|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
38-312 |
4.92e-141 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 400.78 E-value: 4.92e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 38 VASVLGTMEMG---RRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGlgggDCRVKIATKANPWDGKSL 114
Cdd:cd19075 1 PKIILGTMTFGsqgRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLG----ERGFKIDTKANPGVGGGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 115 KPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEG------------------------------- 163
Cdd:cd19075 77 SPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGkfkefglsnysawevaeiveickengwvlpt 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 164 ----MYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKdgKQPVGRFFGNS-WAETYRNRFWKEHHFEAI 238
Cdd:cd19075 157 vyqgMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSED--KAGGGRFDPNNaLGKLYRDRYWKPSYFEAL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1004393738 239 ALVEKALQAaygaSAPSVTSAALRWMYHHSQLQGAHGDAVILGMSSLEQLEQNLAATEEGPLEPAVVDAFNQAW 312
Cdd:cd19075 235 EKVEEAAEK----EGISLAEAALRWLYHHSALDGEKGDGVILGASSLEQLEENLAALEKGPLPEEVVKAIDEAW 304
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
42-312 |
5.24e-48 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 163.43 E-value: 5.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 42 LGTMEMGR---RMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcrVKIATKA-----NPWDGKS 113
Cdd:COG0667 18 LGTMTFGGpwgGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPRDD--VVIATKVgrrmgPGPNGRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 114 LKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEG------------------------------ 163
Cdd:COG0667 96 LSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGkiryigvsnysaeqlrralaiaeglppiva 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 164 ---MYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKqpvgrffGNSWAETYRNRFWKEHHFEAIAL 240
Cdd:COG0667 176 vqnEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPE-------GDRAATNFVQGYLTERNLALVDA 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1004393738 241 VeKALQAAYGASAPSVtsaALRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAATEEgPLEPAVVDAFNQAW 312
Cdd:COG0667 249 L-RAIAAEHGVTPAQL---ALAWLLAQPGV-----TSVIPGARSPEQLEENLAAADL-ELSAEDLAALDAAL 310
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
37-296 |
6.56e-39 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 139.63 E-value: 6.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 37 RVASV-LGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLglgggDCR--VKIATKA------N 107
Cdd:cd19087 12 KVSRLcLGTMNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIA-----GRRddIVLATKVfgpmgdD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 108 PWD-GKSLKpdSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEG----------------------- 163
Cdd:cd19087 87 PNDrGLSRR--HIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGkiryigvsnfaawqiakaqgiaa 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 164 ------------MYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKyedKDGKQPVGRFFGNswaETYRNRFWK 231
Cdd:cd19087 165 rrgllrfvseqpMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYG---KGKRPESGRLVER---ARYQARYGL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1004393738 232 EHHFEAIALVEkALQAAYGASAPSVtsaALRWMYHHSQLQGAhgdavILGMSSLEQLEQNLAATE 296
Cdd:cd19087 239 EEYRDIAERFE-ALAAEAGLTPASL---ALAWVLSHPAVTSP-----IIGPRTLEQLEDSLAALE 294
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
41-312 |
4.57e-38 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 136.67 E-value: 4.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 41 VLGTMEMG---RRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANPWDGK---SL 114
Cdd:pfam00248 2 GLGTWQLGggwGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKVPDGDGPwpsGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 115 KPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGM------------------------------ 164
Cdd:pfam00248 82 SKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKiraigvsnfdaeqiekaltkgkipivavqv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 165 -YNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNSWAETYrnrfwkehhfEAIALVEK 243
Cdd:pfam00248 162 eYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLKKGTPLNL----------EALEALEE 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1004393738 244 aLQAAYGASAPSVtsaALRWMYHHSQlqgahGDAVILGMSSLEQLEQNLAATeEGPLEPAVVDAFNQAW 312
Cdd:pfam00248 232 -IAKEHGVSPAQV---ALRWALSKPG-----VTIPIPGASNPEQLEDNLGAL-EFPLSDEEVARIDELL 290
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
64-296 |
9.81e-38 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 136.12 E-value: 9.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATK-ANPWDG-----KSLKPDSVRSQLETSLKRLQCPQVDL 137
Cdd:cd19084 35 IDLGINFFDTAPVYGFGHSEEILGKALKGRRD---DVVIATKcGLRWDGgkgvtKDLSPESIRKEVEQSLRRLQTDYIDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 138 FYLHAPDHGTPVEETLHACQRLHQEGM-----------------------------YNATTRQVETELFPCLRHFGLRFY 188
Cdd:cd19084 112 YQIHWPDPNTPIEETAEALEKLKKEGKiryigvsnfsveqleearkygpivslqppYSMLEREIEEELLPYCRENGIGVL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 189 AYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNswaetYRNRFWkEHHFEAIALVeKALQAAYGASAPSVtsaALRWMYHHS 268
Cdd:cd19084 192 PYGPLAQGLLTGKYKKEPTFPPDDRRSRFPF-----FRGENF-EKNLEIVDKL-KEIAEKYGKSLAQL---AIAWTLAQP 261
|
250 260
....*....|....*....|....*...
gi 1004393738 269 QLqgahgDAVILGMSSLEQLEQNLAATE 296
Cdd:cd19084 262 GV-----TSAIVGAKNPEQLEENAGALD 284
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
41-309 |
1.49e-37 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 135.80 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 41 VLGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYSD-------GQSETILGGLGLGLGGGDcRVKIATKANPW---D 110
Cdd:cd19081 13 CLGTMVFGWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRGKRD-RVVIATKVGFPmgpN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 111 GKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEG--------------------------- 163
Cdd:cd19081 92 GPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGkvryigasnysawrlqealelsrqhgl 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 164 --------MYNATTRQ-VETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPvgrffgnsWAETYRNRFWKEHH 234
Cdd:cd19081 172 pryvslqpEYNLVDREsFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGST--------RRGEAAKRYLNERG 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1004393738 235 FEAIALVEkALQAAYGASAPSVtsaALRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAATeEGPLEPAVVDAFN 309
Cdd:cd19081 244 LRILDALD-EVAAEHGATPAQV---ALAWLLARPGV-----TAPIAGARTVEQLEDLLAAA-GLRLTDEEVARLD 308
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
41-293 |
4.86e-37 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 132.26 E-value: 4.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 41 VLGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcRVKIATKA-----NPWDGKSLK 115
Cdd:cd06660 4 GLGTMTFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGNRD-DVVIATKGghppgGDPSRSRLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 116 PDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGM------------------------------- 164
Cdd:cd06660 83 PEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKiryigvsnwsaerlaealayakahglpgfaa 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 165 ----YN-ATTRQVETELFPCLRHFGLRFYAYNPLAGGLltgkykyedkdgkqpvgrffgnswaetyrnrfwkehhfeaia 239
Cdd:cd06660 163 vqpqYSlLDRSPMEEELLDWAEENGLPLLAYSPLARGP------------------------------------------ 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1004393738 240 lvekalqaaygasapsvTSAALRWMYHHSqlqgaHGDAVILGMSSLEQLEQNLA 293
Cdd:cd06660 201 -----------------AQLALAWLLSQP-----FVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
64-311 |
1.76e-34 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 127.32 E-value: 1.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLglgggDCR--VKIATKANPwdgKSLKPDSVRSQLETSLKRLQCPQVDLFYLH 141
Cdd:cd19085 33 LDAGINFFDTAEAYGDGHSEEVLGKALK-----GRRddVVIATKVSP---DNLTPEDVRKSCERSLKRLGTDYIDLYQIH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 142 APDHGTPVEETLHACQRLHQEGM-----------------------------YNATTRQVETELFPCLRHFGLRFYAYNP 192
Cdd:cd19085 105 WPSSDVPLEETMEALEKLKEEGKiraigvsnfgpaqleealdagridsnqlpYNLLWRAIEYEILPFCREHGIGVLAYSP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 193 LAGGLLTGKYkyeDKDGKQPVGR--------FFGNSWAETyrnrfwkehhFEAIALVeKALQAAYGAsapSVTSAALRWM 264
Cdd:cd19085 185 LAQGLLTGKF---SSAEDFPPGDartrlfrhFEPGAEEET----------FEALEKL-KEIADELGV---TMAQLALAWV 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1004393738 265 YHHSQLqgahgDAVILGMSSLEQLEQNLAATEEgPLEPAVVDAFNQA 311
Cdd:cd19085 248 LQQPGV-----TSVIVGARNPEQLEENAAAVDL-ELSPSVLERLDEI 288
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
64-296 |
5.01e-32 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 121.17 E-value: 5.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATK-ANPWDGKSL------KPDSVRSQLETSLKRLQCPQVD 136
Cdd:cd19076 42 LELGVTFLDTADMYGPGTNEELLGKALKDRRD---EVVIATKfGIVRDPGSGfrgvdgRPEYVRAACEASLKRLGTDVID 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 137 LFYLHAPDHGTPVEETLHACQRLHQEGM-----------------------------YNATTRQVETELFPCLRHFGLRF 187
Cdd:cd19076 119 LYYQHRVDPNVPIEETVGAMAELVEEGKvryiglseasadtirrahavhpitavqseYSLWTRDIEDEVLPTCRELGIGF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 188 YAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGnswaetyrnRFWKEhHFEA-IALVEK--ALQAAYGASAPSVtsaALRWM 264
Cdd:cd19076 199 VAYSPLGRGFLTGAIKSPEDLPEDDFRRNNP---------RFQGE-NFDKnLKLVEKleAIAAEKGCTPAQL---ALAWV 265
|
250 260 270
....*....|....*....|....*....|...
