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Conserved domains on  [gi|159795323|pdb|2QR1|C]
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Chain C, SNF1-like protein kinase ssp2

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
AdenylateSensor pfam16579
Adenylate sensor of SNF1-like protein kinase; AdenylateSensor is a family found at the ...
 12-134 1.37e-72

Adenylate sensor of SNF1-like protein kinase; AdenylateSensor is a family found at the C-terminus of SNF1-like protein kinases snf other protein-kinases.


:

Pssm-ID: 406881  Cd Length: 118  Bit Score: 212.60  E-value: 1.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QR1_C         12 KWHFGVRCRGDAPEILLAVYRALQRAGAQFTVPKPvngkyRSDMYTIKSRWEIPHCKREGKNTYAYIELQLYEVMPGCFM 91
Cdd:pfam16579   1 RWHFGIRSRSYPLDVMGEIYRALKNLGAEWAKPST-----EEELWTIKVRWKYPHCETEGRNDLMKMQIQLFQIEPNNYL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
2QR1_C         92 LDVKSNGYKDIYSHPERTADHGMDDLKSSFPFLDLCAMLVCKL 134
Cdd:pfam16579  76 VDFKFDGWEDSYSHPESTADEDEDDVFSAYPFLHLATRLIMEL 118
 
Name Accession Description Interval E-value
AdenylateSensor pfam16579
Adenylate sensor of SNF1-like protein kinase; AdenylateSensor is a family found at the ...
 12-134 1.37e-72

Adenylate sensor of SNF1-like protein kinase; AdenylateSensor is a family found at the C-terminus of SNF1-like protein kinases snf other protein-kinases.


Pssm-ID: 406881  Cd Length: 118  Bit Score: 212.60  E-value: 1.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QR1_C         12 KWHFGVRCRGDAPEILLAVYRALQRAGAQFTVPKPvngkyRSDMYTIKSRWEIPHCKREGKNTYAYIELQLYEVMPGCFM 91
Cdd:pfam16579   1 RWHFGIRSRSYPLDVMGEIYRALKNLGAEWAKPST-----EEELWTIKVRWKYPHCETEGRNDLMKMQIQLFQIEPNNYL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
2QR1_C         92 LDVKSNGYKDIYSHPERTADHGMDDLKSSFPFLDLCAMLVCKL 134
Cdd:pfam16579  76 VDFKFDGWEDSYSHPESTADEDEDDVFSAYPFLHLATRLIMEL 118
AMPKA_C cd12122
C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK) alpha catalytic subunit; ...
 10-134 1.67e-39

C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK) alpha catalytic subunit; AMPK, a serine/threonine protein kinase (STK), catalyzes the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. It acts as a sensor for the energy status of the cell and is activated by cellular stresses that lead to ATP depletion such as hypoxia, heat shock, and glucose deprivation, among others. AMPK is a heterotrimer of three subunits: alpha, beta, and gamma. Co-expression of the three subunits is required for kinase activity; in the absence of one, the other two subunits get degraded. The AMPK alpha subunit is the catalytic subunit and it contains an N-terminal kinase domain and a C-terminal regulatory domain (RD). Vertebrates contain two isoforms of the alpha subunit, alpha1 and alpha2, which are encoded by different genes, PRKAA1 and PRKAA2, respectively. The C-terminal RD of the AMPK alpha subunit is involved in AMPK heterotrimer formation. It mainly interacts with the C-terminal region of the beta subunit to form a tight alpha-beta complex that is associated with the gamma subunit. The AMPK alpha subunit RD also contains an auto-inhibitory region that interacts with the kinase domain; this inhibition is negated by the interaction with the AMPK gamma subunit. AMPK is conserved throughout evolution; the AMPK alpha subunit homologs in yeast and plants are called Snf1 and SnRK1 (Snf1 related kinase), respectively.


Pssm-ID: 213378  Cd Length: 132  Bit Score: 129.12  E-value: 1.67e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QR1_C       10 RNKWHFGVRCRGDAPEILLAVYRALQRAGAQFTVPKPvngkyrsdmYTIKSRWEIPHCKREG----------------KN 73
Cdd:cd12122   1 ERRWHLGIRSQSHPHEIMLEVYRALKALGFEWKKISP---------YHIKCRWKNPVVGKPGgssgesssadgpgaarQP 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
2QR1_C       74 TYAYIELQLYEVMPGCFMLDVKSNGYKDIYSHPERTADHGMDDLKSSFPFLDLCAMLVCKL 134
Cdd:cd12122  72 TVVKMELQLYKVDDNKYLLDFQSLDYEEERTGPGESAEDAEPQVGSTFLFFDLCAKLITEL 132
 
Name Accession Description Interval E-value
AdenylateSensor pfam16579
Adenylate sensor of SNF1-like protein kinase; AdenylateSensor is a family found at the ...
 12-134 1.37e-72

Adenylate sensor of SNF1-like protein kinase; AdenylateSensor is a family found at the C-terminus of SNF1-like protein kinases snf other protein-kinases.


