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Conserved domains on  [gi|1002256505|ref|XP_015632556|]
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universal stress protein PHOS34 isoform X2 [Oryza sativa Japonica Group]

Protein Classification

universal stress protein( domain architecture ID 19229820)

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
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
 14-191 1.16e-44

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: 144.69  E-value: 1.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  14 RRILVAVDEGDESVHALKWCLASFAKRGggggaappDTIILLYVRPPPPtysvLDASGYVFSDEVAAAIDGYSKEVAEAV 93
Cdd:cd23659     1 RKVLIAVDGSEESEYALEWALENLHRPG--------DEVVLLHVIEPPS----LPAASLGSGSEEWEALEEEAREKAEKL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  94 VEKAQKLCtlygkevggdgEAGHEMKVEVKVAVGDARNVICQMADKLGADVLVMGSHGYGLFKRslkrsrfqsqklALLG 173
Cdd:cd23659    69 LEKYEKKL-----------KEEKGIKVKVEVVAGDPGEVICKAAEELKADLIVMGSRGLGALKR------------TLLG 125

                         170
                  ....*....|....*...
gi 1002256505 174 SVSDYCVRNANCPVLIVK 191
Cdd:cd23659   126 SVSDYVVHHSPCPVLVVR 143
 
Name Accession Description Interval E-value
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
 14-191 1.16e-44

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: 144.69  E-value: 1.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  14 RRILVAVDEGDESVHALKWCLASFAKRGggggaappDTIILLYVRPPPPtysvLDASGYVFSDEVAAAIDGYSKEVAEAV 93
Cdd:cd23659     1 RKVLIAVDGSEESEYALEWALENLHRPG--------DEVVLLHVIEPPS----LPAASLGSGSEEWEALEEEAREKAEKL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  94 VEKAQKLCtlygkevggdgEAGHEMKVEVKVAVGDARNVICQMADKLGADVLVMGSHGYGLFKRslkrsrfqsqklALLG 173
Cdd:cd23659    69 LEKYEKKL-----------KEEKGIKVKVEVVAGDPGEVICKAAEELKADLIVMGSRGLGALKR------------TLLG 125

                         170
                  ....*....|....*...
gi 1002256505 174 SVSDYCVRNANCPVLIVK 191
Cdd:cd23659   126 SVSDYVVHHSPCPVLVVR 143
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
14-190 8.89e-28

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 101.54  E-value: 8.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  14 RRILVAVDEGDESVHALKWcLASFAKRGGGggaappdTIILLYVRPPPPTYSVLdasgyvfSDEVAAAIDGYSKEVAEAV 93
Cdd:COG0589     3 KRILVPTDGSEEAERALEY-AAELAKALGA-------ELHLLHVVDPPPSAAAG-------PEELEEELREEAEEALEEA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  94 VEKAQklctlygkevggdgEAGHEmkVEVKVAVGDARNVICQMADKLGADVLVMGSHGYGLFKRslkrsrfqsqklALLG 173
Cdd:COG0589    68 AERLE--------------EAGVE--VETVVREGDPAEAILEAAEELDADLIVMGSRGRSGLRR------------LLLG 119

                         170
                  ....*....|....*..
gi 1002256505 174 SVSDYCVRNANCPVLIV 190
Cdd:COG0589   120 SVAERVLRHAPCPVLVV 136
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 16-191 3.29e-26

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: 97.48  E-value: 3.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  16 ILVAVDEGDESVHALKWCLAsFAKRGGgggaappDTIILLYVRPPPPTYSVLDASGYVfsdevaaaidgyskEVAEAVVE 95
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAE-LAKARG-------AELILLHVIDPPPSGAASLADESA--------------EEEELELE 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  96 KAQKLCTLYGKEVGGDGEaghemKVEVKVAVGDARNVICQMADKLGADVLVMGSHGYGLFKRslkrsrfqsqklALLGSV 175
Cdd:pfam00582  59 LAEAEALAAAAAAEAGGV-----KVEVVVVVGDPAEEILEVAEEEDADLIVMGSRGRSGLSR------------LLLGSV 121

                         170
                  ....*....|....*.
gi 1002256505 176 SDYCVRNANCPVLIVK 191
Cdd:pfam00582 122 AEYVLRHAPCPVLVVR 137
PRK15005 PRK15005
universal stress protein UspF;
117-191 1.64e-06

universal stress protein UspF;


Pssm-ID: 184967 [Multi-domain]  Cd Length: 144  Bit Score: 45.56  E-value: 1.64e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002256505 117 EMKVEVKVAVGDARNVICQMADKLGADVLVMGSHgyglfkrslkRSRFQSQklaLLGSVSDYCVRNANCPVLIVK 191
Cdd:PRK15005   83 TDRVHVHVEEGSPKDRILELAKKIPADMIIIASH----------RPDITTY---LLGSNAAAVVRHAECSVLVVR 144
 
Name Accession Description Interval E-value
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
 14-191 1.16e-44

