NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|307184504|gb|EFN70893|]
View 

Myosin regulatory light chain 2 [Camponotus floridanus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTZ00184 super family cl33172
calmodulin; Provisional
 1095-1234 1.75e-24

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 100.61  E-value: 1.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504 1095 MFSQKQVAEFKEAFQLMDADKDGIIGKNDLRAAFDSVGRLASDKELDEMLNEASA----PINFTQLLNLFAVRMSgsgGT 1170
Cdd:PTZ00184    4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAdgngTIDFPEFLTLMARKMK---DT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 307184504 1171 DDDDVVINAFKTFDVDGK--IDGERLRHALMTWGDKFTSKEVDDAFDQMFIDDKGFIDTASLIAML 1234
Cdd:PTZ00184   81 DSEEEIKEAFKVFDRDGNgfISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMM 146
Sod_Cu pfam00080
Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion ...
 579-704 1.30e-12

Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold.


:

Pssm-ID: 459663  Cd Length: 129  Bit Score: 66.05  E-value: 1.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504   579 LQQTEYDATNVEVSLEGLNGKMSGYHVHMTPvenDLEFPCegTSLYGHWNPLGVDTNKVPATEegtldqYEMGDLsgkyG 658
Cdd:pfam00080    7 FTQAGGGPVRVTGNLTGLTPGKHGFHIHEFG---DCTNGC--TSAGGHFNPTGKQHGGPNDDG------RHVGDL----G 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 307184504   659 SL--DNKKRYAITYNDTMLPLFGPRSILGRSIVIHKKEKNL----------RWACSTI 704
Cdd:pfam00080   72 NItaDADGVATVEFTDSLISLSGGNSIIGRALVVHAGPDDLgtqptgnagaRIACGVI 129
Sod_Cu pfam00080
Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion ...
 729-881 3.50e-09

Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold.


:

Pssm-ID: 459663  Cd Length: 129  Bit Score: 56.03  E-value: 3.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504   729 VYGYIKMTQlvykdGSQSETVIEVNLRH--PGKHdrnitknhnwAIYVNPVGvDATvkvkdTRCVAGGYMWNPYFTQLAD 806
Cdd:pfam00080    1 VSGTVTFTQ-----AGGGPVRVTGNLTGltPGKH----------GFHIHEFG-DCT-----NGCTSAGGHFNPTGKQHGG 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504   807 PLNDDlyrqecgpdlplrCYVGDISarvgpiNI-----GEKRQVFTDQNFPLGGSVSAIGRSIVIYDK--DFASN----- 874
Cdd:pfam00080   60 PNDDG-------------RHVGDLG------NItadadGVATVEFTDSLISLSGGNSIIGRALVVHAGpdDLGTQptgna 120


                   ....*....
gi 307184504   875 --RFACANI 881
Cdd:pfam00080  121 gaRIACGVI 129
Sod_Cu super family cl46696
Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion ...
 399-550 8.43e-06

Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold.


The actual alignment was detected with superfamily member pfam00080:

Pssm-ID: 459663  Cd Length: 129  Bit Score: 46.40  E-value: 8.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504   399 IVGRILFRQPKDDPemdttIIIEhlvyADGNANNTADHRWMIH---DNPPGkdfynwtarCLSAGSPYNPYKVE--WKSD 473
Cdd:pfam00080    1 VSGTVTFTQAGGGP-----VRVT----GNLTGLTPGKHGFHIHefgDCTNG---------CTSAGGHFNPTGKQhgGPND 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504   474 SSCSiaepllcrLGDLtrhetleiaGR-KANASELTRKLFTDTMLPLSGSHALFGKSLVIY---DDHGPV---ARGERLA 546
Cdd:pfam00080   63 DGRH--------VGDL---------GNiTADADGVATVEFTDSLISLSGGNSIIGRALVVHagpDDLGTQptgNAGARIA 125


                   ....
gi 307184504   547 CSII 550
Cdd:pfam00080  126 CGVI 129
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 1095-1234 1.75e-24

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 100.61  E-value: 1.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504 1095 MFSQKQVAEFKEAFQLMDADKDGIIGKNDLRAAFDSVGRLASDKELDEMLNEASA----PINFTQLLNLFAVRMSgsgGT 1170
Cdd:PTZ00184    4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAdgngTIDFPEFLTLMARKMK---DT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 307184504 1171 DDDDVVINAFKTFDVDGK--IDGERLRHALMTWGDKFTSKEVDDAFDQMFIDDKGFIDTASLIAML 1234
Cdd:PTZ00184   81 DSEEEIKEAFKVFDRDGNgfISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMM 146
Sod_Cu pfam00080
Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion ...
 579-704 1.30e-12

Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold.


