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Conserved domains on  [gi|7303935|gb|AAF58979|]
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alicorn, isoform A [Drosophila melanogaster]

Protein Classification

E_set_AMPKbeta_like_N and AMPKBI domain-containing protein (domain architecture ID 11244030)

E_set_AMPKbeta_like_N and AMPKBI domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AMPKBI smart01010
5'-AMP-activated protein kinase beta subunit, interation domain; This region is found in the ...
254-341 5.65e-42

5'-AMP-activated protein kinase beta subunit, interation domain; This region is found in the beta subunit of the 5'-AMP-activated protein kinase complex, and its yeast homologues Sip1, Sip2 and Gal83, which are found in the SNF1 kinase complex. This region is sufficient for interaction of this subunit with the kinase complex, but is not solely responsible for the interaction, and the interaction partner is not known. The isoamylase N-terminal domain is sometimes found in proteins belonging to this family.


:

Pssm-ID: 214973  Cd Length: 100  Bit Score: 141.30  E-value: 5.65e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7303935     254 AEKEYSQEVPQV---------KPWEKVSGPPVLPPHLLQVILNK-DTPLSCEPTLLPEPNHVMLNHLYALSIKDGVMVLS 323
Cdd:smart01010   3 PPESYTNEIPACftdddfieeSPEEKWKEPPALPPHLEKVILNTsSTATREDPSLLPIPNHVVLNHLYTSSIKDGVLAVA 82
                           90
                   ....*....|....*...
gi 7303935     324 ATHRYRKKYVTTLLYKPI 341
Cdd:smart01010  83 ATTRYRGKYVTQVLYKPL 100
AMPK1_CBM pfam16561
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in ...
156-233 2.42e-37

Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in close association with AMPKBI pfam04739. The surface of AMPK1_CBM reveals a carbohydrate-binding pocket.


:

Pssm-ID: 339778 [Multi-domain]  Cd Length: 80  Bit Score: 128.37  E-value: 2.42e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7303935    156 PTVLRWDGGGKNVTISGTFSDWKPM-AMVRSHQNFVTIIDLPEGDHQYKFCVDGEWKHDPKLKSVENAEGQRNNLVSVR 233
Cdd:pfam16561   2 PTVIRWRGGGKKVYVTGSFDNWKKKiPLQRSGGDFSTILDLPPGTHQYKFIVDGEWRHDPDLPTATDDMGNLNNYIEVK 80
 
Name Accession Description Interval E-value
AMPKBI smart01010
5'-AMP-activated protein kinase beta subunit, interation domain; This region is found in the ...
254-341 5.65e-42

5'-AMP-activated protein kinase beta subunit, interation domain; This region is found in the beta subunit of the 5'-AMP-activated protein kinase complex, and its yeast homologues Sip1, Sip2 and Gal83, which are found in the SNF1 kinase complex. This region is sufficient for interaction of this subunit with the kinase complex, but is not solely responsible for the interaction, and the interaction partner is not known. The isoamylase N-terminal domain is sometimes found in proteins belonging to this family.


Pssm-ID: 214973  Cd Length: 100  Bit Score: 141.30  E-value: 5.65e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7303935     254 AEKEYSQEVPQV---------KPWEKVSGPPVLPPHLLQVILNK-DTPLSCEPTLLPEPNHVMLNHLYALSIKDGVMVLS 323
Cdd:smart01010   3 PPESYTNEIPACftdddfieeSPEEKWKEPPALPPHLEKVILNTsSTATREDPSLLPIPNHVVLNHLYTSSIKDGVLAVA 82
                           90
                   ....*....|....*...
gi 7303935     324 ATHRYRKKYVTTLLYKPI 341
Cdd:smart01010  83 ATTRYRGKYVTQVLYKPL 100
AMPKBI pfam04739
5'-AMP-activated protein kinase beta subunit, interaction domain; This region is found in the ...
274-339 8.02e-38

5'-AMP-activated protein kinase beta subunit, interaction domain; This region is found in the beta subunit of the 5'-AMP-activated protein kinase complex, and its yeast homologs Sip1, Sip2 and Gal83, which are found in the SNF1 kinase complex. This region is sufficient for interaction of this subunit with the kinase complex, but is not solely responsible for the interaction, and the interaction partner is not known. The isoamylase N-terminal domain (pfam02922) is sometimes found in proteins belonging to this family.