gi 1004393738 265 YHhsqlQGAhgDAV-ILGMSSLEQLEQNLAATE 296
Cdd:cd19076 266 LA----QGD--DIVpIPGTKRIKYLEENVGALD 292
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
64-296 |
2.08e-30 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 116.94 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATKANPWDGKSlkPDSV---RSQL----ETSLKRLQCPQVD 136
Cdd:cd19091 49 LDAGINFFDTADVYSEGESEEILGKALKGRRD---DVLIATKVRGRMGEG--PNDVglsRHHIiravEASLKRLGTDYID 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 137 LFYLHAPDHGTPVEETLHACQRLHQEGM-----------------------------------YNATTRQVETELFPCLR 181
Cdd:cd19091 124 LYQLHGFDALTPLEETLRALDDLVRQGKvryigvsnfsawqimkalgiserrglarfvalqayYSLLGRDLEHELMPLAL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 182 HFGLRFYAYNPLAGGLLTGKYKyedKDGKQPVGRFFGNSWAETYrnRFWKEHHFEAI-ALVEKAlqAAYGASAPSVtsaA 260
Cdd:cd19091 204 DQGVGLLVWSPLAGGLLSGKYR---RGQPAPEGSRLRRTGFDFP--PVDRERGYDVVdALREIA--KETGATPAQV---A 273
|
250 260 270
....*....|....*....|....*....|....*.
gi 1004393738 261 LRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAATE 296
Cdd:cd19091 274 LAWL-----LSRPTVSSVIIGARNEEQLEDNLGAAG 304
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
42-296 |
2.83e-30 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 116.55 E-value: 2.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 42 LGTM----EMGRRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATK----ANPWD--- 110
Cdd:cd19080 15 LGTMtfgtEWGWGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNRD---RIVLATKytmnRRPGDpna 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 111 -GKSLKpdSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHA-------------------------CQRLHQ--- 161
Cdd:cd19080 92 gGNHRK--NLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRAlddlvragkvlyvgisdtpawvvarANTLAElrg 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 162 -------EGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKY-KYEDKDGKQPVGRFFGNSwAETYRNrfwkeh 233
Cdd:cd19080 170 wspfvalQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYqRGEEGRAGEAKGVTVGFG-KLTERN------ 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1004393738 234 hfEAIALVEKALQAAYGASAPSVtsaALRWMYHHSQlqgahGDAVILGMSSLEQLEQNLAATE 296
Cdd:cd19080 243 --WAIVDVVAAVAEELGRSAAQV---ALAWVRQKPG-----VVIPIIGARTLEQLKDNLGALD 295
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
64-297 |
1.80e-27 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 109.05 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcrVKIATK-ANPWDGKSLK----PDSVRSQLETSLKRLQCPQVDLF 138
Cdd:cd19083 43 LDNGVNLLDTAFIYGLGRSEELVGEVLKEYNRNE--VVIATKgAHKFGGDGSVlnnsPEFLRSAVEKSLKRLNTDYIDLY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 139 YLHAPDHGTPVEETLHACQRLHQEGM-----------------------------YNATTRQVETELFPCLRHFGLRFYA 189
Cdd:cd19083 121 YIHFPDGETPKAEAVGALQELKDEGKiraigvsnfsleqlkeankdgyvdvlqgeYNLLQREAEEDILPYCVENNISFIP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 190 YNPLAGGLLTGKY----KYEDKDGKQPVGRFFGnswaETYRNRFWKEHHFEAIAlvekalqAAYGASAPSVtsaALRWMY 265
Cdd:cd19083 201 YFPLASGLLAGKYtkdtKFPDNDLRNDKPLFKG----ERFSENLDKVDKLKSIA-------DEKGVTVAHL---ALAWYL 266
|
250 260 270
....*....|....*....|....*....|....*..
gi 1004393738 266 HHSQLqgahgDAVILGMSSLEQLEQNLAA-----TEE 297
Cdd:cd19083 267 TRPAI-----DVVIPGAKRAEQVIDNLKAldvtlTEE 298
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
64-296 |
1.78e-25 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 103.43 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcRVKIATKANP-----WDGKSLKPDSVRSQLETSLKRLQCPQVDLF 138
Cdd:cd19079 45 LDLGINFFDTANVYSGGASEEILGRALKEFAPRD-EVVIATKVYFpmgdgPNGRGLSRKHIMAEVDASLKRLGTDYIDLY 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 139 YLHAPDHGTPVEETLHA-----------------------CQRLH---QEGM---------YNATTRQVETELFPCLRHF 183
Cdd:cd19079 124 QIHRWDYETPIEETLEAlhdvvksgkvryigassmyawqfAKALHlaeKNGWtkfvsmqnhYNLLYREEEREMIPLCEEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 184 GLRFYAYNPLAGGLLTGKYKyedKDGKQPVGRFFGNSWAETYRnrfwKEHHFEAIALVEKaLQAAYGASAPSVtsaALRW 263
Cdd:cd19079 204 GIGVIPWSPLARGRLARPWG---DTTERRRSTTDTAKLKYDYF----TEADKEIVDRVEE-VAKERGVSMAQV---ALAW 272
|
250 260 270
....*....|....*....|....*....|...
gi 1004393738 264 MYHHSQlqgahGDAVILGMSSLEQLEQNLAATE 296
Cdd:cd19079 273 LLSKPG-----VTAPIVGATKLEHLEDAVAALD 300
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-296 |
3.18e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 102.75 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATKANP-WDGK-----SLKPDSVRSQLETSLKRLQCPQVDL 137
Cdd:cd19102 36 LDLGINWIDTAAVYGLGHSEEVVGRALKGLRD---RPIVATKCGLlWDEEgrirrSLKPASIRAECEASLRRLGVDVIDL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 138 FYLHAPDHGTPVEETLHACQRLHQEG-----------------------------MYNATTRQVETELFPCLRHFGLRFY 188
Cdd:cd19102 113 YQIHWPDPDEPIEEAWGALAELKEEGkvraigvsnfsvdqmkrcqaihpiaslqpPYSLLRRGIEAEILPFCAEHGIGVI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 189 AYNPLAGGLLTGKYkyedkdGKQPVGRFFGNSWAEtyRNRFWKEHHF-EAIALVE--KALQAAYGASAPSVtsaALRWMY 265
Cdd:cd19102 193 VYSPMQSGLLTGKM------TPERVASLPADDWRR--RSPFFQEPNLaRNLALVDalRPIAERHGRTVAQL---AIAWVL 261
|
250 260 270
....*....|....*....|....*....|.
gi 1004393738 266 HHSQLQGAhgdavILGMSSLEQLEQNLAATE 296
Cdd:cd19102 262 RRPEVTSA-----IVGARRPDQIDETVGAAD 287
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
42-309 |
8.54e-25 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 101.87 E-value: 8.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 42 LGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYS-------DGQSETILGGLGLGLGGGDcRVKIATKA------NP 108
Cdd:cd19094 6 LGTMTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKGNRD-KVVLATKVagpgegIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 109 W---DGKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPV------------------EETLHACQRLHQEG---- 163
Cdd:cd19094 85 WprgGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPLfgggyytepseeedsvsfEEQLEALGELVKAGkirh 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 164 -----------M--------------------YNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQp 212
Cdd:cd19094 165 iglsnetpwgvMkflelaeqlglprivsiqnpYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDGAARPEG- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 213 vGRFFGNSWaetYRNRFWKEHHFEAI-ALVEKALQAAYgasapSVTSAALRWMYHHSqlqgaHGDAVILGMSSLEQLEQN 291
Cdd:cd19094 244 -GRLNLFPG---YMARYRSPQALEAVaEYVKLARKHGL-----SPAQLALAWVRSRP-----FVTSTIIGATTLEQLKEN 309
|
330
....*....|....*...
gi 1004393738 292 LAATeEGPLEPAVVDAFN 309
Cdd:cd19094 310 IDAF-DVPLSDELLAEID 326
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
102-303 |
3.63e-24 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 100.02 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 102 IATKA--NPW-----DGKSLKpdSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGM---------- 164
Cdd:cd19089 80 ISTKAgyGMWpgpygDGGSRK--YLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKalyvgisnyp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 165 ------------------------YNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYkyedKDGKQPVGRFFGNS 220
Cdd:cd19089 158 gakarraiallrelgvpliihqprYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKY----LNGIPPDSRRAAES 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 221 WaetyrnrFWKEHHF-EAIALVEKALQAAYGASAPSVTSAALRWMYHHSQLQgahgdAVILGMSSLEQLEQNLAATEEGP 299
Cdd:cd19089 234 K-------FLTEEALtPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVT-----SVLIGASSPSQLEDNVAALKNLD 301
|
....
gi 1004393738 300 LEPA 303
Cdd:cd19089 302 FSEE 305
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
34-264 |
5.60e-24 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 99.30 E-value: 5.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 34 PPPRVAsvLGTMEMGRRM----DAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcRVKIATKAN-P 108
Cdd:cd19148 3 PVSRIA--LGTWAIGGWMwggtDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYGKRD-RVVIATKVGlE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 109 WDGKSLK-----PDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEG--------------M----- 164
Cdd:cd19148 80 WDEGGEVvrnssPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGkiraigvsnfspeqMetfrk 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 165 ----------YNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGK----YKYEDKDGKQPVGRFFGnswaetyrNRFw 230
Cdd:cd19148 160 vaplhtvqppYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKmtkdTKFEGDDLRRTDPKFQE--------PRF- 230
|
250 260 270
....*....|....*....|....*....|....
