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Conserved domains on  [gi|1278882185|gb|PJD69531|]
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universal stress protein UspC [Enterobacter kobei]

Protein Classification

universal stress protein UspC( domain architecture ID 10793342)

universal stress protein UspC is required for resistance to DNA-damaging agents

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10116 PRK10116
universal stress protein UspC; Provisional
1-142 8.65e-89

universal stress protein UspC; Provisional


:

Pssm-ID: 182248  Cd Length: 142  Bit Score: 254.63  E-value: 8.65e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882185   1 MSYSHLLVSVAVSPESHLLVSRAVSIARPSNARISLITLAAEPEMYNQLAAPMLEDIREVLQEETQQFLRELVEKAQYPV 80
Cdd:PRK10116    1 MSYSNILVAVAVTPESQQLLAKAVSIARPVNGKISLITLASDPEMYNQFAAPMLEDLRSVMQEETQSFLDKLIQDADYPI 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278882185  81 YETVIATGELNAHILDMCRKQNIDLVICGNHNHSFLSRAACAAKSIVASSQVDVLLVPLGGS 142
Cdd:PRK10116   81 EKTFIAYGELSEHILEVCRKHHFDLVICGNHNHSFFSRASCSAKRVIASSEVDVLLVPLTGD 142
 
Name Accession Description Interval E-value
PRK10116 PRK10116
universal stress protein UspC; Provisional
1-142 8.65e-89

universal stress protein UspC; Provisional


Pssm-ID: 182248  Cd Length: 142  Bit Score: 254.63  E-value: 8.65e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882185   1 MSYSHLLVSVAVSPESHLLVSRAVSIARPSNARISLITLAAEPEMYNQLAAPMLEDIREVLQEETQQFLRELVEKAQYPV 80
Cdd:PRK10116    1 MSYSNILVAVAVTPESQQLLAKAVSIARPVNGKISLITLASDPEMYNQFAAPMLEDLRSVMQEETQSFLDKLIQDADYPI 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278882185  81 YETVIATGELNAHILDMCRKQNIDLVICGNHNHSFLSRAACAAKSIVASSQVDVLLVPLGGS 142
Cdd:PRK10116   81 EKTFIAYGELSEHILEVCRKHHFDLVICGNHNHSFFSRASCSAKRVIASSEVDVLLVPLTGD 142
USP-A-like cd23657
universal stress protein A and similar proteins; The universal stress protein UspA is a small ...
3-139 9.18e-37

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: 122.80  E-value: 9.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882185   3 YSHLLVSVAVSPESHLLVSRAVSIARPSNARISLITLAAEPEMYNQLAA----PMLEDIREVLQEETQQFLRELVEkaqY 78
Cdd:cd23657     1 YKHILVAVDLSPESQSLVDKAVEIARENDAKLSLIHVDEDISEYYTGLIdvdiAALQDLESTMLEEALKNLSELAG---Y 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278882185  79 PVYETVIATGELNAHILDMCRKQNIDLVICGNHNHSFLSRAACAAKSIVASSQVDVLLVPL 139
Cdd:cd23657    78 PVDHTFIGYGDLKEEILEVAKKHNVDLIVCGHHGDFGLSLLGSSARAVLNSAPCDVLIVPL 138
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
3-137 3.32e-17

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 72.65  E-value: 3.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882185   3 YSHLLVSVAVSPESHLLVSRAVSIARPSNARISLITLAAEPEMYnqlaAPMLEDIREVLQEETQQFLRELVEKAQYP--V 80
Cdd:COG0589     2 YKRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSA----AAGPEELEEELREEAEEALEEAAERLEEAgvE 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1278882185  81 YETVIATGELNAHILDMCRKQNIDLVICGNHNHSFLSRAAC--AAKSIVASSQVDVLLV 137
Cdd:COG0589    78 VETVVREGDPAEAILEAAEELDADLIVMGSRGRSGLRRLLLgsVAERVLRHAPCPVLVV 136
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
10-138 9.35e-13

