1G7O


Conserved Protein Domain Family
Glutaredoxin2_C

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pfam04399: Glutaredoxin2_C 
Glutaredoxin 2, C terminal domain
Glutaredoxins are a multifunctional family of glutathione-dependent disulphide oxidoreductases. Unlike other glutaredoxins, glutaredoxin 2 (Grx2) cannot reduce ribonucleotide reductase. Grx2 has significantly higher catalytic activity in the reduction of mixed disulphides with glutathione (GSH) compared with other glutaredoxins. The active site residues (Cys9-Pro10-Tyr11-Cys12, in Escherichia coli Grx2), which are found at the interface between the N- and C-terminal domains are identical to other glutaredoxins, but there is no other similarity between glutaredoxin 2 and other glutaredoxins. Grx2 is structurally similar to glutathione-S-transferases (GST), but there is no obvious sequence similarity. The inter-domain contacts are mainly hydrophobic, suggesting that the two domains are unlikely to be stable on their own. Both domains are needed for correct folding and activity of Grx2. It is thought that the primary function of Grx2 is to catalyze reversible glutathionylation of proteins with GSH in cellular redox regulation including the response to oxidative stress.
Statistics
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PSSM-Id: 398207
Aligned: 37 rows
Threshold Bit Score: 117.294
Threshold Setting Gi: 503768295
Created: 20-May-2020
Updated: 7-Aug-2020
Structure
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Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
1G7O_A          85 AIEEWLRKVNGYANKLLLPRFAKSAFDE--FSTPAARKYFVDKKEASAG-NFADLLAHSD-GLIKNISDDLRALDKLIVK 160
WP_014205145    86 NIAEWQRQIAPFNGPLVHPRWMMIELPE--FQLPEAKAWYTKNKSAMIGmSFDDAYAKSA-EFLAPMNALLAQLDWLVLP 162 Vibrio furnissii
WP_022562015    86 KISGWLGQSFEFSGPLLYPRWLMIELPE--YGSEDAKAWFTKNKSAMIGmSFEEAYANTD-EYLAKMNAHLEQLEWLTLP 162 Vibrio nigrip...
Q5NH24          85 fvkgciTDLEPHYRRIIYPRIPHHPRNEcdFPTQSAKEYFINKKSQYIG-DFDALLRNPPyDSIRAINQILAKIDPFI-K 162 Francisella t...
WP_012601055    84 qatlfQSRAFPLTQQIGRPRWWNLDLAE--YRSAGAKEAWRVSKETEGF-NFEELLEKTP-QYVQLINPLLKDAELLLEL 159 Vibrio tasman...
Q87J67          84 pVLDWQKQAFLPLQKVGYPRWSNMTLPE--FATETAKQAWREKKETEAL-NFEALINDTP-AIAKEVAALIEQTKPLLNL 159 Vibrio paraha...
Q7MBY7          84 SVLDWQRSAFLPLQKIGYPRWSNMDLPE--FATQSARQAWRMKKETDAL-NFDALLQDTP-NIATEVEALIERAKSVLNL 159 Vibrio vulnif...
Q9KKV8          84 ATLDWQRSAFLPLQKIGYPRWSNMNLPE--FKTASAQQAWRVKKETTEL-HFESLLKDTS-QIALQVQACIDAVKPLLKL 159 Vibrio cholerae
Q6D1S0          85 EIEAWCKSVSNAVFNLAVPRFTKADFKE--LSTPEARHAYILREEKAFG-DLDGLIAKTP-ELIAEVEQKLEALESRLA- 159 Pectobacteriu...
jgi:Fraau_0867  85 AIEAWVKSVWRITIRLAVPRFVEGDFPE--LATTEAREAFRAREIRAFG-DLDALIEQSP-EWIADINHQLQALEALLAA 160 Frateuria aur...
1G7O_A         161 PNAVNG-ELSEDDIQLFPLLRNLTLVAG-INWPSRVADYRDNMAKQTQINLLSSMA 214
WP_014205145   163 SERGH--TLSYDDVNMYPTLRNLTVVKG-IEFPARVRQYIDEVTALTHIPLYDDVA 215 Vibrio furnissii
WP_022562015   163 SERGN--AISYDDVNLYPHLRNLTVVKG-IQFPTHVRQYIDEVTKLTKIRLFDAVA 215 Vibrio nigripulchritudo
Q5NH24         163 TPFINSeKFSWDDINIFPIFFILTMSKDlLEIPTNITNYIKNIEAKTNIELY---- 214 Francisella tularensis subsp. tularensis
WP_012601055   160 ENGESSlPL-IDQALYFSMLRGFCVEPS-IEWPPALEHWLEKQSKTLSIMLLr--- 210 Vibrio tasmaniensis
Q87J67         160 SSEKQT-SL-VDQAIMFSILRGFFSAPE-VQWDPAVLHWMATARKATNVPVLi--- 209 Vibrio parahaemolyticus
Q7MBY7         160 DSYQHA-TL-VDEAIVFSILRGFFSAAE-IQWDSVVKDWMESVSDKTHVPLLk--- 209 Vibrio vulnificus YJ016
Q9KKV8         160 HSYQHV-AL-IDEAIIFSILRGFFSAPE-IQWDSEVRDWMVSVSQKTQVRLLQEPl 212 Vibrio cholerae
Q6D1S0         160 ----NInAISTTDFILFPILLSLTIVKG-LQFGPNVHAYLERVSTASKVALLTDKA 210 Pectobacterium atrosepticum
jgi:Fraau_0867 161 HKGLNL-----ADFSLFPVLRSLTIVEG-VKFGPLAQAYAEHFSAKTGVALLDpa- 209 Frateuria aurantia DSM 6220
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