gi 1004393738 231 kEHHFEAIALVEKALQAAYGAsapSVTSAALRWM 264
Cdd:cd19148 231 -SQYLAAVEELDKLAQERYGK---SVIHLAVRWL 260
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
42-296 |
1.11e-23 |
|
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381298 [Multi-domain] Cd Length: 263 Bit Score: 97.68 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 42 LGTMEMGRRM-----DAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcrVKIATKANPWdgkSLKP 116
Cdd:cd19072 9 LGTWGIGGGMskdysDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDRED--LFITTKVSPD---HLKY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 117 DSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGM-------------------------------- 164
Cdd:cd19072 84 DDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKiryigvsnfsleeleeaqsylkkgpivanqve 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 165 YNATTRQVETELFP-CLRHfGLRFYAYNPLAGGLLTGKYKYEDkdgkqpvgrffgnswaetyrnrfwkehhfeaiaLVEk 243
Cdd:cd19072 164 YNLFDREEESGLLPyCQKN-GIAIIAYSPLEKGKLSNAKGSPL---------------------------------LDE- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1004393738 244 aLQAAYGASAPSVtsaALRWMYHHSqlqgahGDAVILGMSSLEQLEQNLAATE 296
Cdd:cd19072 209 -IAKKYGKTPAQI---ALNWLISKP------NVIAIPKASNIEHLEENAGALG 251
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
64-294 |
3.14e-23 |
|
Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381300 [Multi-domain] Cd Length: 297 Bit Score: 97.28 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGD----CRVKIATKANPWD-GKSLKpdSVRSQLETSLKRLQCPQVDLF 138
Cdd:cd19074 32 YDLGINFFDTADVYAAGQAEEVLGKALKGWPRESyvisTKVFWPTGPGPNDrGLSRK--HIFESIHASLKRLQLDYVDIY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 139 YLHAPDHGTPVEETLHACQRL--------------------------HQEGM---------YNATTRQVETELFPCLRHF 183
Cdd:cd19074 110 YCHRYDPETPLEETVRAMDDLirqgkilywgtsewsaeqiaeahdlaRQFGLippvveqpqYNMLWREIEEEVIPLCEKN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 184 GLRFYAYNPLAGGLLTGKYkyedKDGK-QPVGRFFGNSWAETYRNRFWKEHHFEAIALVeKALQAAYGASAPsvtSAALR 262
Cdd:cd19074 190 GIGLVVWSPLAQGLLTGKY----RDGIpPPSRSRATDEDNRDKKRRLLTDENLEKVKKL-KPIADELGLTLA---QLALA 261
|
250 260 270
....*....|....*....|....*....|..
gi 1004393738 263 WMyhhsqLQGAHGDAVILGMSSLEQLEQNLAA 294
Cdd:cd19074 262 WC-----LRNPAVSSAIIGASRPEQLEENVKA 288
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
64-304 |
9.99e-22 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 92.62 E-value: 9.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYsdGQSETILGGLGLGLGGGdcRVKIATKANPWDGKSLK--PDSVRSQLETSLKRLQCPQVDLFYLH 141
Cdd:cd19090 30 LDLGINYIDTAPAY--GDSEERLGLALAELPRE--PLVLSTKVGRLPEDTADysADRVRRSVEESLERLGRDRIDLLMIH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 142 APDHGTPVEET-----LHACQRLHQEGM-------------------------------YNATTRQVETELFP-CLRHfG 184
Cdd:cd19090 106 DPERVPWVDILapggaLEALLELKEEGLikhiglgggppdllrraietgdfdvvltanrYTLLDQSAADELLPaAARH-G 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 185 LRFYAYNPLAGGLLTGKYKyedkdgkqpvgrffgnSWAETYRNRFWKEHHFEAIALveKALQAAYGASAPsvtSAALRWM 264
Cdd:cd19090 185 VGVINASPLGMGLLAGRPP----------------ERVRYTYRWLSPELLDRAKRL--YELCDEHGVPLP---ALALRFL 243
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1004393738 265 YHHSQLqgahgDAVILGMSSLEQLEQNLAATeEGPLEPAV 304
Cdd:cd19090 244 LRDPRI-----STVLVGASSPEELEQNVAAA-EGPLPEEL 277
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
64-296 |
1.08e-21 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 93.07 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATK--------ANPWDGKSLKPDSVRSQLETSLKRLQCPQV 135
Cdd:cd19078 35 VELGITFFDTAEVYGPYTNEELVGEALKPFRD---QVVIATKfgfkidggKPGPLGLDSRPEHIRKAVEGSLKRLQTDYI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 136 DLFYLHAPDHGTPVEETLHACQRLHQEGM-----------------------------YNATTRQVETELFPCLRHFGLR 186
Cdd:cd19078 112 DLYYQHRVDPNVPIEEVAGTMKELIKEGKirhwglseagvetirrahavcpvtavqseYSMMWREPEKEVLPTLEELGIG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 187 FYAYNPLAGGLLTGKYkyeDKDGKqpvgrfFGnswAETYRN---RFWKEHHFEAIALVE--KALQAAYGAsapsvTSA-- 259
Cdd:cd19078 192 FVPFSPLGKGFLTGKI---DENTK------FD---EGDDRAslpRFTPEALEANQALVDllKEFAEEKGA-----TPAqi 254
|
250 260 270
....*....|....*....|....*....|....*...
gi 1004393738 260 ALRWMYHhsqlQGAHgdAV-ILGMSSLEQLEQNLAATE 296
Cdd:cd19078 255 ALAWLLA----KKPW--IVpIPGTTKLSRLEENIGAAD 286
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
64-294 |
1.12e-21 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 93.11 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATKAN-PWDG---------------KSLKPDSVRSQLETSL 127
Cdd:cd19149 43 LDLGINLIDTAPAYGFGHSEEIVGKAIKGRRD---KVVLATKCGlRWDReggsfffvrdgvtvyKNLSPESIREEVEQSL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 128 KRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEG-----------------------------MYNATTRQVETELFP 178
Cdd:cd19149 120 KRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGkiraigasnvsveqikeyvkagqldiiqeKYSMLDRGIEKELLP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 179 -CLRHfGLRFYAYNPLAGGLLTGKYKyedkdgkqPVGRFFGNSWaetyRNR---FWKEHHFEAIALVE--KALQAAYGAS 252
Cdd:cd19149 200 yCKKN-NIAFQAYSPLEQGLLTGKIT--------PDREFDAGDA----RSGipwFSPENREKVLALLEkwKPLCEKYGCT 266
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1004393738 253 APSVtsaALRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAA 294
Cdd:cd19149 267 LAQL---VIAWTLAQPGI-----TSALCGARKPEQAEENAKA 300
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
72-307 |
4.05e-20 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 88.81 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 72 DTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANpWDGKSLKPDS-------VRSQLETSLKRLQCPQVDLFYLHAPD 144
Cdd:cd19143 49 DNAEVYANGQSEEIMGQAIKELGWPRSDYVVSTKIF-WGGGGPPPNDrglsrkhIVEGTKASLKRLQLDYVDLVFCHRPD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 145 HGTPVEETLHA-----------------------------CQRLHQEG------MYNATTRQ-VETELFPCLRHFGLRFY 188
Cdd:cd19143 128 PATPIEETVRAmndlidqgkafywgtsewsaqqieeaheiADRLGLIPpvmeqpQYNLFHRErVEVEYAPLYEKYGLGTT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 189 AYNPLAGGLLTGKYkyedKDGKQPVGRFFGNSWaetyrnrFWKEHHFEA-----IALVEKALQAA--YGASAPSVtsaAL 261
Cdd:cd19143 208 TWSPLASGLLTGKY----NNGIPEGSRLALPGY-------EWLKDRKEElgqekIEKVRKLKPIAeeLGCSLAQL---AI 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1004393738 262 RWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAATEEGP-LEPAVVDA 307
Cdd:cd19143 274 AWC-----LKNPNVSTVITGATKVEQLEENLKALEVLPkLTPEVMEK 315
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
64-294 |
3.18e-19 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 86.13 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcRVKIATK--ANPWdgkSLKPDSVRSQLETSLKRLQCPQVDLFYLH 141
Cdd:cd19093 36 LEAGVNLFDTAEVYGTGRSERLLGRFLKELGDRD-EVVIATKfaPLPW---RLTRRSVVKALKASLERLGLDSIDLYQLH 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 142 APDH-GTPVEETLHACQRLHQEGM--------YNA-----------------TTRQVE----------TELFPCLRHFGL 185
Cdd:cd19093 112 WPGPwYSQIEALMDGLADAVEEGLvravgvsnYSAdqlrrahkalkergvplASNQVEysllyrdpeqNGLLPACDELGI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 186 RFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNSWAETYrnrfwkehhfeaiALVE--KALQAAYGASAPSVtsaALRW 263
Cdd:cd19093 192 TLIAYSPLAQGLLTGKYSPENPPPGGRRRLFGRKNLEKVQ-------------PLLDalEEIAEKYGKTPAQV---ALNW 255
|
250 260 270
....*....|....*....|....*....|.
