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Conserved domains on  [gi|1946572779|ref|WP_198182842|]
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universal stress protein [Bifidobacterium choladohabitans]

Protein Classification

universal stress protein( domain architecture ID 10785635)

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
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
7-142 3.09e-24

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


:

Pssm-ID: 440354  Cd Length: 136  Bit Score: 96.14  E-value: 3.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779   7 VLVGVDGSDASYKAAWWAANYAKHAGLTLQIVCAYSLPSYAAVSFDATYTTMGDDvaahndAQEILSKAKAIADEQGVGA 86
Cdd:COG0589     5 ILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEELEEELREE------AEEALEEAAERLEEAGVEV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1946572779  87 ATLIVTGDPSSVFVELSR--NYRLIVIGNRGKGGLAERLLGTTSSSLPAYAYCPIVVV 142
Cdd:COG0589    79 ETVVREGDPAEAILEAAEelDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
AANH_superfamily super family cl00292
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ...
 161-292 4.30e-23

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 cd23661:

Pssm-ID: 469708 [Multi-domain]  Cd Length: 133  Bit Score: 92.96  E-value: 4.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779 161 VAVGSDESKWGLKALQIAAAFADSWNAELDVMSAVPNIsGLTGTGSAEERSVMDSYLDDLNTRIEPLMKTYPDLRINKTV 240
Cdd:cd23661     2 VVVGVDGSPASELATEIAFDEASRRGVDLVALHAWSDM-GPGGFLGIDWRESEQDQERMLAERLAGWQERYPDVHVHKVV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1946572779 241 VPGSAVEALTQASKTHDVVVVGSRGRGGFTGLLLGSTSQGLLQHAVSPVYVV 292
Cdd:cd23661    81 VRDRPARVLLEASERAQLVVVGSHGRGGFAGMLLGSVSRAVLHSAPCPVIVV 132
 
Name Accession Description Interval E-value
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
7-142 3.09e-24

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 96.14  E-value: 3.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779   7 VLVGVDGSDASYKAAWWAANYAKHAGLTLQIVCAYSLPSYAAVSFDATYTTMGDDvaahndAQEILSKAKAIADEQGVGA 86
Cdd:COG0589     5 ILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEELEEELREE------AEEALEEAAERLEEAGVEV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1946572779  87 ATLIVTGDPSSVFVELSR--NYRLIVIGNRGKGGLAERLLGTTSSSLPAYAYCPIVVV 142
Cdd:COG0589    79 ETVVREGDPAEAILEAAEelDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
USP_Rv2623_repeat2 cd23661
universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis ...
 161-292 4.30e-23

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: 92.96  E-value: 4.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779 161 VAVGSDESKWGLKALQIAAAFADSWNAELDVMSAVPNIsGLTGTGSAEERSVMDSYLDDLNTRIEPLMKTYPDLRINKTV 240
Cdd:cd23661     2 VVVGVDGSPASELATEIAFDEASRRGVDLVALHAWSDM-GPGGFLGIDWRESEQDQERMLAERLAGWQERYPDVHVHKVV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1946572779 241 VPGSAVEALTQASKTHDVVVVGSRGRGGFTGLLLGSTSQGLLQHAVSPVYVV 292
Cdd:cd23661    81 VRDRPARVLLEASERAQLVVVGSHGRGGFAGMLLGSVSRAVLHSAPCPVIVV 132
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
158-292 6.76e-23

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 92.68  E-value: 6.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779 158 IKRVAVGSDESKWGLKALQIAAAFADSWNAELDVMSAVPNISGLTGTGSAEERSVMD---SYLDDLNTRIEPLmktypDL 234
Cdd:COG0589     2 YKRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEELEEELREeaeEALEEAAERLEEA-----GV 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779 235 RINKTVVPGSAVEALTQASKTH--DVVVVGSRGRGGFTGLLLGSTSQGLLQHAVSPVYVV 292
Cdd:COG0589    77 EVETVVREGDPAEAILEAAEELdaDLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
USP_Rv2623_repeat1 cd23944
universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis ...
 7-143 4.06e-22

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: 90.54  E-value: 4.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779   7 VLVGVDGSDASYKAAWWAANYAKHAGLTLQIVCAYS--LPSYAAVSFdatYTTMGDDVAAHndAQEILSKAKAIADE--- 81
Cdd:cd23944     2 IIVGVDGSPASDAAVRWAAREAQLRQIPLTLVHVVPpvVVSWPEGPR---PAEVLDWQQDE--ARQVIEQARKVAEEasg 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1946572779  82 --QGVGAATLIVTGDPSSVFVELSRNYRLIVIGNRGKGGLAERLLGTTSSSLPAYAYCPIVVVP 143
Cdd:cd23944    77 egPPVKVETEIVPGSPVPTLVEASRDATMVVVGSRGIGALAGLLLGSVSTSLVRHAHCPVAVIH 140
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 7-143 1.37e-18