Pssm-ID: 309744  Cd Length: 69  Bit Score: 129.20  E-value: 8.02e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7303935    274 PPVLPPHLLQVILNKDTPLSCEPTLLPEPNHVMLNHLYALSIKDGVMVLSATHRYRKKYVTTLLYK 339
Cdd:pfam04739   4 PPALPPHLLLTILNKPPSSSDDPSVLPRPNHVVLNHLYTSSIKDGVLALGTTTRYRSKYVTTVLYK 69
AMPK1_CBM pfam16561
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in ...
156-233 2.42e-37

Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in close association with AMPKBI pfam04739. The surface of AMPK1_CBM reveals a carbohydrate-binding pocket.


Pssm-ID: 339778 [Multi-domain]  Cd Length: 80  Bit Score: 128.37  E-value: 2.42e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7303935    156 PTVLRWDGGGKNVTISGTFSDWKPM-AMVRSHQNFVTIIDLPEGDHQYKFCVDGEWKHDPKLKSVENAEGQRNNLVSVR 233
Cdd:pfam16561   2 PTVIRWRGGGKKVYVTGSFDNWKKKiPLQRSGGDFSTILDLPPGTHQYKFIVDGEWRHDPDLPTATDDMGNLNNYIEVK 80
E_set_AMPKbeta_like_N cd02859
N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain ...
156-232 1.90e-27

N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain of AMP-activated protein kinase beta subunit; E or "early" set domains are associated with the catalytic domain of AMP-activated protein kinase beta subunit glycogen binding domain at the N-terminal end. AMPK is a metabolic stress sensing protein that senses AMP/ATP and has recently been found to act as a glycogen sensor as well. The protein functions as an alpha-beta-gamma heterotrimer. This N-terminal domain is the glycogen binding domain of the beta subunit. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, and isoamylase.


Pssm-ID: 199889 [Multi-domain]  Cd Length: 80  Bit Score: 102.68  E-value: 1.90e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7303935  156 PTVLRWDG-GGKNVTISGTFSDWK-PMAMVRSHQN-FVTIIDLPEGDHQYKFCVDGEWKHDPKLKSVENAEGQRNNLVSV 232
Cdd:cd02859   1 PVTFRWPGpGGKEVYVTGSFDNWQqPIPLEKSGDGeFSATVELPPGRYEYKFIVDGEWVHDPDLPTVTDEFGNLNNVLEV 80
 
Name Accession Description Interval E-value
AMPKBI smart01010
5'-AMP-activated protein kinase beta subunit, interation domain; This region is found in the ...
254-341 5.65e-42

5'-AMP-activated protein kinase beta subunit, interation domain; This region is found in the beta subunit of the 5'-AMP-activated protein kinase complex, and its yeast homologues Sip1, Sip2 and Gal83, which are found in the SNF1 kinase complex. This region is sufficient for interaction of this subunit with the kinase complex, but is not solely responsible for the interaction, and the interaction partner is not known. The isoamylase N-terminal domain is sometimes found in proteins belonging to this family.