gi 1004393738 264 MYHHSQLqgahgdaVILGMSSLEQLEQNLAA 294
Cdd:cd19093 256 LIAKGVV-------PIPGAKNAEQAEENAGA 279
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
64-294 |
2.61e-18 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 84.03 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDgqSETILGGLGLGLGGGDCRVKIATK----ANPWDGK---SLKPDSVRSQLETSLKRLQCPQVD 136
Cdd:cd19144 44 FELGCTFWDTADIYGD--SEELIGRWFKQNPGKREKIFLATKfgieKNVETGEysvDGSPEYVKKACETSLKRLGVDYID 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 137 LFYLHAPDHGTPVEETLHACQRLHQEG--------------------MYNATTRQVE------------TELFPCLRHFG 184
Cdd:cd19144 122 LYYQHRVDGKTPIEKTVAAMAELVQEGkikhiglsecsaetlrrahaVHPIAAVQIEyspfsldierpeIGVLDTCRELG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 185 LRFYAYNPLAGGLLTGKYKYEDKdgkqpvgrFFGNSWaETYRNRFWKEHHFEAIALVEKaLQAAygASAPSVTSA--ALR 262
Cdd:cd19144 202 VAIVAYSPLGRGFLTGAIRSPDD--------FEEGDF-RRMAPRFQAENFPKNLELVDK-IKAI--AKKKNVTAGqlTLA 269
|
250 260 270
....*....|....*....|....*....|....
gi 1004393738 263 WMYhhsqlqgAHGDAV--ILGMSSLEQLEQNLAA 294
Cdd:cd19144 270 WLL-------AQGDDIipIPGTTKLKRLEENLGA 296
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
41-296 |
1.48e-17 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 81.45 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 41 VLGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYSD----GQSETILGGLGLGLGGGDcRVKIATKA-----NPWDG 111
Cdd:cd19082 4 VLGTADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRGNRD-KVVIATKGghpdlEDMSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 112 KSLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGMYNA-------TTRQVETELFpCLRH-- 182
Cdd:cd19082 83 SRLSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAfgasnwsTERIAEANAY-AKAHgl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 183 ---------FGL---------------------RFY--------AYNPLAGGLLTGKYKYEDKDGKQpvgrffgnswaet 224
Cdd:cd19082 162 pgfaasspqWSLarpneppwpgptlvamdeemrAWHeenqlpvfAYSSQARGFFSKRAAGGAEDDSE------------- 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1004393738 225 YRNRFWKEHHFEAIALVeKALQAAYGAsapSVTSAALRWMYHHSQLQGAhgdavILGMSSLEQLEQNLAATE 296
Cdd:cd19082 229 LRRVYYSEENFERLERA-KELAEEKGV---SPTQIALAYVLNQPFPTVP-----IIGPRTPEQLRDSLAAAD 291
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
64-294 |
5.30e-17 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 78.67 E-value: 5.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLglgggDCR--VKIATKANPWDGKSLK------PDSVRSQLETSLKRLQCPQV 135
Cdd:cd19086 34 LDLGINFFDTADVYGDGHSERLLGKALK-----GRRdkVVIATKFGNRFDGGPErpqdfsPEYIREAVEASLKRLGTDYI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 136 DLFYLH-APDHGTPVEETLHACQRLHQEG-----------------------------MYNATTRQVETELFPCLRHFGL 185
Cdd:cd19086 109 DLYQLHnPPDEVLDNDELFEALEKLKQEGkiraygvsvgdpeealaalrrggidvvqvIYNLLDQRPEEELFPLAEEHGV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 186 RFYAYNPLAGGLLTGKykyedkdgkqpvgrffgnswaetyrnrfwkehhfeaiaLVEKALQaaYGASAPSVTSaalrwmy 265
Cdd:cd19086 189 GVIARVPLASGLLTGK--------------------------------------LAQAALR--FILSHPAVST------- 221
|
250 260
....*....|....*....|....*....
gi 1004393738 266 hhsqlqgahgdaVILGMSSLEQLEQNLAA 294
Cdd:cd19086 222 ------------VIPGARSPEQVEENAAA 238
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
41-296 |
5.34e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 79.68 E-value: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 41 VLGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYS-------DGQSETILGGLGLGLGGGDcRVKIATK-------- 105
Cdd:cd19752 4 CLGTMYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRGNRD-DVVIATKvgagprdp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 106 -ANPWDGKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGMY----------------NAT 168
Cdd:cd19752 83 dGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVraigasnfaawrleraRQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 169 TRQVETELFPCL--RH----------FG------------------LRFYAYNPLAGGLltgkykYEDKDGKQPvgrffg 218
Cdd:cd19752 163 ARQQGWAEFSAIqqRHsylrprpgadFGvqrivtdelldyassrpdLTLLAYSPLLSGA------YTRPDRPLP------ 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1004393738 219 nswaETYRNRFwKEHHFEAIALVEKALqaayGASAPSVtsaALRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAATE 296
Cdd:cd19752 231 ----EQYDGPD-SDARLAVLEEVAGEL----GATPNQV---VLAWL-----LHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
64-296 |
4.59e-16 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 76.49 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLGLgggDCRVKIATKA-------NPW--DGKslkPDSVRSQLETSLKRLQCPQ 134
Cdd:cd19088 34 LELGVNFIDTADSYGPDVNERLIAEALHPY---PDDVVIATKGglvrtgpGWWgpDGS---PEYLRQAVEASLRRLGLDR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 135 VDLFYLHAPDHGTPVEETLHACQRLHQEGMY------NATTRQVET--ELFP---------------------CLRHfGL 185
Cdd:cd19088 108 IDLYQLHRIDPKVPFEEQLGALAELQDEGLIrhiglsNVTVAQIEEarAIVRivsvqnrynlanrddegvldyCEAA-GI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 186 RFYAYNPLAGGLLTgkykyedkdgkQPVGRFfgnswaetyrnrfwkehhfeaialveKALQAAYGASAPSVtsaALRWMY 265
Cdd:cd19088 187 AFIPWFPLGGGDLA-----------QPGGLL--------------------------AEVAARLGATPAQV---ALAWLL 226
|
250 260 270
....*....|....*....|....*....|.
gi 1004393738 266 HHSQlqgahGDAVILGMSSLEQLEQNLAATE 296
Cdd:cd19088 227 ARSP-----VMLPIPGTSSVEHLEENLAAAG 252
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
67-294 |
7.73e-15 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 73.62 E-value: 7.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 67 GHTELDTAFMYSDGQSETILGGLGLGLGGGdcRVKIATK---ANPWDGKSL---KPDSVRSQLETSLKRLQCPQVDLFYL 140
Cdd:cd19145 46 GVTFLDTSDIYGPNTNEVLLGKALKDGPRE--KVQLATKfgiHEIGGSGVEvrgDPAYVRAACEASLKRLDVDYIDLYYQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 141 HAPDHGTPVEETLHACQRLHQEGM-----------------------------YNATTRQVETELFPCLRHFGLRFYAYN 191
Cdd:cd19145 124 HRIDTTVPIEITMGELKKLVEEGKikyiglseasadtirrahavhpitavqleWSLWTRDIEEEIIPTCRELGIGIVPYS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 192 PLAGGLLTGKYKYE----DKDGKQPVGRFFGNSWaetyrnrfwkEHH---FEAIAlvekALQAAYGASaPSvtSAALRWM 264
Cdd:cd19145 204 PLGRGFFAGKAKLEelleNSDVRKSHPRFQGENL----------EKNkvlYERVE----ALAKKKGCT-PA--QLALAWV 266
|
250 260 270
....*....|....*....|....*....|..
gi 1004393738 265 YHhsqlqgaHGDAV--ILGMSSLEQLEQNLAA 294
Cdd:cd19145 267 LH-------QGEDVvpIPGTTKIKNLNQNIGA 291
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-294 |
1.03e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 72.62 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdCRVKIATKANPWDGKSlKPDSVRSQLETSLKRLQCPQVDLFYLHAP 143
Cdd:cd19105 35 LDLGINYFDTAEGYGNGNSEEIIGEALKGLRR--DKVFLATKASPRLDKK-DKAELLKSVEESLKRLQTDYIDIYQLHGV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 144 DHGTP---VEETLHACQRLHQEGMynattrqvetelfpcLRHFGlrFYAYNPLAGGLL----TGKYkyedkDGKQPvgrf 216
Cdd:cd19105 112 DTPEErllNEELLEALEKLKKEGK---------------VRFIG--FSTHDNMAEVLQaaieSGWF-----DVIMV---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 217 fgnswaeTYRNRFWKEHHFEAIA---------LVEKALQAAYG---------ASAPSVTSAALRWMYHHSQLqgahgDAV 278
Cdd:cd19105 166 -------AYNFLNQPAELEEALAaaaekgigvVAMKTLAGGYLqpallsvlkAKGFSLPQAALKWVLSNPRV-----DTV 233
|
250
....*....|....*.
