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Conserved domains on  [gi|757600353|ref|WP_042847987|]
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MULTISPECIES: universal stress protein [Providencia]

Protein Classification

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

AANH (adenine nucleotide alpha hydrolase) family protein

Graphical summary

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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 ...
 1-145 2.58e-42

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 PRK15005:

Pssm-ID: 469708 [Multi-domain]  Cd Length: 144  Bit Score: 137.24  E-value: 2.58e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600353   1 MYNTILVPIDVTEDALTNLLVPHVNSLQKLNNATVHFLAVTaPISNYLRYGGTILPGDFPDDAKQAELILAELKEKIKLF 80
Cdd:PRK15005   1 MNRTILVPIDISDSELTQRVISHVEAEAKIDDAEVHFLTVI-PSLPYYASLGLAYSAELPAMDDLKAEAKSQLEEIIKKF 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757600353  81 SVPADKVHAKATIGSVKDEIIAVAEDINADIILLGSRRPSMSTYLLGSNAASVVRYAKTSVLVVR 145
Cdd:PRK15005  80 KLPTDRVHVHVEEGSPKDRILELAKKIPADMIIIASHRPDITTYLLGSNAAAVVRHAECSVLVVR 144
 
Name Accession Description Interval E-value
PRK15005 PRK15005
universal stress protein UspF;
1-145 2.58e-42

universal stress protein UspF;


Pssm-ID: 184967 [Multi-domain]  Cd Length: 144  Bit Score: 137.24  E-value: 2.58e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600353   1 MYNTILVPIDVTEDALTNLLVPHVNSLQKLNNATVHFLAVTaPISNYLRYGGTILPGDFPDDAKQAELILAELKEKIKLF 80
Cdd:PRK15005   1 MNRTILVPIDISDSELTQRVISHVEAEAKIDDAEVHFLTVI-PSLPYYASLGLAYSAELPAMDDLKAEAKSQLEEIIKKF 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757600353  81 SVPADKVHAKATIGSVKDEIIAVAEDINADIILLGSRRPSMSTYLLGSNAASVVRYAKTSVLVVR 145
Cdd:PRK15005  80 KLPTDRVHVHVEEGSPKDRILELAKKIPADMIIIASHRPDITTYLLGSNAAAVVRHAECSVLVVR 144
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
1-144 2.87e-26

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 95.76  E-value: 2.87e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600353   1 MYNTILVPIDVTEDALtnLLVPHVNSLQKLNNATVHFLAVTAPISnylryGGTILPGDFPDDA-KQAELILAELKEKIKL 79
Cdd:COG0589    1 MYKRILVPTDGSEEAE--RALEYAAELAKALGAELHLLHVVDPPP-----SAAAGPEELEEELrEEAEEALEEAAERLEE 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757600353  80 FSVPadkVHAKATIGSVKDEIIAVAEDINADIILLGSR-RPSMSTYLLGSNAASVVRYAKTSVLVV 144
Cdd:COG0589   74 AGVE---VETVVREGDPAEAILEAAEELDADLIVMGSRgRSGLRRLLLGSVAERVLRHAPCPVLVV 136
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
 4-144 3.62e-19

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: 77.77  E-value: 3.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600353   4 TILVPIDVTEDAltNLLVPHVNSLQKLNNATVHFLAVTAPISNYLRYGGtiLPGDFPDDAKQAELILAELKekiKLFSVP 83
Cdd:cd00293    1 KILVAVDGSEES--ERALEWALELAKRPGAELTLLHVVDPPPSSSLSGG--LEELADELKEEAEELLEEAK---KLAEEA 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757600353  84 ADKVHAKATIGSVKDEIIAVAEDINADIILLGSRRPS-MSTYLLGSNAASVVRYAKTSVLVV 144
Cdd:cd00293   74 GVEVETIVVEGDPAEAILEEAKELGADLIVMGSRGRSgLKRLLLGSVSEYVLRHAPCPVLVV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 5-145 6.18e-17

