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Conserved domains on  [gi|489505290|ref|WP_003410171|]
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MULTISPECIES: universal stress protein [Mycobacterium]

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 ...
 10-141 3.07e-17

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 cd23944:

Pssm-ID: 469708  Cd Length: 140  Bit Score: 76.29  E-value: 3.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489505290  10 IVVGIDGSKPAVQAALWAVDEAASRDIPLRLLYAIEPDDPGYAAH----GAAARKLAAAENAVRYAFTAVEAA---DRPV 82
Cdd:cd23944    2 IIVGVDGSPASDAAVRWAAREAQLRQIPLTLVHVVPPVVVSWPEGprpaEVLDWQQDEARQVIEQARKVAEEAsgeGPPV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489505290  83 KVEVEITQERPVTSLIRASAAAALVCVGAIGVHHFRPERVGSTAAALALSAQCPVAIVR 141
Cdd:cd23944   82 KVETEIVPGSPVPTLVEASRDATMVVVGSRGIGALAGLLLGSVSTSLVRHAHCPVAVIH 140
AANH_superfamily super family cl00292
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ...
 154-274 2.01e-04

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: 40.57  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489505290 154 IVVEADGSSDIGVLLGAVMAEARLRDSPVRVV-TCRQSGVGD--------TGDDVRASLDRWLARWQPRYPDVRVQSAAV 224
Cdd:cd23661    2 VVVGVDGSPASELATEIAFDEASRRGVDLVALhAWSDMGPGGflgidwreSEQDQERMLAERLAGWQERYPDVHVHKVVV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489505290 225 HGELLDYLAGLGRSVHMVVL-SASDQEHVEQLVGAPGNAVLQEAGCTLLVV 274
Cdd:cd23661   82 RDRPARVLLEASERAQLVVVgSHGRGGFAGMLLGSVSRAVLHSAPCPVIVV 132
 
Name Accession Description Interval E-value
USP_Rv2623_repeat1 cd23944
universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis ...
 10-141 3.07e-17

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: 76.29  E-value: 3.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489505290  10 IVVGIDGSKPAVQAALWAVDEAASRDIPLRLLYAIEPDDPGYAAH----GAAARKLAAAENAVRYAFTAVEAA---DRPV 82
Cdd:cd23944    2 IIVGVDGSPASDAAVRWAAREAQLRQIPLTLVHVVPPVVVSWPEGprpaEVLDWQQDEARQVIEQARKVAEEAsgeGPPV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489505290  83 KVEVEITQERPVTSLIRASAAAALVCVGAIGVHHFRPERVGSTAAALALSAQCPVAIVR 141
Cdd:cd23944   82 KVETEIVPGSPVPTLVEASRDATMVVVGSRGIGALAGLLLGSVSTSLVRHAHCPVAVIH 140
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 10-141 4.42e-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: 59.34  E-value: 4.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489505290   10 IVVGIDGSKPAVQAALWAVDEAASRDIPLRLLYAIEPDDPGYA-----AHGAAARKLAAAENAVRYAFTAVEAADRPVKV 84
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAELILLHVIDPPPSGAAsladeSAEEEELELELAEAEALAAAAAAEAGGVKVEV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489505290   85 EVEITQERPVTSLIRASAAAALVCVGAIGVHHFRPERVGSTAAALALSAQCPVAIVR 141
Cdd:pfam00582  81 VVVVGDPAEEILEVAEEEDADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
10-118 5.06e-08

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 50.69  E-value: 5.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489505290  10 IVVGIDGSKPAVQAALWAVDEAASRDIPLRLLYAIEPDDPGYAAHGAAA-RKLAAAENAVRYAFTAVEAADrpVKVEVEI 88
Cdd:COG0589    5 ILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEELEeELREEAEEALEEAAERLEEAG--VEVETVV 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489505290  89 TQERPVTSLIRASAA--AALVCVGAIGVHHFR 118
Cdd:COG0589   83 REGDPAEAILEAAEEldADLIVMGSRGRSGLR 114
USP_Rv2623_repeat2 cd23661
universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis ...
 154-274 2.01e-04

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: 40.57  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489505290 154 IVVEADGSSDIGVLLGAVMAEARLRDSPVRVV-TCRQSGVGD--------TGDDVRASLDRWLARWQPRYPDVRVQSAAV 224
Cdd:cd23661    2 VVVGVDGSPASELATEIAFDEASRRGVDLVALhAWSDMGPGGflgidwreSEQDQERMLAERLAGWQERYPDVHVHKVVV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489505290 225 HGELLDYLAGLGRSVHMVVL-SASDQEHVEQLVGAPGNAVLQEAGCTLLVV 274
Cdd:cd23661   82 RDRPARVLLEASERAQLVVVgSHGRGGFAGMLLGSVSRAVLHSAPCPVIVV 132
 
Name Accession Description Interval E-value
USP_Rv2623_repeat1 cd23944
universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis ...
 10-141 3.07e-17

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: 76.29  E-value: 3.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489505290  10 IVVGIDGSKPAVQAALWAVDEAASRDIPLRLLYAIEPDDPGYAAH----GAAARKLAAAENAVRYAFTAVEAA---DRPV 82
Cdd:cd23944    2 IIVGVDGSPASDAAVRWAAREAQLRQIPLTLVHVVPPVVVSWPEGprpaEVLDWQQDEARQVIEQARKVAEEAsgeGPPV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489505290  83 KVEVEITQERPVTSLIRASAAAALVCVGAIGVHHFRPERVGSTAAALALSAQCPVAIVR 141
Cdd:cd23944   82 KVETEIVPGSPVPTLVEASRDATMVVVGSRGIGALAGLLLGSVSTSLVRHAHCPVAVIH 140
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 10-141 4.42e-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: 59.34  E-value: 4.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489505290   10 IVVGIDGSKPAVQAALWAVDEAASRDIPLRLLYAIEPDDPGYA-----AHGAAARKLAAAENAVRYAFTAVEAADRPVKV 84
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAELILLHVIDPPPSGAAsladeSAEEEELELELAEAEALAAAAAAEAGGVKVEV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489505290   85 EVEITQERPVTSLIRASAAAALVCVGAIGVHHFRPERVGSTAAALALSAQCPVAIVR 141
Cdd:pfam00582  81 VVVVGDPAEEILEVAEEEDADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
10-118 5.06e-08

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 50.69  E-value: 5.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489505290  10 IVVGIDGSKPAVQAALWAVDEAASRDIPLRLLYAIEPDDPGYAAHGAAA-RKLAAAENAVRYAFTAVEAADrpVKVEVEI 88
Cdd:COG0589    5 ILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEELEeELREEAEEALEEAAERLEEAG--VEVETVV 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489505290  89 TQERPVTSLIRASAA--AALVCVGAIGVHHFR 118
Cdd:COG0589   83 REGDPAEAILEAAEEldADLIVMGSRGRSGLR 114
USP_Rv2623_repeat2 cd23661
universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis ...
 10-141 7.00e-07

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: 47.50  E-value: 7.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489505290  10 IVVGIDGSKPAVQAALWAVDEAASRDIPLRLLYAIEPDDPGYAAHGAAARKLAAAENAVRYAFTAVEAADRPVKVEVEIT 89
Cdd:cd23661    2 VVVGVDGSPASELATEIAFDEASRRGVDLVALHAWSDMGPGGFLGIDWRESEQDQERMLAERLAGWQERYPDVHVHKVVV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489505290  90 QERPVTSLIRASAAAALVCVGAIGVHHFRPERVGSTAAALALSAQCPVAIVR 141
Cdd:cd23661   82 RDRPARVLLEASERAQLVVVGSHGRGGFAGMLLGSVSRAVLHSAPCPVIVVR 133
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
 10-140 4.62e-06

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: 45.03  E-value: 4.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489505290  10 IVVGIDGSKPAVQAALWAVDEAASRDIPLRLLYAIEPDDPGYAAHGAAARKLAAAENAVRYAFTAVEAADRP-VKVEVEI 88
Cdd:cd00293    2 ILVAVDGSEESERALEWALELAKRPGAELTLLHVVDPPPSSSLSGGLEELADELKEEAEELLEEAKKLAEEAgVEVETIV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489505290  89 TQERPVTSLIRASAA--AALVCVGAIGVHHFRPERVGSTAAALALSAQCPVAIV 140
Cdd:cd00293   82 VEGDPAEAILEEAKElgADLIVMGSRGRSGLKRLLLGSVSEYVLRHAPCPVLVV 135
USP_Rv2623_repeat2 cd23661
universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis ...
 154-274 2.01e-04

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: 40.57  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489505290 154 IVVEADGSSDIGVLLGAVMAEARLRDSPVRVV-TCRQSGVGD--------TGDDVRASLDRWLARWQPRYPDVRVQSAAV 224
Cdd:cd23661    2 VVVGVDGSPASELATEIAFDEASRRGVDLVALhAWSDMGPGGflgidwreSEQDQERMLAERLAGWQERYPDVHVHKVVV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489505290 225 HGELLDYLAGLGRSVHMVVL-SASDQEHVEQLVGAPGNAVLQEAGCTLLVV 274
Cdd:cd23661   82 RDRPARVLLEASERAQLVVVgSHGRGGFAGMLLGSVSRAVLHSAPCPVIVV 132
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
 10-110 1.81e-03

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: 37.99  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489505290  10 IVVGIDGSKPAVQAALWAVDEAASRDIPLRLLYAIEPDDPGYAAHGAAARKLAAAENAVRYAFTAVEA-------ADRPV 82
Cdd:cd23659    3 VLIAVDGSEESEYALEWALENLHRPGDEVVLLHVIEPPSLPAASLGSGSEEWEALEEEAREKAEKLLEkyekklkEEKGI 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 489505290  83 KVEVEITQERPVTSLIRASAA--AALVCVG 110
Cdd:cd23659   83 KVKVEVVAGDPGEVICKAAEElkADLIVMG 112
 
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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