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Conserved domains on  [gi|186519755|ref|NP_195962|]
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5'-AMP-activated protein kinase-like protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AMPK1_CBM super family cl48298
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in ...
 513-595 1.34e-22

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.


The actual alignment was detected with superfamily member pfam16561:

Pssm-ID: 465176 [Multi-domain]  Cd Length: 85  Bit Score: 91.82  E-value: 1.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186519755  513 VVIEYCGDGNAVEVTGSFNGWQHRVGMelqasksIGKQKCWSTLLWLYPGTYEIKFIVDGQWITDPQKDSVT--RGHIsN 590
Cdd:pfam16561   3 TVITWRGGGKKVYVTGSFDNWKKKIPL-------QKSGGDFTTILDLPPGTHQYKFIVDGEWRHDPDLPTATddMGNL-N 74


                  ....*
gi 186519755  591 NILKV 595
Cdd:pfam16561  75 NYIEV 79
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 437-516 8.24e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 8.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186519755 437 ETRKRENQVEIDRLRFMLDQKELELSRLKEQIEKEKLSLSVLQRQ---AETEIQKAQMLISEKEVELQEAEESLSGLQEV 513
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEE 105


                 ...
gi 186519755 514 VIE 516
Cdd:COG4942  106 LAE 108
 
Name Accession Description Interval E-value
AMPK1_CBM pfam16561
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in ...
 513-595 1.34e-22

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: 465176 [Multi-domain]  Cd Length: 85  Bit Score: 91.82  E-value: 1.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186519755  513 VVIEYCGDGNAVEVTGSFNGWQHRVGMelqasksIGKQKCWSTLLWLYPGTYEIKFIVDGQWITDPQKDSVT--RGHIsN 590
Cdd:pfam16561   3 TVITWRGGGKKVYVTGSFDNWKKKIPL-------QKSGGDFTTILDLPPGTHQYKFIVDGEWRHDPDLPTATddMGNL-N 74


                  ....*
gi 186519755  591 NILKV 595
Cdd:pfam16561  75 NYIEV 79
E_set_AMPKbeta_like_N cd02859
N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain ...
 512-595 3.37e-22

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: 90.74  E-value: 3.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186519755 512 EVVIEYCG-DGNAVEVTGSFNGWQHRVGMELQasksigKQKCWSTLLWLYPGTYEIKFIVDGQWITDPQKDSVT--RGHI 588
Cdd:cd02859    1 PVTFRWPGpGGKEVYVTGSFDNWQQPIPLEKS------GDGEFSATVELPPGRYEYKFIVDGEWVHDPDLPTVTdeFGNL 74


                 ....*..
gi 186519755 589 sNNILKV 595
Cdd:cd02859   75 -NNVLEV 80
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 437-516 8.24e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 8.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186519755 437 ETRKRENQVEIDRLRFMLDQKELELSRLKEQIEKEKLSLSVLQRQ---AETEIQKAQMLISEKEVELQEAEESLSGLQEV 513
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEE 105


                 ...
gi 186519755 514 VIE 516
Cdd:COG4942  106 LAE 108
IFT20 pfam14931
Intraflagellar transport complex B, subunit 20; IFT20 is subunit 20 of the intraflagellar ...
 461-501 1.71e-03

Intraflagellar transport complex B, subunit 20; IFT20 is subunit 20 of the intraflagellar transport complex B. The intraflagellar transport complex assembles and maintains eukaryotic cilia and flagella. IFT20 is localized to the Golgi complex and is anchored there by the Golgi polypeptide, GMAP210, whereas all other subunits except IFT172 localize to cilia and the peri-basal body or centrosomal region at the base of cilia. IFT20 accompanies Golgi-derived vesicles to the point of exocytosis near the basal bodies where the other IFT polypeptides are present, and where the intact IFT particle is assembled in association with the inner surface of the cell membrane. Passage of the IFT complex then follows, through the flagellar pore recognition site at the transition region, into the ciliary compartment. There also appears to be a role of intraflagellar transport (IFT) polypeptides in the formation of the immune synapse in non ciliated cells. The flagellum, in addition to being a sensory and motile organelle, is also a secretory organelle. A number of IFT components are expressed in haematopoietic cells, which have no cilia, indicating an unexpected role of IFT proteins in immune synapse-assembly and intracellular membrane trafficking in T lymphocytes; this suggests that the immune synapse could represent the functional homolog of the primary cilium in these cells.


Pssm-ID: 464383 [Multi-domain]  Cd Length: 109  Bit Score: 38.33  E-value: 1.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 186519755  461 LSRLKEQIEKEKLS-------LSVLQRQAETEIQKAQMLISEKEVELQ 501
Cdd:pfam14931  48 VDTLAKKVEKEKLKaigarnlLKSEAKQREAEQQQLQALILEKKVELE 95
PRK12704 PRK12704
phosphodiesterase; Provisional
 436-511 2.66e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 2.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186519755 436 HETRKRENQVEIDRLRFMLDQKELELSRLKEQIEKEKLSLSVLQRQAET---EIQKAQMLISEKEVELQEAEESLSGLQ 511
Cdd:PRK12704  73 FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQkqqELEKKEEELEELIEEQLQELERISGLT 151
 
Name Accession Description Interval E-value
AMPK1_CBM pfam16561
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in ...
 513-595 1.34e-22

