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Conserved domains on  [gi|495983923|ref|WP_008708502|]
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class II SORL domain-containing protein [Cloacibacillus evryensis]

Protein Classification

class II SORL domain-containing protein( domain architecture ID 10123590)

class II SORL (superoxide reductase-like) domain-containing protein is a mononuclear non-heme iron protein that scavenges superoxide anion radicals as a defense mechanism against reactive oxygen species

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SORL_classII cd03172
Superoxide reductase-like (SORL) domain, class II; SORL-domains are present in a family of ...
 10-125 2.83e-35

Superoxide reductase-like (SORL) domain, class II; SORL-domains are present in a family of mononuclear non-heme iron proteins that includes superoxide reductase and desulfoferrodoxin. Superoxide reductase-like proteins scavenge superoxide anion radicals as a defense mechanism against reactive oxygen species and are found in anaerobic bacteria and archeae, and microaerophilic Treponema pallidum. The SORL domain contains an active iron site, Fe[His4Cys(Glu)], which in the reduced state loses the glutamate ligand. Superoxide reductase (class II) forms a homotetramer with four Fe[His4Cys(Glu)] centers.


:

Pssm-ID: 239422  Cd Length: 104  Bit Score: 117.48  E-value: 2.83e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495983923  10 GDFKAEKHVPTIEAPEKVKLGEEALVKVMVGQEIKHPNTPLHHIRWIQLYFKPddatpvIEVAKFDYSAHSDTMnpdmpg 89
Cdd:cd03172    1 KTDKEEKHVPVIECPEAVKAGEPFEVTVSVGKEIPHPNTTEHHIEWIELYFGV------YLLGRVEFTAHGGVY------ 68

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495983923  90 caaADPASCVKVKLT---KSGTFIAVSYCNIHGLWESAK 125
Cdd:cd03172   69 ---TKPEATFTVKIPkkgKKGKLVALSYCNIHGLWESEK 104
 
Name Accession Description Interval E-value
SORL_classII cd03172
Superoxide reductase-like (SORL) domain, class II; SORL-domains are present in a family of ...
 10-125 2.83e-35

Superoxide reductase-like (SORL) domain, class II; SORL-domains are present in a family of mononuclear non-heme iron proteins that includes superoxide reductase and desulfoferrodoxin. Superoxide reductase-like proteins scavenge superoxide anion radicals as a defense mechanism against reactive oxygen species and are found in anaerobic bacteria and archeae, and microaerophilic Treponema pallidum. The SORL domain contains an active iron site, Fe[His4Cys(Glu)], which in the reduced state loses the glutamate ligand. Superoxide reductase (class II) forms a homotetramer with four Fe[His4Cys(Glu)] centers.


Pssm-ID: 239422  Cd Length: 104  Bit Score: 117.48  E-value: 2.83e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495983923  10 GDFKAEKHVPTIEAPEKVKLGEEALVKVMVGQEIKHPNTPLHHIRWIQLYFKPddatpvIEVAKFDYSAHSDTMnpdmpg 89
Cdd:cd03172    1 KTDKEEKHVPVIECPEAVKAGEPFEVTVSVGKEIPHPNTTEHHIEWIELYFGV------YLLGRVEFTAHGGVY------ 68

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495983923  90 caaADPASCVKVKLT---KSGTFIAVSYCNIHGLWESAK 125
Cdd:cd03172   69 ---TKPEATFTVKIPkkgKKGKLVALSYCNIHGLWESEK 104
Desulfoferrodox pfam01880
Desulfoferrodoxin; Desulfoferrodoxins contains two types of iron: an Fe-S4 site very similar ...
 10-123 3.67e-35

Desulfoferrodoxin; Desulfoferrodoxins contains two types of iron: an Fe-S4 site very similar to that found in desulforedoxin from Desulfovibrio gigas and an octahedral coordinated high-spin ferrous site most probably with nitrogen/oxygen-containing ligands. Due to this rather unusual combination of active centres, this novel protein is named desulfoferrodoxin.


