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Conserved domains on  [gi|5832839|emb|CAB55074|]
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AMP-Activated Kinase Beta subunit [Caenorhabditis elegans]

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 ...
190-274 1.33e-40

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: 135.53  E-value: 1.33e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5832839     190 SFTQEIPSM---------DMLRKAAGPPVIPPQLMQVLLNK-ETPESCDPNVLPEPNHVMLNHMYALSIKDSVMVLSSTQ 259
Cdd:smart01010   6 SYTNEIPACftdddfieeSPEEKWKEPPALPPHLEKVILNTsSTATREDPSLLPIPNHVVLNHLYTSSIKDGVLAVAATT 85
                           90
                   ....*....|....*
gi 5832839     260 RYRKKFVTTLLYKPV 274
Cdd:smart01010  86 RYRGKYVTQVLYKPL 100
AMPK1_CBM pfam16561
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in ...
62-144 2.55e-32

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: 113.73  E-value: 2.55e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5832839     62 PVVFRWSftQNAqpRVVHIVGSWDNWQTRIPMVKSTNDFSTIIDLQPGQYEYKFQVDGSWVVDDNQGKAQDVHGNENNMI 141
Cdd:pfam16561   2 PTVIRWR--GGG--KKVYVTGSFDNWKKKIPLQRSGGDFSTILDLPPGTHQYKFIVDGEWRHDPDLPTATDDMGNLNNYI 77

                  ...
gi 5832839    142 NIQ 144
Cdd:pfam16561  78 EVK 80
 
Name Accession Description Interval E-value
AMPKBI smart01010
5'-AMP-activated protein kinase beta subunit, interation domain; This region is found in the ...
190-274 1.33e-40

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: 135.53  E-value: 1.33e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5832839     190 SFTQEIPSM---------DMLRKAAGPPVIPPQLMQVLLNK-ETPESCDPNVLPEPNHVMLNHMYALSIKDSVMVLSSTQ 259
Cdd:smart01010   6 SYTNEIPACftdddfieeSPEEKWKEPPALPPHLEKVILNTsSTATREDPSLLPIPNHVVLNHLYTSSIKDGVLAVAATT 85
                           90
                   ....*....|....*
gi 5832839     260 RYRKKFVTTLLYKPV 274
Cdd:smart01010  86 RYRGKYVTQVLYKPL 100
AMPKBI pfam04739
5'-AMP-activated protein kinase beta subunit, interaction domain; This region is found in the ...
207-272 4.36e-36

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: 123.04  E-value: 4.36e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5832839    207 PPVIPPQLMQVLLNKETPESCDPNVLPEPNHVMLNHMYALSIKDSVMVLSSTQRYRKKFVTTLLYK 272
Cdd:pfam04739   4 PPALPPHLLLTILNKPPSSSDDPSVLPRPNHVVLNHLYTSSIKDGVLALGTTTRYRSKYVTTVLYK 69
AMPK1_CBM pfam16561
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in ...
62-144 2.55e-32

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: 113.73  E-value: 2.55e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5832839     62 PVVFRWSftQNAqpRVVHIVGSWDNWQTRIPMVKSTNDFSTIIDLQPGQYEYKFQVDGSWVVDDNQGKAQDVHGNENNMI 141
Cdd:pfam16561   2 PTVIRWR--GGG--KKVYVTGSFDNWKKKIPLQRSGGDFSTILDLPPGTHQYKFIVDGEWRHDPDLPTATDDMGNLNNYI 77

                  ...
gi 5832839    142 NIQ 144
Cdd:pfam16561  78 EVK 80
E_set_AMPKbeta_like_N cd02859
N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain ...
62-143 4.09e-32

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: 113.08  E-value: 4.09e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5832839   62 PVVFRWSftqNAQPRVVHIVGSWDNWQTRIPMVKSTN-DFSTIIDLQPGQYEYKFQVDGSWVVDDNQGKAQDVHGNENNM 140
Cdd:cd02859   1 PVTFRWP---GPGGKEVYVTGSFDNWQQPIPLEKSGDgEFSATVELPPGRYEYKFIVDGEWVHDPDLPTVTDEFGNLNNV 77

                ...
gi 5832839  141 INI 143
Cdd:cd02859  78 LEV 80
 
Name Accession Description Interval E-value
AMPKBI smart01010
5'-AMP-activated protein kinase beta subunit, interation domain; This region is found in the ...
190-274 1.33e-40