Pssm-ID: 459663  Cd Length: 129  Bit Score: 66.05  E-value: 1.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504   579 LQQTEYDATNVEVSLEGLNGKMSGYHVHMTPvenDLEFPCegTSLYGHWNPLGVDTNKVPATEegtldqYEMGDLsgkyG 658
Cdd:pfam00080    7 FTQAGGGPVRVTGNLTGLTPGKHGFHIHEFG---DCTNGC--TSAGGHFNPTGKQHGGPNDDG------RHVGDL----G 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 307184504   659 SL--DNKKRYAITYNDTMLPLFGPRSILGRSIVIHKKEKNL----------RWACSTI 704
Cdd:pfam00080   72 NItaDADGVATVEFTDSLISLSGGNSIIGRALVVHAGPDDLgtqptgnagaRIACGVI 129
Cu-Zn_Superoxide_Dismutase cd00305
Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of ...
 566-697 1.65e-09

Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of superoxide radicals to molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene causes familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Cytoplasmic and periplasmic SODs exist as dimers, whereas chloroplastic and extracellular enzymes exist as tetramers. Structure supports independent functional evolution in prokaryotes (P-class) and eukaryotes (E-class) [PMID:.8176730].


Pssm-ID: 238186  Cd Length: 144  Bit Score: 57.66  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504  566 NGEQISLKGKLELLQQTeyDATNVEVSLEGLNGKMSGYHVHmtpvEN-DLEFPCEGTSlyGHWNPLGvdtnkvpaTEEGT 644
Cdd:cd00305     8 KGPDGKVVGTVTFTQQS--GGVTITGELSGLTPGLHGFHIH----EFgDCTNGCTSAG--GHFNPFG--------KKHGG 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 307184504  645 LDQYE--MGDLsgkyGSL--DNKKRYAITYNDTMLPLFGPRSILGRSIVIHKKEKNL 697
Cdd:cd00305    72 PNDEGrhAGDL----GNIvaDKDGVATVSVLDPLISLKGGNSIIGRSLVVHAGQDDL 124
Sod_Cu pfam00080
Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion ...
 729-881 3.50e-09

Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold.


Pssm-ID: 459663  Cd Length: 129  Bit Score: 56.03  E-value: 3.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504   729 VYGYIKMTQlvykdGSQSETVIEVNLRH--PGKHdrnitknhnwAIYVNPVGvDATvkvkdTRCVAGGYMWNPYFTQLAD 806
Cdd:pfam00080    1 VSGTVTFTQ-----AGGGPVRVTGNLTGltPGKH----------GFHIHEFG-DCT-----NGCTSAGGHFNPTGKQHGG 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504   807 PLNDDlyrqecgpdlplrCYVGDISarvgpiNI-----GEKRQVFTDQNFPLGGSVSAIGRSIVIYDK--DFASN----- 874
Cdd:pfam00080   60 PNDDG-------------RHVGDLG------NItadadGVATVEFTDSLISLSGGNSIIGRALVVHAGpdDLGTQptgna 120


                   ....*....
gi 307184504   875 --RFACANI 881
Cdd:pfam00080  121 gaRIACGVI 129
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 1103-1147 4.82e-09

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 53.71  E-value: 4.82e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 307184504 1103 EFKEAFQLMDADKDGIIGKNDLRAAFDSVGRLASDKELDEMLNEA 1147
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREV 45
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1100-1226 2.74e-08

