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Conserved domains on  [gi|15599524|ref|NP_253018|]
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hypothetical protein PA4328 [Pseudomonas aeruginosa PAO1]

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 ...
151-300 1.04e-53

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 cd23660:

Pssm-ID: 469708  Cd Length: 148  Bit Score: 172.07  E-value: 1.04e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524 151 GQRLCAALDPLHASDKPAALDHRLIAAARQLEASLGlraDYLHTHAAMPRSLLFDAE--MLAGYERFVLQHEERHRQAFD 228
Cdd:cd23660   1 GGRILVAVDPSNEEEYHEDLNLRLIELAYSLAAQLK---AELHLVSAWPVTPENIAIelPEFDPTEYVDAIRGRHLEAMK 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599524 229 DLLAAYpEIAAERRHLLAGYAEQAIPDFVRANDIDLLLMGAVARGHLDNALIGQTAERVLEEVECDLLVLKP 300
Cdd:cd23660  78 ALRQKF-GIDEEQTHVLEGLPEEVIPDFAEELDADIVVLGTVARTGLSGALIGNTAEHVLDHLNCDLLALKP 148
AANH_superfamily super family cl00292
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ...
5-144 1.10e-18

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 cd23943:

Pssm-ID: 469708  Cd Length: 143  Bit Score: 80.67  E-value: 1.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524   5 NLLVVVDPSSDEQPALTRAQWIAEHSGASVELLLCDFNPALDGGLFFDSHSLQRARDLYLDERVTWLEQLSMPLQQAGIR 84
Cdd:cd23943   3 NMLVVIDPNQDDQPALRRAVYLVQRIGGKIKAFLPIYDLSYEMTTLLSPDERTAMRQGVISQRTAWIREQAKYYLEAGIP 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524  85 TQVEAQWGKPLDRMVLQRVGETRPDLVLKSTRKHNLLRRLLLGNSDWQLIRHCPQPLWLV 144
Cdd:cd23943  83 IEIKVVWHNRPFEAIIQEVIAGNHDLVLKMAHQHDRLESLIFTPTDWHLLRKCPSPVWMV 142
 
Name Accession Description Interval E-value
USP-E_repeat2 cd23660
Universal stress protein E, repeat 2; UspE is a tandem-type USP that consists of two USP ...
151-300 1.04e-53

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: 172.07  E-value: 1.04e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524 151 GQRLCAALDPLHASDKPAALDHRLIAAARQLEASLGlraDYLHTHAAMPRSLLFDAE--MLAGYERFVLQHEERHRQAFD 228
Cdd:cd23660   1 GGRILVAVDPSNEEEYHEDLNLRLIELAYSLAAQLK---AELHLVSAWPVTPENIAIelPEFDPTEYVDAIRGRHLEAMK 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599524 229 DLLAAYpEIAAERRHLLAGYAEQAIPDFVRANDIDLLLMGAVARGHLDNALIGQTAERVLEEVECDLLVLKP 300
Cdd:cd23660  78 ALRQKF-GIDEEQTHVLEGLPEEVIPDFAEELDADIVVLGTVARTGLSGALIGNTAEHVLDHLNCDLLALKP 148
PRK11175 PRK11175
universal stress protein UspE; Provisional
1-300 1.60e-37

universal stress protein UspE; Provisional


Pssm-ID: 236871 [Multi-domain]  Cd Length: 305  Bit Score: 135.01  E-value: 1.60e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524    1 MNLHNLLVVVDPSSDEQPALTRAQWIAEHSGASVELLLC--DFNpaldgglfFDSHSL----QRA--RDLYLDERVTWLE 72
Cdd:PRK11175   1 AKYQNILVVIDPNQDDQPALRRAVYLAQRNGGKITAFLPiyDFS--------YEMTTLlspdEREamRQGVISQRTAWIR 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524   73 QLSMPLQQAGIRTQVEAQW-GKPLDrMVLQRVGETRPDLVLKSTRKHNLLRRLLLGNSDWQLIRHCPQPLWLVHHDAWRG 151
Cdd:PRK11175  73 EQAKPYLDAGIPIEIKVVWhNRPFE-AIIQEVIAGGHDLVVKMTHQHDKLESVIFTPTDWHLLRKCPCPVLMVKDQDWPE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524  152 QR--LCAaldpLH-ASDKPA--ALDHRLIAAARQLeASLGLRADyLHTHAAMPRSLL--------FDAEmlaGYERFV-L 217
Cdd:PRK11175 152 GGkiLVA----VNvASEEPYhdALNEKLVEEAIDL-AEQLNHAE-VHLVNAYPVTPIniaielpeFDPS---VYNDAIrG 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524  218 QHEER---HRQAFDdllaaypeIAAERRHLLAGYAEQAIPDFVRANDIDLLLMGAVARGHLDNALIGQTAERVLEEVECD 294
Cdd:PRK11175 223 QHLLAmkaLRQKFG--------IDEEQTHVEEGLPEEVIPDLAEHLDAELVILGTVGRTGLSAAFLGNTAEHVIDHLNCD 294

