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Conserved domains on  [gi|157804751|gb|ABV80015|]
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AprA, partial [Thiocapsa pendens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FAD_binding_2 super family cl46878
FAD binding domain; This family includes members that bind FAD. This family includes the ...
7-272 3.69e-143

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


The actual alignment was detected with superfamily member PRK06854:

Pssm-ID: 481218 [Multi-domain]  Cd Length: 608  Bit Score: 414.71  E-value: 3.69e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751   7 NPEIVEEEVDILIIGGGMGACGAAYEIGPWLDqakkegyDLKVKLVDKAAMDRSGAVAQGLSAINTYLGE-QDPADYARM 85
Cdd:PRK06854   4 NPEVVEVDTDILIIGGGMAGCGAAFEAKEWAP-------DLKVLIVEKANIKRSGAVAQGLSAINAYIGEgETPEDYVRY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751  86 VSNDLMGITRDDLAYDLGRHVDDSVHLFEEWGLPIWKQpgdegkplvEGGKPVRLGKWQIMINGESYKWIVAEAAKKALG 165
Cdd:PRK06854  77 VRKDLMGIVREDLVYDIARHVDSVVHLFEEWGLPIWKD---------ENGKYVRRGRWQIMINGESYKPIVAEAAKKALG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751 166 tERIQERVFIVKLVNDKNdknRIAGAIGFSVREHKVFVYKFKACLLVAGGCVNIFRPRSVGEGTGRAWYPVWNAGSTYAM 245
Cdd:PRK06854 148 -DNVLNRVFITDLLVDDN---RIAGAVGFSVRENKFYVFKAKAVIVATGGAAGIYRPRSPGEGRGRMWYPPFNTGSGYAM 223
                        250       260
                 ....*....|....*....|....*..
gi 157804751 246 AAEAGAELTMMENRFVPARFKDGYGPV 272
Cdd:PRK06854 224 GIRAGAEMTTFENRFIPLRFKDGYGPV 250
 
Name Accession Description Interval E-value
PRK06854 PRK06854
adenylyl-sulfate reductase subunit alpha;
7-272 3.69e-143

adenylyl-sulfate reductase subunit alpha;


Pssm-ID: 235879 [Multi-domain]  Cd Length: 608  Bit Score: 414.71  E-value: 3.69e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751   7 NPEIVEEEVDILIIGGGMGACGAAYEIGPWLDqakkegyDLKVKLVDKAAMDRSGAVAQGLSAINTYLGE-QDPADYARM 85
Cdd:PRK06854   4 NPEVVEVDTDILIIGGGMAGCGAAFEAKEWAP-------DLKVLIVEKANIKRSGAVAQGLSAINAYIGEgETPEDYVRY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751  86 VSNDLMGITRDDLAYDLGRHVDDSVHLFEEWGLPIWKQpgdegkplvEGGKPVRLGKWQIMINGESYKWIVAEAAKKALG 165
Cdd:PRK06854  77 VRKDLMGIVREDLVYDIARHVDSVVHLFEEWGLPIWKD---------ENGKYVRRGRWQIMINGESYKPIVAEAAKKALG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751 166 tERIQERVFIVKLVNDKNdknRIAGAIGFSVREHKVFVYKFKACLLVAGGCVNIFRPRSVGEGTGRAWYPVWNAGSTYAM 245
Cdd:PRK06854 148 -DNVLNRVFITDLLVDDN---RIAGAVGFSVRENKFYVFKAKAVIVATGGAAGIYRPRSPGEGRGRMWYPPFNTGSGYAM 223
                        250       260
                 ....*....|....*....|....*..
gi 157804751 246 AAEAGAELTMMENRFVPARFKDGYGPV 272
Cdd:PRK06854 224 GIRAGAEMTTFENRFIPLRFKDGYGPV 250
aprA TIGR02061
adenosine phosphosulphate reductase, alpha subunit; During dissimilatory sulfate reduction or ...
16-272 3.06e-125

