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Conserved domains on  [gi|449436499|ref|XP_004136030|]
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universal stress protein PHOS34 [Cucumis sativus]

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 ...
 8-156 6.79e-43

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: 139.29  E-value: 6.79e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449436499   8 VMVVGIDDSAHSLYALEWTLDHLLVPTspvnspFKLIIVHAKPSASSAVSLAGPGAAEVLPYVDSDLKKiAARVIEKAKE 87
Cdd:cd23659    2 KVLIAVDGSEESEYALEWALENLHRPG------DEVVLLHVIEPPSLPAASLGSGSEEWEALEEEAREK-AEKLLEKYEK 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 449436499  88 LCLARSVHDVLLEVIEGDARNVLCEAVEKHHASMLVVGSHGYGAIKRAVLGSVSDYCAHHAHCTVMIVK 156
Cdd:cd23659   75 KLKEEKGIKVKVEVVAGDPGEVICKAAEELKADLIVMGSRGLGALKRTLLGSVSDYVVHHSPCPVLVVR 143
 
Name Accession Description Interval E-value
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
 8-156 6.79e-43

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: 139.29  E-value: 6.79e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449436499   8 VMVVGIDDSAHSLYALEWTLDHLLVPTspvnspFKLIIVHAKPSASSAVSLAGPGAAEVLPYVDSDLKKiAARVIEKAKE 87
Cdd:cd23659    2 KVLIAVDGSEESEYALEWALENLHRPG------DEVVLLHVIEPPSLPAASLGSGSEEWEALEEEAREK-AEKLLEKYEK 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 449436499  88 LCLARSVHDVLLEVIEGDARNVLCEAVEKHHASMLVVGSHGYGAIKRAVLGSVSDYCAHHAHCTVMIVK 156
Cdd:cd23659   75 KLKEEKGIKVKVEVVAGDPGEVICKAAEELKADLIVMGSRGLGALKRTLLGSVSDYVVHHSPCPVLVVR 143
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 9-156 1.43e-24

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: 92.09  E-value: 1.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449436499    9 MVVGIDDSAHSLYALEWTLDHLLVPTSPvnspfkLIIVHAKPSASSAVSLAGPGAAEvlpyvDSDLKKIAARVIEKAKEL 88
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAE------LILLHVIDPPPSGAASLADESAE-----EEELELELAEAEALAAAA 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 449436499   89 CLARSVHDVLLEVIEGDARNVLCEAVEKHHASMLVVGSHGYGAIKRAVLGSVSDYCAHHAHCTVMIVK 156
Cdd:pfam00582  70 AAEAGGVKVEVVVVVGDPAEEILEVAEEEDADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
9-155 6.61e-22

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 85.36  E-value: 6.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449436499   9 MVVGIDDSAHSLYALEWTLDhlLVPTSPVnspfKLIIVHAKPSAssavslagPGAAEVLPYVDSDLKKIAARVIEKAKEL 88
Cdd:COG0589    5 ILVPTDGSEEAERALEYAAE--LAKALGA----ELHLLHVVDPP--------PSAAAGPEELEEELREEAEEALEEAAER 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449436499  89 CLARSVhDVLLEVIEGDARNVLCEAVEKHHASMLVVGSHGYGAIKRAVLGSVSDYCAHHAHCTVMIV 155
Cdd:COG0589   71 LEEAGV-EVETVVREGDPAEAILEAAEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
 
Name Accession Description Interval E-value
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
 8-156 6.79e-43

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: 139.29  E-value: 6.79e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449436499   8 VMVVGIDDSAHSLYALEWTLDHLLVPTspvnspFKLIIVHAKPSASSAVSLAGPGAAEVLPYVDSDLKKiAARVIEKAKE 87
Cdd:cd23659    2 KVLIAVDGSEESEYALEWALENLHRPG------DEVVLLHVIEPPSLPAASLGSGSEEWEALEEEAREK-AEKLLEKYEK 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 449436499  88 LCLARSVHDVLLEVIEGDARNVLCEAVEKHHASMLVVGSHGYGAIKRAVLGSVSDYCAHHAHCTVMIVK 156
Cdd:cd23659   75 KLKEEKGIKVKVEVVAGDPGEVICKAAEELKADLIVMGSRGLGALKRTLLGSVSDYVVHHSPCPVLVVR 143
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
 9-155 3.21e-25

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: 93.95  E-value: 3.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449436499   9 MVVGIDDSAHSLYALEWTLDHLLVPTSpvnspfKLIIVHAKPSASSAVSlagpgaAEVLPYVDSDLKKIAARVIEKAKEL 88
Cdd:cd00293    2 ILVAVDGSEESERALEWALELAKRPGA------ELTLLHVVDPPPSSSL------SGGLEELADELKEEAEELLEEAKKL 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449436499  89 CLARSVhDVLLEVIEGDARNVLCEAVEKHHASMLVVGSHGYGAIKRAVLGSVSDYCAHHAHCTVMIV 155
Cdd:cd00293   70 AEEAGV-EVETIVVEGDPAEAILEEAKELGADLIVMGSRGRSGLKRLLLGSVSEYVLRHAPCPVLVV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 9-156 1.43e-24

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: 92.09  E-value: 1.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449436499    9 MVVGIDDSAHSLYALEWTLDHLLVPTSPvnspfkLIIVHAKPSASSAVSLAGPGAAEvlpyvDSDLKKIAARVIEKAKEL 88
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAE------LILLHVIDPPPSGAASLADESAE-----EEELELELAEAEALAAAA 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 449436499   89 CLARSVHDVLLEVIEGDARNVLCEAVEKHHASMLVVGSHGYGAIKRAVLGSVSDYCAHHAHCTVMIVK 156
Cdd:pfam00582  70 AAEAGGVKVEVVVVVGDPAEEILEVAEEEDADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
9-155 6.61e-22