Pssm-ID: 214973  Cd Length: 100  Bit Score: 141.30  E-value: 5.65e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7303935     254 AEKEYSQEVPQV---------KPWEKVSGPPVLPPHLLQVILNK-DTPLSCEPTLLPEPNHVMLNHLYALSIKDGVMVLS 323
Cdd:smart01010   3 PPESYTNEIPACftdddfieeSPEEKWKEPPALPPHLEKVILNTsSTATREDPSLLPIPNHVVLNHLYTSSIKDGVLAVA 82
                           90
                   ....*....|....*...
gi 7303935     324 ATHRYRKKYVTTLLYKPI 341
Cdd:smart01010  83 ATTRYRGKYVTQVLYKPL 100
AMPKBI pfam04739
5'-AMP-activated protein kinase beta subunit, interaction domain; This region is found in the ...
274-339 8.02e-38

5'-AMP-activated protein kinase beta subunit, interaction domain; This region is found in the beta subunit of the 5'-AMP-activated protein kinase complex, and its yeast homologs Sip1, Sip2 and Gal83, which are found in the SNF1 kinase complex. This region is sufficient for interaction of this subunit with the kinase complex, but is not solely responsible for the interaction, and the interaction partner is not known. The isoamylase N-terminal domain (pfam02922) is sometimes found in proteins belonging to this family.


Pssm-ID: 309744  Cd Length: 69  Bit Score: 129.20  E-value: 8.02e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7303935    274 PPVLPPHLLQVILNKDTPLSCEPTLLPEPNHVMLNHLYALSIKDGVMVLSATHRYRKKYVTTLLYK 339
Cdd:pfam04739   4 PPALPPHLLLTILNKPPSSSDDPSVLPRPNHVVLNHLYTSSIKDGVLALGTTTRYRSKYVTTVLYK 69
AMPK1_CBM pfam16561
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in ...
156-233 2.42e-37

Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in close association with AMPKBI pfam04739. The surface of AMPK1_CBM reveals a carbohydrate-binding pocket.


Pssm-ID: 339778 [Multi-domain]  Cd Length: 80  Bit Score: 128.37  E-value: 2.42e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7303935    156 PTVLRWDGGGKNVTISGTFSDWKPM-AMVRSHQNFVTIIDLPEGDHQYKFCVDGEWKHDPKLKSVENAEGQRNNLVSVR 233
Cdd:pfam16561   2 PTVIRWRGGGKKVYVTGSFDNWKKKiPLQRSGGDFSTILDLPPGTHQYKFIVDGEWRHDPDLPTATDDMGNLNNYIEVK 80
E_set_AMPKbeta_like_N cd02859
N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain ...
156-232 1.90e-27

N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain of AMP-activated protein kinase beta subunit; E or "early" set domains are associated with the catalytic domain of AMP-activated protein kinase beta subunit glycogen binding domain at the N-terminal end. AMPK is a metabolic stress sensing protein that senses AMP/ATP and has recently been found to act as a glycogen sensor as well. The protein functions as an alpha-beta-gamma heterotrimer. This N-terminal domain is the glycogen binding domain of the beta subunit. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, and isoamylase.


Pssm-ID: 199889 [Multi-domain]  Cd Length: 80  Bit Score: 102.68  E-value: 1.90e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7303935  156 PTVLRWDG-GGKNVTISGTFSDWK-PMAMVRSHQN-FVTIIDLPEGDHQYKFCVDGEWKHDPKLKSVENAEGQRNNLVSV 232
Cdd:cd02859   1 PVTFRWPGpGGKEVYVTGSFDNWQqPIPLEKSGDGeFSATVELPPGRYEYKFIVDGEWVHDPDLPTVTDEFGNLNNVLEV 80
E_set_Isoamylase_like_N cd07184
N-terminal Early set domain associated with the catalytic domain of isoamylase-like (also ...
162-232 4.80e-06

N-terminal Early set domain associated with the catalytic domain of isoamylase-like (also called glycogen 6-glucanohydrolase) proteins; E or "early" set domains are associated with the catalytic domain of isoamylase-like proteins at the N-terminal end. Isoamylase is one of the starch-debranching enzymes that catalyze the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen. Isoamylase contains a bound calcium ion, but this is not in the same position as the conserved calcium ion that has been reported in other alpha-amylase family enzymes. The N-terminal domain of isoamylase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, and the beta subunit of AMP-activated protein kinase.