Pssm-ID: 396450  Cd Length: 97  Bit Score: 116.66  E-value: 3.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495983923   10 GDFKAEKHVPTIEAPEKVKLGEEALVKVMVGqEIKHPNTPLHHIRWIQLYFKPDDAtpvievAKFDYSAHSdtmnpdmpg 89
Cdd:pfam01880   2 GDWKEEKHVPVIECPDVVKAGEPFEVKVSVG-KIPHPMTEEHHIAWIELYFGEEGL------ARAEFTPHE--------- 65

                          90       100       110
                  ....*....|....*....|....*....|....
gi 495983923   90 caaADPASCVKVKLTKSGTFIAVSYCNIHGLWES 123
Cdd:pfam01880  66 ---TEPEVTFTVKLKKSGKLYALSYCNLHGLWEN 96
SORL COG2033
Desulfoferrodoxin, superoxide reductase-like (SORL) domain [Energy production and conversion];
10-123 6.94e-24

Desulfoferrodoxin, superoxide reductase-like (SORL) domain [Energy production and conversion];


Pssm-ID: 441636 [Multi-domain]  Cd Length: 125  Bit Score: 88.84  E-value: 6.94e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495983923  10 GDFKAEKHVPTIEApekvklgEEALVKVMVGqEIKHPNTPLHHIRWIQLYFKPddatpviEVAKFDYSahsdtmnpdmPG 89
Cdd:COG2033   40 ADAAKEKHVPVIEA-------EGFGVKVKVG-EVPHPMTEEHYIEWIELYTGD-------GVGRKELK----------PG 94

                         90       100       110
                 ....*....|....*....|....*....|....
gi 495983923  90 caaADPASCVKVKlTKSGTFIAVSYCNIHGLWES 123
Cdd:COG2033   95 ---DEPEATFKVK-DKSGTLTAREYCNLHGLWES 124
neela_ferrous TIGR00332
desulfoferrodoxin ferrous iron-binding domain; This domain comprises essentially the full ...
 11-130 1.34e-20

desulfoferrodoxin ferrous iron-binding domain; This domain comprises essentially the full length of neelaredoxin, a monomeric, blue, non-heme iron protein of Desulfovibrio gigas said to bind two iron atoms per monomer with identical spectral properties. Neelaredoxin was shown recently to have significant superoxide dismutase activity. This domain is also found (in a form in which the distance between the motifs H[HWYF]IXW and CN[IL]HGXW is somewhat shorter) as the C-terminal domain of desulfoferrodoxin, which is said to bind a single ferrous iron atom.The N-terminal domain of desulfoferrodoxin is described in a separate model, dfx_rbo (TIGR00320). [Energy metabolism, Electron transport]


Pssm-ID: 273018  Cd Length: 106  Bit Score: 80.02  E-value: 1.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495983923   11 DFKAEKHVPTIEAPEKVKLGEEalVKVMVGQEIKHPNTPLHHIRWIQLYFKPddatpviEVAKFDYSAHsdtmnpDMPGC 90
Cdd:TIGR00332   4 DWGKEKHVPVIEVLRREGGVVY--VKVSVGKEIPHPMEENHHIAWIELIFGD-------EVSRKPLVPG------DAPFA 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 495983923   91 AAADPASCVKVKltKSGTFIAVSYCNIHGLWESAKKIEVE 130
Cdd:TIGR00332  69 EFASVDGPNKVE--MSGKLTARSYCNIHGLWMYEATLSLE 106
 
Name Accession Description Interval E-value
SORL_classII cd03172
Superoxide reductase-like (SORL) domain, class II; SORL-domains are present in a family of ...
 10-125 2.83e-35

Superoxide reductase-like (SORL) domain, class II; SORL-domains are present in a family of mononuclear non-heme iron proteins that includes superoxide reductase and desulfoferrodoxin. Superoxide reductase-like proteins scavenge superoxide anion radicals as a defense mechanism against reactive oxygen species and are found in anaerobic bacteria and archeae, and microaerophilic Treponema pallidum. The SORL domain contains an active iron site, Fe[His4Cys(Glu)], which in the reduced state loses the glutamate ligand. Superoxide reductase (class II) forms a homotetramer with four Fe[His4Cys(Glu)] centers.


Pssm-ID: 239422  Cd Length: 104  Bit Score: 117.48  E-value: 2.83e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495983923  10 GDFKAEKHVPTIEAPEKVKLGEEALVKVMVGQEIKHPNTPLHHIRWIQLYFKPddatpvIEVAKFDYSAHSDTMnpdmpg 89
Cdd:cd03172    1 KTDKEEKHVPVIECPEAVKAGEPFEVTVSVGKEIPHPNTTEHHIEWIELYFGV------YLLGRVEFTAHGGVY------ 68

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495983923  90 caaADPASCVKVKLT---KSGTFIAVSYCNIHGLWESAK 125
Cdd:cd03172   69 ---TKPEATFTVKIPkkgKKGKLVALSYCNIHGLWESEK 104
Desulfoferrodox pfam01880
Desulfoferrodoxin; Desulfoferrodoxins contains two types of iron: an Fe-S4 site very similar ...
 10-123 3.67e-35

Desulfoferrodoxin; Desulfoferrodoxins contains two types of iron: an Fe-S4 site very similar to that found in desulforedoxin from Desulfovibrio gigas and an octahedral coordinated high-spin ferrous site most probably with nitrogen/oxygen-containing ligands. Due to this rather unusual combination of active centres, this novel protein is named desulfoferrodoxin.


Pssm-ID: 396450  Cd Length: 97  Bit Score: 116.66  E-value: 3.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495983923   10 GDFKAEKHVPTIEAPEKVKLGEEALVKVMVGqEIKHPNTPLHHIRWIQLYFKPDDAtpvievAKFDYSAHSdtmnpdmpg 89
Cdd:pfam01880   2 GDWKEEKHVPVIECPDVVKAGEPFEVKVSVG-KIPHPMTEEHHIAWIELYFGEEGL------ARAEFTPHE--------- 65

                          90       100       110
                  ....*....|....*....|....*....|....
gi 495983923   90 caaADPASCVKVKLTKSGTFIAVSYCNIHGLWES 123
Cdd:pfam01880  66 ---TEPEVTFTVKLKKSGKLYALSYCNLHGLWEN 96
SORL cd00524
Superoxide reductase-like (SORL) domain; present in a family of mononuclear non-heme iron ...
 15-122 2.05e-24

Superoxide reductase-like (SORL) domain; present in a family of mononuclear non-heme iron proteins that includes superoxide reductase and desulfoferrodoxin. Superoxide reductase-like proteins scavenge superoxide anion radicals as a defense mechanism against reactive oxygen species and are found in anaerobic bacteria and archeae, and microaerophilic Treponema pallidum. The SORL domain contains an active iron site, Fe[His4Cys(Glu)], which in the reduced state loses the glutamate ligand. Superoxide reductase (class II) forms a homotetramer with four Fe[His4Cys(Glu)] centers. Desulfoferrodoxin (class I) is a homodimeric protein, with each protomer comprised of two domains, the N-terminal desulforedoxin (DSRD) domain and C-terminal SORL domain. Each domain has a distinct iron center: the DSRD iron center I, Fe(S-Cys)4; and the SORL iron center II, Fe[His4Cys(Glu)].


Pssm-ID: 238290  Cd Length: 86  Bit Score: 89.30  E-value: 2.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495983923  15 EKHVPTIEAPEKVKLGEealVKVMVGqEIKHPNTPLHHIRWIQLYFKPDdatpviEVAKFDYSAHSDtmnpdmpgcaaad 94
Cdd:cd00524    2 EKHVPVIEKPDSVEPFD---VKVKVG-SVPHPMTEEHYIEWIELYFGDE------KVGRVELTPGTK------------- 58

                         90       100
                 ....*....|....*....|....*...
gi 495983923  95 PASCVKVKLTKSGTFIAVSYCNIHGLWE 122
Cdd:cd00524   59 PEATFTVKAPKKGKLVALSYCNLHGLWE 86
SORL COG2033
Desulfoferrodoxin, superoxide reductase-like (SORL) domain [Energy production and conversion];
10-123 6.94e-24

Desulfoferrodoxin, superoxide reductase-like (SORL) domain [Energy production and conversion];


Pssm-ID: 441636 [Multi-domain]  Cd Length: 125  Bit Score: 88.84  E-value: 6.94e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495983923  10 GDFKAEKHVPTIEApekvklgEEALVKVMVGqEIKHPNTPLHHIRWIQLYFKPddatpviEVAKFDYSahsdtmnpdmPG 89
Cdd:COG2033   40 ADAAKEKHVPVIEA-------EGFGVKVKVG-EVPHPMTEEHYIEWIELYTGD-------GVGRKELK----------PG 94

                         90       100       110
                 ....*....|....*....|....*....|....
gi 495983923  90 caaADPASCVKVKlTKSGTFIAVSYCNIHGLWES 123
Cdd:COG2033   95 ---DEPEATFKVK-DKSGTLTAREYCNLHGLWES 124
neela_ferrous TIGR00332
desulfoferrodoxin ferrous iron-binding domain; This domain comprises essentially the full ...
 11-130 1.34e-20

desulfoferrodoxin ferrous iron-binding domain; This domain comprises essentially the full length of neelaredoxin, a monomeric, blue, non-heme iron protein of Desulfovibrio gigas said to bind two iron atoms per monomer with identical spectral properties. Neelaredoxin was shown recently to have significant superoxide dismutase activity. This domain is also found (in a form in which the distance between the motifs H[HWYF]IXW and CN[IL]HGXW is somewhat shorter) as the C-terminal domain of desulfoferrodoxin, which is said to bind a single ferrous iron atom.The N-terminal domain of desulfoferrodoxin is described in a separate model, dfx_rbo (TIGR00320). [Energy metabolism, Electron transport]