Pssm-ID: 406881  Cd Length: 118  Bit Score: 212.60  E-value: 1.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QR1_C         12 KWHFGVRCRGDAPEILLAVYRALQRAGAQFTVPKPvngkyRSDMYTIKSRWEIPHCKREGKNTYAYIELQLYEVMPGCFM 91
Cdd:pfam16579   1 RWHFGIRSRSYPLDVMGEIYRALKNLGAEWAKPST-----EEELWTIKVRWKYPHCETEGRNDLMKMQIQLFQIEPNNYL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
2QR1_C         92 LDVKSNGYKDIYSHPERTADHGMDDLKSSFPFLDLCAMLVCKL 134
Cdd:pfam16579  76 VDFKFDGWEDSYSHPESTADEDEDDVFSAYPFLHLATRLIMEL 118
AMPKA_C cd12122
C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK) alpha catalytic subunit; ...
 10-134 1.67e-39

C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK) alpha catalytic subunit; AMPK, a serine/threonine protein kinase (STK), catalyzes the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. It acts as a sensor for the energy status of the cell and is activated by cellular stresses that lead to ATP depletion such as hypoxia, heat shock, and glucose deprivation, among others. AMPK is a heterotrimer of three subunits: alpha, beta, and gamma. Co-expression of the three subunits is required for kinase activity; in the absence of one, the other two subunits get degraded. The AMPK alpha subunit is the catalytic subunit and it contains an N-terminal kinase domain and a C-terminal regulatory domain (RD). Vertebrates contain two isoforms of the alpha subunit, alpha1 and alpha2, which are encoded by different genes, PRKAA1 and PRKAA2, respectively. The C-terminal RD of the AMPK alpha subunit is involved in AMPK heterotrimer formation. It mainly interacts with the C-terminal region of the beta subunit to form a tight alpha-beta complex that is associated with the gamma subunit. The AMPK alpha subunit RD also contains an auto-inhibitory region that interacts with the kinase domain; this inhibition is negated by the interaction with the AMPK gamma subunit. AMPK is conserved throughout evolution; the AMPK alpha subunit homologs in yeast and plants are called Snf1 and SnRK1 (Snf1 related kinase), respectively.


Pssm-ID: 213378  Cd Length: 132  Bit Score: 129.12  E-value: 1.67e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QR1_C       10 RNKWHFGVRCRGDAPEILLAVYRALQRAGAQFTVPKPvngkyrsdmYTIKSRWEIPHCKREG----------------KN 73
Cdd:cd12122   1 ERRWHLGIRSQSHPHEIMLEVYRALKALGFEWKKISP---------YHIKCRWKNPVVGKPGgssgesssadgpgaarQP 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
2QR1_C       74 TYAYIELQLYEVMPGCFMLDVKSNGYKDIYSHPERTADHGMDDLKSSFPFLDLCAMLVCKL 134
Cdd:cd12122  72 TVVKMELQLYKVDDNKYLLDFQSLDYEEERTGPGESAEDAEPQVGSTFLFFDLCAKLITEL 132
AMPKA_C_like cd12120
C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK) alpha subunit and ...
 10-134 2.01e-39

C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK) alpha subunit and similar domains; This family is composed of AMPKs, microtubule-associated protein/microtubule affinity regulating kinases (MARKs), yeast Kcc4p-like proteins, plant calcineurin B-Like (CBL)-interacting protein kinases (CIPKs), and similar proteins. They are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. AMPKs act as sensors for the energy status of the cell and are activated by cellular stresses that lead to ATP depletion such as hypoxia, heat shock, and glucose deprivation, among others. MARKs phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Kcc4p and related proteins are septin-associated proteins that are involved in septin organization and in the yeast morphogenesis checkpoint coordinating the cell cycle with bud formation. CIPKs interact with the calcineurin B-like (CBL) calcium sensors to form a signaling network that decode specific calcium signals triggered by a variety of environmental stimuli including salinity, drought, cold, light, and mechanical perturbation, among others. All members of this family contain an N-terminal catalytic kinase domain and a C-terminal regulatory domain which is also called kinase associated domain 1 (KA1) in some cases. The C-terminal regulatory domain serves as a protein interaction domain in AMPKs and CIPKs. In MARKs and Kcc4p-like proteins, this domain binds phospholipids and may be involved in membrane localization.