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: 72.06  E-value: 6.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600353    5 ILVPIDVTEDALtnLLVPHVNSLQKLNNATVHFLAVTAPISnylRYGGTILPGDFPDDAKQAELILAELKEKIKLFSVPA 84
Cdd:pfam00582   1 ILVAVDGSEESK--RALEWAAELAKARGAELILLHVIDPPP---SGAASLADESAEEEELELELAEAEALAAAAAAEAGG 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757600353   85 DKVHAKATIGSVKDEIIAVAEDINADIILLGSR-RPSMSTYLLGSNAASVVRYAKTSVLVVR 145
Cdd:pfam00582  76 VKVEVVVVVGDPAEEILEVAEEEDADLIVMGSRgRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
 
Name Accession Description Interval E-value
PRK15005 PRK15005
universal stress protein UspF;
1-145 2.58e-42

universal stress protein UspF;


Pssm-ID: 184967 [Multi-domain]  Cd Length: 144  Bit Score: 137.24  E-value: 2.58e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600353   1 MYNTILVPIDVTEDALTNLLVPHVNSLQKLNNATVHFLAVTaPISNYLRYGGTILPGDFPDDAKQAELILAELKEKIKLF 80
Cdd:PRK15005   1 MNRTILVPIDISDSELTQRVISHVEAEAKIDDAEVHFLTVI-PSLPYYASLGLAYSAELPAMDDLKAEAKSQLEEIIKKF 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757600353  81 SVPADKVHAKATIGSVKDEIIAVAEDINADIILLGSRRPSMSTYLLGSNAASVVRYAKTSVLVVR 145
Cdd:PRK15005  80 KLPTDRVHVHVEEGSPKDRILELAKKIPADMIIIASHRPDITTYLLGSNAAAVVRHAECSVLVVR 144
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
1-144 2.87e-26

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 95.76  E-value: 2.87e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600353   1 MYNTILVPIDVTEDALtnLLVPHVNSLQKLNNATVHFLAVTAPISnylryGGTILPGDFPDDA-KQAELILAELKEKIKL 79
Cdd:COG0589    1 MYKRILVPTDGSEEAE--RALEYAAELAKALGAELHLLHVVDPPP-----SAAAGPEELEEELrEEAEEALEEAAERLEE 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757600353  80 FSVPadkVHAKATIGSVKDEIIAVAEDINADIILLGSR-RPSMSTYLLGSNAASVVRYAKTSVLVV 144
Cdd:COG0589   74 AGVE---VETVVREGDPAEAILEAAEELDADLIVMGSRgRSGLRRLLLGSVAERVLRHAPCPVLVV 136
PRK15456 PRK15456
universal stress protein UspG; Provisional
 1-145 2.89e-24

universal stress protein UspG; Provisional


Pssm-ID: 185353  Cd Length: 142  Bit Score: 91.15  E-value: 2.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600353   1 MYNTILVPIDVTEDALTNLLVPHVNSLQKlNNATVHFLAVtapisnylryggtiLPGD-------FPDDAKQAELIL--- 70
Cdd:PRK15456   1 MYKTIIMPVDVFEMELSDKAVRHAEFLAQ-DDGVIHLLHV--------------LPGSaslslhrFAADVRRFEEHLqhe 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757600353  71 --AELKEKIKLFSVPADKVHAKATIGSVKDEIIAVAEDINADIILLGSRRPSMSTYLLGSNAASVVRYAKTSVLVVR 145
Cdd:PRK15456  66 aeERLQTMVSHFTIDPSRIKQHVRFGSVRDEVNELAEELGADVVVIGSRNPSISTHLLGSNASSVIRHANLPVLVVR 142
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
 4-144 3.62e-19