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: 80.91  E-value: 1.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779   7 VLVGVDGSDASYKAAWWAANYAKHAGLTLQIVCAYSLPSYAAVSfdATYTTMGDDVAAHNDAQEILSKAKAIADEQGVGA 86
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAELILLHVIDPPPSGAAS--LADESAEEEELELELAEAEALAAAAAAEAGGVKV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1946572779  87 ATLIVTGDPSSVFVEL--SRNYRLIVIGNRGKGGLAERLLGTTSSSLPAYAYCPIVVVP 143
Cdd:pfam00582  79 EVVVVVGDPAEEILEVaeEEDADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 161-293 7.51e-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: 70.51  E-value: 7.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779 161 VAV-GSDESKwglKALQIAAAFADSWNAELDVMSAVP--NISGLTGTGSAEERSVMDSYLDDLNTRIEPLMKTYPDLRIN 237
Cdd:pfam00582   3 VAVdGSEESK---RALEWAAELAKARGAELILLHVIDppPSGAASLADESAEEEELELELAEAEALAAAAAAEAGGVKVE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1946572779 238 KTVVPGSAVEALTQASKTH--DVVVVGSRGRGGFTGLLLGSTSQGLLQHAVSPVYVVP 293
Cdd:pfam00582  80 VVVVVGDPAEEILEVAEEEdaDLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
PRK15005 PRK15005
universal stress protein UspF;
189-292 1.20e-03

universal stress protein UspF;


Pssm-ID: 184967 [Multi-domain]  Cd Length: 144  Bit Score: 38.63  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779 189 LDVMSAVPNISGLtGTGSAEERSVMDSYLDDLNTRIEPLMKTY--PDLRINKTVVPGSAVEALTQASKT--HDVVVVGSR 264
Cdd:PRK15005   38 LTVIPSLPYYASL-GLAYSAELPAMDDLKAEAKSQLEEIIKKFklPTDRVHVHVEEGSPKDRILELAKKipADMIIIASH 116

                          90       100
                  ....*....|....*....|....*...
gi 1946572779 265 gRGGFTGLLLGSTSQGLLQHAVSPVYVV 292
Cdd:PRK15005  117 -RPDITTYLLGSNAAAVVRHAECSVLVV 143
 
Name Accession Description Interval E-value
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
7-142 3.09e-24

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 96.14  E-value: 3.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779   7 VLVGVDGSDASYKAAWWAANYAKHAGLTLQIVCAYSLPSYAAVSFDATYTTMGDDvaahndAQEILSKAKAIADEQGVGA 86
Cdd:COG0589     5 ILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEELEEELREE------AEEALEEAAERLEEAGVEV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1946572779  87 ATLIVTGDPSSVFVELSR--NYRLIVIGNRGKGGLAERLLGTTSSSLPAYAYCPIVVV 142
Cdd:COG0589    79 ETVVREGDPAEAILEAAEelDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
USP_Rv2623_repeat2 cd23661
universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis ...
 161-292 4.30e-23

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: 92.96  E-value: 4.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779 161 VAVGSDESKWGLKALQIAAAFADSWNAELDVMSAVPNIsGLTGTGSAEERSVMDSYLDDLNTRIEPLMKTYPDLRINKTV 240
Cdd:cd23661     2 VVVGVDGSPASELATEIAFDEASRRGVDLVALHAWSDM-GPGGFLGIDWRESEQDQERMLAERLAGWQERYPDVHVHKVV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1946572779 241 VPGSAVEALTQASKTHDVVVVGSRGRGGFTGLLLGSTSQGLLQHAVSPVYVV 292
Cdd:cd23661    81 VRDRPARVLLEASERAQLVVVGSHGRGGFAGMLLGSVSRAVLHSAPCPVIVV 132
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
158-292 6.76e-23

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 92.68  E-value: 6.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779 158 IKRVAVGSDESKWGLKALQIAAAFADSWNAELDVMSAVPNISGLTGTGSAEERSVMD---SYLDDLNTRIEPLmktypDL 234
Cdd:COG0589     2 YKRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEELEEELREeaeEALEEAAERLEEA-----GV 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779 235 RINKTVVPGSAVEALTQASKTH--DVVVVGSRGRGGFTGLLLGSTSQGLLQHAVSPVYVV 292
Cdd:COG0589    77 EVETVVREGDPAEAILEAAEELdaDLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
USP_Rv2623_repeat1 cd23944
universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis ...
 7-143 4.06e-22

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: 90.54  E-value: 4.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779   7 VLVGVDGSDASYKAAWWAANYAKHAGLTLQIVCAYS--LPSYAAVSFdatYTTMGDDVAAHndAQEILSKAKAIADE--- 81
Cdd:cd23944     2 IIVGVDGSPASDAAVRWAAREAQLRQIPLTLVHVVPpvVVSWPEGPR---PAEVLDWQQDE--ARQVIEQARKVAEEasg 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1946572779  82 --QGVGAATLIVTGDPSSVFVELSRNYRLIVIGNRGKGGLAERLLGTTSSSLPAYAYCPIVVVP 143
Cdd:cd23944    77 egPPVKVETEIVPGSPVPTLVEASRDATMVVVGSRGIGALAGLLLGSVSTSLVRHAHCPVAVIH 140
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
 7-142 6.99e-22

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: 6.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779   7 VLVGVDGSDASYKAAWWAANYAKHAGLTLQIVCAYSLPSYAAVSFDATYTTMGddvaAHNDAQEILSKAKAIADEQGVGA 86
Cdd:cd00293     2 ILVAVDGSEESERALEWALELAKRPGAELTLLHVVDPPPSSSLSGGLEELADE----LKEEAEELLEEAKKLAEEAGVEV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1946572779  87 ATLIVTGDPSSVFVELSR--NYRLIVIGNRGKGGLAERLLGTTSSSLPAYAYCPIVVV 142
Cdd:cd00293    78 ETIVVEGDPAEAILEEAKelGADLIVMGSRGRSGLKRLLLGSVSEYVLRHAPCPVLVV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 7-143 1.37e-18

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: 80.91  E-value: 1.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779   7 VLVGVDGSDASYKAAWWAANYAKHAGLTLQIVCAYSLPSYAAVSfdATYTTMGDDVAAHNDAQEILSKAKAIADEQGVGA 86
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAELILLHVIDPPPSGAAS--LADESAEEEELELELAEAEALAAAAAAEAGGVKV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1946572779  87 ATLIVTGDPSSVFVEL--SRNYRLIVIGNRGKGGLAERLLGTTSSSLPAYAYCPIVVVP 143
Cdd:pfam00582  79 EVVVVVGDPAEEILEVaeEEDADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
 5-143 2.02e-17

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: 78.05  E-value: 2.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779   5 KAVLVGVDGSDASYKAAWWAANYAKHAGLTLQIVCAYSLPSYAAVSFDATYTTMGD-DVAAHNDAQEILSKAKAIADEQ- 82
Cdd:cd23659     1 RKVLIAVDGSEESEYALEWALENLHRPGDEVVLLHVIEPPSLPAASLGSGSEEWEAlEEEAREKAEKLLEKYEKKLKEEk 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1946572779  83 GVGAATLIVTGDPSSVFVELSRNYR--LIVIGNRGKGGLAERLLGTTSSSLPAYAYCPIVVVP 143
Cdd:cd23659    81 GIKVKVEVVAGDPGEVICKAAEELKadLIVMGSRGLGALKRTLLGSVSDYVVHHSPCPVLVVR 143
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
 160-292 4.35e-16

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: 73.92  E-value: 4.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779 160 RVAVGSDESKWGLKALQIAAAFADSWNAELDVMSAVPNISgltgtgSAEERSVMDSYLDDLNTRIEPLMKTY------PD 233
Cdd:cd00293     1 KILVAVDGSEESERALEWALELAKRPGAELTLLHVVDPPP------SSSLSGGLEELADELKEEAEELLEEAkklaeeAG 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1946572779 234 LRINKTVVPGSAVEALTQASKTH--DVVVVGSRGRGGFTGLLLGSTSQGLLQHAVSPVYVV 292
Cdd:cd00293    75 VEVETIVVEGDPAEAILEEAKELgaDLIVMGSRGRSGLKRLLLGSVSEYVLRHAPCPVLVV 135
USP_Rv2623_repeat1 cd23944
universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis ...
 161-293 5.94e-15

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: 70.90  E-value: 5.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779 161 VAVGSDESKWGLKALQIAAAFADSWNAELDVMSAVPNI--SGLTGTGSAEERSVMDSY----LDDLNTRIEPLMKTYPDL 234
Cdd:cd23944     2 IIVGVDGSPASDAAVRWAAREAQLRQIPLTLVHVVPPVvvSWPEGPRPAEVLDWQQDEarqvIEQARKVAEEASGEGPPV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1946572779 235 RINKTVVPGSAVEALTQASKTHDVVVVGSRGRGGFTGLLLGSTSQGLLQHAVSPVYVVP 293
Cdd:cd23944    82 KVETEIVPGSPVPTLVEASRDATMVVVGSRGIGALAGLLLGSVSTSLVRHAHCPVAVIH 140
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 161-293 7.51e-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: 70.51  E-value: 7.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779 161 VAV-GSDESKwglKALQIAAAFADSWNAELDVMSAVP--NISGLTGTGSAEERSVMDSYLDDLNTRIEPLMKTYPDLRIN 237
Cdd:pfam00582   3 VAVdGSEESK---RALEWAAELAKARGAELILLHVIDppPSGAASLADESAEEEELELELAEAEALAAAAAAEAGGVKVE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1946572779 238 KTVVPGSAVEALTQASKTH--DVVVVGSRGRGGFTGLLLGSTSQGLLQHAVSPVYVVP 293
Cdd:pfam00582  80 VVVVVGDPAEEILEVAEEEdaDLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
USP_Rv2623_repeat2 cd23661
universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis ...
 7-142 3.09e-13

