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Conserved domains on  [gi|15829900|ref|NP_308673|]
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universal stress protein UP12 [Escherichia coli O157:H7 str. Sakai]

Protein Classification

adenine nucleotide alpha hydrolase family protein; NAD(+) synthase( domain architecture ID 10794167)

AANH (adenine nucleotide alpha hydrolase) family protein| NAD(+) synthase, utilizing glutamine or NH(3) as nitrogen source, converts deamido-NAD+ to NAD+

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK15456 PRK15456
universal stress protein UspG; Provisional
1-142 3.29e-90

universal stress protein UspG; Provisional


:

Pssm-ID: 185353  Cd Length: 142  Bit Score: 257.95  E-value: 3.29e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829900    1 MYKTIIMPVDVFEMELSDKAVRHAEFLAQDDGVIHLLHVLPGSASLSLHRFAADVRRFEEHLQHEAEERLQTMVSHFTID 80
Cdd:PRK15456   1 MYKTIIMPVDVFEMELSDKAVRHAEFLAQDDGVIHLLHVLPGSASLSLHRFAADVRRFEEHLQHEAEERLQTMVSHFTID 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829900   81 PSRIKQHVRFGSVRDEVNELAEELGADVVVIGSRNPSISTHLLGSNASSVIRHANLPVLVVR 142
Cdd:PRK15456  81 PSRIKQHVRFGSVRDEVNELAEELGADVVVIGSRNPSISTHLLGSNASSVIRHANLPVLVVR 142
 
Name Accession Description Interval E-value
PRK15456 PRK15456
universal stress protein UspG; Provisional
1-142 3.29e-90

universal stress protein UspG; Provisional


Pssm-ID: 185353  Cd Length: 142  Bit Score: 257.95  E-value: 3.29e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829900    1 MYKTIIMPVDVFEMELSDKAVRHAEFLAQDDGVIHLLHVLPGSASLSLHRFAADVRRFEEHLQHEAEERLQTMVSHFTID 80
Cdd:PRK15456   1 MYKTIIMPVDVFEMELSDKAVRHAEFLAQDDGVIHLLHVLPGSASLSLHRFAADVRRFEEHLQHEAEERLQTMVSHFTID 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829900   81 PSRIKQHVRFGSVRDEVNELAEELGADVVVIGSRNPSISTHLLGSNASSVIRHANLPVLVVR 142
Cdd:PRK15456  81 PSRIKQHVRFGSVRDEVNELAEELGADVVVIGSRNPSISTHLLGSNASSVIRHANLPVLVVR 142
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
1-141 7.95e-28

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 99.61  E-value: 7.95e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829900   1 MYKTIIMPVDvfEMELSDKAVRHAEFLAQDDGV-IHLLHVLPGSASlslhrFAADVRRFEEHLQHEAEERLQTMVSHFTI 79
Cdd:COG0589   1 MYKRILVPTD--GSEEAERALEYAAELAKALGAeLHLLHVVDPPPS-----AAAGPEELEEELREEAEEALEEAAERLEE 73
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829900  80 DPSRIKQHVRFGSVRDEVNELAEELGADVVVIGSR-NPSISTHLLGSNASSVIRHANLPVLVV 141
Cdd:COG0589  74 AGVEVETVVREGDPAEAILEAAEELDADLIVMGSRgRSGLRRLLLGSVAERVLRHAPCPVLVV 136
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
15-141 6.74e-23

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: 87.02  E-value: 6.74e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829900  15 ELSDKAVRHA-EFLAQDDGVIHLLHVLPGSASLSLHRFAADVRrfeEHLQHEAEERLQTMVSHFTIDPSRIKQHVRFGSV 93
Cdd:cd00293  10 EESERALEWAlELAKRPGAELTLLHVVDPPPSSSLSGGLEELA---DELKEEAEELLEEAKKLAEEAGVEVETIVVEGDP 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15829900  94 RDEVNELAEELGADVVVIGSRNPS-ISTHLLGSNASSVIRHANLPVLVV 141
Cdd:cd00293  87 AEAILEEAKELGADLIVMGSRGRSgLKRLLLGSVSEYVLRHAPCPVLVV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
5-142 1.01e-22

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: 86.69  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829900     5 IIMPVDvfEMELSDKAVRHAEFLAQD-DGVIHLLHVLPGSASLSLHRFAADVRRFEEHLQhEAEERLQTMVSHFTIDPSR 83
Cdd:pfam00582   1 ILVAVD--GSEESKRALEWAAELAKArGAELILLHVIDPPPSGAASLADESAEEEELELE-LAEAEALAAAAAAEAGGVK 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829900    84 IKQHVRFGSVRDEVNELAEELGADVVVIGSR-NPSISTHLLGSNASSVIRHANLPVLVVR 142
Cdd:pfam00582  78 VEVVVVVGDPAEEILEVAEEEDADLIVMGSRgRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
 
Name Accession Description Interval E-value
PRK15456 PRK15456
universal stress protein UspG; Provisional
1-142 3.29e-90

universal stress protein UspG; Provisional


Pssm-ID: 185353  Cd Length: 142  Bit Score: 257.95  E-value: 3.29e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829900    1 MYKTIIMPVDVFEMELSDKAVRHAEFLAQDDGVIHLLHVLPGSASLSLHRFAADVRRFEEHLQHEAEERLQTMVSHFTID 80
Cdd:PRK15456   1 MYKTIIMPVDVFEMELSDKAVRHAEFLAQDDGVIHLLHVLPGSASLSLHRFAADVRRFEEHLQHEAEERLQTMVSHFTID 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829900   81 PSRIKQHVRFGSVRDEVNELAEELGADVVVIGSRNPSISTHLLGSNASSVIRHANLPVLVVR 142
Cdd:PRK15456  81 PSRIKQHVRFGSVRDEVNELAEELGADVVVIGSRNPSISTHLLGSNASSVIRHANLPVLVVR 142
PRK15005 PRK15005
universal stress protein UspF;
1-142 9.90e-34

universal stress protein UspF;


Pssm-ID: 184967 [Multi-domain]  Cd Length: 144  Bit Score: 115.29  E-value: 9.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829900    1 MYKTIIMPVDVFEMELSDKAVRHAEFLAQ-DDGVIHLLHVLPG---SASLSLhRFAADVRRFEEhLQHEAEERLQTMVSH 76
Cdd:PRK15005   1 MNRTILVPIDISDSELTQRVISHVEAEAKiDDAEVHFLTVIPSlpyYASLGL-AYSAELPAMDD-LKAEAKSQLEEIIKK 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829900   77 FTIDPSRIKQHVRFGSVRDEVNELAEELGADVVVIGSRNPSISTHLLGSNASSVIRHANLPVLVVR 142
Cdd:PRK15005  79 FKLPTDRVHVHVEEGSPKDRILELAKKIPADMIIIASHRPDITTYLLGSNAAAVVRHAECSVLVVR 144
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
1-141 7.95e-28

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 99.61  E-value: 7.95e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829900   1 MYKTIIMPVDvfEMELSDKAVRHAEFLAQDDGV-IHLLHVLPGSASlslhrFAADVRRFEEHLQHEAEERLQTMVSHFTI 79
Cdd:COG0589   1 MYKRILVPTD--GSEEAERALEYAAELAKALGAeLHLLHVVDPPPS-----AAAGPEELEEELREEAEEALEEAAERLEE 73
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829900  80 DPSRIKQHVRFGSVRDEVNELAEELGADVVVIGSR-NPSISTHLLGSNASSVIRHANLPVLVV 141
Cdd:COG0589  74 AGVEVETVVREGDPAEAILEAAEELDADLIVMGSRgRSGLRRLLLGSVAERVLRHAPCPVLVV 136
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
15-141 6.74e-23

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: 87.02  E-value: 6.74e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829900  15 ELSDKAVRHA-EFLAQDDGVIHLLHVLPGSASLSLHRFAADVRrfeEHLQHEAEERLQTMVSHFTIDPSRIKQHVRFGSV 93
Cdd:cd00293  10 EESERALEWAlELAKRPGAELTLLHVVDPPPSSSLSGGLEELA---DELKEEAEELLEEAKKLAEEAGVEVETIVVEGDP 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15829900  94 RDEVNELAEELGADVVVIGSRNPS-ISTHLLGSNASSVIRHANLPVLVV 141
Cdd:cd00293  87 AEAILEEAKELGADLIVMGSRGRSgLKRLLLGSVSEYVLRHAPCPVLVV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
5-142 1.01e-22

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: 86.69  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829900     5 IIMPVDvfEMELSDKAVRHAEFLAQD-DGVIHLLHVLPGSASLSLHRFAADVRRFEEHLQhEAEERLQTMVSHFTIDPSR 83
Cdd:pfam00582   1 ILVAVD--GSEESKRALEWAAELAKArGAELILLHVIDPPPSGAASLADESAEEEELELE-LAEAEALAAAAAAEAGGVK 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829900    84 IKQHVRFGSVRDEVNELAEELGADVVVIGSR-NPSISTHLLGSNASSVIRHANLPVLVVR 142
Cdd:pfam00582  78 VEVVVVVGDPAEEILEVAEEEDADLIVMGSRgRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
3-142 1.53e-15

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: 68.42  E-value: 1.53e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829900   3 KTIIMPVDvfEMELSDKAVRHA-EFLAQDDGVIHLLHVLPG--SASLSLHRFAADVRRFEEHLQHEAEERLQTMVSHFTI 79
Cdd:cd23659   1 RKVLIAVD--GSEESEYALEWAlENLHRPGDEVVLLHVIEPpsLPAASLGSGSEEWEALEEEAREKAEKLLEKYEKKLKE 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829900  80 DPS-RIKQHVRFGSVRDEVNELAEELGADVVVIGSRNPS-ISTHLLGSNASSVIRHANLPVLVVR 142
Cdd:cd23659  79 EKGiKVKVEVVAGDPGEVICKAAEELKADLIVMGSRGLGaLKRTLLGSVSDYVVHHSPCPVLVVR 143
USP-A-like cd23657
universal stress protein A and similar proteins; The universal stress protein UspA is a small ...
2-142 2.71e-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: 46.53  E-value: 2.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829900   2 YKTIIMPVDVFE--MELSDKAVrhaEFLAQDDGVIHLLHVLPGSASLSLHRFAADVRRFEEHLQHEAEERLQTMVSHFTI 79
Cdd:cd23657   1 YKHILVAVDLSPesQSLVDKAV---EIARENDAKLSLIHVDEDISEYYTGLIDVDIAALQDLESTMLEEALKNLSELAGY 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829900  80 DPSriKQHVRFGSVRDEVNELAEELGADVVVIGSRNPSISThLLGSNASSVIRHANLPVLVVR 142
Cdd:cd23657  78 PVD--HTFIGYGDLKEEILEVAKKHNVDLIVCGHHGDFGLS-LLGSSARAVLNSAPCDVLIVP 137
USP-E_repeat2 cd23660
Universal stress protein E, repeat 2; UspE is a tandem-type USP that consists of two USP ...
15-140 1.54e-06

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: 44.95  E-value: 1.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829900  15 ELSDKAVRHAEFLA-QDDGVIHLLHVLPgsasLSLHRFAADVRRFE-EHLQHEAEER----LQTMVSHFTIDPSRIkqHV 88
Cdd:cd23660  19 DLNLRLIELAYSLAaQLKAELHLVSAWP----VTPENIAIELPEFDpTEYVDAIRGRhleaMKALRQKFGIDEEQT--HV 92
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15829900  89 RFGSVRDEVNELAEELGADVVVIGS--RNpSISTHLLGSNASSVIRHANLPVLV 140
Cdd:cd23660  93 LEGLPEEVIPDFAEELDADIVVLGTvaRT-GLSGALIGNTAEHVLDHLNCDLLA 145
PRK11175 PRK11175
universal stress protein UspE; Provisional
14-142 6.99e-06

universal stress protein UspE; Provisional


Pssm-ID: 236871 [Multi-domain]  Cd Length: 305  Bit Score: 44.10  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829900   14 MELSDKAVRHAEFLAQ--DDGVIHLLHVLPG---SASLSLHRFAADVrrFEEHLQHEAEERLQTMVSHFTIDPSriKQHV 88
Cdd:PRK11175 169 DALNEKLVEEAIDLAEqlNHAEVHLVNAYPVtpiNIAIELPEFDPSV--YNDAIRGQHLLAMKALRQKFGIDEE--QTHV 244
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15829900   89 RFGSVRDEVNELAEELGADVVVIGS--RNpSISTHLLGSNASSVIRHANLPVLVVR 142
Cdd:PRK11175 245 EEGLPEEVIPDLAEHLDAELVILGTvgRT-GLSAAFLGNTAEHVIDHLNCDLLAIK 299
USP_Rv2623_repeat1 cd23944
universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis ...
17-142 1.60e-04

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: 39.31  E-value: 1.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829900  17 SDKAVRHAEFLAQDDGV-IHLLHVLPG--SASLSLHRFAADVRRFEEHLQH---EAEERLQTMVShfTIDPSRIKQHVRF 90
Cdd:cd23944  12 SDAAVRWAAREAQLRQIpLTLVHVVPPvvVSWPEGPRPAEVLDWQQDEARQvieQARKVAEEASG--EGPPVKVETEIVP 89
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15829900  91 GSVRDEVNELAEElgADVVVIGSRNP-SISTHLLGSNASSVIRHANLPVLVVR 142
Cdd:cd23944  90 GSPVPTLVEASRD--ATMVVVGSRGIgALAGLLLGSVSTSLVRHAHCPVAVIH 140
 
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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