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: 144.69  E-value: 1.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  14 RRILVAVDEGDESVHALKWCLASFAKRGggggaappDTIILLYVRPPPPtysvLDASGYVFSDEVAAAIDGYSKEVAEAV 93
Cdd:cd23659     1 RKVLIAVDGSEESEYALEWALENLHRPG--------DEVVLLHVIEPPS----LPAASLGSGSEEWEALEEEAREKAEKL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  94 VEKAQKLCtlygkevggdgEAGHEMKVEVKVAVGDARNVICQMADKLGADVLVMGSHGYGLFKRslkrsrfqsqklALLG 173
Cdd:cd23659    69 LEKYEKKL-----------KEEKGIKVKVEVVAGDPGEVICKAAEELKADLIVMGSRGLGALKR------------TLLG 125

                         170
                  ....*....|....*...
gi 1002256505 174 SVSDYCVRNANCPVLIVK 191
Cdd:cd23659   126 SVSDYVVHHSPCPVLVVR 143
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
 15-190 1.42e-28

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: 103.58  E-value: 1.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  15 RILVAVDEGDESVHALKWCLAsFAKRGGgggaappDTIILLYVRPPPPTYSVLDASGYVFSDEvaaaidgysKEVAEAVV 94
Cdd:cd00293     1 KILVAVDGSEESERALEWALE-LAKRPG-------AELTLLHVVDPPPSSSLSGGLEELADEL---------KEEAEELL 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  95 EKAQKLCTLYGkevggdgeagheMKVEVKVAVGDARNVICQMADKLGADVLVMGSHGYGLFKRslkrsrfqsqklALLGS 174
Cdd:cd00293    64 EEAKKLAEEAG------------VEVETIVVEGDPAEAILEEAKELGADLIVMGSRGRSGLKR------------LLLGS 119

                         170
                  ....*....|....*.
gi 1002256505 175 VSDYCVRNANCPVLIV 190
Cdd:cd00293   120 VSEYVLRHAPCPVLVV 135
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
14-190 8.89e-28

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 101.54  E-value: 8.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  14 RRILVAVDEGDESVHALKWcLASFAKRGGGggaappdTIILLYVRPPPPTYSVLdasgyvfSDEVAAAIDGYSKEVAEAV 93
Cdd:COG0589     3 KRILVPTDGSEEAERALEY-AAELAKALGA-------ELHLLHVVDPPPSAAAG-------PEELEEELREEAEEALEEA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  94 VEKAQklctlygkevggdgEAGHEmkVEVKVAVGDARNVICQMADKLGADVLVMGSHGYGLFKRslkrsrfqsqklALLG 173
Cdd:COG0589    68 AERLE--------------EAGVE--VETVVREGDPAEAILEAAEELDADLIVMGSRGRSGLRR------------LLLG 119

                         170
                  ....*....|....*..
gi 1002256505 174 SVSDYCVRNANCPVLIV 190
Cdd:COG0589   120 SVAERVLRHAPCPVLVV 136
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
 16-191 3.29e-26

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: 97.48  E-value: 3.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  16 ILVAVDEGDESVHALKWCLAsFAKRGGgggaappDTIILLYVRPPPPTYSVLDASGYVfsdevaaaidgyskEVAEAVVE 95
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAE-LAKARG-------AELILLHVIDPPPSGAASLADESA--------------EEEELELE 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  96 KAQKLCTLYGKEVGGDGEaghemKVEVKVAVGDARNVICQMADKLGADVLVMGSHGYGLFKRslkrsrfqsqklALLGSV 175
Cdd:pfam00582  59 LAEAEALAAAAAAEAGGV-----KVEVVVVVGDPAEEILEVAEEEDADLIVMGSRGRSGLSR------------LLLGSV 121

                         170
                  ....*....|....*.
gi 1002256505 176 SDYCVRNANCPVLIVK 191
Cdd:pfam00582 122 AEYVLRHAPCPVLVVR 137
USP_STK_Ubox_N cd01989
N-terminal USP domain of serine threonine kinases (STK) and U-box domain proteins; This model ...
 15-179 4.21e-10

N-terminal USP domain of serine threonine kinases (STK) and U-box domain proteins; This model represents the N-terminal domain found in some plant serine threonine kinases (STK, EC 2.7.11.-) and U-box domain-containing proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They play a role in the regulation of cell proliferation, programmed cell death (apoptosis), cell differentiation, and embryonic development. These enzymes belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. U-box domain-containing proteins function as E3 ubiquitin ligases (EC 2.3.2.27), mediating the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin. The N-terminal domain of these proteins is homologous to the universal stress protein (USP) family which has an ATP binding fold. The N-terminal domain is predicted to be involved in ATP binding.