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: 135.53  E-value: 1.33e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5832839     190 SFTQEIPSM---------DMLRKAAGPPVIPPQLMQVLLNK-ETPESCDPNVLPEPNHVMLNHMYALSIKDSVMVLSSTQ 259
Cdd:smart01010   6 SYTNEIPACftdddfieeSPEEKWKEPPALPPHLEKVILNTsSTATREDPSLLPIPNHVVLNHLYTSSIKDGVLAVAATT 85
                           90
                   ....*....|....*
gi 5832839     260 RYRKKFVTTLLYKPV 274
Cdd:smart01010  86 RYRGKYVTQVLYKPL 100
AMPKBI pfam04739
5'-AMP-activated protein kinase beta subunit, interaction domain; This region is found in the ...
207-272 4.36e-36

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: 123.04  E-value: 4.36e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5832839    207 PPVIPPQLMQVLLNKETPESCDPNVLPEPNHVMLNHMYALSIKDSVMVLSSTQRYRKKFVTTLLYK 272
Cdd:pfam04739   4 PPALPPHLLLTILNKPPSSSDDPSVLPRPNHVVLNHLYTSSIKDGVLALGTTTRYRSKYVTTVLYK 69
AMPK1_CBM pfam16561
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in ...
62-144 2.55e-32

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: 113.73  E-value: 2.55e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5832839     62 PVVFRWSftQNAqpRVVHIVGSWDNWQTRIPMVKSTNDFSTIIDLQPGQYEYKFQVDGSWVVDDNQGKAQDVHGNENNMI 141
Cdd:pfam16561   2 PTVIRWR--GGG--KKVYVTGSFDNWKKKIPLQRSGGDFSTILDLPPGTHQYKFIVDGEWRHDPDLPTATDDMGNLNNYI 77

                  ...
gi 5832839    142 NIQ 144
Cdd:pfam16561  78 EVK 80
E_set_AMPKbeta_like_N cd02859
N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain ...
62-143 4.09e-32

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: 113.08  E-value: 4.09e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5832839   62 PVVFRWSftqNAQPRVVHIVGSWDNWQTRIPMVKSTN-DFSTIIDLQPGQYEYKFQVDGSWVVDDNQGKAQDVHGNENNM 140
Cdd:cd02859   1 PVTFRWP---GPGGKEVYVTGSFDNWQQPIPLEKSGDgEFSATVELPPGRYEYKFIVDGEWVHDPDLPTVTDEFGNLNNV 77

                ...
gi 5832839  141 INI 143
Cdd:cd02859  78 LEV 80
E_set_Isoamylase_like_N cd07184
N-terminal Early set domain associated with the catalytic domain of isoamylase-like (also ...
61-139 4.28e-12

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: 60.33  E-value: 4.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5832839   61 CPVVFRWSFTQNAQPrvVHIVGSWDNWQT-RIPMVKSTN-DFSTIIDLQPGQ-YEYKFQVDGS-WVVDDNQGKAQDVHGN 136
Cdd:cd07184   1 CKVTFELPAEQGADS--VSLVGDFNDWDPqATPMKKLKNgTFSATLDLPAGReYQFRYLIDGErWVNDPEADAYAPNGFG 78

                ...
gi 5832839  137 ENN 139
Cdd:cd07184  79 EEN 81
E_set cd02688
Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the ...
62-125 1.29e-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: 42.53  E-value: 1.29e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5832839   62 PVVFRWsFTQNAqpRVVHIVGSWDNWQ--TRIPMVKSTND-FSTIIDLQPGQYEYKFQVDGSWVVDD 125
Cdd:cd02688   1 GVTFRI-FAPGA--KSVYLIGSFNGWWqaQALPMTKNGGGvWSATIPLPLGTYEYKYVIDGGKNVLP 64
CBM53 pfam16760
Starch/carbohydrate-binding module (family 53);
78-129 6.74e-03

Starch/carbohydrate-binding module (family 53);


Pssm-ID: 339815  Cd Length: 78  Bit Score: 34.54  E-value: 6.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 5832839     78 VHIVGSWDNWQTR--IPMVKSTND-FSTIIDLQPGQYEYKFQV-DGSWVVDDNQGK 129
Cdd:pfam16760  17 VYLHYGFNNWRNVqdVPMEKTSGDgWEATVPVPEDAYRLNFCFrDGANNWDNNNGK 72
 
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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