adenosine phosphosulphate reductase, alpha subunit; During dissimilatory sulfate reduction or sulfur oxidation, adenylylsulfate (APS) reductase catalyzes reversibly the two-electron reduction of APS to sulfite and AMP. Found in several bacterial lineages and in Archaeoglobales, APS reductase is a heterodimer composed of an alpha subunit containing a noncovalently bound FAD, and a beta subunit containing two [4Fe-4S] clusters. Described by this model is the alpha subunit of APS reductase, sharing common evolutionary origin with fumarate reductase/succinate dehydrogenase flavoproteins. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273946 [Multi-domain]  Cd Length: 614  Bit Score: 369.21  E-value: 3.06e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751   16 DILIIGGGMGACGAAYEIGPWLDQakkegYDLKVKLVDKAAMDRSGAVAQGLSAINTYLG----EQDPADYARMVSNDLM 91
Cdd:TIGR02061   1 DLLIVGGGMGGCGAAFEAVYWGDK-----KGLKIVLVEKANLERSGAVAQGLSAINTYLGtrfgENNAEDYVRYVRTDLM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751   92 GITRDDLAYDLGRHVDDSVHLFEEWGLPIWKQPGDegkplvegGKPVRLGKWQIMINGESYKWIVAEAAKKALGteRIQE 171
Cdd:TIGR02061  76 GLVREDLIFDMARHVDDSVHLFEEWGLPLWIKPED--------GKYVREGRWQIMIHGESYKPIVAEAAKNALG--DIFE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751  172 RVFIVKLVNDKNDKNRIAGAIGFSVREHKVFVYKFKACLLVAGGCVNIFRPRSVGEGTGRAWYPVWNAGSTYAMAAEAGA 251
Cdd:TIGR02061 146 RIFIVKLLLDKNTPNRIAGAVGFNVRANEVHVFKAKTVIVAAGGAVNVYRPRSVGEGAGRAWYAVWNAGSTYTMCAQAGA 225
                         250       260
                  ....*....|....*....|.
gi 157804751  252 ELTMMENRFVPARFKDGYGPV 272
Cdd:TIGR02061 226 EMTQMENRFVPARFKDGYGPV 246
NadB COG0029
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ...
161-261 5.81e-06

Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439800 [Multi-domain]  Cd Length: 521  Bit Score: 47.02  E-value: 5.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751 161 KKALGTERIQ--ERVFIVKLVndKNDKNRIAGAIGFSVREHKVFVYKFKACLLVAGGCVNIFR-----PRSVGEGtgraw 233
Cdd:COG0029  138 EAVRAHPNITvlENHFAVDLI--TDADGRCVGAYVLDEKTGEVETIRAKAVVLATGGAGQLYAyttnpDVATGDG----- 210
                         90       100
                 ....*....|....*....|....*...
gi 157804751 234 ypvwnagstYAMAAEAGAELTMMEnrFV 261
Cdd:COG0029  211 ---------IAMAYRAGARLADME--FV 227
 
Name Accession Description Interval E-value
PRK06854 PRK06854
adenylyl-sulfate reductase subunit alpha;
7-272 3.69e-143

adenylyl-sulfate reductase subunit alpha;


Pssm-ID: 235879 [Multi-domain]  Cd Length: 608  Bit Score: 414.71  E-value: 3.69e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751   7 NPEIVEEEVDILIIGGGMGACGAAYEIGPWLDqakkegyDLKVKLVDKAAMDRSGAVAQGLSAINTYLGE-QDPADYARM 85
Cdd:PRK06854   4 NPEVVEVDTDILIIGGGMAGCGAAFEAKEWAP-------DLKVLIVEKANIKRSGAVAQGLSAINAYIGEgETPEDYVRY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751  86 VSNDLMGITRDDLAYDLGRHVDDSVHLFEEWGLPIWKQpgdegkplvEGGKPVRLGKWQIMINGESYKWIVAEAAKKALG 165
Cdd:PRK06854  77 VRKDLMGIVREDLVYDIARHVDSVVHLFEEWGLPIWKD---------ENGKYVRRGRWQIMINGESYKPIVAEAAKKALG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751 166 tERIQERVFIVKLVNDKNdknRIAGAIGFSVREHKVFVYKFKACLLVAGGCVNIFRPRSVGEGTGRAWYPVWNAGSTYAM 245
Cdd:PRK06854 148 -DNVLNRVFITDLLVDDN---RIAGAVGFSVRENKFYVFKAKAVIVATGGAAGIYRPRSPGEGRGRMWYPPFNTGSGYAM 223
                        250       260
                 ....*....|....*....|....*..
gi 157804751 246 AAEAGAELTMMENRFVPARFKDGYGPV 272
Cdd:PRK06854 224 GIRAGAEMTTFENRFIPLRFKDGYGPV 250
aprA TIGR02061
adenosine phosphosulphate reductase, alpha subunit; During dissimilatory sulfate reduction or ...
16-272 3.06e-125