gi 1004393738 279 ILGMSSLEQLEQNLAA 294
Cdd:cd19105 234 VPGMRNFAELEENLAA 249
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
64-294 |
1.19e-13 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 69.22 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYsDGQSETILGGLGLGLGGGDcrVKIATKANPwdgKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAP 143
Cdd:cd19073 24 LELGYRHIDTAEIY-NNEAEVGEAIAESGVPRED--LFITTKVWR---DHLRPEDLKKSVDRSLEKLGTDYVDLLLIHWP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 144 DHGTPVEETLHACQRLHQE------GMYNATTRQVE--------------TELFPCLRHFGLRFY---------AYNPLA 194
Cdd:cd19073 98 NPTVPLEETLGALKELKEAgkvksiGVSNFTIELLEealdisplpiavnqVEFHPFLYQAELLEYcrendivitAYSPLA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 195 GGLLtgkykyedkdgkqpvgrffgnswaetyrnrfwkEHHFEAIALVEKalqaaYGASAPSVtsaALRWMYhhsqlqgAH 274
Cdd:cd19073 178 RGEV---------------------------------LRDPVIQEIAEK-----YDKTPAQV---ALRWLV-------QK 209
|
250 260
....*....|....*....|
gi 1004393738 275 GDAVILGMSSLEQLEQNLAA 294
Cdd:cd19073 210 GIVVIPKASSEDHLKENLAI 229
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
64-296 |
5.46e-13 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 67.66 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETIlgglgLGLGGGDCR--VKIATKANPWDGkslKPDSVRSQLETSLKRLQCPQVDLFYLH 141
Cdd:cd19138 39 IDLGMTLIDTAEMYGDGGSEEL-----VGEAIRGRRdkVFLVSKVLPSNA---SRQGTVRACERSLRRLGTDYLDLYLLH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 142 APDhGTPVEETLHACQRLHQEG--------------------------------MYNATTRQVETELFPCLRHFGLRFYA 189
Cdd:cd19138 111 WRG-GVPLAETVAAMEELKKEGkirawgvsnfdtddmeelwavpgggncaanqvLYNLGSRGIEYDLLPWCREHGVPVMA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 190 YNPLAGGLLTGKYKYEDKDGKqpvgrffgnswaetyrnrfwkehhfeAIAlvekalqAAYGASAPSVtsaALRWMYHHSq 269
Cdd:cd19138 190 YSPLAQGGLLRRGLLENPTLK--------------------------EIA-------ARHGATPAQV---ALAWVLRDG- 232
|
250 260
....*....|....*....|....*..
gi 1004393738 270 lqgahGDAVILGMSSLEQLEQNLAATE 296
Cdd:cd19138 233 -----NVIAIPKSGSPEHARENAAAAD 254
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
102-295 |
7.78e-13 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 67.81 E-value: 7.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 102 IATKAN--PWDGK-----SLKpdSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGM---------- 164
Cdd:cd19151 81 ISTKAGytMWPGPygdwgSKK--YLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKalyvgisnyp 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 165 ------------------------YNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKY---EDKDGKQPvgrff 217
Cdd:cd19151 159 peeareaaailkdlgtpclihqpkYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNgipEDSRAAKG----- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 218 gnswaetyrNRFWKEHHF--EAIALVeKALQAAYGASAPSVTSAALRWMYHHSQLQgahgdAVILGMSSLEQLEQNLAAT 295
Cdd:cd19151 234 ---------SSFLKPEQIteEKLAKV-RRLNEIAQARGQKLAQMALAWVLRNKRVT-----SVLIGASKPSQIEDAVGAL 298
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
102-294 |
1.52e-12 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 67.32 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 102 IATKA--NPWDGKSLKPDSVR---SQLETSLKRLQCPQVDLFYLHAPDHGTPVEETL----HACQR-------------- 158
Cdd:PRK09912 94 ISTKAgyDMWPGPYGSGGSRKyllASLDQSLKRMGLEYVDIFYSHRVDENTPMEETAsalaHAVQSgkalyvgissyspe 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 159 -----------------LHQEGmYNATTRQVE-TELFPCLRHFGLRFYAYNPLAGGLLTGKY-------KYEDKDGKQPV 213
Cdd:PRK09912 174 rtqkmvellrewkipllIHQPS-YNLLNRWVDkSGLLDTLQNNGVGCIAFTPLAQGLLTGKYlngipqdSRMHREGNKVR 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 214 GrffgnswaetYRNRFWKEHHFEAIALVEKALQaaygASAPSVTSAALRWMYHHSQLQgahgdAVILGMSSLEQLEQNLA 293
Cdd:PRK09912 253 G----------LTPKMLTEANLNSLRLLNEMAQ----QRGQSMAQMALSWLLKDERVT-----SVLIGASRAEQLEENVQ 313
|
.
gi 1004393738 294 A 294
Cdd:PRK09912 314 A 314
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
63-298 |
4.31e-12 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 64.89 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 63 FLERGHTELDTAFMYSDGQSETILGGLGLGLGGGdcRVKIATKANPWDGKSlkPDSVRSQLETSLKRLQCPQVDLFYLHA 142
Cdd:cd19096 30 AIDAGINYFDTAYGYGGGKSEEILGEALKEGPRE--KFYLATKLPPWSVKS--AEDFRRILEESLKRLGVDYIDFYLLHG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 143 PDHGtpveETLHACQRLhqeGMYNATTRQVETELFpclRHFGLRFYAYNPLAGGLLtgkykyedkdgkqpvgrffgnswa 222
Cdd:cd19096 106 LNSP----EWLEKARKG---GLLEFLEKAKKEGLI---RHIGFSFHDSPELLKEIL------------------------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 223 ETYRNRF---------WKehHFEAIALVEKAlqAAYG--------------ASAPSVT------------SAALRWMYHH 267
Cdd:cd19096 152 DSYDFDFvqlqynyldQE--NQAGRPGIEYA--AKKGmgviimeplkggglANNPPEAlailcgaplspaEWALRFLLSH 227
|
250 260 270
....*....|....*....|....*....|.
gi 1004393738 268 sqlQGAHgdAVILGMSSLEQLEQNLAATEEG 298
Cdd:cd19096 228 ---PEVT--TVLSGMSTPEQLDENIAAADEF 253
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
102-294 |
4.32e-12 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 65.08 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 102 IATKANPWDgksLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGtPVEETLHACQRLHQEGMY------NATTRQVET- 174
Cdd:COG0656 63 VTTKVWNDN---HGYDDTLAAFEESLERLGLDYLDLYLIHWPGPG-PYVETWRALEELYEEGLIraigvsNFDPEHLEEl 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 175 -------------ELFPCLRHFGLRFY---------AYNPLA-GGLLtgkykyedkdgKQPVgrffgnswaetyrnrfwk 231
Cdd:COG0656 139 laetgvkpavnqvELHPYLQQRELLAFcrehgivveAYSPLGrGKLL-----------DDPV------------------ 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1004393738 232 ehhFEAIAlvekalqAAYGASAPSVtsaALRWmyhHSQlqgaHGDAVILGMSSLEQLEQNLAA 294
Cdd:COG0656 190 ---LAEIA-------EKHGKTPAQV---VLRW---HLQ----RGVVVIPKSVTPERIRENLDA 232
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
42-294 |
4.74e-12 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 65.91 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 42 LGTMEMGRR-------MDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVkIATK--------- 105
Cdd:cd19146 16 LGAMSFGEAwksmmgeCDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRGNRDEMV-LATKyttgyrrgg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 106 ----ANPWDGKSLKpdSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRL---------------------- 159
Cdd:cd19146 95 pikiKSNYQGNHAK--SLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLvaagkvlylgvsdtpawvvska 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 160 ------H-------QEGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGlltgkyKYEDKDGKQPVGRFFGNSWAETyr 226
Cdd:cd19146 173 nayaraHgltqfvvYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQG------QFRTEEEFKRRGRSGRKGGPQT-- 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 227 nrfwkEHHFEAIALVEKaLQAAYGASApsvTSAALRWMYHHSQLqgahgdaV--ILGMSSLEQLEQNLAA 294
Cdd:cd19146 245 -----EKERKVSEKLEK-VAEEKGTAI---TSVALAYVMHKAPY-------VfpIVGGRKVEHLKGNIEA 298
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
65-294 |
1.02e-11 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 64.78 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 65 ERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANpWDGKS-----LKPDSVRSQLETSLKRLQCPQVDLFY 139
Cdd:cd19141 41 ENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTKIF-WGGKAetergLSRKHIIEGLKASLERLQLEYVDIVF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 140 LHAPDHGTPVEETLHACQRLHQEG--MYNATTR------------------------QVETELF---------PCLRH-F 183
Cdd:cd19141 120 ANRPDPNTPMEEIVRAFTHVINQGmaMYWGTSRwsameimeaysvarqfnlippiveQAEYHLFqrekvemqlPELFHkI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 184 GLRFYAYNPLAGGLLTGKYkyedKDGKQPVGR--FFGNSWaetYRNRFWKEHHFEAIALVeKALQAAYGASAPSVTSAAL 261
Cdd:cd19141 200 GVGAMTWSPLACGILSGKY----DDGVPEYSRasLKGYQW---LKEKILSEEGRRQQAKL-KELQIIADRLGCTLPQLAI 271
|
250 260 270
....*....|....*....|....*....|...
gi 1004393738 262 RWMYHHsqlQGAHGdaVILGMSSLEQLEQNLAA 294
Cdd:cd19141 272 AWCLKN---EGVSS--VLLGASSTEQLYENLQA 299
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-300 |
5.20e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 62.16 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYsdGQSETILGGLGLGLGggdcRVKIATK--ANPWDGKSLKpDSVRSQLETSLKRLQCPQVDLFYLH 141
Cdd:cd19097 36 LKAGINTLDTAPAY--GDSEKVLGKFLKRLD----KFKIITKlpPLKEDKKEDE-AAIEASVEASLKRLKVDSLDGLLLH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 142 APD----HGTPVEETLHACQRlhqEGM--------YNattrqvETELFPCLRHFGL------------RFYAYNPLAG-- 195
Cdd:cd19097 109 NPDdllkHGGKLVEALLELKK---EGLirkigvsvYS------PEELEKALESFKIdiiqlpfnildqRFLKSGLLAKlk 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 196 --------------GLLTgkykyedKDGKQPVGRFfgnswaetyrnRFWKEHH--FEAIAlvekalqAAYGASAPsvtSA 259
Cdd:cd19097 180 kkgieiharsvflqGLLL-------MEPDKLPAKF-----------APAKPLLkkLHELA-------KKLGLSPL---EL 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1004393738 260 ALRWMYHHSqlqgaHGDAVILGMSSLEQLEQNLAATEEGPL 300
Cdd:cd19097 232 ALGFVLSLP-----EIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
64-296 |
6.34e-11 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 62.19 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKA--------NPWDGKS--LKPDSVRSQLETSLKRLQCP 133
Cdd:cd19092 34 LELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKCgirlgddpRPGRIKHydTSKEHILASVEGSLKRLGTD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 134 QVDLFYLHAPDHGTPVEETLHACQRLHQEG----------------MYNA------TTRQVE-----TELFP------CL 180
Cdd:cd19092 114 YLDLLLLHRPDPLMDPEEVAEAFDELVKSGkvryfgvsnftpsqieLLQSyldqplVTNQIElsllhTEAIDdgtldyCQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 181 RHfGLRFYAYNPLAGglltgkykyedkdgkqpvGRFFGNSWAETYRNRfwkehhfeaiALVEKaLQAAYGASApsvTSAA 260
Cdd:cd19092 194 LL-DITPMAWSPLGG------------------GRLFGGFDERFQRLR----------AALEE-LAEEYGVTI---EAIA 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1004393738 261 LRW-MYHHSQLQgahgdaVILGMSSLEQLEQNLAATE 296
Cdd:cd19092 241 LAWlLRHPARIQ------PILGTTNPERIRSAVKALD 271
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-301 |
7.11e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 61.97 E-value: 7.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcrVKIATKANPwDGKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAP 143
Cdd:cd19103 42 MAAGLNLWDTAAVYGMGASEKILGEFLKRYPRED--YIISTKFTP-QIAGQSADPVADMLEGSLARLGTDYIDIYWIHNP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 144 D---HGTP-----VEE-----------TLHACQR----LHQEGM--------YNATTRQVETE--LFPCLRHfGLRFYAY 190
Cdd:cd19103 119 AdveRWTPeliplLKSgkvkhvgvsnhNLAEIKRaneiLAKAGVslsavqnhYSLLYRSSEEAgiLDYCKEN-GITFFAY 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 191 NPLAGGLLTGKYkyedkDGKQPVGRffGNSWAETYrNRFWKEhhFEAIALVEKALQAAYGASAPSVTSAALRwmyhhsql 270
Cdd:cd19103 198 MVLEQGALSGKY-----DTKHPLPE--GSGRAETY-NPLLPQ--LEELTAVMAEIGAKHGASIAQVAIAWAI-------- 259
|
250 260 270
....*....|....*....|....*....|....*...
gi 1004393738 271 qgAHGDAVILGMSSLEQLEQ-------NLAATEEGPLE 301
Cdd:cd19103 260 --AKGTTPIIGVTKPHHVEDaaraasiTLTDDEIKELE 295
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
99-313 |
1.18e-10 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 61.76 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 99 RVKIATKANPWdgkSLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHgtpvEETLH----------ACQRLHQEGM---- 164
Cdd:COG1453 69 KVILATKLPPW---VRDPEDMRKDLEESLKRLQTDYIDLYLIHGLNT----EEDLEkvlkpggaleALEKAKAEGKirhi 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 165 --------------------------YNA--TTRQVETELFPCLRHFGLRFYAYNPLAGGLLTgkykyedkdgkqpvgrf 216
Cdd:COG1453 142 gfsthgslevikeaidtgdfdfvqlqYNYldQDNQAGEEALEAAAEKGIGVIIMKPLKGGRLA----------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 217 fgnswaetyrnrfwkEHHFEAIALVEKALqaaygasapSVTSAALRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAATE 296
Cdd:COG1453 205 ---------------NPPEKLVELLCPPL---------SPAEWALRFLLSHPEV-----TTVLSGMSTPEQLDENLKTAD 255
|
250 260
....*....|....*....|.
gi 1004393738 297 EG-PL---EPAVVDAFNQAWH 313
Cdd:COG1453 256 NLePLteeELAILERLAEELG 276
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
65-299 |
1.57e-10 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 61.21 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 65 ERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANpWDGKS-----LKPDSVRSQLETSLKRLQCPQVDLFY 139
Cdd:cd19159 42 ESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLY-WGGKAetergLSRKHIIEGLKGSLQRLQLEYVDVVF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 140 LHAPDHGTPVEETLHACQRLHQEG--MYNATTR------------------------QVETELF---------PCLRH-F 183
Cdd:cd19159 121 ANRPDSNTPMEEIVRAMTHVINQGmaMYWGTSRwsameimeaysvarqfnmippvceQAEYHLFqrekvevqlPELYHkI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 184 GLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFgnSW------AETYRNRFWKEHHFEAIAlvEKalqaaYGASAPSVt 257
Cdd:cd19159 201 GVGAMTWSPLACGIISGKYGNGVPESSRASLKCY--QWlkerivSEEGRKQQNKLKDLSPIA--ER-----LGCTLPQL- 270
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1004393738 258 saALRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAATEEGP 299
Cdd:cd19159 271 --AVAWC-----LRNEGVSSVLLGSSTPEQLIENLGAIQVLP 305
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
102-294 |
1.81e-10 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 60.93 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 102 IATKA--NPWDGK-----SLKpdSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGM---------- 164
Cdd:cd19150 81 ISTKAgyDMWPGPygewgSRK--YLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKalyvgissys 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 165 ------------------------YNATTRQVE-TELFPCLRHFGLRFYAYNPLAGGLLTGKYKyedkdGKQPVGrffgn 219
Cdd:cd19150 159 pertreaaailrelgtpllihqpsYNMLNRWVEeSGLLDTLQELGVGCIAFTPLAQGLLTDKYL-----NGIPEG----- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 220 swaetyrNRFWKEHHFEAIALVE------KALQAAYGASAPSVTSAALRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLA 293
Cdd:cd19150 229 -------SRASKERSLSPKMLTEanlnsiRALNEIAQKRGQSLAQMALAWV-----LRDGRVTSALIGASRPEQLEENVG 296
|
.
gi 1004393738 294 A 294
Cdd:cd19150 297 A 297
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
41-294 |
2.66e-10 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 60.61 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 41 VLGTMEMG-------RRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcRVKIATK-------- 105
Cdd:cd19147 14 ILGAMSIGdawsgfmGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKNRD-QIVIATKfttdykay 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 106 ------ANPWDGKSLKpdSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQ------------------ 161
Cdd:cd19147 93 evgkgkAVNYCGNHKR--SLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQqgkvlylgvsdtpawvvs 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 162 -----------------EGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGG-LLTGKYKYEDKDGKQPVGRFFGNSwae 223
Cdd:cd19147 171 aanyyatahgktpfsvyQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGkFQSKKAVEERKKNGEGLRSFVGGT--- 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1004393738 224 tyrnrfwkEHHFEAIALVEKALQAAYGASAPSVTSAALRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAA 294
Cdd:cd19147 248 --------EQTPEEVKISEALEKVAEEHGTESVTAIALAYV-----RSKAPNVFPLVGGRKIEHLKDNIEA 305
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
65-299 |
4.41e-10 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 59.71 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 65 ERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANpWDGKS-----LKPDSVRSQLETSLKRLQCPQVDLFY 139
Cdd:cd19158 42 DNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIF-WGGKAetergLSRKHIIEGLKASLERLQLEYVDVVF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 140 LHAPDHGTPVEETLHACQRLHQEG--MYNATTR------------------------QVETELF---------PCLRH-F 183
Cdd:cd19158 121 ANRPDPNTPMEETVRAMTHVINQGmaMYWGTSRwssmeimeaysvarqfnlippiceQAEYHMFqrekvevqlPELFHkI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 184 GLRFYAYNPLAGGLLTGKYkyedKDGKQPVGR--FFGNSWaetYRNRFWKEHHFEAIALVeKALQAAYGASAPSVTSAAL 261
Cdd:cd19158 201 GVGAMTWSPLACGIVSGKY----DSGIPPYSRasLKGYQW---LKDKILSEEGRRQQAKL-KELQAIAERLGCTLPQLAI 272
|
250 260 270
....*....|....*....|....*....|....*...
gi 1004393738 262 RWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAATEEGP 299
Cdd:cd19158 273 AWC-----LRNEGVSSVLLGASNAEQLMENIGAIQVLP 305
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
65-310 |
3.41e-09 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 57.30 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 65 ERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANpWDGKS-----LKPDSVRSQLETSLKRLQCPQVDLFY 139
Cdd:cd19160 44 EHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVTTKIY-WGGQAetergLSRKHIIEGLRGSLDRLQLEYVDIVF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 140 LHAPDHGTPVEETLHACQRLHQEG--MYNATTR------------------------QVETELF---------PCLRH-F 183
Cdd:cd19160 123 ANRSDPNSPMEEIVRAMTYVINQGmaMYWGTSRwsameimeaysvarqfnlippvceQAEYHLFqrekvemqlPELYHkI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 184 GLRFYAYNPLAGGLLTGkyKYEDKDGKQPVGRFFGNSW-AETYRNRFWKEHHFEAIALVEKALQAAYgasapSVTSAALR 262
Cdd:cd19160 203 GVGSVTWSPLACGLITG--KYDGRVPDTCRAAVKGYQWlKEKVQSEEGKKQQAKVKELHPIADRLGC-----TVAQLAIA 275
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1004393738 263 WMyhhsqLQGAHGDAVILGMSSLEQLEQNLAATEE-GPLEPAVVDAFNQ 310
Cdd:cd19160 276 WC-----LRSEGVSSVLLGVSSAEQLIENLGSIQVlSQLTPQTVMEIDA 319
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
64-164 |
6.25e-09 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 56.04 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcrVKIATKANPwdgKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAP 143
Cdd:cd19137 36 IELGYTHIDTAEMYGGGHTEELVGKAIKDFPRED--LFIVTKVWP---TNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP 110
|
90 100
....*....|....*....|.
gi 1004393738 144 DHGTPVEETLHACQRLHQEGM 164
Cdd:cd19137 111 NPNIPLEETLSAMAEGVRQGL 131
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-312 |
8.77e-09 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 55.73 E-value: 8.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATKA--NPWDGKSLKpDSVRSQLETSLKRLQCPQVDLFYLH 141
Cdd:cd19104 42 LDLGINFFDTAPSYGDGKSEENLGRALKGLPA---GPYITTKVrlDPDDLGDIG-GQIERSVEKSLKRLKRDSVDLLQLH 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 142 ---------------APDHGTPVEETLHACQRLHQEGM-----------YNATTRQVETELFPClrhfglrFYAY----N 191
Cdd:cd19104 118 nrigderdkpvggtlSTTDVLGLGGVADAFERLRSEGKirfigitglgnPPAIRELLDSGKFDA-------VQVYynllN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 192 PLAGGLLTGKYKYEDKDG------KQPVG----RFFGNSWAETYRNRFWKEHHFEAIALVE-----KALQAAYGASAPSV 256
Cdd:cd19104 191 PSAAEARPRGWSAQDYGGiidaaaEHGVGvmgiRVLAAGALTTSLDRGREAPPTSDSDVAIdfrraAAFRALAREWGETL 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1004393738 257 TSAALRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAATEEGPLEPAVVDAFNQAW 312
Cdd:cd19104 271 AQLAHRFALSNPGV-----STVLVGVKNREELEEAVAAEAAGPLPAENLARLEALW 321
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
42-294 |
1.19e-08 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 54.93 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 42 LGTMEMGR---RMDAPASAAAVRAFLERGHTELDTAFMYsdGQSETILGGLGLGLGGGDcrVKIATKA-----NPWDGKS 113
Cdd:cd19095 5 LGTSGIGRvwgVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALAGLRRDD--LFIATKVgthgeGGRDRKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 114 LKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGM-----YNATT----RQVETELFPCLRhfg 184
Cdd:cd19095 81 FSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKvryigVSGDGeeleAAIASGVFDVVQ--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 185 LRFYAYNPLAGGLLtgkykyeDKDGKQPVG----RFFGNSWAetyrnrFWKEHHFEAIALVEKALQAAYGASAPSVTSAA 260
Cdd:cd19095 158 LPYNVLDREEEELL-------PLAAEAGLGvivnRPLANGRL------RRRVRRRPLYADYARRPEFAAEIGGATWAQAA 224
|
250 260 270
....*....|....*....|....*....|....
gi 1004393738 261 LRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAA 294
Cdd:cd19095 225 LRFVLSHPGV-----SSAIVGTTNPEHLEENLAA 253
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
63-294 |
3.11e-08 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 54.14 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 63 FLERGHTELDTAFMYsdGQSETIL---GGLGLGLGGGDCRVKIATKANPWDGK-SLKPDSVRSQLETSLKRLQCPQVDLF 138
Cdd:cd19101 32 YVDAGLTTFDCADIY--GPAEELIgefRKRLRRERDAADDVQIHTKWVPDPGElTMTRAYVEAAIDRSLKRLGVDRLDLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 139 YLHAPDHGTP-VEETLHACQRLHQEGMYN--ATT----------------------------RQVETELFP-CLRHfGLR 186
Cdd:cd19101 110 QFHWWDYSDPgYLDAAKHLAELQEEGKIRhlGLTnfdterlreildagvpivsnqvqyslldRRPENGMAAlCEDH-GIK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 187 FYAYNPLAGGLLTGKYKyedkdGKQPVGRFFGNSWAETYRNRFWKEH----HFEAIALVEKALQAAYGASAPSVtsaALR 262
Cdd:cd19101 189 LLAYGTLAGGLLSEKYL-----GVPEPTGPALETRSLQKYKLMIDEWggwdLFQELLRTLKAIADKHGVSIANV---AVR 260
|
250 260 270
....*....|....*....|....*....|..
gi 1004393738 263 WMyhhsqLQGAHGDAVILGMSSLEQLEQNLAA 294
Cdd:cd19101 261 WV-----LDQPGVAGVIVGARNSEHIDDNVRA 287
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
109-294 |
3.87e-08 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 53.78 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 109 WDGKSLKPDS----VRSQLETSLKRLQCPQ-VDLFYLHAPDHGTPVEETLHACQRLHQEGMY--------NATTRQ---- 171
Cdd:cd19077 82 LDPDTLRPDGspeaVRKSIENILRALGGTKkIDIFEPARVDPNVPIEETIKALKELVKEGKIrgiglsevSAETIRraha 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 172 ------VETELFPCLRH------------FGLRFYAYNPLAGGLLTGKYKyedKDGKQPVGRFFGNSwaetyrNRFWKEh 233
Cdd:cd19077 162 vhpiaaVEVEYSLFSREieengvletcaeLGIPIIAYSPLGRGLLTGRIK---SLADIPEGDFRRHL------DRFNGE- 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1004393738 234 HFEA-IALVE--KALQAAYGASAPSVtsaALRWMYHHSqlqgahGDAV--ILGMSSLEQLEQNLAA 294
Cdd:cd19077 232 NFEKnLKLVDalQELAEKKGCTPAQL---ALAWILAQS------GPKIipIPGSTTLERVEENLKA 288
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
64-301 |
1.09e-07 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 52.55 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGggdcRVK--IATKA-----NPWDGKSLKPDSVRSQLETSLKRLQCPQVD 136
Cdd:cd19163 43 LDSGINYIDTAPWYGQGRSETVLGKALKGIP----RDSyyLATKVgryglDPDKMFDFSAERITKSVEESLKRLGLDYID 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 137 LFYLH----APDHGTPVEETLHACQRLHQEG------------------MYNATTRqVETELFPClrHFGL------RFY 188
Cdd:cd19163 119 IIQVHdiefAPSLDQILNETLPALQKLKEEGkvrfigitgypldvlkevLERSPVK-IDTVLSYC--HYTLndtsllELL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 189 AY-----------NPLAGGLLTgkykyedKDGKQPvgrffgnswaetyrnrfWKEHHFEAIALVEKAlqAAYGASAPSVT 257
Cdd:cd19163 196 PFfkekgvgvinaSPLSMGLLT-------ERGPPD-----------------WHPASPEIKEACAKA--AAYCKSRGVDI 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1004393738 258 SA-ALRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAATEEGPLE 301
Cdd:cd19163 250 SKlALQFALSNPDI-----ATTLVGTASPENLRKNLEAAEEPLDA 289
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
64-293 |
4.70e-07 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 50.33 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYsdGQSETILGGLGLGLGGGDcRVKIATKANPWDgksLKPDSVRSQLETSLKRLQCPQVDLFYLHAP 143
Cdd:cd19140 31 LELGYRHIDTAQMY--GNEAQVGEAIAASGVPRD-ELFLTTKVWPDN---YSPDDFLASVEESLRKLRTDYVDLLLLHWP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 144 DHGTPVEETLHACQRLHQEGMY------NATTRQ-------VETELF-------PCL---------RHFGLRFYAYNPLA 194
Cdd:cd19140 105 NKDVPLAETLGALNEAQEAGLArhigvsNFTVALlreavelSEAPLFtnqveyhPYLdqrklldaaREHGIALTAYSPLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 195 gglltgkykyedkdgkqpvgrffgnswaetyRNRFWKEHHFEAIAlvekalqAAYGASAPSVtsaALRWMyhhsqLQGAh 274
Cdd:cd19140 185 -------------------------------RGEVLKDPVLQEIG-------RKHGKTPAQV---ALRWL-----LQQE- 217
|
250
....*....|....*....
gi 1004393738 275 GDAVILGMSSLEQLEQNLA 293
Cdd:cd19140 218 GVAAIPKATNPERLEENLD 236
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-293 |
5.15e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 49.79 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYsdGQSET-----ILgglglglgggDCR--VKIATKANPWDgkslkPDSVRSQLETSLKRLQCPQVD 136
Cdd:cd19100 37 LDLGINYFDTAPSY--GDSEEkigkaLK----------GRRdkVFLATKTGARD-----YEGAKRDLERSLKRLGTDYID 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 137 LFYLHAPDHGTPVEET------LHACQRLHQEGM----------YNATTRQVETELFPCLrHFglrfyAYNplagglltg 200
Cdd:cd19100 100 LYQLHAVDTEEDLDQVfgpggaLEALLEAKEEGKirfigisghsPEVLLRALETGEFDVV-LF-----PIN--------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 201 kykyedkdgkqPVGRFFGNswaetYRNRFWKEHHFEAIA-LVEKALQAAYGASAPSVT-SAALRWMyhhsqLQGAHGDAV 278
Cdd:cd19100 165 -----------PAGDHIDS-----FREELLPLAREKGVGvIAMKVLAGGRLLSGDPLDpEQALRYA-----LSLPPVDVV 223
|
250
....*....|....*
gi 1004393738 279 ILGMSSLEQLEQNLA 293
Cdd:cd19100 224 IVGMDSPEELDENLA 238
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-143 |
7.26e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 50.01 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDGQSE-----TILGGLGLGLGGGDcRVKIATKA-----------NPW------------------ 109
Cdd:cd19099 31 LDSGINVIDTAINYRGGRSErligkALRELIEKGGIKRD-EVVIVTKAgyipgdgdeplRPLkyleeklgrglidvadsa 109
|
90 100 110
....*....|....*....|....*....|....*
gi 1004393738 110 -DGKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAP 143
Cdd:cd19099 110 gLRHCISPAYLEDQIERSLKRLGLDTIDLYLLHNP 144
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
64-163 |
2.49e-06 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 48.26 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYsdGQSETILGGLGLGLGGGDCR---VKIATKANPWDgksLKPDSVRSQLETSLKRLQCPQVDLFYL 140
Cdd:cd19111 27 LFVGYRHIDTALSY--QNEKAIGEALKWWLKNGKLKreeVFITTKLPPVY---LEFKDTEKSLEKSLENLKLPYVDLYLI 101
|
90 100 110
....*....|....*....|....*....|....*.
