Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 58865806   186 NLLIHERTHTDERPYTCDICHKAFRR 211
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865806  18 LTNYSFLQAVNTFPAAVDHLQGL---YGLSA-----VQTMHMNHWTLGYPNVHEITRSTITEMAAAQGLVDARFPFPALP 89
Cdd:cd05643   8 ISRYHRVQGSRGYVKAAEEVKELleeLGLEAklisdIYDGGERILTPQSPISWELIEGELNETLPILYAIIGKETPPEIA 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 58865806  90 FATHLFHPKQGA------------IAHVLPALHKDRPRFDFANLAVA 124
Cdd:cd05643  88 FVAHLCHPKPGAndnasgsallleVARVLAKLILNRPKRGICFLWVP 134

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 58865806   186 NLLIHERTHTDERPYTCDICHKAFRR 211
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                          10        20
                  ....*....|....*....|...
gi 58865806   172 FICKFCGRHFTKSYNLLIHERTH 194
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 58865806   186 NLLIHERTHTDERPYTCDICHKAFRR 211
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

hypothetical protein

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 58865806  164 LPSKTKKEFICKFCGRHFTKSYNLLIHER--THTDerpyTCDICHKAFRRQDHLRDH 218
Cdd:PHA00733  66 LTSKAVSPYVCPLCLMPFSSSVSLKQHIRytEHSK----VCPVCGKEFRNTDSTLDH 118

M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They typically have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This protein subfamily conserves some of the metal-coordinating residues of the typically co-catalytic M28 family which might suggest binding of a single metal ion.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865806  18 LTNYSFLQAVNTFPAAVDHLQGL---YGLSA-----VQTMHMNHWTLGYPNVHEITRSTITEMAAAQGLVDARFPFPALP 89
Cdd:cd05643   8 ISRYHRVQGSRGYVKAAEEVKELleeLGLEAklisdIYDGGERILTPQSPISWELIEGELNETLPILYAIIGKETPPEIA 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 58865806  90 FATHLFHPKQGA------------IAHVLPALHKDRPRFDFANLAVA 124
Cdd:cd05643  88 FVAHLCHPKPGAndnasgsallleVARVLAKLILNRPKRGICFLWVP 134