adenosine phosphosulphate reductase, alpha subunit; During dissimilatory sulfate reduction or sulfur oxidation, adenylylsulfate (APS) reductase catalyzes reversibly the two-electron reduction of APS to sulfite and AMP. Found in several bacterial lineages and in Archaeoglobales, APS reductase is a heterodimer composed of an alpha subunit containing a noncovalently bound FAD, and a beta subunit containing two [4Fe-4S] clusters. Described by this model is the alpha subunit of APS reductase, sharing common evolutionary origin with fumarate reductase/succinate dehydrogenase flavoproteins. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273946 [Multi-domain]  Cd Length: 614  Bit Score: 369.21  E-value: 3.06e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751   16 DILIIGGGMGACGAAYEIGPWLDQakkegYDLKVKLVDKAAMDRSGAVAQGLSAINTYLG----EQDPADYARMVSNDLM 91
Cdd:TIGR02061   1 DLLIVGGGMGGCGAAFEAVYWGDK-----KGLKIVLVEKANLERSGAVAQGLSAINTYLGtrfgENNAEDYVRYVRTDLM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751   92 GITRDDLAYDLGRHVDDSVHLFEEWGLPIWKQPGDegkplvegGKPVRLGKWQIMINGESYKWIVAEAAKKALGteRIQE 171
Cdd:TIGR02061  76 GLVREDLIFDMARHVDDSVHLFEEWGLPLWIKPED--------GKYVREGRWQIMIHGESYKPIVAEAAKNALG--DIFE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751  172 RVFIVKLVNDKNDKNRIAGAIGFSVREHKVFVYKFKACLLVAGGCVNIFRPRSVGEGTGRAWYPVWNAGSTYAMAAEAGA 251
Cdd:TIGR02061 146 RIFIVKLLLDKNTPNRIAGAVGFNVRANEVHVFKAKTVIVAAGGAVNVYRPRSVGEGAGRAWYAVWNAGSTYTMCAQAGA 225
                         250       260
                  ....*....|....*....|.
gi 157804751  252 ELTMMENRFVPARFKDGYGPV 272
Cdd:TIGR02061 226 EMTQMENRFVPARFKDGYGPV 246
PRK08275 PRK08275
putative oxidoreductase; Provisional
39-271 4.64e-18

putative oxidoreductase; Provisional


Pssm-ID: 181346 [Multi-domain]  Cd Length: 554  Bit Score: 83.56  E-value: 4.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751  39 QAKKEGYDLKVKLVDKAAMDRSGAVAQGLSAINTYL--GEQDPADYAR--MVSNDlmGITRDDLAYDLGRHVDDSVHLFE 114
Cdd:PRK08275  27 KAKERNPALRVLLLEKANVKRSGAISMGMDGLNNAVipGHATPEQYTKeiTIAND--GIVDQKAVYAYAEHSFETIQQLD 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751 115 EWGLpiwKQPGDE-GKPLVEggKPVRLGKWQI-MINGESYKWIVAEAAKKAlgTERIQERVFIVKLVNDKNdkNRIAGAI 192
Cdd:PRK08275 105 RWGV---KFEKDEtGDYAVK--KVHHMGSYVLpMPEGHDIKKVLYRQLKRA--RVLITNRIMATRLLTDAD--GRVAGAL 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157804751 193 GFSVREHKVFVYKFKACLLVAGGCVNIFRPRSvGEGTGRAWYPVwNAGSTYAMAAEAGAELTMMENRFVPARFKDGYGP 271
Cdd:PRK08275 176 GFDCRTGEFLVIRAKAVILCCGAAGRLGLPAS-GYLFGTYENPT-NAGDGYAMAYHAGAELANLECFQINPLIKDYNGP 252
PRK13800 PRK13800
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
49-271 5.99e-09

fumarate reductase/succinate dehydrogenase flavoprotein subunit;


Pssm-ID: 237512 [Multi-domain]  Cd Length: 897  Bit Score: 56.40  E-value: 5.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751  49 VKLVDKAAMDRSGAVAQGLSAINTYL--GEQDPADYARMVS--NDlmGITRDDLAYDLGRHVDDSVHLFEEWGLPIWKqp 124
Cdd:PRK13800  39 VLLLEKAHVRHSGALAMGMDGVNNAVipGKAEPEDYVAEITraND--GIVNQRTVYQTATRGFAMVQRLERYGVKFEK-- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751 125 gDE-GKPLVEggKPVRLGKWQI-MINGESYKWIVAEAAKKALGTE--RIQERVFIVKLVndkNDKNRIAGAIGFSVREHK 200
Cdd:PRK13800 115 -DEhGEYAVR--RVHRSGSYVLpMPEGKDVKKALYRVLRQRSMREriRIENRLMPVRVL---TEGGRAVGAAALNTRTGE 188
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157804751 201 VFVYKFKACLLVAGGCVNIFRPRSvGEGTGRAWYPVwNAGSTYAMAAEAGAELTMMENRFVPARFKDGYGP 271
Cdd:PRK13800 189 FVTVGAKAVILATGPCGRLGLPAS-GYLYGTYENPT-NAGDGYSMAYHAGAELSGIECFQINPLIKDYNGP 257
sdhA PRK06263
succinate dehydrogenase flavoprotein subunit; Reviewed
164-257 1.23e-06