Pssm-ID: 467493  Cd Length: 154  Bit Score: 55.76  E-value: 4.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  15 RILVAVDEGD-ESVHALKWCLASFAKRGggggaappDTIILLYVRPPPPTYSVLDAS--GYVFSDEVAAAIDGYSKEVAE 91
Cdd:cd01989     1 KVAVAVDGDDkKSKSALKWALDNLAPRG--------AKIVLVHVHPPVTMIPTPSGKvpPIQLREEEVSAYRKQEREKTE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  92 AVVEKAQKLCTlygkevggdgeaghEMKVEVKVAV---GDARNVICQMADKLGADVLVMGSHGYGLFKRSLKRSRFQSQk 168
Cdd:cd01989    73 KMLLPYLDMCS--------------RKKVQAEKVViesDDVAKGIVELISQHGITKLVMGAASDNHFSMKLKKSDVASS- 137

                         170
                  ....*....|.
gi 1002256505 169 laLLGSVSDYC 179
Cdd:cd01989   138 --VMKAAPDFC 146
USP_Rv2623_repeat1 cd23944
universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis ...
 16-190 7.93e-08

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: 49.32  E-value: 7.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  16 ILVAVDEGDESVHALKWCLASFAKRGGgggaappdTIILLYVRPPP-PTYSVLDASGYVFSDEVAAAidgyskevaEAVV 94
Cdd:cd23944     2 IIVGVDGSPASDAAVRWAAREAQLRQI--------PLTLVHVVPPVvVSWPEGPRPAEVLDWQQDEA---------RQVI 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  95 EKAQKLCtlygKEVGGdgeAGHEMKVEVKVAVGDARNVICQMADklGADVLVMGSHGYGLFKRSLkrsrfqsqklalLGS 174
Cdd:cd23944    65 EQARKVA----EEASG---EGPPVKVETEIVPGSPVPTLVEASR--DATMVVVGSRGIGALAGLL------------LGS 123

                         170
                  ....*....|....*.
gi 1002256505 175 VSDYCVRNANCPVLIV 190
Cdd:cd23944   124 VSTSLVRHAHCPVAVI 139
PRK15005 PRK15005
universal stress protein UspF;
117-191 1.64e-06

universal stress protein UspF;


Pssm-ID: 184967 [Multi-domain]  Cd Length: 144  Bit Score: 45.56  E-value: 1.64e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002256505 117 EMKVEVKVAVGDARNVICQMADKLGADVLVMGSHgyglfkrslkRSRFQSQklaLLGSVSDYCVRNANCPVLIVK 191
Cdd:PRK15005   83 TDRVHVHVEEGSPKDRILELAKKIPADMIIIASH----------RPDITTY---LLGSNAAAVVRHAECSVLVVR 144
PRK15456 PRK15456
universal stress protein UspG; Provisional
 119-191 1.09e-04

universal stress protein UspG; Provisional


Pssm-ID: 185353  Cd Length: 142  Bit Score: 40.69  E-value: 1.09e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002256505 119 KVEVKVAVGDARNVICQMADKLGADVLVMGshgyglfkrslkrSRFQSQKLALLGSVSDYCVRNANCPVLIVK 191
Cdd:PRK15456   83 RIKQHVRFGSVRDEVNELAEELGADVVVIG-------------SRNPSISTHLLGSNASSVIRHANLPVLVVR 142
USP-A-like cd23657
universal stress protein A and similar proteins; The universal stress protein UspA is a small ...
 14-191 5.13e-04

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: 38.44  E-value: 5.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  14 RRILVAVDEGDESvhalkwclASFAKRGGGGGAAPPDTIILLYVRPPPPTYsvldASGYVFSDEVAaaidgySKEVAEAV 93
Cdd:cd23657     2 KHILVAVDLSPES--------QSLVDKAVEIARENDAKLSLIHVDEDISEY----YTGLIDVDIAA------LQDLESTM 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  94 VEKAQK-LCTLYGKEVggdgeaghemkVEVKVAVGDARNVICQMADKLGADVLVMGSHGyglfkrslkrsRFQSQKlalL 172
Cdd:cd23657    64 LEEALKnLSELAGYPV-----------DHTFIGYGDLKEEILEVAKKHNVDLIVCGHHG-----------DFGLSL---L 118

                         170
                  ....*....|....*....
gi 1002256505 173 GSVSDYCVRNANCPVLIVK 191
Cdd:cd23657   119 GSSARAVLNSAPCDVLIVP 137
USP-E_repeat2 cd23660
Universal stress protein E, repeat 2; UspE is a tandem-type USP that consists of two USP ...
 78-191 2.16e-03

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: 36.86  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256505  78 VAAAID-----GYSKEVAEAVVEKAQKLCTLYGKEVG------------------------GDGEAGHEM---------- 118
Cdd:cd23660     4 ILVAVDpsneeEYHEDLNLRLIELAYSLAAQLKAELHlvsawpvtpeniaielpefdpteyVDAIRGRHLeamkalrqkf 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002256505 119 -KVEVKVAV--GDARNVICQMADKLGADVLVMGshgyglfkrSLKRSRFQSqklALLGSVSDYCVRNANCPVLIVK 191
Cdd:cd23660    84 gIDEEQTHVleGLPEEVIPDFAEELDADIVVLG---------TVARTGLSG---ALIGNTAEHVLDHLNCDLLALK 147
 
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.
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