gi 1004393738 141 HAP-------------DHGTPVEETLHACQRLHQEG 163
Cdd:cd19111 102 HHPcgfvnkkdkgereLASSDVTSVWRAMEALVSEG 137
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
102-294 |
2.95e-06 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 47.86 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 102 IATKANPWDgksLKPDSVRSQLETSLKRLQCPQVDLFYLHAP------DHGTPVEETLHACQRLHQEG------------ 163
Cdd:cd19071 59 ITTKLWPTD---HGYERVREALEESLKDLGLDYLDLYLIHWPvpgkegGSKEARLETWRALEELVDEGlvrsigvsnfnv 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 164 -----MYNATTR-----QVET-------EL--FpCLRHfGLRFYAYNPLAGGlltgkykyedkdgkqpvgrffgnswaet 224
Cdd:cd19071 136 ehleeLLAAARIkpavnQIELhpylqqkELveF-CKEH-GIVVQAYSPLGRG---------------------------- 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 225 yRNRFWKEHHFEAIAlvekalqAAYGASAPSVtsaALRWmyhhsQLQgaHGDAVILGMSSLEQLEQNLAA 294
Cdd:cd19071 186 -RRPLLDDPVLKEIA-------KKYGKTPAQV---LLRW-----ALQ--RGVVVIPKSSNPERIKENLDV 237
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
113-294 |
5.86e-06 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 46.96 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 113 SLKPDSVRSQLETSLKRLQCPQVDLFYLH--APDHGTPVEETLHACQRLHQEGMY-----------------------NA 167
Cdd:cd19139 67 NLSKDKLLPSLEESLEKLRTDYVDLTLIHwpSPNDEVPVEEYIGALAEAKEQGLTrhigvsnftialldeaiavvgagAI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 168 TTRQVetELFP----------CLRHfGLRFYAYNPLAGGlltgkykyedKDGKQPVgrffgnswaetyrnrfwkehhFEA 237
Cdd:cd19139 147 ATNQI--ELSPylqnrklvahCKQH-GIHVTSYMTLAYG----------KVLDDPV---------------------LAA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1004393738 238 IAlvekalqAAYGASAPSVtsaALRWMYHhsqlqgaHGDAVILGMSSLEQLEQNLAA 294
Cdd:cd19139 193 IA-------ERHGATPAQI---ALAWAMA-------RGYAVIPSSTKREHLRSNLLA 232
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
42-292 |
2.16e-05 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 45.62 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 42 LGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMY-------SDGQSETILGGLGLGLGGGDcRVKIATK-ANPWDG-- 111
Cdd:PRK10625 18 LGTMTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYpvpprpeTQGLTETYIGNWLAKRGSRE-KLIIASKvSGPSRNnd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 112 KSLKPD------SVRSQLETSLKRLQCPQVDLFYLHAPDHGT--------------PVE---ETLHA---CQR------- 158
Cdd:PRK10625 97 KGIRPNqaldrkNIREALHDSLKRLQTDYLDLYQVHWPQRPTncfgklgyswtdsaPAVsllETLDAlaeQQRagkiryi 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 159 -------------LHQ------------EGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYkyedKDGKQPV 213
Cdd:PRK10625 177 gvsnetafgvmryLHLaekhdlprivtiQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGTLTGKY----LNGAKPA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 214 G-------RFfgnswaetyrNRFWKEHHFEAIAlVEKALQAAYGASAPSVTSAALRwmyhhsqlQGAHGDAVILGMSSLE 286
Cdd:PRK10625 253 GarntlfsRF----------TRYSGEQTQKAVA-AYVDIAKRHGLDPAQMALAFVR--------RQPFVASTLLGATTME 313
|
....*.
gi 1004393738 287 QLEQNL 292
Cdd:PRK10625 314 QLKTNI 319
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
117-294 |
1.76e-04 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 42.73 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 117 DSVRSQLETSLKRLQCPQVDLFYLHAPDHG--TPVEETLHACQRLHQEGM------------------------------ 164
Cdd:cd19162 93 DGIRRSIEASLERLGLDRLDLVFLHDPDRHllQALTDAFPALEELRAEGVvgaigvgvtdwaallraarradvdvvmvag 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 165 -YNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGkykyedkdGKQPVGRFFGNSWAETYRNRfwkehhfeAIALVEK 243
Cdd:cd19162 173 rYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILAT--------DDPAGDRYDYRPATPEVLAR--------ARRLAAV 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1004393738 244 AlqAAYGASAPsvtSAALRWMYHHSQLQgahgdAVILGMSSLEQLEQNLAA 294
Cdd:cd19162 237 C--RRYGVPLP---AAALQFPLRHPAVA-----SVVVGAASPAELRDNLAL 277
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
117-163 |
9.67e-04 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 40.05 E-value: 9.67e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1004393738 117 DSVRSQLETSLKRLQCPQVDLFYLH--APDHGTPVeETLHACQRLHQEG 163
Cdd:cd19131 80 DSTLRAFDESLRKLGLDYVDLYLIHwpVPAQDKYV-ETWKALIELKKEG 127
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
64-143 |
1.20e-03 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 40.09 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYsdgQSETILGGLGLGLGGGDcRVK-----IATKANPwdgKSLKPDSVRSQLETSLKRLQCPQVDLF 138
Cdd:cd19154 35 LKAGYRLIDTAFLY---QNEEAIGEALAELLEEG-VVKredlfITTKLWT---HEHAPEDVEEALRESLKKLQLEYVDLY 107
|
....*
gi 1004393738 139 YLHAP 143
Cdd:cd19154 108 LIHAP 112
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
102-294 |
1.93e-03 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 39.37 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 102 IATKANpWDGKS----LKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEG--MYNATTR--QVE 173
Cdd:cd19142 79 VSTKIY-WSYGSeergLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGliMYWGTSRwsPVE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 174 -TELFPCLRHF-------------------------------GLRFYAYNPLAGGLLTGK--------YKYEDKDGKQPV 213
Cdd:cd19142 158 iMEAFSIARQFncptpiceqseyhmfcrekmelympelynkvGVGLITWSPLSLGLDPGIseetrrlvTKLSFKSSKYKV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 214 GRFFGNSWAETYRNrfwKEHHFEAIALVEKalqaaYGAsapSVTSAALRWmyhhsQLQGAHGDAVILGMSSLEQLEQNLA 293
Cdd:cd19142 238 GSDGNGIHEETRRA---SHKLRELSLIAER-----LGC---DLTQLLIAW-----SLKNENVQCVLIGASSLEQLYSQLN 301
|
.
gi 1004393738 294 A 294
Cdd:cd19142 302 S 302
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
113-143 |
2.74e-03 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 38.75 E-value: 2.74e-03
10 20 30
....*....|....*....|....*....|.
gi 1004393738 113 SLKPDSVRSQLETSLKRLQCPQVDLFYLHAP 143
Cdd:cd19108 84 FHRPELVRPALEKSLKKLQLDYVDLYLIHFP 114
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
117-294 |
3.19e-03 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 38.74 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 117 DSVRSQLETSLKRLQCPQVDLFYLHAPD---HGTPVEETLHA------------------------------CQRLHQE- 162
Cdd:cd19152 103 DGILRSIEDSLQRLGLSRIDLLSIHDPDedlAGAESDEHFAQaikgafraleelreegvikaiglgvndwevILRILEEa 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 163 --------GMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPvgrffgNSWAETYRNRFW---K 231
Cdd:cd19152 183 dldwvmlaGRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAGGDNFDYYEYGPA------PPELIARRDRIEalcE 256
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1004393738 232 EHHfeaIALVEKALQAAYgasAPSVTSaalrwmyhhsqlqgahgdAVILGMSSLEQLEQNLAA 294
Cdd:cd19152 257 QHG---VSLAAAALQFAL---APPAVA------------------SVAPGASSPERVEENVAL 295
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
64-164 |
4.03e-03 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 38.37 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004393738 64 LERGHTELDTAFMYSDgQSETILGGLGLGLGGGDcrVKIATKANPwdgkslKPDSVRSQLETSLKRLQCPQVDLFYLHAP 143
Cdd:cd19120 35 LKAGFRHIDTAEMYGN-EKEVGEALKESGVPRED--LFITTKVSP------GIKDPREALRKSLAKLGVDYVDLYLIHSP 105
|
90 100
....*....|....*....|....*
gi 1004393738 144 ----DHGTPVEETLHACQRLHQEGM 164
Cdd:cd19120 106 ffakEGGPTLAEAWAELEALKDAGL 130
|
|
| |