                 ....*.
gi 15599524  295 LLVLKP 300
Cdd:PRK11175 295 LLAIKP 300
USP-E_repeat1 cd23943
Universal stress protein E, repeat 1; UspE is a tandem-type USP that consists of two USP ...
5-144 1.10e-18

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: 80.67  E-value: 1.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524   5 NLLVVVDPSSDEQPALTRAQWIAEHSGASVELLLCDFNPALDGGLFFDSHSLQRARDLYLDERVTWLEQLSMPLQQAGIR 84
Cdd:cd23943   3 NMLVVIDPNQDDQPALRRAVYLVQRIGGKIKAFLPIYDLSYEMTTLLSPDERTAMRQGVISQRTAWIREQAKYYLEAGIP 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524  85 TQVEAQWGKPLDRMVLQRVGETRPDLVLKSTRKHNLLRRLLLGNSDWQLIRHCPQPLWLV 144
Cdd:cd23943  83 IEIKVVWHNRPFEAIIQEVIAGNHDLVLKMAHQHDRLESLIFTPTDWHLLRKCPSPVWMV 142
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
157-299 6.71e-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: 70.13  E-value: 6.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524   157 ALDPLHASDKpaALDHrLIAAARQLEASLGLradyLHTHAAMPRSLLFDAEMLAGYERFVLQHEERHRQAFDDLLAAypE 236
Cdd:pfam00582   4 AVDGSEESKR--ALEW-AAELAKARGAELIL----LHVIDPPPSGAASLADESAEEEELELELAEAEALAAAAAAEA--G 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599524   237 IAAERRHLLAGYAEQAIPDFVRANDIDLLLMGAVARGHLDNALIGQTAERVLEEVECDLLVLK 299
Cdd:pfam00582  75 GVKVEVVVVVGDPAEEILEVAEEEDADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
168-297 4.82e-12

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 62.25  E-value: 4.82e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524 168 AALDHrLIAAARQLEASLGLradyLHTHAAMPRSLLFDAEMLAgyerfvlQHEERHRQAFDDLLAAYPEIAAE-RRHLLA 246
Cdd:COG0589  17 RALEY-AAELAKALGAELHL----LHVVDPPPSAAAGPEELEE-------ELREEAEEALEEAAERLEEAGVEvETVVRE 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15599524 247 GYAEQAIPDFVRANDIDLLLMGAVARGHLDNALIGQTAERVLEEVECDLLV 297
Cdd:COG0589  85 GDPAEAILEAAEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
6-145 1.89e-11

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: 60.50  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524     6 LLVVVDPSSDEQPALTRAQWIAEHSGASVELLLCDFNPALDGGLFFDSHSLQRARDLYLDERVtwLEQLSMPLQQAGIRT 85
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAELILLHVIDPPPSGAASLADESAEEEELELELAEAE--ALAAAAAAEAGGVKV 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524    86 QVEAQWGKPlDRMVLQRVGETRPDLVLKSTRKHNLLRRLLLGNSDWQLIRHCPQPLWLVH 145
Cdd:pfam00582  79 EVVVVVGDP-AEEILEVAEEEDADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
4-144 4.22e-09

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 54.16  E-value: 4.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524   4 HNLLVVVDPSSDEQPALTRAQWIAEHSGASVELLLCDFNPALDGGLFFDshslqrARDLYLDERVTWLEQLSMPLQQAGI 83
Cdd:COG0589   3 KRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEE------LEEELREEAEEALEEAAERLEEAGV 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599524  84 RTQVEAQWGKPlDRMVLQRVGETRPDLVLKSTRKHNLLRRLLLGNSDWQLIRHCPQPLWLV 144
Cdd:COG0589  77 EVETVVREGDP-AEAILEAAEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
 
Name Accession Description Interval E-value
USP-E_repeat2 cd23660
Universal stress protein E, repeat 2; UspE is a tandem-type USP that consists of two USP ...
151-300 1.04e-53

