NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1320058663|gb|PLN00037|]
View 

universal stress protein [Klebsiella quasipneumoniae]

Protein Classification

adenine nucleotide alpha hydrolase family protein( domain architecture ID 188)

AANH (adenine nucleotide alpha hydrolase) family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AANH_superfamily super family cl00292
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ...
 4-136 2.22e-10

Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


The actual alignment was detected with superfamily member cd23657:

Pssm-ID: 469708  Cd Length: 138  Bit Score: 54.62  E-value: 2.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320058663   4 YHHALVLINSSQDGVPLLEHAARMAEENGMRITIAHISTDYRALN--YVSDSLRDDQVSQEVIQAKALLNeLACTVSLPV 81
Cdd:cd23657     1 YKHILVAVDLSPESQSLVDKAVEIARENDAKLSLIHVDEDISEYYtgLIDVDIAALQDLESTMLEEALKN-LSELAGYPV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1320058663  82 DTLSLVTTRRFEDVETCVRQRQIDLIIAGHHNR-LLGVLSSHSLEYINHLTIDVLI 136
Cdd:cd23657    80 DHTFIGYGDLKEEILEVAKKHNVDLIVCGHHGDfGLSLLGSSARAVLNSAPCDVLI 135
 
Name Accession Description Interval E-value
USP-A-like cd23657
universal stress protein A and similar proteins; The universal stress protein UspA is a small ...
 4-136 2.22e-10

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: 54.62  E-value: 2.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320058663   4 YHHALVLINSSQDGVPLLEHAARMAEENGMRITIAHISTDYRALN--YVSDSLRDDQVSQEVIQAKALLNeLACTVSLPV 81
Cdd:cd23657     1 YKHILVAVDLSPESQSLVDKAVEIARENDAKLSLIHVDEDISEYYtgLIDVDIAALQDLESTMLEEALKN-LSELAGYPV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1320058663  82 DTLSLVTTRRFEDVETCVRQRQIDLIIAGHHNR-LLGVLSSHSLEYINHLTIDVLI 136
Cdd:cd23657    80 DHTFIGYGDLKEEILEVAKKHNVDLIVCGHHGDfGLSLLGSSARAVLNSAPCDVLI 135
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
4-136 1.27e-07

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 47.22  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320058663   4 YHHALVLINSSQDGVPLLEHAARMAEENGMRITIAHISTDYRALNYVSDSLRDDQVSqeviQAKALLNELACTVS---LP 80
Cdd:COG0589     2 YKRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEELEEELRE----EAEEALEEAAERLEeagVE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1320058663  81 VDTLsLVTTRRFEDVETCVRQRQIDLIIAGHHNR------LLGvlsSHSLEYINHLTIDVLI 136
Cdd:COG0589    78 VETV-VREGDPAEAILEAAEELDADLIVMGSRGRsglrrlLLG---SVAERVLRHAPCPVLV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 8-136 8.67e-07

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: 45.09  E-value: 8.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320058663   8 LVLINSSQDGVPLLEHAARMAEENGMRITIAHISTDYRALNYVSDSLRDDQVSQEVIQAKALLNELACTVSLPVDTLSLV 87
Cdd:pfam00582   2 LVAVDGSEESKRALEWAAELAKARGAELILLHVIDPPPSGAASLADESAEEEELELELAEAEALAAAAAAEAGGVKVEVV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1320058663  88 TTRRFEDVETC--VRQRQIDLIIAGHH--NRLLGVL-SSHSLEYINHLTIDVLI 136
Cdd:pfam00582  82 VVVGDPAEEILevAEEEDADLIVMGSRgrSGLSRLLlGSVAEYVLRHAPCPVLV 135
PRK15118 PRK15118
universal stress protein UspA;
4-136 2.42e-05

universal stress protein UspA;


Pssm-ID: 185073  Cd Length: 144  Bit Score: 41.41  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320058663   4 YHHALVLINSSQDGVPLLEHAARMAEENGMRITIAHISTDYRAL--NYVSDSLRDDQ--VSQEVIQAkalLNELACTVSL 79
Cdd:PRK15118    3 YKHILIAVDLSPESKVLVEKAVSMARPYNAKVSLIHVDVNYSDLytGLIDVNLGDMQkrISEETHHA---LTELSTNAGY 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1320058663  80 PVDTLSLVTTRRFEDVETCVRQRQIDLIIAGHHNRLLGVLSSHSLEYINHLTIDVLI 136
Cdd:PRK15118   80 PITETLSGSGDLGQVLVDAIKKYDMDLVVCGHHQDFWSKLMSSARQLINTVHVDMLI 136
 
Name Accession Description Interval E-value
USP-A-like cd23657
universal stress protein A and similar proteins; The universal stress protein UspA is a small ...
 4-136 2.22e-10

