMEEAGYPFLVPHKRVH 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870   81 ELFIRRVSEYRVRFQAGEDVGDELKGLLSRWLFNHIRNDDAGYVDAVRHSMSELVKDKSEGGWLSRSMKR 150
Cdd:PRK00808  81 ELFIKRVEEYRERFQAGEDVADELHGMLSRWLFNHIRNDDAAYVDAVKANMDGISREKEGGGWLARTLKR 150
bact_hemeryth NF033749
bacteriohemerythrin; Bacteriohemerythrin, an O2-carrying protein that lacks a heme moiety, is ...
 4-128 4.12e-54

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: 166.90  E-value: 4.12e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870    4 LVWQDDLNTGIQVIDNQHKRIVEMINHLHDA--QQGKEHAAIAEVIEELVDYTLSHFAFEETLMEDAGYQFSRAHKKIHE 81
Cdd:NF033749   2 ITWSDELSVGIKEIDEQHKKLVDLINELHDAmkTGGKGREVLGKILDELIDYTVYHFATEEKLMEKYGYPDYEAHKAEHD 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15596870   82 LFIRRVSEYRVRFQAGE-DVGDELKGLLSRWLFNHIRNDDAGYVDAVR 128
Cdd:NF033749  82 KLVAKVLDLQKKFEAGEaTLSIELLNFLKDWLVNHILGTDKKYGPFLN 129
COG2703 COG2703
Hemerythrin [Signal transduction mechanisms];
4-128 3.42e-41

Hemerythrin [Signal transduction mechanisms];


Pssm-ID: 442023  Cd Length: 132  Bit Score: 133.98  E-value: 3.42e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870   4 LVWQDDLNTGIQVIDNQHKRIVEMINHLHDA-QQGKEHAAIAEVIEELVDYTLSHFAFEETLMEDAGYQFSRAHKKIHEL 82
Cdd:COG2703   1 LEWSDELSVGIPEIDEQHKELFELINELYDAlESGKGREELAELLDELLDYTEEHFAREEALMEEYGYPDLEEHKAEHRR 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15596870  83 FIRRVSEYRVRFQAG-EDVGDELKGLLSRWLFNHIRNDDAGYVDAVR 128
Cdd:COG2703  81 FLEELEELRERLEAGdLELARELLEFLKDWLVNHILKEDKKYARYLK 127
hemeryth_dom TIGR02481
hemerythrin-like metal-binding domain; This model describes both members of the hemerythrin ...
 5-125 2.44e-36

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: 121.68  E-value: 2.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870     5 VWQDDLNTGIQVIDNQHKRIVEMINHLHDA-QQGKEHAAIAEVIEELVDYTLSHFAFEETLMEDAGYQFSRAHKKIHELF 83
Cdd:TIGR02481   1 KWDDSLSTGIEEIDAQHKELFELINELYDAlSAGRGKDELKEILKELIDYTENHFADEERLMEAYGYPDLEEHKKEHEKF 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15596870    84 IRRVSEYRVRFQAG--EDVGDELKGLLSRWLFNHIRNDDAGYVD 125
Cdd:TIGR02481  81 VKKIEELQEAVAEGadESLAEELLDFLKDWLVNHILKEDKKYAP 124
Hemerythrin cd12107
Hemerythrin; Hemerythrin (Hr) is a non-heme diiron oxygen transport protein found in four ...
 15-125 1.06e-32

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: 112.06  E-value: 1.06e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870  15 QVIDNQHKRIVEMINHLHDA-QQGKEHAAIAEVIEELVDYTLSHFAFEETLMEDAGYQFSRAHKKIHELFIRRVSEYRVR 93
Cdd:cd12107   1 PEIDEQHKELFELINRLYEAiAAGDGKEELAELLDELIDYTREHFATEEALMEEIGYPDLEEHKAEHRRFLEKLEELKAR 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 15596870  94 FQAG-EDVGDELKGLLSRWLFNHIRNDDAGYVD 125
Cdd:cd12107  81 LEAGdLELAEELLDFLKDWLVNHILGEDKKLAR 113
Hemerythrin pfam01814
Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to ...
 12-127 2.10e-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: 52.23  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870    12 TGIQVIDNQHKRIVEMINHLHDAQQGKEH---AAIAEVIEELVDYTLSHFAFEETLM-------EDAGYQFSRAHKKIHE 81
Cdd:pfam01814   1 TIIELLDAEHRRLRELLALLRALADALGDshlRKLAELLDELVDELEAHHAAEEELLfpalerrSPGGEAPIEVLRKEHD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 15596870    82 LFIRRVSEYRVRFQAGEDVGDELKGL--LSRWLFNHIRNDDAGYVDAV 127
Cdd:pfam01814  81 EIRELLEELEALLKGAEPGAAFAELLeaLAEWLREHIAKEEEVLFPLL 128
 
Name Accession Description Interval E-value
PRK00808 PRK00808
bacteriohemerythrin;
1-150 1.75e-92

bacteriohemerythrin;


Pssm-ID: 179132  Cd Length: 150  Bit Score: 264.62  E-value: 1.75e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870    1 MAHLVWQDDLNTGIQVIDNQHKRIVEMINHLHDAQQGKEHAAIAEVIEELVDYTLSHFAFEETLMEDAGYQFSRAHKKIH 80
Cdd:PRK00808   1 MALLVWQSDLNTGIDVIDQQHKRIVDYINHLHDAQDSPDRLAVAEVIDELIDYTLSHFAFEESLMEEAGYPFLVPHKRVH 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870   81 ELFIRRVSEYRVRFQAGEDVGDELKGLLSRWLFNHIRNDDAGYVDAVRHSMSELVKDKSEGGWLSRSMKR 150
Cdd:PRK00808  81 ELFIKRVEEYRERFQAGEDVADELHGMLSRWLFNHIRNDDAAYVDAVKANMDGISREKEGGGWLARTLKR 150
bact_hemeryth NF033749
bacteriohemerythrin; Bacteriohemerythrin, an O2-carrying protein that lacks a heme moiety, is ...
 4-128 4.12e-54

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: 166.90  E-value: 4.12e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870    4 LVWQDDLNTGIQVIDNQHKRIVEMINHLHDA--QQGKEHAAIAEVIEELVDYTLSHFAFEETLMEDAGYQFSRAHKKIHE 81
Cdd:NF033749   2 ITWSDELSVGIKEIDEQHKKLVDLINELHDAmkTGGKGREVLGKILDELIDYTVYHFATEEKLMEKYGYPDYEAHKAEHD 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15596870   82 LFIRRVSEYRVRFQAGE-DVGDELKGLLSRWLFNHIRNDDAGYVDAVR 128
Cdd:NF033749  82 KLVAKVLDLQKKFEAGEaTLSIELLNFLKDWLVNHILGTDKKYGPFLN 129
COG2703 COG2703
Hemerythrin [Signal transduction mechanisms];
4-128 3.42e-41

Hemerythrin [Signal transduction mechanisms];


Pssm-ID: 442023  Cd Length: 132  Bit Score: 133.98  E-value: 3.42e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870   4 LVWQDDLNTGIQVIDNQHKRIVEMINHLHDA-QQGKEHAAIAEVIEELVDYTLSHFAFEETLMEDAGYQFSRAHKKIHEL 82
Cdd:COG2703   1 LEWSDELSVGIPEIDEQHKELFELINELYDAlESGKGREELAELLDELLDYTEEHFAREEALMEEYGYPDLEEHKAEHRR 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15596870  83 FIRRVSEYRVRFQAG-EDVGDELKGLLSRWLFNHIRNDDAGYVDAVR 128
Cdd:COG2703  81 FLEELEELRERLEAGdLELARELLEFLKDWLVNHILKEDKKYARYLK 127
hemeryth_dom TIGR02481
hemerythrin-like metal-binding domain; This model describes both members of the hemerythrin ...
 5-125 2.44e-36

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: 121.68  E-value: 2.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870     5 VWQDDLNTGIQVIDNQHKRIVEMINHLHDA-QQGKEHAAIAEVIEELVDYTLSHFAFEETLMEDAGYQFSRAHKKIHELF 83
Cdd:TIGR02481   1 KWDDSLSTGIEEIDAQHKELFELINELYDAlSAGRGKDELKEILKELIDYTENHFADEERLMEAYGYPDLEEHKKEHEKF 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15596870    84 IRRVSEYRVRFQAG--EDVGDELKGLLSRWLFNHIRNDDAGYVD 125
Cdd:TIGR02481  81 VKKIEELQEAVAEGadESLAEELLDFLKDWLVNHILKEDKKYAP 124
Hemerythrin cd12107
Hemerythrin; Hemerythrin (Hr) is a non-heme diiron oxygen transport protein found in four ...
 15-125 1.06e-32

