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Conserved domains on  [gi|110738420|dbj|BAF01136|]
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hypothetical protein [Arabidopsis thaliana]

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 ...
 59-263 1.60e-103

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: 299.94  E-value: 1.60e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110738420   59 VPHVHQLASWDCGLACVLMVLRASGIASCTLEDLAEICS----TNSIWTVDLAYLLQKFCVEFSYYTITFGANPNYSIEE 134
Cdd:pfam09778   1 VPHIQQRYNWDCGLACVLMVLRTLGQRSCFLKNFEEICKeegfTTSIWTIDLAYLLKRFGVRHRFYTQTLGVNPNYKNQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110738420  135 FYKEQLPEDLVRVDLLFRKAHESGIIIQCRSVSIHEISCLLLSGNyIAIALVDQDKLS----KSWLEEVLVSGLHSSNSC 210
Cdd:pfam09778  81 FYKKTFDKDEKRVNKLFAKAKACGIDVEKRSVSMQEIVEHLASGG-PAIVLVNASLLHcdlcKSNKYSCFGRRCLGRKPG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110738420  211 YTGHYVVICGYDAVRDEFEIRDPASSKIHERISSKCLENARKSFGTDEDLLLI 263
Cdd:pfam09778 160 YQGHYVVLCGYDAATDKFLYRNPASSDRVCRISFDALEEARKSFGTDEDIIFI 212
 
Name Accession Description Interval E-value
Guanylate_cyc_2 pfam09778
Guanylylate cyclase; Members of this family of proteins catalyze the conversion of guanosine ...
 59-263 1.60e-103

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: 299.94  E-value: 1.60e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110738420   59 VPHVHQLASWDCGLACVLMVLRASGIASCTLEDLAEICS----TNSIWTVDLAYLLQKFCVEFSYYTITFGANPNYSIEE 134
Cdd:pfam09778   1 VPHIQQRYNWDCGLACVLMVLRTLGQRSCFLKNFEEICKeegfTTSIWTIDLAYLLKRFGVRHRFYTQTLGVNPNYKNQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110738420  135 FYKEQLPEDLVRVDLLFRKAHESGIIIQCRSVSIHEISCLLLSGNyIAIALVDQDKLS----KSWLEEVLVSGLHSSNSC 210
Cdd:pfam09778  81 FYKKTFDKDEKRVNKLFAKAKACGIDVEKRSVSMQEIVEHLASGG-PAIVLVNASLLHcdlcKSNKYSCFGRRCLGRKPG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110738420  211 YTGHYVVICGYDAVRDEFEIRDPASSKIHERISSKCLENARKSFGTDEDLLLI 263
Cdd:pfam09778 160 YQGHYVVLCGYDAATDKFLYRNPASSDRVCRISFDALEEARKSFGTDEDIIFI 212
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 57-98 1.14e-04

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 43.28  E-value: 1.14e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 110738420  57 MDVPHVHQLASWDCGLACVLMVLRASGIAsCTLEDLAEICST 98
Cdd:COG2274    2 RKVPFVLQMEAADCGLACLAMIARYYGRP-VSLEELREALGV 42
 
Name Accession Description Interval E-value
Guanylate_cyc_2 pfam09778
Guanylylate cyclase; Members of this family of proteins catalyze the conversion of guanosine ...
 59-263 1.60e-103

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: 299.94  E-value: 1.60e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110738420   59 VPHVHQLASWDCGLACVLMVLRASGIASCTLEDLAEICS----TNSIWTVDLAYLLQKFCVEFSYYTITFGANPNYSIEE 134
Cdd:pfam09778   1 VPHIQQRYNWDCGLACVLMVLRTLGQRSCFLKNFEEICKeegfTTSIWTIDLAYLLKRFGVRHRFYTQTLGVNPNYKNQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110738420  135 FYKEQLPEDLVRVDLLFRKAHESGIIIQCRSVSIHEISCLLLSGNyIAIALVDQDKLS----KSWLEEVLVSGLHSSNSC 210
Cdd:pfam09778  81 FYKKTFDKDEKRVNKLFAKAKACGIDVEKRSVSMQEIVEHLASGG-PAIVLVNASLLHcdlcKSNKYSCFGRRCLGRKPG 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110738420  211 YTGHYVVICGYDAVRDEFEIRDPASSKIHERISSKCLENARKSFGTDEDLLLI 263
Cdd:pfam09778 160 YQGHYVVLCGYDAATDKFLYRNPASSDRVCRISFDALEEARKSFGTDEDIIFI 212
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 57-98 1.14e-04

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 43.28  E-value: 1.14e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 110738420  57 MDVPHVHQLASWDCGLACVLMVLRASGIAsCTLEDLAEICST 98
Cdd:COG2274    2 RKVPFVLQMEAADCGLACLAMIARYYGRP-VSLEELREALGV 42
Peptidase_C39 pfam03412
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ...
 58-98 2.21e-04

Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as precursor peptides containing N-terminal extensions (leader peptides) which are cleaved off during maturation. Most non-lantibiotics and also some lantibiotics have leader peptides of the so-called double-glycine type. These leader peptides share consensus sequences and also a common processing site with two conserved glycine residues in positions -1 and -2. The double- glycine-type leader peptides are unrelated to the N-terminal signal sequences which direct proteins across the cytoplasmic membrane via the sec pathway. Their processing sites are also different from typical signal peptidase cleavage sites, suggesting that a different processing enzyme is involved. Peptide bacteriocins are exported across the cytoplasmic membrane by a dedicated ATP-binding cassette (ABC) transporter. The ABC transporter is the maturation protease and its proteolytic domain resides in the N-terminal part of the protein. This peptidase domain is found in a wide range of ABC transporters, however the presumed catalytic cysteine and histidine are not conserved in all members of this family.


Pssm-ID: 367483 [Multi-domain]  Cd Length: 133  Bit Score: 40.29  E-value: 2.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 110738420   58 DVPHVHQLASWDCGLACVLMVLRASGIAsCTLEDLAEICST 98
Cdd:pfam03412   1 KYKIVLQVDENDCGLACLAMILKYYGSN-VSLEELRELAGT 40
 
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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