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Conserved domains on  [gi|495624371|ref|WP_008348950|]
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MULTISPECIES: universal stress protein [Bacillus]

Protein Classification

universal stress protein( domain architecture ID 10001747)

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

CATH:  3.40.50.620
Gene Ontology:  GO:0042802
PubMed:  23745136|9405142|12732303
SCOP:  8083864

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
5-167 8.57e-35

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


:

Pssm-ID: 440354  Cd Length: 136  Bit Score: 118.48  E-value: 8.57e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371   5 DRMVVAFDGHEDSKKALKKAIALAKTLHAKLTIAYAHDGKSSRqvfdaprpmtggayigggmadlqtPPVYVPHDEQqsp 84
Cdd:COG0589    3 KRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSA------------------------AAGPEELEEE--- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371  85 liFEDHTEEVVAEARMLLNEEQFEAAIEIVEGEPAEAIIEYAEEISADLIVMGARDQSRLKKMLFGSVSEKLSSKSDIPV 164
Cdd:COG0589   56 --LREEAEEALEEAAERLEEAGVEVETVVREGDPAEAILEAAEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPV 133


                 ...
gi 495624371 165 LIV 167
Cdd:COG0589  134 LVV 136
 
Name Accession Description Interval E-value
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
5-167 8.57e-35

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 118.48  E-value: 8.57e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371   5 DRMVVAFDGHEDSKKALKKAIALAKTLHAKLTIAYAHDGKSSRqvfdaprpmtggayigggmadlqtPPVYVPHDEQqsp 84
Cdd:COG0589    3 KRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSA------------------------AAGPEELEEE--- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371  85 liFEDHTEEVVAEARMLLNEEQFEAAIEIVEGEPAEAIIEYAEEISADLIVMGARDQSRLKKMLFGSVSEKLSSKSDIPV 164
Cdd:COG0589   56 --LREEAEEALEEAAERLEEAGVEVETVVREGDPAEAILEAAEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPV 133


                 ...
gi 495624371 165 LIV 167
Cdd:COG0589  134 LVV 136
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
 6-167 1.56e-33

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: 115.14  E-value: 1.56e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371   6 RMVVAFDGHEDSKKALKKAIALAKTLHAKLTIAYAHDGKSSRQVFDAPRPMTGGayigggmadlqtppvyvphdeqqspl 85
Cdd:cd00293    1 KILVAVDGSEESERALEWALELAKRPGAELTLLHVVDPPPSSSLSGGLEELADE-------------------------- 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371  86 iFEDHTEEVVAEARMLLNEEQFEAAIEIVEGEPAEAIIEYAEEISADLIVMGARDQSRLKKMLFGSVSEKLSSKSDIPVL 165
Cdd:cd00293   55 -LKEEAEELLEEAKKLAEEAGVEVETIVVEGDPAEAILEEAKELGADLIVMGSRGRSGLKRLLLGSVSEYVLRHAPCPVL 133


                 ..
gi 495624371 166 IV 167
Cdd:cd00293  134 VV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 7-168 7.89e-29

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: 103.26  E-value: 7.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371    7 MVVAFDGHEDSKKALKKAIALAKTLHAKLTIAYAHDgkssrqvfdaprpmtggayigggmaDLQTPPVYVPHDEQQSPLI 86
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAELILLHVID-------------------------PPPSGAASLADESAEEEEL 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371   87 FEDHTEEVVAEARMLLNEEQFEAAIEIVEGEPAEAIIEYAEEISADLIVMGARDQSRLKKMLFGSVSEKLSSKSDIPVLI 166
Cdd:pfam00582  56 ELELAEAEALAAAAAAEAGGVKVEVVVVVGDPAEEILEVAEEEDADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLV 135