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: 77.77  E-value: 3.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600353   4 TILVPIDVTEDAltNLLVPHVNSLQKLNNATVHFLAVTAPISNYLRYGGtiLPGDFPDDAKQAELILAELKekiKLFSVP 83
Cdd:cd00293    1 KILVAVDGSEES--ERALEWALELAKRPGAELTLLHVVDPPPSSSLSGG--LEELADELKEEAEELLEEAK---KLAEEA 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757600353  84 ADKVHAKATIGSVKDEIIAVAEDINADIILLGSRRPS-MSTYLLGSNAASVVRYAKTSVLVV 144
Cdd:cd00293   74 GVEVETIVVEGDPAEAILEEAKELGADLIVMGSRGRSgLKRLLLGSVSEYVLRHAPCPVLVV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 5-145 6.18e-17

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: 72.06  E-value: 6.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600353    5 ILVPIDVTEDALtnLLVPHVNSLQKLNNATVHFLAVTAPISnylRYGGTILPGDFPDDAKQAELILAELKEKIKLFSVPA 84
Cdd:pfam00582   1 ILVAVDGSEESK--RALEWAAELAKARGAELILLHVIDPPP---SGAASLADESAEEEELELELAEAEALAAAAAAEAGG 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757600353   85 DKVHAKATIGSVKDEIIAVAEDINADIILLGSR-RPSMSTYLLGSNAASVVRYAKTSVLVVR 145
Cdd:pfam00582  76 VKVEVVVVVGDPAEEILEVAEEEDADLIVMGSRgRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
 4-145 1.30e-10

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: 55.70  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600353   4 TILVPIDVTED-------ALTNLLVPhvnslqklnNATVHFLAVTAPISNYLRYGGTIlPGDFPDDAKQAELILAELKEK 76
Cdd:cd23659    2 KVLIAVDGSEEseyalewALENLHRP---------GDEVVLLHVIEPPSLPAASLGSG-SEEWEALEEEAREKAEKLLEK 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757600353  77 IKLFSVPADKVHAKATI--GSVKDEIIAVAEDINADIILLGSR-RPSMSTYLLGSNAASVVRYAKTSVLVVR 145
Cdd:cd23659   72 YEKKLKEEKGIKVKVEVvaGDPGEVICKAAEELKADLIVMGSRgLGALKRTLLGSVSDYVVHHSPCPVLVVR 143
USP-A-like cd23657
universal stress protein A and similar proteins; The universal stress protein UspA is a small ...
 2-145 2.90e-09

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: 51.92  E-value: 2.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600353   2 YNTILVPIDVTEDAltNLLVPHVNSLQKLNNATVHFLAVTAPISNYlrYGGTIlpgdFPDDAKQAELILAELKEKIKLFS 81
Cdd:cd23657    1 YKHILVAVDLSPES--QSLVDKAVEIARENDAKLSLIHVDEDISEY--YTGLI----DVDIAALQDLESTMLEEALKNLS 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757600353  82 ----VPADKVHAKAtiGSVKDEIIAVAEDINADIILLGSRRPSMSTyLLGSNAASVVRYAKTSVLVVR 145
Cdd:cd23657   73 elagYPVDHTFIGY--GDLKEEILEVAKKHNVDLIVCGHHGDFGLS-LLGSSARAVLNSAPCDVLIVP 137
USP-E_repeat2 cd23660
Universal stress protein E, repeat 2; UspE is a tandem-type USP that consists of two USP ...
 4-143 1.13e-07

Universal stress protein E, repeat 2; UspE is a tandem-type USP that consists of two USP domains. The UspE expression levels of Escherichia coli become elevated in response to oxidative stress and DNA damaging agents, including exposure to mitomycin C, cadmium, and hydrogen peroxide. 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.


Pssm-ID: 467506  Cd Length: 148  Bit Score: 48.03  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600353   4 TILVPIDV-----TEDALTNLLVPHVNSLQKLNNATVHFLAV--TAPIsNYLRYGGTILPGDFPDDAKQAELILaeLKEK 76
Cdd:cd23660    3 RILVAVDPsneeeYHEDLNLRLIELAYSLAAQLKAELHLVSAwpVTPE-NIAIELPEFDPTEYVDAIRGRHLEA--MKAL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757600353  77 IKLFSVPADKVHAKAtiGSVKDEIIAVAEDINADIILLGS-RRPSMSTYLLGSNAASVVRYAKTSVLV 143
Cdd:cd23660   80 RQKFGIDEEQTHVLE--GLPEEVIPDFAEELDADIVVLGTvARTGLSGALIGNTAEHVLDHLNCDLLA 145
USP_NhaS5_C cd01988
C-terminal USP domain(s) of Na(+)/H(+) antiporter NhaS5 and similar proteins; Na(+)/H(+) ...
 58-145 6.85e-04

C-terminal USP domain(s) of Na(+)/H(+) antiporter NhaS5 and similar proteins; Na(+)/H(+) exchange proteins eject protons from cells, effectively eliminating excess acid from actively metabolizing cells. Na(+)/H(+) exchange activity is also crucial for the regulation of cell volume, and for the reabsorption of NaCl across renal, intestinal, and other epithelia. These antiporters exchange Na(+) for H(+) in an electroneutral manner, and this activity is carried out by a family of Na(+)/H(+) exchangers, or NHEs, which are known to be present in both prokaryotic and eukaryotic cells. These exchangers are highly-regulated (glyco)phosphoproteins, which, based on their primary structure, appear to contain 10-12 membrane-spanning regions (M) at the N-terminus and a large cytoplasmic region at the C-terminus. The transmembrane regions M3-M12 share identity with other members of the family. The M6 and M7 regions are highly conserved. This is thought to be the region that is involved in the transport of sodium and hydrogen ions. The C-terminal region contains one or two domains that show homology with universal stress protein (USP), 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.


Pssm-ID: 467492  Cd Length: 125  Bit Score: 37.48  E-value: 6.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600353  58 DFPDDAKQAELILAELKEKIKLFSVPADKVHakatiGSVKDEIIAVAEDINADIILLGSRRPSMSTYLLGSNAASVVRYA 137
Cdd:cd01988   43 DDKELEQAEQRFEELMELLNGVNVHPIVRIS-----HSVAARVTAREAKSFADLIVMGWRRTFLGNVLLGSTIDKVLMKA 117


                 ....*...
gi 757600353 138 KTSVLVVR 145
Cdd:cd01988  118 PTDVAVTR 125
USP_Rv2623_repeat1 cd23944
universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis ...
 39-145 1.17e-03

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: 37.00  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600353  39 AVTAPISNYLryGGTILPGDFPDDAKQAELILAELKEKIK--LFSVPADKVHAKATIGSVKDEIIAVAEDinADIILLGS 116
Cdd:cd23944   35 VVPPVVVSWP--EGPRPAEVLDWQQDEARQVIEQARKVAEeaSGEGPPVKVETEIVPGSPVPTLVEASRD--ATMVVVGS 110

                         90       100       110
                 ....*....|....*....|....*....|
gi 757600353 117 R-RPSMSTYLLGSNAASVVRYAKTSVLVVR 145
Cdd:cd23944  111 RgIGALAGLLLGSVSTSLVRHAHCPVAVIH 140
PRK11175 PRK11175
universal stress protein UspE; Provisional
 5-145 6.04e-03

universal stress protein UspE; Provisional


Pssm-ID: 236871 [Multi-domain]  Cd Length: 305  Bit Score: 35.62  E-value: 6.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600353   5 ILVPIDV-----TEDALTNLLVPHVNSL-QKLNNATVHFlaVTApisnylrYGGTI------LPgDF-PD---DA--KQA 66
Cdd:PRK11175 155 ILVAVNVaseepYHDALNEKLVEEAIDLaEQLNHAEVHL--VNA-------YPVTPiniaieLP-EFdPSvynDAirGQH 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600353  67 ELILAELKEKiklFSVPADKVHAKAtiGSVKDEIIAVAEDINADIILLGS-RRPSMSTYLLGSNAASVVRYAKTSVLVVR 145
Cdd:PRK11175 225 LLAMKALRQK---FGIDEEQTHVEE--GLPEEVIPDLAEHLDAELVILGTvGRTGLSAAFLGNTAEHVIDHLNCDLLAIK 299
 
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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