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: 65.99  E-value: 3.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779   7 VLVGVDGSDASYKAAWWAANYAKHAGLTLQIVCAYSLPSYAAVsfdatytTMGDDVAAHNDAQEILSKAKAIADEQ--GV 84
Cdd:cd23661     2 VVVGVDGSPASELATEIAFDEASRRGVDLVALHAWSDMGPGGF-------LGIDWRESEQDQERMLAERLAGWQERypDV 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1946572779  85 GAATLIVTGDPSSVFVELSRNYRLIVIGNRGKGGLAERLLGTTSSSLPAYAYCPIVVV 142
Cdd:cd23661    75 HVHKVVVRDRPARVLLEASERAQLVVVGSHGRGGFAGMLLGSVSRAVLHSAPCPVIVV 132
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
 159-293 1.05e-11

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: 61.87  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779 159 KRVAVGSDESKWGLKALQIAAAFADSWNAELDVMSAVPNISgLTGTGSAEERSVMDSYLDDLNTRIEPLMKTYPDLRINK 238
Cdd:cd23659     1 RKVLIAVDGSEESEYALEWALENLHRPGDEVVLLHVIEPPS-LPAASLGSGSEEWEALEEEAREKAEKLLEKYEKKLKEE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1946572779 239 T-------VVPGSAVEALTQASKTH--DVVVVGSRGRGGFTGLLLGSTSQGLLQHAVSPVYVVP 293
Cdd:cd23659    80 KgikvkveVVAGDPGEVICKAAEELkaDLIVMGSRGLGALKRTLLGSVSDYVVHHSPCPVLVVR 143
USP-A-like cd23657
universal stress protein A and similar proteins; The universal stress protein UspA is a small ...
 5-143 1.16e-05

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: 44.61  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779   5 KAVLVGVDGSDASYKAAWWAANYAKHAGLTLQIVcayslpsYAAVSFDATYTTMGDDVAA--HNDAQEILSKA-KAIADE 81
Cdd:cd23657     2 KHILVAVDLSPESQSLVDKAVEIARENDAKLSLI-------HVDEDISEYYTGLIDVDIAalQDLESTMLEEAlKNLSEL 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1946572779  82 QGVGAA-TLIVTGDPSSVFVELSRNYR--LIVIGNRGKGGLAerLLGTTSSSLPAYAYCPIVVVP 143
Cdd:cd23657    75 AGYPVDhTFIGYGDLKEEILEVAKKHNvdLIVCGHHGDFGLS--LLGSSARAVLNSAPCDVLIVP 137
PRK15005 PRK15005
universal stress protein UspF;
189-292 1.20e-03

universal stress protein UspF;


Pssm-ID: 184967 [Multi-domain]  Cd Length: 144  Bit Score: 38.63  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946572779 189 LDVMSAVPNISGLtGTGSAEERSVMDSYLDDLNTRIEPLMKTY--PDLRINKTVVPGSAVEALTQASKT--HDVVVVGSR 264
Cdd:PRK15005   38 LTVIPSLPYYASL-GLAYSAELPAMDDLKAEAKSQLEEIIKKFklPTDRVHVHVEEGSPKDRILELAKKipADMIIIASH 116

                          90       100
                  ....*....|....*....|....*...
gi 1946572779 265 gRGGFTGLLLGSTSQGLLQHAVSPVYVV 292
Cdd:PRK15005  117 -RPDITTYLLGSNAAAVVRHAECSVLVV 143
PRK15456 PRK15456
universal stress protein UspG; Provisional
 221-292 6.86e-03

universal stress protein UspG; Provisional


Pssm-ID: 185353  Cd Length: 142  Bit Score: 36.46  E-value: 6.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946572779 221 NTRIEPLMK--TYPDLRINKTVVPGSAVEALTQASK--THDVVVVGSRGRGgFTGLLLGSTSQGLLQHAVSPVYVV 292
Cdd:PRK15456   67 EERLQTMVShfTIDPSRIKQHVRFGSVRDEVNELAEelGADVVVIGSRNPS-ISTHLLGSNASSVIRHANLPVLVV 141
 
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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