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.03  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504 1100 QVAEFKEAFQLMDADKDGIIGKNDLRAAFD-SVGRLASDKELDemlneASAPINFTQllnlFAVRMSGSGGTDDDDVVIN 1178
Cdd:COG5126     3 QRRKLDRRFDLLDADGDGVLERDDFEALFRrLWATLFSEADTD-----GDGRISREE----FVAGMESLFEATVEPFARA 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 307184504 1179 AFKTFDV--DGKIDGERLRHALMTWGdkFTSKEVDDAFDQMFIDDKGFID 1226
Cdd:COG5126    74 AFDLLDTdgDGKISADEFRRLLTALG--VSEEEADELFARLDTDGDGKIS 121
SodC COG2032
Cu/Zn superoxide dismutase [Inorganic ion transport and metabolism];
579-707 2.09e-06

Cu/Zn superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 441635  Cd Length: 171  Bit Score: 49.10  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504  579 LQQTEYdATNVEVSLEGLNGKMSGYHVHMTPVendlefpCE---GTSLYGHWNPLGvdtnkvpaTEEGTL--DQYEMGDL 653
Cdd:COG2032    46 FTETPG-GVLVTVELSGLPPGEHGFHIHEKGD-------CSapdFKSAGGHFNPTG--------TKHGGPnpDGPHAGDL 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 307184504  654 ----SGKYGSLDnkkryaITYNDTMLPLFGPRSILGRSIVIHKKEKNL----------RWACSTIERG 707
Cdd:COG2032   110 pnlyVDADGTAT------LEVLAPRLTLGGLNDLDGRALIIHAGPDDYstqpsgnagaRIACGVIKAA 171
Sod_Cu pfam00080
Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion ...
 399-550 8.43e-06

Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold.


Pssm-ID: 459663  Cd Length: 129  Bit Score: 46.40  E-value: 8.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504   399 IVGRILFRQPKDDPemdttIIIEhlvyADGNANNTADHRWMIH---DNPPGkdfynwtarCLSAGSPYNPYKVE--WKSD 473
Cdd:pfam00080    1 VSGTVTFTQAGGGP-----VRVT----GNLTGLTPGKHGFHIHefgDCTNG---------CTSAGGHFNPTGKQhgGPND 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504   474 SSCSiaepllcrLGDLtrhetleiaGR-KANASELTRKLFTDTMLPLSGSHALFGKSLVIY---DDHGPV---ARGERLA 546
Cdd:pfam00080   63 DGRH--------VGDL---------GNiTADADGVATVEFTDSLISLSGGNSIIGRALVVHagpDDLGTQptgNAGARIA 125


                   ....
gi 307184504   547 CSII 550
Cdd:pfam00080  126 CGVI 129
PLN02386 PLN02386
superoxide dismutase [Cu-Zn]
 572-697 1.31e-05

superoxide dismutase [Cu-Zn]


Pssm-ID: 166027 [Multi-domain]  Cd Length: 152  Bit Score: 46.44  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504  572 LKGKLELLQQTEyDATNVEVSLEGLNGKMSGYHVHMTpveNDLEFPCEGTSlyGHWNPLGvDTNKVPATEegtldQYEMG 651
Cdd:PLN02386   14 VKGTIFFTQEGD-GPTTVTGSLSGLKPGLHGFHVHAL---GDTTNGCMSTG--PHFNPAG-KEHGAPEDE-----NRHAG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 307184504  652 DLSGKYGSLDNKKRYAITynDTMLPLFGPRSILGRSIVIHKKEKNL 697
Cdd:PLN02386   82 DLGNVTVGDDGTATFTIV--DKQIPLTGPNSIVGRAVVVHADPDDL 125
EF-hand_6 pfam13405
EF-hand domain;
1103-1132 1.96e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 39.47  E-value: 1.96e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 307184504  1103 EFKEAFQLMDADKDGIIGKNDLRAAFDSVG 1132
Cdd:pfam13405    1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 1103-1128 2.48e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 36.59  E-value: 2.48e-03
                            10        20
                    ....*....|....*....|....*.
gi 307184504   1103 EFKEAFQLMDADKDGIIGKNDLRAAF 1128
Cdd:smart00054    1 ELKEAFRLFDKDGDGKIDFEEFKDLL 26
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 1095-1234 1.75e-24

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 100.61  E-value: 1.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504 1095 MFSQKQVAEFKEAFQLMDADKDGIIGKNDLRAAFDSVGRLASDKELDEMLNEASA----PINFTQLLNLFAVRMSgsgGT 1170
Cdd:PTZ00184    4 QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAdgngTIDFPEFLTLMARKMK---DT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 307184504 1171 DDDDVVINAFKTFDVDGK--IDGERLRHALMTWGDKFTSKEVDDAFDQMFIDDKGFIDTASLIAML 1234
Cdd:PTZ00184   81 DSEEEIKEAFKVFDRDGNgfISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMM 146
Sod_Cu pfam00080
Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion ...
 579-704 1.30e-12

Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold.