                  ..
gi 495624371  167 VK 168
Cdd:pfam00582 136 VR 137
PRK11175 PRK11175
universal stress protein UspE; Provisional
 118-168 7.25e-06

universal stress protein UspE; Provisional


Pssm-ID: 236871 [Multi-domain]  Cd Length: 305  Bit Score: 44.48  E-value: 7.25e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495624371 118 PAEAIIEYAEEISADLIVMGARDQSRLKKMLFGSVSEKLSSKSDIPVLIVK 168
Cdd:PRK11175  95 PFEAIIQEVIAGGHDLVVKMTHQHDKLESVIFTPTDWHLLRKCPCPVLMVK 145
 
Name Accession Description Interval E-value
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
5-167 8.57e-35

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 118.48  E-value: 8.57e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371   5 DRMVVAFDGHEDSKKALKKAIALAKTLHAKLTIAYAHDGKSSRqvfdaprpmtggayigggmadlqtPPVYVPHDEQqsp 84
Cdd:COG0589    3 KRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSA------------------------AAGPEELEEE--- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371  85 liFEDHTEEVVAEARMLLNEEQFEAAIEIVEGEPAEAIIEYAEEISADLIVMGARDQSRLKKMLFGSVSEKLSSKSDIPV 164
Cdd:COG0589   56 --LREEAEEALEEAAERLEEAGVEVETVVREGDPAEAILEAAEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPV 133


                 ...
gi 495624371 165 LIV 167
Cdd:COG0589  134 LVV 136
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
 6-167 1.56e-33

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: 115.14  E-value: 1.56e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371   6 RMVVAFDGHEDSKKALKKAIALAKTLHAKLTIAYAHDGKSSRQVFDAPRPMTGGayigggmadlqtppvyvphdeqqspl 85
Cdd:cd00293    1 KILVAVDGSEESERALEWALELAKRPGAELTLLHVVDPPPSSSLSGGLEELADE-------------------------- 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371  86 iFEDHTEEVVAEARMLLNEEQFEAAIEIVEGEPAEAIIEYAEEISADLIVMGARDQSRLKKMLFGSVSEKLSSKSDIPVL 165
Cdd:cd00293   55 -LKEEAEELLEEAKKLAEEAGVEVETIVVEGDPAEAILEEAKELGADLIVMGSRGRSGLKRLLLGSVSEYVLRHAPCPVL 133


                 ..
gi 495624371 166 IV 167
Cdd:cd00293  134 VV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 7-168 7.89e-29

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: 103.26  E-value: 7.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371    7 MVVAFDGHEDSKKALKKAIALAKTLHAKLTIAYAHDgkssrqvfdaprpmtggayigggmaDLQTPPVYVPHDEQQSPLI 86
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAELILLHVID-------------------------PPPSGAASLADESAEEEEL 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371   87 FEDHTEEVVAEARMLLNEEQFEAAIEIVEGEPAEAIIEYAEEISADLIVMGARDQSRLKKMLFGSVSEKLSSKSDIPVLI 166
Cdd:pfam00582  56 ELELAEAEALAAAAAAEAGGVKVEVVVVVGDPAEEILEVAEEEDADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLV 135


                  ..
gi 495624371  167 VK 168
Cdd:pfam00582 136 VR 137
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
 6-168 5.25e-25

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: 93.84  E-value: 5.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371   6 RMVVAFDGHEDSKKALKKAIalaKTLHA---KLTIAYAHdgkssrqvfdaPRPMTGGAYIGGGMADLQTPPVYVPHDeqq 82
Cdd:cd23659    2 KVLIAVDGSEESEYALEWAL---ENLHRpgdEVVLLHVI-----------EPPSLPAASLGSGSEEWEALEEEAREK--- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371  83 splifedhTEEVVAEARMLLNEE-QFEAAIEIVEGEPAEAIIEYAEEISADLIVMGARDQSRLKKMLFGSVSEKLSSKSD 161
Cdd:cd23659   65 --------AEKLLEKYEKKLKEEkGIKVKVEVVAGDPGEVICKAAEELKADLIVMGSRGLGALKRTLLGSVSDYVVHHSP 136


                 ....*..
gi 495624371 162 IPVLIVK 168
Cdd:cd23659  137 CPVLVVR 143
USP_Rv2623_repeat2 cd23661
universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis ...
 88-168 1.05e-08

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: 50.97  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371  88 EDHTEEVVAEARMLLNEEQFEAAI--EIVEGEPAEAIIEYAEEisADLIVMGARDQSRLKKMLFGSVSEKLSSKSDIPVL 165
Cdd:cd23661   53 EQDQERMLAERLAGWQERYPDVHVhkVVVRDRPARVLLEASER--AQLVVVGSHGRGGFAGMLLGSVSRAVLHSAPCPVI 130


                 ...
gi 495624371 166 IVK 168
Cdd:cd23661  131 VVR 133
USP_KdpD-like cd01987
USP domain of the osmosensitive K+ channel histidine kinase family; The KdpDE two component ...
 6-167 1.04e-07

USP domain of the osmosensitive K+ channel histidine kinase family; The KdpDE two component system is widespread in bacteria and archaea; it controls potassium homeostasis and virulence by regulating the transcription of multiple genes, including a kdpFABC operon, which encodes a high-affinity P-type ATPase transporter. The KdpD histidine kinase (HK, EC:2.7.13.3) contain an N-terminal sensory cytoplasmic region (NTR) composed of KdpD' and universal stress protein (USP) domains, a canonical transmembrane domain, and a cytoplasmic C-terminal region with a transmitter GAF domain and an EnvZ-like catalytic HK domain. Proteins containing the USP domain are induced by many environmental stressors such as nutrient starvation, drought, extreme temperatures, high salinity, and the presence of uncouplers, antibiotics, and metals. It enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity.


Pssm-ID: 467491 [Multi-domain]  Cd Length: 124  Bit Score: 48.01  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371   6 RMVVAFDGHEDSKKALKKAIALAKTLHAKLTIAYAHDGKSSRQvfdaprpmtggayigggmadlqtppvyvphDEQQspl 85
Cdd:cd01987    1 RILVCISSSPTSEKLIRRAARLAERLNGELTAVYVETPEESRL------------------------------DEES--- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371  86 ifedhtEEVVAEARMLLneEQFEAAIEIVEGE-PAEAIIEYAEEISADLIVMGARDQSRLKKMLFGSVSEKLSSK-SDIP 163
Cdd:cd01987   48 ------QRRLLTNLKLA--EELGAEVVSVEGDdVAEAIVEFARERNVTQIVLGQSRRRRWRRLFKGSLVDRLLREaPNID 119


                 ....
gi 495624371 164 VLIV 167
Cdd:cd01987  120 VHIV 123
USP_Rv2623_repeat1 cd23944
universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis ...
 88-167 1.72e-07

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: 47.78  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371  88 EDHTEEVVAEARMLLNE---EQFEAAI--EIVEGEPAEAIIEYAEEisADLIVMGARDQSRLKKMLFGSVSEKLSSKSDI 162
Cdd:cd23944   57 QDEARQVIEQARKVAEEasgEGPPVKVetEIVPGSPVPTLVEASRD--ATMVVVGSRGIGALAGLLLGSVSTSLVRHAHC 134


                 ....*
gi 495624371 163 PVLIV 167
Cdd:cd23944  135 PVAVI 139
PRK11175 PRK11175
universal stress protein UspE; Provisional
 118-168 7.25e-06

universal stress protein UspE; Provisional


Pssm-ID: 236871 [Multi-domain]  Cd Length: 305  Bit Score: 44.48  E-value: 7.25e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495624371 118 PAEAIIEYAEEISADLIVMGARDQSRLKKMLFGSVSEKLSSKSDIPVLIVK 168
Cdd:PRK11175  95 PFEAIIQEVIAGGHDLVVKMTHQHDKLESVIFTPTDWHLLRKCPCPVLMVK 145
USP-E_repeat1 cd23943
Universal stress protein E, repeat 1; UspE is a tandem-type USP that consists of two USP ...
 7-168 4.81e-05

Universal stress protein E, repeat 1; 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: 467508  Cd Length: 143  Bit Score: 41.38  E-value: 4.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371   7 MVVAFDGHEDSKKALKKAIALAKTLHAKLtiayahdgKSSRQVFDAPRPMTGgayigggmadLQTPpvyvphdEQQSPL- 85
Cdd:cd23943    4 MLVVIDPNQDDQPALRRAVYLVQRIGGKI--------KAFLPIYDLSYEMTT----------LLSP-------DERTAMr 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371  86 --IFEDHTEEVVAEARMLLNEEqFEAAIEIV-EGEPAEAIIEYAEEISADLIVMGARDQSRLKKMLFGSVSEKLSSKSDI 162
Cdd:cd23943   59 qgVISQRTAWIREQAKYYLEAG-IPIEIKVVwHNRPFEAIIQEVIAGNHDLVLKMAHQHDRLESLIFTPTDWHLLRKCPS 137


                 ....*.
gi 495624371 163 PVLIVK 168
Cdd:cd23943  138 PVWMVK 143
USP-E_repeat2 cd23660
Universal stress protein E, repeat 2; UspE is a tandem-type USP that consists of two USP ...
 5-154 5.59e-05

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: 41.10  E-value: 5.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371   5 DRMVVAFD-GHEDSK------KALKKAIALAKTLHAKLTIAYAHDgkssrqvfdaprpmtggayigggmadlQTPPVYVP 77
Cdd:cd23660    2 GRILVAVDpSNEEEYhedlnlRLIELAYSLAAQLKAELHLVSAWP---------------------------VTPENIAI 54

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495624371  78 HDEQQSPLIFEDHTEEVVAEA-RMLLNEEQF-EAAIEIVEGEPAEAIIEYAEEISADLIVMGARDQSRLKKMLFGSVSE 154
Cdd:cd23660   55 ELPEFDPTEYVDAIRGRHLEAmKALRQKFGIdEEQTHVLEGLPEEVIPDFAEELDADIVVLGTVARTGLSGALIGNTAE 133
USP-A-like cd23657
universal stress protein A and similar proteins; The universal stress protein UspA is a small ...
 9-168 6.37e-04

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: 38.06  E-value: 6.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371   9 VAFDGHEDSKKALKKAIALAKTLHAKLTIAYAHDGKSSrqvfdaprpmtggAYIGGGMADLQTppvyvphdeqqspliFE 88
Cdd:cd23657    6 VAVDLSPESQSLVDKAVEIARENDAKLSLIHVDEDISE-------------YYTGLIDVDIAA---------------LQ 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624371  89 DHTEEVVAEARMLLNE-------EQFeaaieIVEGEPAEAIIEYAEEISADLIVMGARDQSRLKKMlfGSVSEKLSSKSD 161
Cdd:cd23657   58 DLESTMLEEALKNLSElagypvdHTF-----IGYGDLKEEILEVAKKHNVDLIVCGHHGDFGLSLL--GSSARAVLNSAP 130


                 ....*..
gi 495624371 162 IPVLIVK 168
Cdd:cd23657  131 CDVLIVP 137
PRK15456 PRK15456
universal stress protein UspG; Provisional
 116-168 9.61e-03

universal stress protein UspG; Provisional


Pssm-ID: 185353  Cd Length: 142  Bit Score: 34.92  E-value: 9.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495624371 116 GEPAEAIIEYAEEISADLIVMGARDQSrLKKMLFGSVSEKLSSKSDIPVLIVK 168
Cdd:PRK15456  91 GSVRDEVNELAEELGADVVVIGSRNPS-ISTHLLGSNASSVIRHANLPVLVVR 142
 
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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