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 85.36  E-value: 6.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449436499   9 MVVGIDDSAHSLYALEWTLDhlLVPTSPVnspfKLIIVHAKPSAssavslagPGAAEVLPYVDSDLKKIAARVIEKAKEL 88
Cdd:COG0589    5 ILVPTDGSEEAERALEYAAE--LAKALGA----ELHLLHVVDPP--------PSAAAGPEELEEELREEAEEALEEAAER 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 449436499  89 CLARSVhDVLLEVIEGDARNVLCEAVEKHHASMLVVGSHGYGAIKRAVLGSVSDYCAHHAHCTVMIV 155
Cdd:COG0589   71 LEEAGV-EVETVVREGDPAEAILEAAEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
USP_Rv2623_repeat1 cd23944
universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis ...
 10-155 1.32e-13

universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis universal stress protein Rv2623 regulates mycobacterial growth in vitro and in vivo and is required for the entry of the tubercle bacillus into the chronic phase of infection in the host. In addition Rv2623 binds ATP and the growth-regulatory attribute of this USP is dependent on its ATP-binding activity. Rv2623 is thought to function as an ATP-dependent signaling intermediate in a pathway that promotes persistent infection. 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: 467509  Cd Length: 140  Bit Score: 63.96  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449436499  10 VVGIDDSAHSLYALEWTLDHllvpTSPVNSPFKLIIVHAKPSASSAVslaGPGAAEVLpyvdSDLKKIAARVIEKAKELC 89
Cdd:cd23944    3 IVGVDGSPASDAAVRWAARE----AQLRQIPLTLVHVVPPVVVSWPE---GPRPAEVL----DWQQDEARQVIEQARKVA 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449436499  90 LARSVHDVLL----EVIEGDARNVLCEAVEKhhASMLVVGSHGYGAIKRAVLGSVSDYCAHHAHCTVMIV 155
Cdd:cd23944   72 EEASGEGPPVkvetEIVPGSPVPTLVEASRD--ATMVVVGSRGIGALAGLLLGSVSTSLVRHAHCPVAVI 139
USP_STK_Ubox_N cd01989
N-terminal USP domain of serine threonine kinases (STK) and U-box domain proteins; This model ...
 10-157 4.66e-08

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: 49.59  E-value: 4.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449436499  10 VVGID-DSAHSLYALEWTLDHLLVPTSpvnspfKLIIVHAKPSASSAVSLAGpgaaEVLPYVDSDLKKIAARVIEKAK-- 86
Cdd:cd01989    3 AVAVDgDDKKSKSALKWALDNLAPRGA------KIVLVHVHPPVTMIPTPSG----KVPPIQLREEEVSAYRKQEREKte 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449436499  87 -------ELCLARSV--HDVLLEviEGDARNVLCEAVEKHHASMLVVGSHGYGAIKRAVLGS-VSDYCAHHA--HCTVMI 154
Cdd:cd01989   73 kmllpylDMCSRKKVqaEKVVIE--SDDVAKGIVELISQHGITKLVMGAASDNHFSMKLKKSdVASSVMKAApdFCTVWV 150


                 ...
gi 449436499 155 VKK 157
Cdd:cd01989  151 VCK 153
USP_Rv2623_repeat2 cd23661
universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis ...
 72-156 5.15e-07

universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis universal stress protein Rv2623 regulates mycobacterial growth in vitro and in vivo and is required for the entry of the tubercle bacillus into the chronic phase of infection in the host. In addition, Rv2623 binds ATP and the growth-regulatory attribute of this USP is dependent on its ATP-binding activity. Rv2623 is thought to function as an ATP-dependent signaling intermediate in a pathway that promotes persistent infection. 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: 467507 [Multi-domain]  Cd Length: 133  Bit Score: 46.35  E-value: 5.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 449436499  72 SDLKKIAARVIEKAKELCLARS----------VHdVLLEVIEGDARNVLCEAVEKhhASMLVVGSHGYGAIKRAVLGSVS 141
Cdd:cd23661   42 GGFLGIDWRESEQDQERMLAERlagwqerypdVH-VHKVVVRDRPARVLLEASER--AQLVVVGSHGRGGFAGMLLGSVS 118

                         90
                 ....*....|....*
gi 449436499 142 DYCAHHAHCTVMIVK 156
Cdd:cd23661  119 RAVLHSAPCPVIVVR 133
USP-A-like cd23657
universal stress protein A and similar proteins; The universal stress protein UspA is a small ...
 104-156 1.67e-03

universal stress protein A and similar proteins; The universal stress protein UspA is a small cytoplasmic bacterial protein whose expression is enhanced several-fold when cellular viability is challenged with heat shock, nutrient starvation, stress agents which arrest cell growth, or DNA-damaging agents. UspA enhances the rate of cell survival during prolonged exposure to such conditions, suggesting that it asserts a general "stress endurance" activity. In general, these proteins form dimers and have domains for nucleotide binding activity. The crystal structure of Haemophilus influenzae UspA reveals an asymmetric dimer with a tertiary alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, but unlike MJ0577, it lacks ATP-binding activity.


Pssm-ID: 467504  Cd Length: 138  Bit Score: 36.52  E-value: 1.67e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 449436499 104 GDARNVLCEAVEKHHASMLVVGSHGYGAIKRavLGSVSDYCAHHAHCTVMIVK 156
Cdd:cd23657   87 GDLKEEILEVAKKHNVDLIVCGHHGDFGLSL--LGSSARAVLNSAPCDVLIVP 137
 
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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