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: 112.06  E-value: 1.06e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870  15 QVIDNQHKRIVEMINHLHDA-QQGKEHAAIAEVIEELVDYTLSHFAFEETLMEDAGYQFSRAHKKIHELFIRRVSEYRVR 93
Cdd:cd12107   1 PEIDEQHKELFELINRLYEAiAAGDGKEELAELLDELIDYTREHFATEEALMEEIGYPDLEEHKAEHRRFLEKLEELKAR 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 15596870  94 FQAG-EDVGDELKGLLSRWLFNHIRNDDAGYVD 125
Cdd:cd12107  81 LEAGdLELAEELLDFLKDWLVNHILGEDKKLAR 113
Hemerythrin TIGR00058
hemerythrin family non-heme iron protein; This family includes oxygen carrier proteins of ...
 5-123 4.31e-13

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: 61.70  E-value: 4.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870     5 VWQDDLNTGIQVIDNQHKRIVEMINHLhdaqqGKEHAAIAevIEELVDYTLSHFAFEETLMEDAGYQFSRAHKKIHELFI 84
Cdd:TIGR00058   6 VWDESFKVFYDNLDEEHKTLFNGIFAL-----AADNSATA--LKELIDVTVLHFLDEEAMMIAANYSDYDEHKKAHDDFL 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 15596870    85 RRVSEYRvrfqAGEDVGDELKGllSRWLFNHIRNDDAGY 123
Cdd:TIGR00058  79 AVLRGLK----APVPQDDLLYA--KDWLVNHIKTTDFKY 111
Hemerythrin pfam01814
Hemerythrin HHE cation binding domain; Iteration of the HHE family found it to be related to ...
 12-127 2.10e-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: 52.23  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870    12 TGIQVIDNQHKRIVEMINHLHDAQQGKEH---AAIAEVIEELVDYTLSHFAFEETLM-------EDAGYQFSRAHKKIHE 81
Cdd:pfam01814   1 TIIELLDAEHRRLRELLALLRALADALGDshlRKLAELLDELVDELEAHHAAEEELLfpalerrSPGGEAPIEVLRKEHD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 15596870    82 LFIRRVSEYRVRFQAGEDVGDELKGL--LSRWLFNHIRNDDAGYVDAV 127
Cdd:pfam01814  81 EIRELLEELEALLKGAEPGAAFAELLeaLAEWLREHIAKEEEVLFPLL 128
PRK01917 PRK01917
cation-binding hemerythrin HHE family protein; Provisional
 1-121 1.16e-06

cation-binding hemerythrin HHE family protein; Provisional


Pssm-ID: 179353  Cd Length: 139  Bit Score: 45.17  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870    1 MAHLVWQDDLNTGIQVIDNQHKRIVEMINHLHDAqqgkEHAAIAEVIEELVDYTLSHFAFEETLMEDAGYQFSRAHKKIH 80
Cdd:PRK01917   1 MPVPEWSEELHLGDPFTDATHAEFVQLLNAVARA----DDADFLQALDAWIDHTRHHFAQEERWMEATKFGPRHCHRAEH 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 15596870   81 E--LFIRRVSEYRVRFQAGEDVGDELKGLLSRWLFNHIRNDDA 121
Cdd:PRK01917  77 DevLAVAADVREKVARDGDFELGRRLVAELPEWFDQHVRTMDA 119
Hemerythrin-like cd00522
Hemerythrin family; Hemerythrin (Hr) and related proteins are found in bacteria, archaea and ...
 15-123 3.90e-05

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: 40.36  E-value: 3.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596870  15 QVIDNQHKRIVEMINHLhDAQQGKehaaiAEVIEELVDYTLSHFAFEETLMEDAGYQFSRAHKKIHElfIRRVSEYRVRF 94
Cdd:cd00522   1 DVFDDEHWRLFQLVFLY-CDKLSK-----AQSLYATFKEFK*HFQIENEYMIGLLQQRSQTIYNVHS--DNHLSF*LSLF 72

                        90       100
                ....*....|....*....|....*....
gi 15596870  95 QAGEDVGDELKGLLSRWLFNHIRNDDAGY 123
Cdd:cd00522  73 EKGLKQLKERLEAFTRWLVNHIKSEDFEY 101
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH