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Conserved domains on  [gi|1063699896|ref|NP_001323815|]
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Adenine nucleotide alpha hydrolases-like superfamily protein [Arabidopsis thaliana]

Protein Classification

universal stress protein( domain architecture ID 19229820)

universal stress protein (USP) enhances the rate of cell survival during prolonged exposure to stress agents

CATH:  3.40.50.620
Gene Ontology:  GO:0005524|GO:0050896
PubMed:  23745136|12012333|36902153
SCOP:  4003850

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
 65-204 3.89e-23

universal stress protein At3g01520 and similar proteins; This subfamily includes plant and fungal proteins of unknown function, including Arabidopsis thaliana At3g01520. A. thaliana contains 44 USP domain-containing proteins; the USP domain is found either in a small protein with unknown physiological function or as an N-terminal portion of a multi-domain protein, usually a protein kinase. The gene At3g01520 of Arabidopsis thaliana encodes a 175-residue universal stress protein (USP)-like protein which is widely found in the genomes of bacteria, as well as fungi, protozoa, and plants. The bound AMP and conservation of residues in the ATP-binding loop suggest that the protein At3g01520 belongs to the ATP-binding USP subfamily. Universal stress proteins (USPs) are small cytoplasmic bacterial proteins whose expression is enhanced when the cell is exposed to stress agents. USP enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity.


:

Pssm-ID: 467505  Cd Length: 143  Bit Score: 90.76  E-value: 3.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699896  65 RKVMVVVDTTSQTKNALQWALTHCVQDEDNITLLHVTRTPVGQA---------IDETQRERNSRAHELVHPLKNFCQLKK 135
Cdd:cd23659     1 RKVLIAVDGSEESEYALEWALENLHRPGDEVVLLHVIEPPSLPAaslgsgseeWEALEEEAREKAEKLLEKYEKKLKEEK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063699896 136 pNVKTEIVVVetAEEKGKTIVEESKKQGAGVLVLGQRKRTSKWRVIwkwrtkggmGGGVVEYCIHNSDC 204
Cdd:cd23659    81 -GIKVKVEVV--AGDPGEVICKAAEELKADLIVMGSRGLGALKRTL---------LGSVSDYVVHHSPC 137
 
Name Accession Description Interval E-value
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
 65-204 3.89e-23

universal stress protein At3g01520 and similar proteins; This subfamily includes plant and fungal proteins of unknown function, including Arabidopsis thaliana At3g01520. A. thaliana contains 44 USP domain-containing proteins; the USP domain is found either in a small protein with unknown physiological function or as an N-terminal portion of a multi-domain protein, usually a protein kinase. The gene At3g01520 of Arabidopsis thaliana encodes a 175-residue universal stress protein (USP)-like protein which is widely found in the genomes of bacteria, as well as fungi, protozoa, and plants. The bound AMP and conservation of residues in the ATP-binding loop suggest that the protein At3g01520 belongs to the ATP-binding USP subfamily. Universal stress proteins (USPs) are small cytoplasmic bacterial proteins whose expression is enhanced when the cell is exposed to stress agents. USP enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity.


Pssm-ID: 467505  Cd Length: 143  Bit Score: 90.76  E-value: 3.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699896  65 RKVMVVVDTTSQTKNALQWALTHCVQDEDNITLLHVTRTPVGQA---------IDETQRERNSRAHELVHPLKNFCQLKK 135
Cdd:cd23659     1 RKVLIAVDGSEESEYALEWALENLHRPGDEVVLLHVIEPPSLPAaslgsgseeWEALEEEAREKAEKLLEKYEKKLKEEK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063699896 136 pNVKTEIVVVetAEEKGKTIVEESKKQGAGVLVLGQRKRTSKWRVIwkwrtkggmGGGVVEYCIHNSDC 204
Cdd:cd23659    81 -GIKVKVEVV--AGDPGEVICKAAEELKADLIVMGSRGLGALKRTL---------LGSVSDYVVHHSPC 137
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
65-204 3.76e-15

Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];


Pssm-ID: 440354  Cd Length: 136  Bit Score: 69.56  E-value: 3.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699896  65 RKVMVVVDTTSQTKNALQWALTHCVQDEDNITLLHVTRTPVG--QAIDETQRERNSRAHELVHPLKNfcQLKKPNVKTEI 142
Cdd:COG0589     3 KRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSaaAGPEELEEELREEAEEALEEAAE--RLEEAGVEVET 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063699896 143 VVVE--TAEEkgktIVEESKKQGAGVLVLGQRKRTSKWRVIWkwrtkggmgGGVVEYCIHNSDC 204
Cdd:COG0589    81 VVREgdPAEA----ILEAAEELDADLIVMGSRGRSGLRRLLL---------GSVAERVLRHAPC 131
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 67-210 6.54e-15

Universal stress protein family; The universal stress protein UspA is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. UspA enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae UspA reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, though UspA lacks ATP-binding activity.


Pssm-ID: 425765 [Multi-domain]  Cd Length: 137  Bit Score: 68.97  E-value: 6.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699896  67 VMVVVDTTSQTKNALQWALTHCVQDEDNITLLHVTRTPVGQAID------ETQRERNSRAHELVHPLKNFCQLKKPNVKT 140
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAELILLHVIDPPPSGAASladesaEEEELELELAEAEALAAAAAAEAGGVKVEV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699896 141 EIVVVETAEEkgktIVEESKKQGAGVLVLGQRKRTskwrviwkwRTKGGMGGGVVEYCIHNSDCMAIAVR 210
Cdd:pfam00582  81 VVVVGDPAEE----ILEVAEEEDADLIVMGSRGRS---------GLSRLLLGSVAEYVLRHAPCPVLVVR 137
 
Name Accession Description Interval E-value
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
 65-204 3.89e-23

universal stress protein At3g01520 and similar proteins; This subfamily includes plant and fungal proteins of unknown function, including Arabidopsis thaliana At3g01520. A. thaliana contains 44 USP domain-containing proteins; the USP domain is found either in a small protein with unknown physiological function or as an N-terminal portion of a multi-domain protein, usually a protein kinase. The gene At3g01520 of Arabidopsis thaliana encodes a 175-residue universal stress protein (USP)-like protein which is widely found in the genomes of bacteria, as well as fungi, protozoa, and plants. The bound AMP and conservation of residues in the ATP-binding loop suggest that the protein At3g01520 belongs to the ATP-binding USP subfamily. Universal stress proteins (USPs) are small cytoplasmic bacterial proteins whose expression is enhanced when the cell is exposed to stress agents. USP enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity.


Pssm-ID: 467505  Cd Length: 143  Bit Score: 90.76  E-value: 3.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699896  65 RKVMVVVDTTSQTKNALQWALTHCVQDEDNITLLHVTRTPVGQA---------IDETQRERNSRAHELVHPLKNFCQLKK 135
Cdd:cd23659     1 RKVLIAVDGSEESEYALEWALENLHRPGDEVVLLHVIEPPSLPAaslgsgseeWEALEEEAREKAEKLLEKYEKKLKEEK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063699896 136 pNVKTEIVVVetAEEKGKTIVEESKKQGAGVLVLGQRKRTSKWRVIwkwrtkggmGGGVVEYCIHNSDC 204
Cdd:cd23659    81 -GIKVKVEVV--AGDPGEVICKAAEELKADLIVMGSRGLGALKRTL---------LGSVSDYVVHHSPC 137
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
 66-209 9.00e-23

universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. USP enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae Usp reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, although USP lacks ATP-binding activity.