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: 172.07  E-value: 1.04e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524 151 GQRLCAALDPLHASDKPAALDHRLIAAARQLEASLGlraDYLHTHAAMPRSLLFDAE--MLAGYERFVLQHEERHRQAFD 228
Cdd:cd23660   1 GGRILVAVDPSNEEEYHEDLNLRLIELAYSLAAQLK---AELHLVSAWPVTPENIAIelPEFDPTEYVDAIRGRHLEAMK 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599524 229 DLLAAYpEIAAERRHLLAGYAEQAIPDFVRANDIDLLLMGAVARGHLDNALIGQTAERVLEEVECDLLVLKP 300
Cdd:cd23660  78 ALRQKF-GIDEEQTHVLEGLPEEVIPDFAEELDADIVVLGTVARTGLSGALIGNTAEHVLDHLNCDLLALKP 148
PRK11175 PRK11175
universal stress protein UspE; Provisional
1-300 1.60e-37

universal stress protein UspE; Provisional


Pssm-ID: 236871 [Multi-domain]  Cd Length: 305  Bit Score: 135.01  E-value: 1.60e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524    1 MNLHNLLVVVDPSSDEQPALTRAQWIAEHSGASVELLLC--DFNpaldgglfFDSHSL----QRA--RDLYLDERVTWLE 72
Cdd:PRK11175   1 AKYQNILVVIDPNQDDQPALRRAVYLAQRNGGKITAFLPiyDFS--------YEMTTLlspdEREamRQGVISQRTAWIR 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524   73 QLSMPLQQAGIRTQVEAQW-GKPLDrMVLQRVGETRPDLVLKSTRKHNLLRRLLLGNSDWQLIRHCPQPLWLVHHDAWRG 151
Cdd:PRK11175  73 EQAKPYLDAGIPIEIKVVWhNRPFE-AIIQEVIAGGHDLVVKMTHQHDKLESVIFTPTDWHLLRKCPCPVLMVKDQDWPE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524  152 QR--LCAaldpLH-ASDKPA--ALDHRLIAAARQLeASLGLRADyLHTHAAMPRSLL--------FDAEmlaGYERFV-L 217
Cdd:PRK11175 152 GGkiLVA----VNvASEEPYhdALNEKLVEEAIDL-AEQLNHAE-VHLVNAYPVTPIniaielpeFDPS---VYNDAIrG 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524  218 QHEER---HRQAFDdllaaypeIAAERRHLLAGYAEQAIPDFVRANDIDLLLMGAVARGHLDNALIGQTAERVLEEVECD 294
Cdd:PRK11175 223 QHLLAmkaLRQKFG--------IDEEQTHVEEGLPEEVIPDLAEHLDAELVILGTVGRTGLSAAFLGNTAEHVIDHLNCD 294

                 ....*.
gi 15599524  295 LLVLKP 300
Cdd:PRK11175 295 LLAIKP 300
USP-E_repeat1 cd23943
Universal stress protein E, repeat 1; UspE is a tandem-type USP that consists of two USP ...
5-144 1.10e-18

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: 80.67  E-value: 1.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524   5 NLLVVVDPSSDEQPALTRAQWIAEHSGASVELLLCDFNPALDGGLFFDSHSLQRARDLYLDERVTWLEQLSMPLQQAGIR 84
Cdd:cd23943   3 NMLVVIDPNQDDQPALRRAVYLVQRIGGKIKAFLPIYDLSYEMTTLLSPDERTAMRQGVISQRTAWIREQAKYYLEAGIP 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524  85 TQVEAQWGKPLDRMVLQRVGETRPDLVLKSTRKHNLLRRLLLGNSDWQLIRHCPQPLWLV 144
Cdd:cd23943  83 IEIKVVWHNRPFEAIIQEVIAGNHDLVLKMAHQHDRLESLIFTPTDWHLLRKCPSPVWMV 142
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
157-299 6.71e-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: 70.13  E-value: 6.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524   157 ALDPLHASDKpaALDHrLIAAARQLEASLGLradyLHTHAAMPRSLLFDAEMLAGYERFVLQHEERHRQAFDDLLAAypE 236
Cdd:pfam00582   4 AVDGSEESKR--ALEW-AAELAKARGAELIL----LHVIDPPPSGAASLADESAEEEELELELAEAEALAAAAAAEA--G 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599524   237 IAAERRHLLAGYAEQAIPDFVRANDIDLLLMGAVARGHLDNALIGQTAERVLEEVECDLLVLK 299
Cdd:pfam00582  75 GVKVEVVVVVGDPAEEILEVAEEEDADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
5-144 2.23e-12

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: 63.14  E-value: 2.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524   5 NLLVVVDPSSDEQPALTRAQWIAEHSGASVELLLCDFNPALdgglFFDSHSLQRARDLYLDERVTWLEQLSMPLQQAGIR 84
Cdd:cd00293   1 KILVAVDGSEESERALEWALELAKRPGAELTLLHVVDPPPS----SSLSGGLEELADELKEEAEELLEEAKKLAEEAGVE 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524  85 TQVEAQWGKPLDrMVLQRVGETRPDLVLKSTRKHNLLRRLLLGNSDWQLIRHCPQPLWLV 144
Cdd:cd00293  77 VETIVVEGDPAE-AILEEAKELGADLIVMGSRGRSGLKRLLLGSVSEYVLRHAPCPVLVV 135
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
168-297 4.82e-12

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 62.25  E-value: 4.82e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524 168 AALDHrLIAAARQLEASLGLradyLHTHAAMPRSLLFDAEMLAgyerfvlQHEERHRQAFDDLLAAYPEIAAE-RRHLLA 246
Cdd:COG0589  17 RALEY-AAELAKALGAELHL----LHVVDPPPSAAAGPEELEE-------ELREEAEEALEEAAERLEEAGVEvETVVRE 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15599524 247 GYAEQAIPDFVRANDIDLLLMGAVARGHLDNALIGQTAERVLEEVECDLLV 297
Cdd:COG0589  85 GDPAEAILEAAEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
6-145 1.89e-11

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: 60.50  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524     6 LLVVVDPSSDEQPALTRAQWIAEHSGASVELLLCDFNPALDGGLFFDSHSLQRARDLYLDERVtwLEQLSMPLQQAGIRT 85
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAELILLHVIDPPPSGAASLADESAEEEELELELAEAE--ALAAAAAAEAGGVKV 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524    86 QVEAQWGKPlDRMVLQRVGETRPDLVLKSTRKHNLLRRLLLGNSDWQLIRHCPQPLWLVH 145
Cdd:pfam00582  79 EVVVVVGDP-AEEILEVAEEEDADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
4-144 4.22e-09

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 54.16  E-value: 4.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524   4 HNLLVVVDPSSDEQPALTRAQWIAEHSGASVELLLCDFNPALDGGLFFDshslqrARDLYLDERVTWLEQLSMPLQQAGI 83
Cdd:COG0589   3 KRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEE------LEEELREEAEEALEEAAERLEEAGV 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599524  84 RTQVEAQWGKPlDRMVLQRVGETRPDLVLKSTRKHNLLRRLLLGNSDWQLIRHCPQPLWLV 144
Cdd:COG0589  77 EVETVVREGDP-AEAILEAAEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
157-297 5.85e-08

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: 50.81  E-value: 5.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524 157 ALDPLHASDKpaALDHrLIAAARQLEASLGLradylhTHAAMPRSLLFDAEmlaGYERFVLQHEERHRQAFDDL--LAAY 234
Cdd:cd00293   5 AVDGSEESER--ALEW-ALELAKRPGAELTL------LHVVDPPPSSSLSG---GLEELADELKEEAEELLEEAkkLAEE 72
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599524 235 PEIAAERrHLLAGYAEQAIPDFVRANDIDLLLMGAVARGHLDNALIGQTAERVLEEVECDLLV 297
Cdd:cd00293  73 AGVEVET-IVVEGDPAEAILEEAKELGADLIVMGSRGRSGLKRLLLGSVSEYVLRHAPCPVLV 134
USP-A-like cd23657
universal stress protein A and similar proteins; The universal stress protein UspA is a small ...
171-300 1.75e-07

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: 49.61  E-value: 1.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599524 171 DHRLIAAARQLEASLGLRADYLH--THAAMPRSLLFDAEMLAGYERFVLQHEERHRQafddlLAAYPEIAAERRHLLAGY 248
Cdd:cd23657  14 SQSLVDKAVEIARENDAKLSLIHvdEDISEYYTGLIDVDIAALQDLESTMLEEALKN-----LSELAGYPVDHTFIGYGD 88
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15599524 249 AEQAIPDFVRANDIDLLLMGAvaRGHLDNALIGQTAERVLEEVECDLLVLKP 300
Cdd:cd23657  89 LKEEILEVAKKHNVDLIVCGH--HGDFGLSLLGSSARAVLNSAPCDVLIVPL 138
 
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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