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Conserved domains on  [gi|402855306|ref|XP_003892271|]
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PREDICTED: glutamate--cysteine ligase regulatory subunit [Papio anubis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Aldo_ket_red super family cl00470
Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief ...
117-256 1.34e-07

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 to 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.


The actual alignment was detected with superfamily member COG0656:

Pssm-ID: 320990  Cd Length: 280  Bit Score: 51.49  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855306 117 LGVAQLDSVIIASPPIEDGVNLsLEHlqpyWEELENLVQSKKIVAIGTSDLDKTQLEQLYQWAQVKPNSNQVNLASCCvM 196
Cdd:COG0656   98 LGLDYVDLYLIHWPVPNKYVVI-EET----WKALEELVDEGLIRAIGVSNFGVEHLEELLSLAKVKPAVNQIEYHPYL-R 171
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402855306 197 PPDLTAFAKQFDIQLLTHNDPkellseASFQEALQESIPDIQAHE----WVPL---WLLR--YSVIVKS 256
Cdd:COG0656  172 QPELLPFCQRHGIAVEAYSPL------AKGGKLLDNPVLAEIAKKygktPAQValrWHIQrgVIVIPKS 234
 
Name Accession Description Interval E-value
ARA1 COG0656
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ...
117-256 1.34e-07

Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 223729  Cd Length: 280  Bit Score: 51.49  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855306 117 LGVAQLDSVIIASPPIEDGVNLsLEHlqpyWEELENLVQSKKIVAIGTSDLDKTQLEQLYQWAQVKPNSNQVNLASCCvM 196
Cdd:COG0656   98 LGLDYVDLYLIHWPVPNKYVVI-EET----WKALEELVDEGLIRAIGVSNFGVEHLEELLSLAKVKPAVNQIEYHPYL-R 171
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402855306 197 PPDLTAFAKQFDIQLLTHNDPkellseASFQEALQESIPDIQAHE----WVPL---WLLR--YSVIVKS 256
Cdd:COG0656  172 QPELLPFCQRHGIAVEAYSPL------AKGGKLLDNPVLAEIAKKygktPAQValrWHIQrgVIVIPKS 234
Aldo_ket_red cd06660
Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief ...
86-212 2.62e-05

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 to 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: 119408  Cd Length: 285  Bit Score: 44.47  E-value: 2.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855306  86 REEMKVSAKLFIVGSNSSSST----RSAVDMACSVLGVAQLDSVIIASPPIEDgvnlslEHLQPYWEELENLVQSKKIVA 161
Cdd:cd06660   71 REEVFIATKVGPRPGDGRDLSpehiRRAVEESLKRLGTDYIDLYLLHWPDPDT------PDIEETLRALEELVKEGKIRA 144
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 402855306 162 IGTSDLDKTQLEQLYQWAQVKPNSNQV--NLAsCCVMPPDLTAFAKQFDIQLL 212
Cdd:cd06660  145 IGVSNFSAEQLEEALAAAGVPPAVNQVeyNLL-DRQAEEELLPYCREHGIGVI 196
Aldo_ket_red pfam00248
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ...
83-262 2.75e-03

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: 278668  Cd Length: 290  Bit Score: 38.45  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855306   83 PDEREEMKVSAKL-FIVGSNSSSSTRSAVDMACSV----LGVAQLDSVIIASP----PIEDGvnlslehlqpyWEELENL 153
Cdd:pfam00248  58 PVKRDKVVIATKVpDGDGPWPSGGSKENIRKSIEEslkrLGTDYIDLLQLHWPdpstPIEET-----------LDALEEL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855306  154 VQSKKIVAIGTSDLDKTQLEQLYQWAQVKPNSNQVNLASCCVMPP-DLTAFAKQFDIQLLTHndpkELLSEASFQEALQE 232
Cdd:pfam00248 127 VKEGKIRAIGVSNFSAEQIEKALKKGKIPIVAVQVEYSLLRRREEeGLLEYCKKLGIPLIAY----SPLGGGLLTGKYTS 202
                         170       180       190
                  ....*....|....*....|....*....|
gi 402855306  233 SiPDIQAHEWVPLWLLRYSVIVKSRGIIKS 262
Cdd:pfam00248 203 D-ADKGDGDRRRLLKRGTPLNLLLLEELEE 231
 
Name Accession Description Interval E-value
ARA1 COG0656
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ...
117-256 1.34e-07

Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 223729  Cd Length: 280  Bit Score: 51.49  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855306 117 LGVAQLDSVIIASPPIEDGVNLsLEHlqpyWEELENLVQSKKIVAIGTSDLDKTQLEQLYQWAQVKPNSNQVNLASCCvM 196
Cdd:COG0656   98 LGLDYVDLYLIHWPVPNKYVVI-EET----WKALEELVDEGLIRAIGVSNFGVEHLEELLSLAKVKPAVNQIEYHPYL-R 171
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 402855306 197 PPDLTAFAKQFDIQLLTHNDPkellseASFQEALQESIPDIQAHE----WVPL---WLLR--YSVIVKS 256
Cdd:COG0656  172 QPELLPFCQRHGIAVEAYSPL------AKGGKLLDNPVLAEIAKKygktPAQValrWHIQrgVIVIPKS 234
Aldo_ket_red cd06660
Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief ...
86-212 2.62e-05

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 to 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: 119408  Cd Length: 285  Bit Score: 44.47  E-value: 2.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855306  86 REEMKVSAKLFIVGSNSSSST----RSAVDMACSVLGVAQLDSVIIASPPIEDgvnlslEHLQPYWEELENLVQSKKIVA 161
Cdd:cd06660   71 REEVFIATKVGPRPGDGRDLSpehiRRAVEESLKRLGTDYIDLYLLHWPDPDT------PDIEETLRALEELVKEGKIRA 144
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 402855306 162 IGTSDLDKTQLEQLYQWAQVKPNSNQV--NLAsCCVMPPDLTAFAKQFDIQLL 212
Cdd:cd06660  145 IGVSNFSAEQLEEALAAAGVPPAVNQVeyNLL-DRQAEEELLPYCREHGIGVI 196
Aldo_ket_red pfam00248
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ...
83-262 2.75e-03

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: 278668  Cd Length: 290  Bit Score: 38.45  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855306   83 PDEREEMKVSAKL-FIVGSNSSSSTRSAVDMACSV----LGVAQLDSVIIASP----PIEDGvnlslehlqpyWEELENL 153
Cdd:pfam00248  58 PVKRDKVVIATKVpDGDGPWPSGGSKENIRKSIEEslkrLGTDYIDLLQLHWPdpstPIEET-----------LDALEEL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402855306  154 VQSKKIVAIGTSDLDKTQLEQLYQWAQVKPNSNQVNLASCCVMPP-DLTAFAKQFDIQLLTHndpkELLSEASFQEALQE 232
Cdd:pfam00248 127 VKEGKIRAIGVSNFSAEQIEKALKKGKIPIVAVQVEYSLLRRREEeGLLEYCKKLGIPLIAY----SPLGGGLLTGKYTS 202
                         170       180       190
                  ....*....|....*....|....*....|
gi 402855306  233 SiPDIQAHEWVPLWLLRYSVIVKSRGIIKS 262
Cdd:pfam00248 203 D-ADKGDGDRRRLLKRGTPLNLLLLEELEE 231
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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