Pssm-ID: 467483 [Multi-domain]  Cd Length: 135  Bit Score: 89.71  E-value: 9.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699896  66 KVMVVVDTTSQTKNALQWALTHCVQDEDNITLLHV----TRTPVGQAIDETQRERNSRAHELVHPLKNFCQLKKPNVKTE 141
Cdd:cd00293     1 KILVAVDGSEESERALEWALELAKRPGAELTLLHVvdppPSSSLSGGLEELADELKEEAEELLEEAKKLAEEAGVEVETI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063699896 142 IVVVETAEEkgktIVEESKKQGAGVLVLGQRKRTSKWRVIWkwrtkggmgGGVVEYCIHNSDCMAIAV 209
Cdd:cd00293    81 VVEGDPAEA----ILEEAKELGADLIVMGSRGRSGLKRLLL---------GSVSEYVLRHAPCPVLVV 135
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
65-204 3.76e-15

Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];


Pssm-ID: 440354  Cd Length: 136  Bit Score: 69.56  E-value: 3.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699896  65 RKVMVVVDTTSQTKNALQWALTHCVQDEDNITLLHVTRTPVG--QAIDETQRERNSRAHELVHPLKNfcQLKKPNVKTEI 142
Cdd:COG0589     3 KRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSaaAGPEELEEELREEAEEALEEAAE--RLEEAGVEVET 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063699896 143 VVVE--TAEEkgktIVEESKKQGAGVLVLGQRKRTSKWRVIWkwrtkggmgGGVVEYCIHNSDC 204
Cdd:COG0589    81 VVREgdPAEA----ILEAAEELDADLIVMGSRGRSGLRRLLL---------GSVAERVLRHAPC 131
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 67-210 6.54e-15

Universal stress protein family; The universal stress protein UspA is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. UspA enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae UspA reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, though UspA lacks ATP-binding activity.


Pssm-ID: 425765 [Multi-domain]  Cd Length: 137  Bit Score: 68.97  E-value: 6.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699896  67 VMVVVDTTSQTKNALQWALTHCVQDEDNITLLHVTRTPVGQAID------ETQRERNSRAHELVHPLKNFCQLKKPNVKT 140
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAELILLHVIDPPPSGAASladesaEEEELELELAEAEALAAAAAAEAGGVKVEV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699896 141 EIVVVETAEEkgktIVEESKKQGAGVLVLGQRKRTskwrviwkwRTKGGMGGGVVEYCIHNSDCMAIAVR 210
Cdd:pfam00582  81 VVVVGDPAEE----ILEVAEEEDADLIVMGSRGRS---------GLSRLLLGSVAEYVLRHAPCPVLVVR 137
USP_STK_Ubox_N cd01989
N-terminal USP domain of serine threonine kinases (STK) and U-box domain proteins; This model ...
 66-186 2.41e-10

N-terminal USP domain of serine threonine kinases (STK) and U-box domain proteins; This model represents the N-terminal domain found in some plant serine threonine kinases (STK, EC 2.7.11.-) and U-box domain-containing proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They play a role in the regulation of cell proliferation, programmed cell death (apoptosis), cell differentiation, and embryonic development. These enzymes belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. U-box domain-containing proteins function as E3 ubiquitin ligases (EC 2.3.2.27), mediating the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin. The N-terminal domain of these proteins is homologous to the universal stress protein (USP) family which has an ATP binding fold. The N-terminal domain is predicted to be involved in ATP binding.


Pssm-ID: 467493  Cd Length: 154  Bit Score: 56.91  E-value: 2.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063699896  66 KVMVVVDTTSQ-TKNALQWALTHCVQDEDNITLLHV------TRTPVGQAIDETQRERNSRAH---------ELVHPLKN 129
Cdd:cd01989     1 KVAVAVDGDDKkSKSALKWALDNLAPRGAKIVLVHVhppvtmIPTPSGKVPPIQLREEEVSAYrkqerekteKMLLPYLD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063699896 130 FCQLKKpnVKTEIVVVETaEEKGKTIVEESKKQGAGVLVLGQRKRTSKWRVIWKWRT 186
Cdd:cd01989    81 MCSRKK--VQAEKVVIES-DDVAKGIVELISQHGITKLVMGAASDNHFSMKLKKSDV 134
 
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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