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 235758 [Multi-domain]  Cd Length: 543  Bit Score: 49.21  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751 164 LGTERIQ--ERVFIVKLVNDKNdkNRIAGAIGFSVREHKVFVYKFKACLLVAGGCVNIFRPRSvgegtgrawYPVWNAGS 241
Cdd:PRK06263 144 LIKERIKilEEVMAIKLIVDEN--REVIGAIFLDLRNGEIFPIYAKATILATGGAGQLYPITS---------NPIQKTGD 212
                         90
                 ....*....|....*.
gi 157804751 242 TYAMAAEAGAELTMME 257
Cdd:PRK06263 213 GFAIAYRAGAELIDME 228
NadB COG0029
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ...
161-261 5.81e-06

Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439800 [Multi-domain]  Cd Length: 521  Bit Score: 47.02  E-value: 5.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751 161 KKALGTERIQ--ERVFIVKLVndKNDKNRIAGAIGFSVREHKVFVYKFKACLLVAGGCVNIFR-----PRSVGEGtgraw 233
Cdd:COG0029  138 EAVRAHPNITvlENHFAVDLI--TDADGRCVGAYVLDEKTGEVETIRAKAVVLATGGAGQLYAyttnpDVATGDG----- 210
                         90       100
                 ....*....|....*....|....*...
gi 157804751 234 ypvwnagstYAMAAEAGAELTMMEnrFV 261
Cdd:COG0029  211 ---------IAMAYRAGARLADME--FV 227
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
12-257 2.81e-04

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 41.74  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751  12 EEEVDILIIgggmgacgaayeigpwldQAKKEGydLKVKLVDKAAMDRSG-AVAQG-LSAINTYLGEQDPADYARMVSND 89
Cdd:COG1053    1 DHEYDVVVVgsggag-------lraalEAAEAG--LKVLVLEKVPPRGGHtAAAQGgINAAGTNVQKAAGEDSPEEHFYD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751  90 LM----GITRDDLAYDLGRHVDDSVHLFEEWGLPiWkQPGDEGKPLVEGGKPV------RLGKWQIMINGesykwiVAEA 159
Cdd:COG1053   72 TVkggdGLADQDLVEALAEEAPEAIDWLEAQGVP-F-SRTPDGRLPQFGGHSVgrtcyaGDGTGHALLAT------LYQA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751 160 AKKaLGTErIQERVFIVKLVndkNDKNRIAGAIGFSvREHKVFVYKFKACLLVAGGCVNIFRPRSVGEGTGRAWYPVWNA 239
Cdd:COG1053  144 ALR-LGVE-IFTETEVLDLI---VDDGRVVGVVARD-RTGEIVRIRAKAVVLATGGFGRNYEMRAEYLPEAEGALSTNAP 217
                        250       260
                 ....*....|....*....|.
gi 157804751 240 GST---YAMAAEAGAELTMME 257
Cdd:COG1053  218 GNTgdgIAMALRAGAALADME 238
sdhA PRK06452
succinate dehydrogenase flavoprotein subunit; Reviewed
42-253 2.67e-03

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 180567 [Multi-domain]  Cd Length: 566  Bit Score: 39.10  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751  42 KEGYdlKVKLVDKAAMDRS-GAVAQGlsAINTYL-GEQDPADYARMVSNDLMG----ITRDDLAYDLGRHVDDSVHLFEE 115
Cdd:PRK06452  26 SAGF--KVAVISKVFPTRShSAAAEG--GIAAYIpGNSDPNDNPDYMTYDTVKggdyLVDQDAAELLSNKSGEIVMLLER 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157804751 116 WGLPIWKQPgdegkplvEGGKPVRlgkwqiMINGESY--KWIVAEAAKKALgTERIQERV-----------FIVKLVndk 182
Cdd:PRK06452 102 WGALFNRQP--------DGRVAVR------YFGGQTYprTRFVGDKTGMAL-LHTLFERTsglnvdfynewFSLDLV--- 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157804751 183 NDKNRIAGAIGFSVREHKVFVYKFKACLLVAGGCVNIFRprsvgeGTGRAWYpvwNAGSTYAMAAEAGAEL 253
Cdd:PRK06452 164 TDNKKVVGIVAMQMKTLTPFFFKTKAVVLATGGMGMLYR------HTTNSYI---NTGDGFGIALRAGAAL 225
 
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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