Subunit B of Class III Extradiol ring-cleavage dioxygenases; Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site of the aromatic ring. Intradiol enzymes cleave the aromatic ring between two hydroxyl groups, whereas extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon. Extradiol dioxygenases can be further divided into three classes. Class I and II enzymes are evolutionary related and show sequence similarity, with the two-domain class II enzymes evolving from the class I enzyme through gene duplication. Class III enzymes are different in sequence and structure and usually have two subunits, designated A and B. This model represents the catalytic subunit B of extradiol dioxygenase class III enzymes. Enzymes belonging to this family include Protocatechuate 4,5-dioxygenase (LigAB), 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase (CarB), 4,5-DOPA Dioxygenase, 2,3-dihydroxyphenylpropionate 1,2-dioxygenase, and 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase (HPCD). There are also some family members that do not show the typical dioxygenase activity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686661118 114 YRSIEHLDKMGMSIIEQLDPVSFSNYLKKYHNTICGRHPIGVLLNAITELQkngmNMSFSFLNYAQSSQCRNWQDSSVSY 193
Cdd:cd07361  186 RESAERLDRKAIEAILALDPEGFYEYLRETGNTACGRGPIAVLLEAAKELG----ALKAELLDYATSGDVSGDRDSVVGY 261

                 ....*
gi 686661118 194 AAGAL 198
Cdd:cd07361  262 ASAAF 266

Memo (mediator of ErbB2-driven cell motility) is co-precipitated with the C terminus of ErbB2, a protein involved in cell motility; This subfamily is composed of Memo (mediator of ErbB2-driven cell motility) and similar proteins. Memo is a protein that is co-precipitated with the C terminus of ErbB2, a protein involved in cell motility. It is required for the ErbB2-driven cell mobility and is found in protein complexes with cofilin, ErbB2 and PLCgamma1. However, Memo is not homologous to any known signaling proteins, and its function in ErbB2 signaling is not known. Structural studies show that Memo binds directly to a specific ErbB2-derived phosphopeptide. Memo is homologous to class III nonheme iron-dependent extradiol dioxygenases, however, no metal binding or enzymatic activity can be detected for Memo. This subfamily also contains a few members containing a C-terminal AMMECR1-like domain. The AMMECR1 protein was proposed to be a regulatory factor that is potentially involved in the development of AMME contiguous gene deletion syndrome.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686661118 114 YRSIEHLDKMGMSIIEQLDPVSFSNYLKKYHNTICGRHPIGVLLNAITELQkngmNMSFSFLNYAQSSQCRNWQDSSVSY 193
Cdd:cd07361  186 RESAERLDRKAIEAILALDPEGFYEYLRETGNTACGRGPIAVLLEAAKELG----ALKAELLDYATSGDVSGDRDSVVGY 261

                 ....*
gi 686661118 194 AAGAL 198
Cdd:cd07361  262 ASAAF 266

AmmeMemoRadiSam system protein B; Members of this protein family belong to the same domain family as the mammalian protein Memo (Mediator of ErbB2-driven cell MOtility). Members of the present family occur as part of a three gene system with an uncharacterized radical SAM enzyme and a homolog of the mammalian protein AMMECR1, a mammalian protein named for AMME - Alport syndrome, Mental Retardation, Midface hypoplasia, and Elliptocytosis. Memo in humans has protein-protein interaction activity with binding of phosphorylated Try, but members of this family may be active as enzymes, as suggested by homology to a class of nonheme iron dioxygenases.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 686661118  120 LDKMGMSIIEQLDPVSFSNYLKKYHNTICGRHPIGVLLNAITELQkngmNMSFSFLNYAQSSQCRNWQDSSVSYAAGAL 198
Cdd:TIGR04336 195 LDRAAIEAILALDPEGLYDVVREKNISMCGAGPIAALLEAAKRLG----ALKAELLDYATSGDVSGDRSRVVGYASIVF 269

Memo (mediator of ErbB2-driven cell motility) is co-precipitated with the C terminus of ErbB2, a protein involved in cell motility; This subfamily is composed of Memo (mediator of ErbB2-driven cell motility) and similar proteins. Memo is a protein that is co-precipitated with the C terminus of ErbB2, a protein involved in cell motility. It is required for the ErbB2-driven cell mobility and is found in protein complexes with cofilin, ErbB2 and PLCgamma1. However, Memo is not homologous to any known signaling proteins, and its function in ErbB2 signaling is not known. Structural studies show that Memo binds directly to a specific ErbB2-derived phosphopeptide. Memo is homologous to class III nonheme iron-dependent extradiol dioxygenases, however, no metal binding or enzymatic activity can be detected for Memo. This subfamily also contains a few members containing a C-terminal AMMECR1-like domain. The AMMECR1 protein was proposed to be a regulatory factor that is potentially involved in the development of AMME contiguous gene deletion syndrome.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686661118 114 YRSIEHLDKMGMSIIEQLDPVSFSNYLKKYHNTICGRHPIGVLLNAITELQkngmNMSFSFLNYAQSSQCRNWQDSSVSY 193
Cdd:cd07361  186 RESAERLDRKAIEAILALDPEGFYEYLRETGNTACGRGPIAVLLEAAKELG----ALKAELLDYATSGDVSGDRDSVVGY 261

                 ....*
gi 686661118 194 AAGAL 198
Cdd:cd07361  262 ASAAF 266

Memo-like protein; This family contains members from all branches of life. The molecular function of this protein is unknown, but Memo (mediator of ErbB2-driven cell motility) a human protein is included in this family. It has been suggested that Memo controls cell migration by relaying extracellular chemotactic signals to the microtubule cytoskeleton.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686661118  103 YSYYDESQG---EIYRSIEhlDKMGMSIIEQLDPVSFSNYLKKYHNTICGRHPIGVLLNAITELQKNgmnmSFSFLNYAQ 179
Cdd:pfam01875 180 FSHYGRRFGlphEIAESIR--DRIGIKAIEELNEEAFYEYLSGTNNTICGYGPIAVILEALKKLGAK----KGKLLDYAT 253

                          90
                  ....*....|....*..
gi 686661118  180 SSQCRNWQDSSVSYAAG 196
Cdd:pfam01875 254 SGDVTGDTDSVVGYAGA 270