Pssm-ID: 213376  Cd Length: 95  Bit Score: 127.67  E-value: 2.01e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QR1_C       10 RNKWHFGVRCRGDAPEILLAVYRALQRAGAQFTVPKPvngkyrsdMYTIKSRWEIPHCKregKNTYAYIELQLYEVMPGC 89
Cdd:cd12120   1 RKKWELEIHSRIDPSEIYEGIHKVLEGWGKNLVFRIT--------NFIITGKLVNDHIL---FLRSTLFEIEVYEVGPGL 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
2QR1_C       90 FMLDVKSNGYkdiyshpertadhgmddlkSSFPFLDLCAMLVCKL 134
Cdd:cd12120  70 FMVDFKKKTG-------------------STKTFTKLATKIQIKL 95
AMPKA1_C cd12199
C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK) alpha 1 catalytic ...
 10-131 9.20e-07

C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK) alpha 1 catalytic subunit; AMPK, a serine/threonine protein kinase (STK), catalyzes the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. It acts as a sensor for the energy status of the cell and is activated by cellular stresses that lead to ATP depletion such as hypoxia, heat shock, and glucose deprivation, among others. AMPK is a heterotrimer of three subunits: alpha, beta, and gamma. Co-expression of the three subunits is required for kinase activity; in the absence of one, the other two subunits get degraded. The AMPK alpha subunit is the catalytic subunit and it contains an N-terminal kinase domain and a C-terminal regulatory domain (RD). Vertebrates contain two isoforms of the alpha subunit, alpha1 and alpha2, which are encoded by different genes, PRKAA1 and PRKAA2, respectively, and show varying expression patterns. AMPKalpha1 is the predominant isoform expressed in bone; it plays a role in bone remodeling in response to hormonal regulation. It is selectively regulated by nucleoside diphosphate kinase (NDPK)-A in an AMP-independent manner. AMPKalpha1 impacts the regulation of fat metabolism through its in vivo target, acetyl coenzyme A carboxylase (ACC). It also mediates the vasoprotective effects of estrogen through phosphorylation of another in vivo substrate, RhoA. The C-terminal RD of the AMPK alpha 1 subunit is involved in AMPK heterotrimer formation. It mainly interacts with the C-terminal region of the beta subunit to form a tight alpha-beta complex that is associated with the gamma subunit. The AMPK alpha subunit RD also contains an auto-inhibitory region that interacts with the kinase domain; this inhibition is negated by the interaction with the AMPK gamma subunit.


Pssm-ID: 213384  Cd Length: 96  Bit Score: 44.31  E-value: 9.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QR1_C       10 RNKWHFGVRCRGDAPEILLAVYRALQRAGAQFTVPKPvngkyrsdmYTIKSRWEIPHckregKNTYAYIELQLYEVMPGC 89
Cdd:cd12199   1 RAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNP---------YYLRVRRKNPV-----TSTFSKMSLQLYQVDSRT 66

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
2QR1_C       90 FMLDVKSNGyKDIYSHpertadhgmddlksSFPFLDLCAMLV 131
Cdd:cd12199  67 YLLDFRSID-DEITSH--------------TIEFFEMCANLI 93
AMPKA2_C cd12200
C-terminal regulatory domain of 5'-AMP-activated serine/threonine kinase, subunit alpha; AMPK, ...
 9-134 2.34e-05

C-terminal regulatory domain of 5'-AMP-activated serine/threonine kinase, subunit alpha; AMPK, a serine/threonine protein kinase (STK), catalyzes the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. It acts as a sensor for the energy status of the cell and is activated by cellular stresses that lead to ATP depletion such as hypoxia, heat shock, and glucose deprivation, among others. AMPK is a heterotrimer of three subunits: alpha, beta, and gamma. Co-expression of the three subunits is required for kinase activity; in the absence of one, the other two subunits get degraded. The AMPK alpha subunit is the catalytic subunit and it contains an N-terminal kinase domain and a C-terminal regulatory domain (RD). Vertebrates contain two isoforms of the alpha subunit, alpha1 and alpha2, which are encoded by different genes, PRKAA1 and PRKAA2, respectively, and show varying expression patterns. AMPKalpha2 shows cytoplasmic and nuclear localization, whereas AMPKalpha1 is localized only in the cytoplasm. The C-terminal RD of the AMPK alpha 1 subunit is involved in AMPK heterotrimer formation. It mainly interacts with the C-terminal region of the beta subunit to form a tight alpha-beta complex that is associated with the gamma subunit. The AMPK alpha subunit RD also contains an auto-inhibitory region that interacts with the kinase domain; this inhibition is negated by the interaction with the AMPK gamma subunit.


Pssm-ID: 213385  Cd Length: 102  Bit Score: 40.83  E-value: 2.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2QR1_C        9 RRNKWHFGVRCRGDAPEILLAVYRALQRAGAQFTVpkpVNGkyrsdmYTIKSRWEIPHckregKNTYAYIELQLYEVMPG 88
Cdd:cd12200   4 KKAKWHLGIRSQSKPYDIMAEVYRAMKQLDFEWKV---VNP------YHLRVRRKNPV-----TGNYVKMSLQLYQVDNR 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
2QR1_C       89 CFMLDVKSngykdIYSHPeRTADHGMDdlkssfpFLDLCAMLVCKL 134
Cdd:cd12200  70 SYLLDFKS-----IDDEP-RLGSHTMD-------FFEMCASLITTL 102
 
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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