Pssm-ID: 199892 [Multi-domain]  Cd Length: 86  Bit Score: 44.15  E-value: 4.80e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7303935  162 DGGGKNVTISGTFSDWKPMA--MVRSHQN-FVTIIDLPEG-DHQYKFCVDGE-WKHDPKLKSVENAEGQRNN-LVSV 232
Cdd:cd07184  10 EQGADSVSLVGDFNDWDPQAtpMKKLKNGtFSATLDLPAGrEYQFRYLIDGErWVNDPEADAYAPNGFGEENsVVSV 86
E_set cd02688
Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the ...
156-214 4.57e-05

Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the N or C terminus; The E or "early" set domains of sugar utilizing enzymes are associated with different types of catalytic domains at either the N-terminal or C-terminal end. These domains may be related to the immunoglobulin and/or fibronectin type III superfamilies. Members of this family include alpha amylase, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. A subset of these members were recently identified as members of the CBM48 (Carbohydrate Binding Module 48) family. Members of the CBM48 family include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, isoamylase, and the beta subunit of AMP-activated protein kinase.


Pssm-ID: 199878 [Multi-domain]  Cd Length: 82  Bit Score: 40.99  E-value: 4.57e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7303935  156 PTVLRWDG-GGKNVTISGTFSDWK---PMAMVRSHQN-FVTIIDLPEGDHQYKFCVDGEWKHDP 214
Cdd:cd02688   1 GVTFRIFApGAKSVYLIGSFNGWWqaqALPMTKNGGGvWSATIPLPLGTYEYKYVIDGGKNVLP 64
E_set_GBE_prok_N cd02855
N-terminal Early set domain associated with the catalytic domain of prokaryotic glycogen ...
166-214 1.80e-04

N-terminal Early set domain associated with the catalytic domain of prokaryotic glycogen branching enzyme; This subfamily is composed of predominantly prokaryotic 1,4 alpha glucan branching enzymes, also called glycogen branching enzymes. E or "early" set domains are associated with the catalytic domain of glycogen branching enzymes at the N-terminal end. Glycogen branching enzyme catalyzes the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage, yielding a non-reducing end oligosaccharide chain, as well as the subsequent attachment of short glucosyl chains to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. The N-terminal domain of the 1,4 alpha glucan branching enzyme may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199885 [Multi-domain]  Cd Length: 105  Bit Score: 40.17  E-value: 1.80e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7303935  166 KNVTISGTFSDWKPMA--MVRSHQN---FVTIIDLPEGDHqYKFCV---DGEW--KHDP 214
Cdd:cd02855  31 KRVSVVGDFNDWDGRAhpMRRIGDSgvwELFIPGAKEGDL-YKYEIetaDGEVllKADP 88
X25_BaPul_like cd12962
X25 domain of Bacillus acidopullulyticus pullulanase and similar proteins; Pullulanase (EC 3.2. ...
168-210 2.81e-03

X25 domain of Bacillus acidopullulyticus pullulanase and similar proteins; Pullulanase (EC 3.2.1.41) cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. BaPul is used industrially in the production of high fructose corn syrup, high maltose content syrups and low calorie and ''light'' beers. Pullulanases, in addition to the catalytic domain, include several carbohydrate-binding domains (CBMs) as well as domains of unknown function (termed ''X'' modules). X25 was identified in Bacillus acidopullulyticus pullulanase, and splits another domain of unknown function (X45). X25 is present in multiple copy in some pullulanases. It has been suggested that X25 and X45 are CBMs which target mixed alpha-1,6/alpha-1,4 linked D-glucan polysaccharides.


Pssm-ID: 240568 [Multi-domain]  Cd Length: 95  Bit Score: 36.45  E-value: 2.81e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7303935  168 VTISGTF-------SDWKP------MAMVRSHQNFVTIIDLPEGDHQYKFCVDGEW 210
Cdd:cd12962   2 VTLVGSFqselgcaGDWDPdclatqLTDDGNDGVYTFTTTLPAGDYEYKVALNGSW 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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