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: 465176 [Multi-domain]  Cd Length: 85  Bit Score: 91.82  E-value: 1.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186519755  513 VVIEYCGDGNAVEVTGSFNGWQHRVGMelqasksIGKQKCWSTLLWLYPGTYEIKFIVDGQWITDPQKDSVT--RGHIsN 590
Cdd:pfam16561   3 TVITWRGGGKKVYVTGSFDNWKKKIPL-------QKSGGDFTTILDLPPGTHQYKFIVDGEWRHDPDLPTATddMGNL-N 74


                  ....*
gi 186519755  591 NILKV 595
Cdd:pfam16561  75 NYIEV 79
E_set_AMPKbeta_like_N cd02859
N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain ...
 512-595 3.37e-22

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: 90.74  E-value: 3.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186519755 512 EVVIEYCG-DGNAVEVTGSFNGWQHRVGMELQasksigKQKCWSTLLWLYPGTYEIKFIVDGQWITDPQKDSVT--RGHI 588
Cdd:cd02859    1 PVTFRWPGpGGKEVYVTGSFDNWQQPIPLEKS------GDGEFSATVELPPGRYEYKFIVDGEWVHDPDLPTVTdeFGNL 74


                 ....*..
gi 186519755 589 sNNILKV 595
Cdd:cd02859   75 -NNVLEV 80
E_set_Isoamylase_like_N cd07184
N-terminal Early set domain associated with the catalytic domain of isoamylase-like (also ...
 520-581 1.13e-05

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: 43.77  E-value: 1.13e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186519755 520 DGNAVEVTGSFNGWQ-HRVGMELQASKSigkqkcWSTLLWLYPG-TYEIKFIVDGQ-WITDPQKD 581
Cdd:cd07184   12 GADSVSLVGDFNDWDpQATPMKKLKNGT------FSATLDLPAGrEYQFRYLIDGErWVNDPEAD 70
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 437-516 8.24e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 8.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186519755 437 ETRKRENQVEIDRLRFMLDQKELELSRLKEQIEKEKLSLSVLQRQ---AETEIQKAQMLISEKEVELQEAEESLSGLQEV 513
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEE 105


                 ...
gi 186519755 514 VIE 516
Cdd:COG4942  106 LAE 108
IFT20 pfam14931
Intraflagellar transport complex B, subunit 20; IFT20 is subunit 20 of the intraflagellar ...
 461-501 1.71e-03

Intraflagellar transport complex B, subunit 20; IFT20 is subunit 20 of the intraflagellar transport complex B. The intraflagellar transport complex assembles and maintains eukaryotic cilia and flagella. IFT20 is localized to the Golgi complex and is anchored there by the Golgi polypeptide, GMAP210, whereas all other subunits except IFT172 localize to cilia and the peri-basal body or centrosomal region at the base of cilia. IFT20 accompanies Golgi-derived vesicles to the point of exocytosis near the basal bodies where the other IFT polypeptides are present, and where the intact IFT particle is assembled in association with the inner surface of the cell membrane. Passage of the IFT complex then follows, through the flagellar pore recognition site at the transition region, into the ciliary compartment. There also appears to be a role of intraflagellar transport (IFT) polypeptides in the formation of the immune synapse in non ciliated cells. The flagellum, in addition to being a sensory and motile organelle, is also a secretory organelle. A number of IFT components are expressed in haematopoietic cells, which have no cilia, indicating an unexpected role of IFT proteins in immune synapse-assembly and intracellular membrane trafficking in T lymphocytes; this suggests that the immune synapse could represent the functional homolog of the primary cilium in these cells.


Pssm-ID: 464383 [Multi-domain]  Cd Length: 109  Bit Score: 38.33  E-value: 1.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 186519755  461 LSRLKEQIEKEKLS-------LSVLQRQAETEIQKAQMLISEKEVELQ 501
Cdd:pfam14931  48 VDTLAKKVEKEKLKaigarnlLKSEAKQREAEQQQLQALILEKKVELE 95
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
444-512 2.06e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 2.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186519755 444 QVEIDRLRFMLDQKELELSRLKEQIEKEKLSLSVLQ---RQAETEIQKAQMLISEKEVELQEAEESLSGLQE 512
Cdd:COG4372   44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEeelEELNEQLQAAQAELAQAQEELESLQEEAEELQE 115
PRK12704 PRK12704
phosphodiesterase; Provisional
 436-511 2.66e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 2.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186519755 436 HETRKRENQVEIDRLRFMLDQKELELSRLKEQIEKEKLSLSVLQRQAET---EIQKAQMLISEKEVELQEAEESLSGLQ 511
Cdd:PRK12704  73 FEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQkqqELEKKEEELEELIEEQLQELERISGLT 151
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 437-512 4.73e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 4.73e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186519755 437 ETRKRENQVEIDRLRFMLDQKELELSRLKEQIEKEKLSLSVLQ---RQAETEIQKAQMLISEKEVELQEAEESLSGLQE 512
Cdd:COG1196  245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQaeeYELLAELARLEQDIARLEERRRELEERLEELEE 323
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
441-512 5.61e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 5.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186519755 441 RENQVEIDRLRFMLDQKELELSRLKEQIE---KEKLSLSVLQRQAETEIQKAQMLISEKEVELQEAEESLSGLQE 512
Cdd:COG4372   90 QAAQAELAQAQEELESLQEEAEELQEELEelqKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 441-516 6.98e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 6.98e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186519755 441 RENQVEIDRLRFMLDQKELELSRLKEQIEKEKLSLSVLQRQAETEIQKAQMLISEKEVE---LQEAEESLSGLQEVVIE 516
Cdd:COG4942  156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAElaeLQQEAEELEALIARLEA 234
 
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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