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Conserved domains on  [gi|1039734066|ref|XP_006514097|]
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protein GUCD1 isoform X1 [Mus musculus]

Protein Classification

Guanylate_cyc_2 domain-containing protein( domain architecture ID 10561103)

Guanylate_cyc_2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Guanylate_cyc_2 pfam09778
Guanylylate cyclase; Members of this family of proteins catalyze the conversion of guanosine ...
 1-196 4.51e-112

Guanylylate cyclase; Members of this family of proteins catalyze the conversion of guanosine triphosphate (GTP) to 3',5'-cyclic guanosine monophosphate (cGMP) and pyrophosphate.


:

Pssm-ID: 462894  Cd Length: 212  Bit Score: 318.43  E-value: 4.51e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039734066   1 MVLRYLGQLDDG--EFENALQELQLTRSIWTIDLAYLMRHFGVRHRFCTQTLGVDKGYKNQSFYRKHFDTEETRVNQLFA 78
Cdd:pfam09778  19 MVLRTLGQRSCFlkNFEEICKEEGFTTSIWTIDLAYLLKRFGVRHRFYTQTLGVNPNYKNQSFYKKTFDKDEKRVNKLFA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039734066  79 QAKACKVQVEKCTVSVQDIQVHLAQGHVAIVLVNSGVLHCDLCSSPvKYCCFtpsGHRCFCRTPDYQGHFIVLRGYNRAT 158
Cdd:pfam09778  99 KAKACGIDVEKRSVSMQEIVEHLASGGPAIVLVNASLLHCDLCKSN-KYSCF---GRRCLGRKPGYQGHYVVLCGYDAAT 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1039734066 159 GCIFYNNPAYADRMCSTSISNFEEARTSYGTDEDILFV 196
Cdd:pfam09778 175 DKFLYRNPASSDRVCRISFDALEEARKSFGTDEDIIFI 212
 
Name Accession Description Interval E-value
Guanylate_cyc_2 pfam09778
Guanylylate cyclase; Members of this family of proteins catalyze the conversion of guanosine ...
 1-196 4.51e-112

Guanylylate cyclase; Members of this family of proteins catalyze the conversion of guanosine triphosphate (GTP) to 3',5'-cyclic guanosine monophosphate (cGMP) and pyrophosphate.


Pssm-ID: 462894  Cd Length: 212  Bit Score: 318.43  E-value: 4.51e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039734066   1 MVLRYLGQLDDG--EFENALQELQLTRSIWTIDLAYLMRHFGVRHRFCTQTLGVDKGYKNQSFYRKHFDTEETRVNQLFA 78
Cdd:pfam09778  19 MVLRTLGQRSCFlkNFEEICKEEGFTTSIWTIDLAYLLKRFGVRHRFYTQTLGVNPNYKNQSFYKKTFDKDEKRVNKLFA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039734066  79 QAKACKVQVEKCTVSVQDIQVHLAQGHVAIVLVNSGVLHCDLCSSPvKYCCFtpsGHRCFCRTPDYQGHFIVLRGYNRAT 158
Cdd:pfam09778  99 KAKACGIDVEKRSVSMQEIVEHLASGGPAIVLVNASLLHCDLCKSN-KYSCF---GRRCLGRKPGYQGHYVVLCGYDAAT 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1039734066 159 GCIFYNNPAYADRMCSTSISNFEEARTSYGTDEDILFV 196
Cdd:pfam09778 175 DKFLYRNPASSDRVCRISFDALEEARKSFGTDEDIIFI 212
Peptidase_C39A cd02549
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 142-185 6.43e-03

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures.


Pssm-ID: 239109 [Multi-domain]  Cd Length: 141  Bit Score: 35.46  E-value: 6.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1039734066 142 PDYQGHFIVLRGYNRAtGCIFYNNPaYADRMCSTSISNFEEART 185
Cdd:cd02549    90 ITPSGHAMVVIGYDRK-GNVYVNDP-GGGRRLVVSFDEFEKAWK 131
 
Name Accession Description Interval E-value
Guanylate_cyc_2 pfam09778
Guanylylate cyclase; Members of this family of proteins catalyze the conversion of guanosine ...
 1-196 4.51e-112

Guanylylate cyclase; Members of this family of proteins catalyze the conversion of guanosine triphosphate (GTP) to 3',5'-cyclic guanosine monophosphate (cGMP) and pyrophosphate.


Pssm-ID: 462894  Cd Length: 212  Bit Score: 318.43  E-value: 4.51e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039734066   1 MVLRYLGQLDDG--EFENALQELQLTRSIWTIDLAYLMRHFGVRHRFCTQTLGVDKGYKNQSFYRKHFDTEETRVNQLFA 78
Cdd:pfam09778  19 MVLRTLGQRSCFlkNFEEICKEEGFTTSIWTIDLAYLLKRFGVRHRFYTQTLGVNPNYKNQSFYKKTFDKDEKRVNKLFA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039734066  79 QAKACKVQVEKCTVSVQDIQVHLAQGHVAIVLVNSGVLHCDLCSSPvKYCCFtpsGHRCFCRTPDYQGHFIVLRGYNRAT 158
Cdd:pfam09778  99 KAKACGIDVEKRSVSMQEIVEHLASGGPAIVLVNASLLHCDLCKSN-KYSCF---GRRCLGRKPGYQGHYVVLCGYDAAT 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1039734066 159 GCIFYNNPAYADRMCSTSISNFEEARTSYGTDEDILFV 196
Cdd:pfam09778 175 DKFLYRNPASSDRVCRISFDALEEARKSFGTDEDIIFI 212
Peptidase_C39A cd02549
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 142-185 6.43e-03

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures.


Pssm-ID: 239109 [Multi-domain]  Cd Length: 141  Bit Score: 35.46  E-value: 6.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1039734066 142 PDYQGHFIVLRGYNRAtGCIFYNNPaYADRMCSTSISNFEEART 185
Cdd:cd02549    90 ITPSGHAMVVIGYDRK-GNVYVNDP-GGGRRLVVSFDEFEKAWK 131
 
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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