IlGF, insulin_like growth factors; specific to vertebrates. Members include a number of peptides including insulin-like growth factors I and II, which play a variety of roles in controlling processes such as growth, differentiation, and reproduction. On a cellular level they affect cell cycle, apoptosis, cell migration, proliferation, and differentiation. Typically, the active forms of these peptide hormones are single chains cross-linked by three disulfide bonds.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189083846  84 PSETLCGGELVDTLQFVCGDRGFYFSRPASR---VSRRSRGIVEECCFRSCDLALLETYCATPAKSE 147
Cdd:cd04368    1 GPETLCGGELVDTLQFVCGDRGFYFSKPTGYgssRRRPNRGIVEECCFRSCDLRLLEMYCAKPKKSE 67

nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189083846   4 PDPQIIVVAPETELASMQVQRT--EDG---VTIIQIFWVGRKGELlrrTPVSS 51
Cdd:cd02164   88 PDLEAIVVSPETYPGALKINRKreENGlspLEIVVVPLVKADEDG---EKISS 137

IlGF, insulin_like growth factors; specific to vertebrates. Members include a number of peptides including insulin-like growth factors I and II, which play a variety of roles in controlling processes such as growth, differentiation, and reproduction. On a cellular level they affect cell cycle, apoptosis, cell migration, proliferation, and differentiation. Typically, the active forms of these peptide hormones are single chains cross-linked by three disulfide bonds.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189083846  84 PSETLCGGELVDTLQFVCGDRGFYFSRPASR---VSRRSRGIVEECCFRSCDLALLETYCATPAKSE 147
Cdd:cd04368    1 GPETLCGGELVDTLQFVCGDRGFYFSKPTGYgssRRRPNRGIVEECCFRSCDLRLLEMYCAKPKKSE 67

Insulin / insulin-like growth factor / relaxin family; Family of proteins including insulin, relaxin, and IGFs. Insulin decreases blood glucose concentration.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189083846    86 ETLCGGELVDTLQFVCGDRGFYFSRPASR-----------VSRRSRGIVEECCFRSCDLALLETYC 140
Cdd:smart00078   1 QHLCGRHLVRALYLVCGERGFFYSPKSRRyapygqvppleERRGKRGIVEQCCHRGCSLYDLESYC 66

phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; The PPAT domain of the bifunctional enzyme with PPAT and DPCK functions. The final two steps of the CoA biosynthesis pathway are catalyzed by phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA (dPCoA) kinase (DPCK). The PPAT reaction involves the reversible adenylation of 4'-phosphopantetheine to form 3'-dPCoA and PPi, and DPCK catalyses phosphorylation of the 3'-hydroxy group of the ribose moiety of dPCoA. In eukaryotes the two enzymes are part of a large multienzyme complex . Studies in Corynebacterium ammoniagenes suggested that separate enzymes were present, and this was confirmed through identification of the bacterial PPAT/CoAD.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189083846   4 PDPQIIVVAPETELASMQVQRT--EDG---VTIIQIFWVGRKGELlrrTPVSS 51
Cdd:cd02164   88 PDLEAIVVSPETYPGALKINRKreENGlspLEIVVVPLVKADEDG---EKISS 137

IlGF, insulin_like growth factors; specific to vertebrates. Members include a number of peptides including insulin-like growth factors I and II, which play a variety of roles in controlling processes such as growth, differentiation, and reproduction. On a cellular level they affect cell cycle, apoptosis, cell migration, proliferation, and differentiation. Typically, the active forms of these peptide hormones are single chains cross-linked by three disulfide bonds.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189083846  84 PSETLCGGELVDTLQFVCGDRGFYFSRPASR---VSRRSRGIVEECCFRSCDLALLETYCATPAKSE 147
Cdd:cd04368    1 GPETLCGGELVDTLQFVCGDRGFYFSKPTGYgssRRRPNRGIVEECCFRSCDLRLLEMYCAKPKKSE 67

Insulin / insulin-like growth factor / relaxin family; Family of proteins including insulin, relaxin, and IGFs. Insulin decreases blood glucose concentration.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189083846    86 ETLCGGELVDTLQFVCGDRGFYFSRPASR-----------VSRRSRGIVEECCFRSCDLALLETYC 140
Cdd:smart00078   1 QHLCGRHLVRALYLVCGERGFFYSPKSRRyapygqvppleERRGKRGIVEQCCHRGCSLYDLESYC 66

Insulin/IGF/Relaxin family; Superfamily includes insulins; relaxins; insulin-like growth factor; and bombyxin. All are secreted regulatory hormones. Disulfide rich, all-alpha fold. Alignment includes B chain, linker (which is processed out of the final product), and A chain.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189083846   86 ETLCGGELVDTLQFVCGDRGFYFSR----------------------PASRVSRRSRGIVEECCFRSCDLALLETYC 140
Cdd:pfam00049   1 QHLCGRHLVRALYLVCGDRGFFYAPkpredpqveqlpdgegaelkylGADEHSRRKRGIVEECCHRPCTLDQLESYC 77

IlGF_like family, insulin_bombyxin_like subgroup. Members include a number of peptides including insulin, insulin-like growth factors I and II, insect prothoracicotropic hormone (bombyxin), locust insulin-related peptide (LIRP), molluscan insulin-related peptides 1 to 5 (MIP), and C. elegans insulin-like peptides. With the exception of insulin-like growth factors, the active forms of these peptide hormones are composed of two chains (A and B) linked by two disulfide bonds; the arrangement of four cysteines is conserved in the "A" chain: Cys1 is linked by a disulfide bond to Cys3, Cys2 and Cys4 are linked by interchain disulfide bonds to cysteines in the "B" chain. This alignment contains both chains, plus the intervening linker region, arranged as found in the propeptide form. Propeptides are cleaved to yield two separate chains linked covalently by the two disulfide bonds.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189083846  88 LCGGELVDTLQFVCGDRGFyfsrpasrvsrRSRGIVEECCFRSCDLALLETYC 140
Cdd:cd04366    1 YCGRHLADTLALLCSEYNS-----------PRRGIVDECCRKSCTLDELLSYC 42

phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; The PPAT domain of the bifunctional enzyme with PPAT and DPCK functions. The final two steps of the CoA biosynthesis pathway are catalyzed by phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA (dPCoA) kinase (DPCK). The PPAT reaction involves the reversible adenylation of 4'-phosphopantetheine to form 3'-dPCoA and PPi, and DPCK catalyses phosphorylation of the 3'-hydroxy group of the ribose moiety of dPCoA. In eukaryotes the two enzymes are part of a large multienzyme complex . Studies in Corynebacterium ammoniagenes suggested that separate enzymes were present, and this was confirmed through identification of the bacterial PPAT/CoAD.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189083846   4 PDPQIIVVAPETELASMQVQRT--EDG---VTIIQIFWVGRKGELlrrTPVSS 51
Cdd:cd02164   88 PDLEAIVVSPETYPGALKINRKreENGlspLEIVVVPLVKADEDG---EKISS 137