Pssm-ID: 273018  Cd Length: 106  Bit Score: 80.02  E-value: 1.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495983923   11 DFKAEKHVPTIEAPEKVKLGEEalVKVMVGQEIKHPNTPLHHIRWIQLYFKPddatpviEVAKFDYSAHsdtmnpDMPGC 90
Cdd:TIGR00332   4 DWGKEKHVPVIEVLRREGGVVY--VKVSVGKEIPHPMEENHHIAWIELIFGD-------EVSRKPLVPG------DAPFA 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 495983923   91 AAADPASCVKVKltKSGTFIAVSYCNIHGLWESAKKIEVE 130
Cdd:TIGR00332  69 EFASVDGPNKVE--MSGKLTARSYCNIHGLWMYEATLSLE 106
SORL_Dfx_classI cd03171
Superoxide reductase-like (SORL) domain, class I; SORL-domains are present in a family of ...
 15-121 3.24e-07

Superoxide reductase-like (SORL) domain, class I; SORL-domains are present in a family of mononuclear non-heme iron proteins that includes superoxide reductase and desulfoferrodoxin. Superoxide reductase-like proteins scavenge superoxide anion radicals as a defense mechanism against reactive oxygen species and are found in anaerobic bacteria and archeae, and microaerophilic Treponema pallidum. Desulfoferrodoxin (class I) is a homodimeric protein, with each protomer comprised of two domains, the N-terminal desulforedoxin (DSRD) domain and C-terminal SORL domain. Each domain has a distinct iron center: the DSRD iron center I, Fe(S-Cys)4; and the SORL iron center II, Fe[His4Cys(Glu)].


Pssm-ID: 239421  Cd Length: 78  Bit Score: 44.68  E-value: 3.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495983923  15 EKHVPTIEapekvklGEEALVKVMVGqEIKHPNTPLHHIRWIQLyfkpddatpvievaKFDYSAHSDTMNP-DMPgcaaa 93
Cdd:cd03171    2 EKHVPVIE-------KIGGGIKVKVG-SVAHPMEEKHYIEWIEL--------------LADGKVYRKHLKPgDAP----- 54

                         90       100
                 ....*....|....*....|....*...
gi 495983923  94 dpascVKVKLTKSGTFIAVSYCNIHGLW 121
Cdd:cd03171   55 -----EAEFSVDADVVTARAYCNLHGLW 77
dfx_rbo TIGR00320
desulfoferrodoxin; The short N-terminal domain contains four conserved Cys for binding of a ...
 1-123 7.97e-06

desulfoferrodoxin; The short N-terminal domain contains four conserved Cys for binding of a ferric iron atom, and is homologous to the small protein desulforedoxin; this domain may also be responsible for dimerization. The remainder of the molecule binds a ferrous iron atom and is similar to neelaredoxin, a monomeric blue non-heme iron protein. The homolog from Treponema pallidum scores between the trusted cutoff for orthology and the noise cutoff. Although essentially a full length homolog, it lacks three of the four Cys residues in the N-terminal domain; the domain may have lost ferric binding ability but may have some conserved structural role such as dimerization, or some new function. This protein is described in some articles as rubredoxin oxidoreductase (rbo), and its gene shares an operon with the rubredoxin gene in Desulfovibrio vulgaris Hildenborough. [Energy metabolism, Electron transport]


Pssm-ID: 273011 [Multi-domain]  Cd Length: 125  Bit Score: 42.15  E-value: 7.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495983923    1 MKIGEVmRDGDFKAEKHVPTIEApekvklgEEALVKVMVGqEIKHPNTPLHHIRWIQLyfkpddatpvieVAkfDYSAHS 80
Cdd:TIGR00320  34 MKLMSE-NTTDAAKEKHVPVIEK-------TGNGYKVKVG-SVAHPMEEKHYIQWIEL------------IA--DDKVYR 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 495983923   81 DTMNP-DMPGCaaadpascvkVKLTKSGTFIAVSYCNIHGLWES 123
Cdd:TIGR00320  91 KFLKPgDAPEA----------EFLIMADKVVAREYCNIHGHWKA 124
 
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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