Pssm-ID: 459663  Cd Length: 129  Bit Score: 66.05  E-value: 1.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504   579 LQQTEYDATNVEVSLEGLNGKMSGYHVHMTPvenDLEFPCegTSLYGHWNPLGVDTNKVPATEegtldqYEMGDLsgkyG 658
Cdd:pfam00080    7 FTQAGGGPVRVTGNLTGLTPGKHGFHIHEFG---DCTNGC--TSAGGHFNPTGKQHGGPNDDG------RHVGDL----G 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 307184504   659 SL--DNKKRYAITYNDTMLPLFGPRSILGRSIVIHKKEKNL----------RWACSTI 704
Cdd:pfam00080   72 NItaDADGVATVEFTDSLISLSGGNSIIGRALVVHAGPDDLgtqptgnagaRIACGVI 129
Cu-Zn_Superoxide_Dismutase cd00305
Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of ...
 566-697 1.65e-09

Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of superoxide radicals to molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene causes familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Cytoplasmic and periplasmic SODs exist as dimers, whereas chloroplastic and extracellular enzymes exist as tetramers. Structure supports independent functional evolution in prokaryotes (P-class) and eukaryotes (E-class) [PMID:.8176730].


Pssm-ID: 238186  Cd Length: 144  Bit Score: 57.66  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504  566 NGEQISLKGKLELLQQTeyDATNVEVSLEGLNGKMSGYHVHmtpvEN-DLEFPCEGTSlyGHWNPLGvdtnkvpaTEEGT 644
Cdd:cd00305     8 KGPDGKVVGTVTFTQQS--GGVTITGELSGLTPGLHGFHIH----EFgDCTNGCTSAG--GHFNPFG--------KKHGG 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 307184504  645 LDQYE--MGDLsgkyGSL--DNKKRYAITYNDTMLPLFGPRSILGRSIVIHKKEKNL 697
Cdd:cd00305    72 PNDEGrhAGDL----GNIvaDKDGVATVSVLDPLISLKGGNSIIGRSLVVHAGQDDL 124
Sod_Cu pfam00080
Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion ...
 729-881 3.50e-09

Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold.


Pssm-ID: 459663  Cd Length: 129  Bit Score: 56.03  E-value: 3.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504   729 VYGYIKMTQlvykdGSQSETVIEVNLRH--PGKHdrnitknhnwAIYVNPVGvDATvkvkdTRCVAGGYMWNPYFTQLAD 806
Cdd:pfam00080    1 VSGTVTFTQ-----AGGGPVRVTGNLTGltPGKH----------GFHIHEFG-DCT-----NGCTSAGGHFNPTGKQHGG 59

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504   807 PLNDDlyrqecgpdlplrCYVGDISarvgpiNI-----GEKRQVFTDQNFPLGGSVSAIGRSIVIYDK--DFASN----- 874
Cdd:pfam00080   60 PNDDG-------------RHVGDLG------NItadadGVATVEFTDSLISLSGGNSIIGRALVVHAGpdDLGTQptgna 120


                   ....*....
gi 307184504   875 --RFACANI 881
Cdd:pfam00080  121 gaRIACGVI 129
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 1103-1147 4.82e-09

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 53.71  E-value: 4.82e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 307184504 1103 EFKEAFQLMDADKDGIIGKNDLRAAFDSVGRLASDKELDEMLNEA 1147
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREV 45
PTZ00183 PTZ00183
centrin; Provisional
 1080-1226 5.33e-09

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 56.62  E-value: 5.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504 1080 RGSRKAKRSGssvfsmFSQKQVAEFKEAFQLMDADKDGIIGKNDLRAAFDSVGRLASDKELDEML----NEASAPINFTQ 1155
Cdd:PTZ00183    1 MRKRRSERPG------LTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIadvdKDGSGKIDFEE 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 307184504 1156 LLNLFAVRMsgsGGTDDDDVVINAFKTFDVD--GKIDGERLRHALMTWGDKFTSKEVDDAFDQMFIDDKGFID 1226
Cdd:PTZ00183   75 FLDIMTKKL---GERDPREEILKAFRLFDDDktGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEIS 144
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1100-1226 2.74e-08

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 54.03  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504 1100 QVAEFKEAFQLMDADKDGIIGKNDLRAAFD-SVGRLASDKELDemlneASAPINFTQllnlFAVRMSGSGGTDDDDVVIN 1178
Cdd:COG5126     3 QRRKLDRRFDLLDADGDGVLERDDFEALFRrLWATLFSEADTD-----GDGRISREE----FVAGMESLFEATVEPFARA 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 307184504 1179 AFKTFDV--DGKIDGERLRHALMTWGdkFTSKEVDDAFDQMFIDDKGFID 1226
Cdd:COG5126    74 AFDLLDTdgDGKISADEFRRLLTALG--VSEEEADELFARLDTDGDGKIS 121
SodC COG2032
Cu/Zn superoxide dismutase [Inorganic ion transport and metabolism];
579-707 2.09e-06

Cu/Zn superoxide dismutase [Inorganic ion transport and metabolism];


Pssm-ID: 441635  Cd Length: 171  Bit Score: 49.10  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504  579 LQQTEYdATNVEVSLEGLNGKMSGYHVHMTPVendlefpCE---GTSLYGHWNPLGvdtnkvpaTEEGTL--DQYEMGDL 653
Cdd:COG2032    46 FTETPG-GVLVTVELSGLPPGEHGFHIHEKGD-------CSapdFKSAGGHFNPTG--------TKHGGPnpDGPHAGDL 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 307184504  654 ----SGKYGSLDnkkryaITYNDTMLPLFGPRSILGRSIVIHKKEKNL----------RWACSTIERG 707
Cdd:COG2032   110 pnlyVDADGTAT------LEVLAPRLTLGGLNDLDGRALIIHAGPDDYstqpsgnagaRIACGVIKAA 171
Sod_Cu pfam00080
Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion ...
 399-550 8.43e-06

Copper/zinc superoxide dismutase (SODC); superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold.


Pssm-ID: 459663  Cd Length: 129  Bit Score: 46.40  E-value: 8.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504   399 IVGRILFRQPKDDPemdttIIIEhlvyADGNANNTADHRWMIH---DNPPGkdfynwtarCLSAGSPYNPYKVE--WKSD 473
Cdd:pfam00080    1 VSGTVTFTQAGGGP-----VRVT----GNLTGLTPGKHGFHIHefgDCTNG---------CTSAGGHFNPTGKQhgGPND 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504   474 SSCSiaepllcrLGDLtrhetleiaGR-KANASELTRKLFTDTMLPLSGSHALFGKSLVIY---DDHGPV---ARGERLA 546
Cdd:pfam00080   63 DGRH--------VGDL---------GNiTADADGVATVEFTDSLISLSGGNSIIGRALVVHagpDDLGTQptgNAGARIA 125


                   ....
gi 307184504   547 CSII 550
Cdd:pfam00080  126 CGVI 129
PLN02386 PLN02386
superoxide dismutase [Cu-Zn]
 572-697 1.31e-05

superoxide dismutase [Cu-Zn]


Pssm-ID: 166027 [Multi-domain]  Cd Length: 152  Bit Score: 46.44  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504  572 LKGKLELLQQTEyDATNVEVSLEGLNGKMSGYHVHMTpveNDLEFPCEGTSlyGHWNPLGvDTNKVPATEegtldQYEMG 651
Cdd:PLN02386   14 VKGTIFFTQEGD-GPTTVTGSLSGLKPGLHGFHVHAL---GDTTNGCMSTG--PHFNPAG-KEHGAPEDE-----NRHAG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 307184504  652 DLSGKYGSLDNKKRYAITynDTMLPLFGPRSILGRSIVIHKKEKNL 697
Cdd:PLN02386   82 DLGNVTVGDDGTATFTIV--DKQIPLTGPNSIVGRAVVVHADPDDL 125
EFh_PEF_CAPN13_14 cd16195
Penta-EF hand, calcium binding motifs, found in calpain-13 (CAPN13), calpain-14 (CAPN14), and ...
 1099-1188 1.91e-04