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: 54.62  E-value: 2.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320058663   4 YHHALVLINSSQDGVPLLEHAARMAEENGMRITIAHISTDYRALN--YVSDSLRDDQVSQEVIQAKALLNeLACTVSLPV 81
Cdd:cd23657     1 YKHILVAVDLSPESQSLVDKAVEIARENDAKLSLIHVDEDISEYYtgLIDVDIAALQDLESTMLEEALKN-LSELAGYPV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1320058663  82 DTLSLVTTRRFEDVETCVRQRQIDLIIAGHHNR-LLGVLSSHSLEYINHLTIDVLI 136
Cdd:cd23657    80 DHTFIGYGDLKEEILEVAKKHNVDLIVCGHHGDfGLSLLGSSARAVLNSAPCDVLI 135
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
4-136 1.27e-07

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 47.22  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320058663   4 YHHALVLINSSQDGVPLLEHAARMAEENGMRITIAHISTDYRALNYVSDSLRDDQVSqeviQAKALLNELACTVS---LP 80
Cdd:COG0589     2 YKRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEELEEELRE----EAEEALEEAAERLEeagVE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1320058663  81 VDTLsLVTTRRFEDVETCVRQRQIDLIIAGHHNR------LLGvlsSHSLEYINHLTIDVLI 136
Cdd:COG0589    78 VETV-VREGDPAEAILEAAEELDADLIVMGSRGRsglrrlLLG---SVAERVLRHAPCPVLV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 8-136 8.67e-07

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: 45.09  E-value: 8.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320058663   8 LVLINSSQDGVPLLEHAARMAEENGMRITIAHISTDYRALNYVSDSLRDDQVSQEVIQAKALLNELACTVSLPVDTLSLV 87
Cdd:pfam00582   2 LVAVDGSEESKRALEWAAELAKARGAELILLHVIDPPPSGAASLADESAEEEELELELAEAEALAAAAAAEAGGVKVEVV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1320058663  88 TTRRFEDVETC--VRQRQIDLIIAGHH--NRLLGVL-SSHSLEYINHLTIDVLI 136
Cdd:pfam00582  82 VVVGDPAEEILevAEEEDADLIVMGSRgrSGLSRLLlGSVAEYVLRHAPCPVLV 135
PRK15118 PRK15118
universal stress protein UspA;
4-136 2.42e-05

universal stress protein UspA;


Pssm-ID: 185073  Cd Length: 144  Bit Score: 41.41  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320058663   4 YHHALVLINSSQDGVPLLEHAARMAEENGMRITIAHISTDYRAL--NYVSDSLRDDQ--VSQEVIQAkalLNELACTVSL 79
Cdd:PRK15118    3 YKHILIAVDLSPESKVLVEKAVSMARPYNAKVSLIHVDVNYSDLytGLIDVNLGDMQkrISEETHHA---LTELSTNAGY 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1320058663  80 PVDTLSLVTTRRFEDVETCVRQRQIDLIIAGHHNRLLGVLSSHSLEYINHLTIDVLI 136
Cdd:PRK15118   80 PITETLSGSGDLGQVLVDAIKKYDMDLVVCGHHQDFWSKLMSSARQLINTVHVDMLI 136
PRK10116 PRK10116
universal stress protein UspC; Provisional
 4-136 2.17e-04

universal stress protein UspC; Provisional


Pssm-ID: 182248  Cd Length: 142  Bit Score: 38.92  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320058663   4 YHHALVLINSSQDGVPLLEHAARMAEENGMRITIAHISTDYRALNYVSDSLRDD--QVSQEviQAKALLNELACTVSLPV 81
Cdd:PRK10116    3 YSNILVAVAVTPESQQLLAKAVSIARPVNGKISLITLASDPEMYNQFAAPMLEDlrSVMQE--ETQSFLDKLIQDADYPI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1320058663  82 DTLSLVTTRRFEDVETCVRQRQIDLIIAGHHN-RLLGVLSSHSLEYINHLTIDVLI 136
Cdd:PRK10116   81 EKTFIAYGELSEHILEVCRKHHFDLVICGNHNhSFFSRASCSAKRVIASSEVDVLL 136
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
 8-136 3.19e-04

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: 38.10  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320058663   8 LVLINSSQDGVPLLEHAARMAEENGMRITIAHISTDYRAlnYVSDSLRDDQVSQEVIQAKALLNELACTVSLPVDTLS-- 85
Cdd:cd00293     3 LVAVDGSEESERALEWALELAKRPGAELTLLHVVDPPPS--SSLSGGLEELADELKEEAEELLEEAKKLAEEAGVEVEti 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1320058663  86 LVTTRRFEDVETCVRQRQIDLIIAGHH------NRLLGvlsSHSLEYINHLTIDVLI 136
Cdd:cd00293    81 VVEGDPAEAILEEAKELGADLIVMGSRgrsglkRLLLG---SVSEYVLRHAPCPVLV 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH