Glutaredoxin;

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 122937349  139 VVIYTTclrvvrTTFERCELVRKIFQNHRVKFEEKNIALNGEYGKELdercRRVSEAPSLPVVFIDGHY 207
Cdd:pfam00462   1 VVLYTK------PTCPFCKRAKRLLKSLGVDFEEIDVDEDPEIREEL----KELSGWPTVPQVFIDGEH 59

Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to plants. Multiple isoforms are found in A. thaliana and O.sativa.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937349  139 VVIYTT---CLrvvrttferCELVRKIFQNHRVKFEEKNIAlNGEYGKELDERCRRVSEAPSLPVVFIDGHYLGGAEKIL 215
Cdd:TIGR02189  10 VVIFSRsscCM---------CHVVKRLLLTLGVNPAVHEID-KEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVM 79

                          90
                  ....*....|....
gi 122937349  216 SMNESGELQDILTK 229
Cdd:TIGR02189  80 ALHISGSLVPMLKQ 93

Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937349 138 RVVIYTTclrvvrTTFERCELVRKIFQNHRVKFEEKNIALNGEYGKELdercRRVSEAPSLPVVFIDGHYLGGAEKILSM 217
Cdd:cd02066    1 KVVVFSK------STCPYCKRAKRLLESLGIEFEEIDILEDGELREEL----KELSGWPTVPQIFINGEFIGGYDDLKAL 70

                 ..
gi 122937349 218 NE 219
Cdd:cd02066   71 HE 72

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 122937349 138 RVVIYTT--ClrvvrttfERCELVRKIFQNHRVKFEEKNIALNGEYGKELdercRRVSEAPSLPVVFIDGHYLGG 210
Cdd:COG0695    1 KVTLYTTpgC--------PYCARAKRLLDEKGIPYEEIDVDEDPEAREEL----RERSGRRTVPVIFIGGEHLGG 63

Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 122937349 180 EYGKELDERCRRVSEAPSLPVVFIDGHYLGGAEKILSMNESGELQDI 226
Cdd:cd03419   36 EDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLVKL 82

Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a recently-identified subfamily composed of SH3BGR and similar proteins possessing significant sequence similarity to GRX, but without a redox active CXXC motif. The SH3BGR gene was cloned in an effort to identify genes mapping to chromosome 21, which could be involved in the pathogenesis of congenital heart disease affecting Down syndrome newborns. Several human SH3BGR-like (SH3BGRL) genes have been identified since, mapping to different locations in the chromosome. Of these, SH3BGRL3 was identified as a tumor necrosis factor (TNF) alpha inhibitory protein and was also named TIP-B1. Upregulation of expression of SH3BGRL3 is associated with differentiation. It has been suggested that it functions as a regulator of differentiation-related signal transduction pathways.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 122937349 167 RVKFEEKNIALNGEYGKELDERCRRVSEAPSLPVVFIDGHYLGGAEKILSMNESGELQDIL 227
Cdd:cd03030   30 KIEFEEVDISMNEENRQWMRENVPNENGKPLPPQIFNGDEYCGDYEAFFEAKENNTLEEFL 90

NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 122937349 138 RVVIYTTclrvvrTTFERCELVRKIFQNHRVKFEEKNIALNGEYGKELdercRRVSEAPSLPVVFIDGHYLGG 210
Cdd:cd02976    1 EVTVYTK------PDCPYCKATKRFLDERGIPFEEVDVDEDPEALEEL----KKLNGYRSVPVVVIGDEHLSG 63