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Conserved domains on  [gi|17539802|ref|NP_501926|]
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Insulin-like domain-containing protein [Caenorhabditis elegans]

Protein Classification

insulin family protein( domain architecture ID 10137877)

insulin family protein may play a variety of roles in controlling processes such as growth, differentiation, and reproduction

PubMed:  11445250|1322139

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IlGF_insulin_bombyxin_like cd04366
IlGF_like family, insulin_bombyxin_like subgroup. Members include a number of peptides ...
 34-103 5.91e-08

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.


:

Pssm-ID: 239832  Cd Length: 42  Bit Score: 45.31  E-value: 5.91e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539802  34 LCGSRLTTTLLAVCRNQLCTgltafkrsadqsyapttrdlfhihhqqkRGGIATECCEKRCSFAYLKTFC 103
Cdd:cd04366   1 YCGRHLADTLALLCSEYNSP----------------------------RRGIVDECCRKSCTLDELLSYC 42
 
Name Accession Description Interval E-value
IlGF_insulin_bombyxin_like cd04366
IlGF_like family, insulin_bombyxin_like subgroup. Members include a number of peptides ...
 34-103 5.91e-08

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.


Pssm-ID: 239832  Cd Length: 42  Bit Score: 45.31  E-value: 5.91e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539802  34 LCGSRLTTTLLAVCRNQLCTgltafkrsadqsyapttrdlfhihhqqkRGGIATECCEKRCSFAYLKTFC 103
Cdd:cd04366   1 YCGRHLADTLALLCSEYNSP----------------------------RRGIVDECCRKSCTLDELLSYC 42
Ins_beta pfam03488
Nematode insulin-related peptide beta type;
32-104 7.74e-03

Nematode insulin-related peptide beta type;


Pssm-ID: 112313  Cd Length: 48  Bit Score: 31.98  E-value: 7.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539802    32 IRLCGSRLTTTLLAVCrNQLCTgltafkrsadqsyapttrdlfhihhQQKRGGIATECCEKRCSFAYLKTFCC 104
Cdd:pfam03488   1 QRACGRRLFKRVFALC-GEACN-------------------------PQNDVDIATKCCTKQCTDDDIKSACC 47
 
Name Accession Description Interval E-value
IlGF_insulin_bombyxin_like cd04366
IlGF_like family, insulin_bombyxin_like subgroup. Members include a number of peptides ...
 34-103 5.91e-08

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.


Pssm-ID: 239832  Cd Length: 42  Bit Score: 45.31  E-value: 5.91e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539802  34 LCGSRLTTTLLAVCRNQLCTgltafkrsadqsyapttrdlfhihhqqkRGGIATECCEKRCSFAYLKTFC 103
Cdd:cd04366   1 YCGRHLADTLALLCSEYNSP----------------------------RRGIVDECCRKSCTLDELLSYC 42
Ins_beta pfam03488
Nematode insulin-related peptide beta type;
32-104 7.74e-03

Nematode insulin-related peptide beta type;


Pssm-ID: 112313  Cd Length: 48  Bit Score: 31.98  E-value: 7.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539802    32 IRLCGSRLTTTLLAVCrNQLCTgltafkrsadqsyapttrdlfhihhQQKRGGIATECCEKRCSFAYLKTFCC 104
Cdd:pfam03488   1 QRACGRRLFKRVFALC-GEACN-------------------------PQNDVDIATKCCTKQCTDDDIKSACC 47
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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