Penta-EF hand, calcium binding motifs, found in calpain-13 (CAPN13), calpain-14 (CAPN14), and similar proteins; CAPN13, also termed calcium-activated neutral proteinase 13 (CANP 13), a 63.6 kDa calpain large subunit that exhibits a restricted tissue distribution with low levels of expression detected only in human testis and lung. In calpain family, CAPN13 is most closely related to calpain-14 (CAPN14). CAPN14, also termed calcium-activated neutral proteinase 14 (CANP 14), is a 76.7 kDa calpain large subunit that is most highly expressed in the oesophagus. Its expression and calpain activity can be induced by IL-13. Both CAPN13 and CAPN14 contain a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain.


Pssm-ID: 320070 [Multi-domain]  Cd Length: 168  Bit Score: 43.35  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504 1099 KQVAEFKEAFQLMDADKDGIIGKNDLRAAFDSVGRLASDkeldemlneasapinftQLLNLFAVRMSGSGGTDDD----- 1173
Cdd:cd16195    70 KKLRKYKDIFQKADVSKSGFLSLSELRNAIQAAGIRVSD-----------------DLLNLMALRYGDSSGRISFesfic 132

                          90       100
                  ....*....|....*....|
gi 307184504 1174 -----DVVINAFKTFDVDGK 1188
Cdd:cd16195   133 lmlrlECMAKIFRNLSKDGG 152
EF-hand_6 pfam13405
EF-hand domain;
1103-1132 1.96e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 39.47  E-value: 1.96e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 307184504  1103 EFKEAFQLMDADKDGIIGKNDLRAAFDSVG 1132
Cdd:pfam13405    1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 1179-1234 2.05e-04

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 40.61  E-value: 2.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 307184504 1179 AFKTFDVD--GKIDGERLRHALMTWGDKFTSKEVDDAFDQMFIDDKGFIDTASLIAML 1234
Cdd:cd00051     5 AFRLFDKDgdGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
PLN02642 PLN02642
copper, zinc superoxide dismutase
 571-697 1.33e-03

copper, zinc superoxide dismutase


Pssm-ID: 178248  Cd Length: 164  Bit Score: 40.84  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307184504  571 SLKGKLELLQQTEyDATNVEVSLEGLNGKMSGYHVHMTpveNDLEFPCEGTSlyGHWNPLgvdtNKV--PATEEgtldQY 648
Cdd:PLN02642   19 NVRGCLQFVQDIF-GTTHVTGKISGLSPGFHGFHIHSF---GDTTNGCISTG--PHFNPL----NRVhgPPNEE----ER 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 307184504  649 EMGDL----SGKYGSLDnkkryaITYNDTMLPLFGPRSILGRSIVIHKKEKNL 697
Cdd:PLN02642   85 HAGDLgnilAGSDGVAE------ILIKDKHIPLSGQYSILGRAVVVHADPDDL 131
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 1103-1128 1.41e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 37.38  E-value: 1.41e-03
                           10        20
                   ....*....|....*....|....*.
gi 307184504  1103 EFKEAFQLMDADKDGIIGKNDLRAAF 1128
Cdd:pfam00036    1 ELKEIFRLFDKDGDGKIDFEEFKELL 26
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1094-1147 1.76e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.16  E-value: 1.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 307184504 1094 SMFSQKQVAEFKEAFQLMDADKDGIIGKNDLRAAFDSVGrlASDKELDEMLNEA 1147
Cdd:COG5126    61 SLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFARL 112
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 1103-1128 2.48e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 36.59  E-value: 2.48e-03
                            10        20
                    ....*....|....*....|....*.
gi 307184504   1103 EFKEAFQLMDADKDGIIGKNDLRAAF 1128
Cdd:smart00054    1 ELKEAFRLFDKDGDGKIDFEEFKDLL 26
EF-hand_7 pfam13499
EF-hand domain pair;
1173-1226 3.42e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.23  E-value: 3.42e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 307184504  1173 DDVVINAFKTFDVD--GKIDGERLRHALMTW--GDKFTSKEVDDAFDQMFIDDKGFID 1226
Cdd:pfam13499    1 EEKLKEAFKLLDSDgdGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRIS 58
 
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