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: 60.88  E-value: 9.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882185  10 VAV--SPESHLLVSRAVSIARPSNARISLITLAAEPEMYNQLAAPMLEDIREVLQEETQQ--FLRELVEKAQYPVYETVI 85
Cdd:pfam00582   3 VAVdgSEESKRALEWAAELAKARGAELILLHVIDPPPSGAASLADESAEEEELELELAEAeaLAAAAAAEAGGVKVEVVV 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1278882185  86 ATGELNAHILDMCRKQNIDLVICGNHNHSFLSRAACA--AKSIVASSQVDVLLVP 138
Cdd:pfam00582  83 VVGDPAEEILEVAEEEDADLIVMGSRGRSGLSRLLLGsvAEYVLRHAPCPVLVVR 137
 
Name Accession Description Interval E-value
PRK10116 PRK10116
universal stress protein UspC; Provisional
1-142 8.65e-89

universal stress protein UspC; Provisional


Pssm-ID: 182248  Cd Length: 142  Bit Score: 254.63  E-value: 8.65e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882185   1 MSYSHLLVSVAVSPESHLLVSRAVSIARPSNARISLITLAAEPEMYNQLAAPMLEDIREVLQEETQQFLRELVEKAQYPV 80
Cdd:PRK10116    1 MSYSNILVAVAVTPESQQLLAKAVSIARPVNGKISLITLASDPEMYNQFAAPMLEDLRSVMQEETQSFLDKLIQDADYPI 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278882185  81 YETVIATGELNAHILDMCRKQNIDLVICGNHNHSFLSRAACAAKSIVASSQVDVLLVPLGGS 142
Cdd:PRK10116   81 EKTFIAYGELSEHILEVCRKHHFDLVICGNHNHSFFSRASCSAKRVIASSEVDVLLVPLTGD 142
USP-A-like cd23657
universal stress protein A and similar proteins; The universal stress protein UspA is a small ...
3-139 9.18e-37

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: 122.80  E-value: 9.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882185   3 YSHLLVSVAVSPESHLLVSRAVSIARPSNARISLITLAAEPEMYNQLAA----PMLEDIREVLQEETQQFLRELVEkaqY 78
Cdd:cd23657     1 YKHILVAVDLSPESQSLVDKAVEIARENDAKLSLIHVDEDISEYYTGLIdvdiAALQDLESTMLEEALKNLSELAG---Y 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278882185  79 PVYETVIATGELNAHILDMCRKQNIDLVICGNHNHSFLSRAACAAKSIVASSQVDVLLVPL 139
Cdd:cd23657    78 PVDHTFIGYGDLKEEILEVAKKHNVDLIVCGHHGDFGLSLLGSSARAVLNSAPCDVLIVPL 138
PRK15118 PRK15118
universal stress protein UspA;
1-139 2.74e-32

universal stress protein UspA;


Pssm-ID: 185073  Cd Length: 144  Bit Score: 111.51  E-value: 2.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882185   1 MSYSHLLVSVAVSPESHLLVSRAVSIARPSNARISLITLAAE-PEMYNQLAAPMLEDIREVLQEETQQFLRELVEKAQYP 79
Cdd:PRK15118    1 MAYKHILIAVDLSPESKVLVEKAVSMARPYNAKVSLIHVDVNySDLYTGLIDVNLGDMQKRISEETHHALTELSTNAGYP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882185  80 VYETVIATGELNAHILDMCRKQNIDLVICGnHNHSFLSRAACAAKSIVASSQVDVLLVPL 139
Cdd:PRK15118   81 ITETLSGSGDLGQVLVDAIKKYDMDLVVCG-HHQDFWSKLMSSARQLINTVHVDMLIVPL 139
PRK09982 PRK09982
universal stress protein UspD; Provisional
1-139 6.09e-21

universal stress protein UspD; Provisional


Pssm-ID: 137627  Cd Length: 142  Bit Score: 82.36  E-value: 6.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882185   1 MSYSHLLVSVAVSPESHLLVSRAVSIARPSNARISLITLA-AEPEMYNQLAAPMLEDIREVLQEETQQFLRELVEKAQYP 79
Cdd:PRK09982    1 MAYKHIGVAISGNEEDALLVNKALELARHNDAHLTLIHIDdGLSELYPGIYFPATEDILQLLKNKSDNKLYKLTKNIQWP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882185  80 VYETVIATGELNAHILDMCRKQNIDLVICGnHNHSFLSRAACAAKSIVASSQVDVLLVPL 139
Cdd:PRK09982   81 KTKLRIERGEMPETLLEIMQKEQCDLLVCG-HHHSFINRLMPAYRGMINKMSADLLIVPF 139
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
3-137 3.32e-17

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 72.65  E-value: 3.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882185   3 YSHLLVSVAVSPESHLLVSRAVSIARPSNARISLITLAAEPEMYnqlaAPMLEDIREVLQEETQQFLRELVEKAQYP--V 80
Cdd:COG0589     2 YKRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSA----AAGPEELEEELREEAEEALEEAAERLEEAgvE 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1278882185  81 YETVIATGELNAHILDMCRKQNIDLVICGNHNHSFLSRAAC--AAKSIVASSQVDVLLV 137
Cdd:COG0589    78 VETVVREGDPAEAILEAAEELDADLIVMGSRGRSGLRRLLLgsVAERVLRHAPCPVLVV 136
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
10-138 9.35e-13

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: 60.88  E-value: 9.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882185  10 VAV--SPESHLLVSRAVSIARPSNARISLITLAAEPEMYNQLAAPMLEDIREVLQEETQQ--FLRELVEKAQYPVYETVI 85
Cdd:pfam00582   3 VAVdgSEESKRALEWAAELAKARGAELILLHVIDPPPSGAASLADESAEEEELELELAEAeaLAAAAAAEAGGVKVEVVV 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1278882185  86 ATGELNAHILDMCRKQNIDLVICGNHNHSFLSRAACA--AKSIVASSQVDVLLVP 138
Cdd:pfam00582  83 VVGDPAEEILEVAEEEDADLIVMGSRGRSGLSRLLLGsvAEYVLRHAPCPVLVVR 137
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
5-137 6.39e-11

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: 56.20  E-value: 6.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882185   5 HLLVSVAVSPESHLLVSRAVSIARPSNARISLITLAAEPEMYNQlaAPMLEDIREVLQEETQQFLRELVEKAQYPV--YE 82
Cdd:cd00293     1 KILVAVDGSEESERALEWALELAKRPGAELTLLHVVDPPPSSSL--SGGLEELADELKEEAEELLEEAKKLAEEAGveVE 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1278882185  83 TVIATGELNAHILDMCRKQNIDLVICGNHNHSFLSRA--ACAAKSIVASSQVDVLLV 137
Cdd:cd00293    79 TIVVEGDPAEAILEEAKELGADLIVMGSRGRSGLKRLllGSVSEYVLRHAPCPVLVV 135
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
8-119 9.20e-06

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: 42.61  E-value: 9.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278882185   8 VSVAV--SPESHLLVSRAVS-IARPSNaRISLITlAAEPEMYNQLAAPMLEDIREVLQEETQQFLRELVEKAQYPV---- 80
Cdd:cd23659     3 VLIAVdgSEESEYALEWALEnLHRPGD-EVVLLH-VIEPPSLPAASLGSGSEEWEALEEEAREKAEKLLEKYEKKLkeek 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1278882185  81 ---YETVIATGELNAHILDMCRKQNIDLVICGNHNHSFLSRA 119
Cdd:cd23659    81 gikVKVEVVAGDPGEVICKAAEELKADLIVMGSRGLGALKRT 122
 
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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