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Conserved domains on  [gi|1522592383|gb|RQE02349|]
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universal stress protein [Lactococcus lactis]

Protein Classification

universal stress protein( domain architecture ID 10001747)

universal stress protein (USP) enhances the rate of cell survival during prolonged exposure to stress agents

CATH:  3.40.50.620
Gene Ontology:  GO:0042802
SCOP:  8083864

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
5-140 6.64e-38

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


:

Pssm-ID: 440354  Cd Length: 136  Bit Score: 125.42  E-value: 6.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383   5 YKKILVAVDGSDQSKEAIHEAVAIAKRNKTSLFVLHVKDETRlrGTPYALAINLDDLETESKEIIAEV-EVLINDEVEFE 83
Cdd:COG0589     2 YKRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPP--SAAAGPEELEEELREEAEEALEEAaERLEEAGVEVE 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1522592383  84 VHAFTGNPKKEIINFAKQFELDLIVVGSNGKGLLDRMLVGSTTSYVVNHAPCNVMVV 140
Cdd:COG0589    80 TVVREGDPAEAILEAAEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
 
Name Accession Description Interval E-value
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
5-140 6.64e-38

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 125.42  E-value: 6.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383   5 YKKILVAVDGSDQSKEAIHEAVAIAKRNKTSLFVLHVKDETRlrGTPYALAINLDDLETESKEIIAEV-EVLINDEVEFE 83
Cdd:COG0589     2 YKRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPP--SAAAGPEELEEELREEAEEALEEAaERLEEAGVEVE 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1522592383  84 VHAFTGNPKKEIINFAKQFELDLIVVGSNGKGLLDRMLVGSTTSYVVNHAPCNVMVV 140
Cdd:COG0589    80 TVVREGDPAEAILEAAEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
7-140 1.91e-36

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: 121.69  E-value: 1.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383   7 KILVAVDGSDQSKEAIHEAVAIAKRNKTSLFVLHVKDETRLRGTPYALAINLDDLETESKEIIAEVEVLIN-DEVEFEVH 85
Cdd:cd00293     1 KILVAVDGSEESERALEWALELAKRPGAELTLLHVVDPPPSSSLSGGLEELADELKEEAEELLEEAKKLAEeAGVEVETI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1522592383  86 AFTGNPKKEIINFAKQFELDLIVVGSNGKGLLDRMLVGSTTSYVVNHAPCNVMVV 140
Cdd:cd00293    81 VVEGDPAEAILEEAKELGADLIVMGSRGRSGLKRLLLGSVSEYVLRHAPCPVLVV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
8-141 8.00e-36

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: 120.21  E-value: 8.00e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383   8 ILVAVDGSDQSKEAIHEAVAIAKRNKTSLFVLHVKDETRLRGTPYALAINLDDLETESKEII---AEVEVLINDEVEFEV 84
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAELILLHVIDPPPSGAASLADESAEEEELELELAEAealAAAAAAEAGGVKVEV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1522592383  85 HAFTGNPKKEIINFAKQFELDLIVVGSNGKGLLDRMLVGSTTSYVVNHAPCNVMVVK 141
Cdd:pfam00582  81 VVVVGDPAEEILEVAEEEDADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
PRK15005 PRK15005
universal stress protein UspF;
5-141 1.32e-10

universal stress protein UspF;


Pssm-ID: 184967 [Multi-domain]  Cd Length: 144  Bit Score: 55.58  E-value: 1.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383   5 YKKILVAVDGSDQS--KEAIHEAVAIAKRNKTSLFVLHVkdetrLRGTPYALAINL---------DDLETESKEIIAEVE 73
Cdd:PRK15005    2 NRTILVPIDISDSEltQRVISHVEAEAKIDDAEVHFLTV-----IPSLPYYASLGLaysaelpamDDLKAEAKSQLEEII 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1522592383  74 VLIN-DEVEFEVHAFTGNPKKEIINFAKQFELDLIVVGSNGKGlLDRMLVGSTTSYVVNHAPCNVMVVK 141
Cdd:PRK15005   77 KKFKlPTDRVHVHVEEGSPKDRILELAKKIPADMIIIASHRPD-ITTYLLGSNAAAVVRHAECSVLVVR 144
 
Name Accession Description Interval E-value
UspA COG0589
Nucleotide-binding universal stress protein, UspA family [Signal transduction mechanisms];
5-140 6.64e-38

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


Pssm-ID: 440354  Cd Length: 136  Bit Score: 125.42  E-value: 6.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383   5 YKKILVAVDGSDQSKEAIHEAVAIAKRNKTSLFVLHVKDETRlrGTPYALAINLDDLETESKEIIAEV-EVLINDEVEFE 83
Cdd:COG0589     2 YKRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPP--SAAAGPEELEEELREEAEEALEEAaERLEEAGVEVE 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1522592383  84 VHAFTGNPKKEIINFAKQFELDLIVVGSNGKGLLDRMLVGSTTSYVVNHAPCNVMVV 140
Cdd:COG0589    80 TVVREGDPAEAILEAAEELDADLIVMGSRGRSGLRRLLLGSVAERVLRHAPCPVLVV 136
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
7-140 1.91e-36

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: 121.69  E-value: 1.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383   7 KILVAVDGSDQSKEAIHEAVAIAKRNKTSLFVLHVKDETRLRGTPYALAINLDDLETESKEIIAEVEVLIN-DEVEFEVH 85
Cdd:cd00293     1 KILVAVDGSEESERALEWALELAKRPGAELTLLHVVDPPPSSSLSGGLEELADELKEEAEELLEEAKKLAEeAGVEVETI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1522592383  86 AFTGNPKKEIINFAKQFELDLIVVGSNGKGLLDRMLVGSTTSYVVNHAPCNVMVV 140
Cdd:cd00293    81 VVEGDPAEAILEEAKELGADLIVMGSRGRSGLKRLLLGSVSEYVLRHAPCPVLVV 135
Usp pfam00582
Universal stress protein family; The universal stress protein UspA is a small cytoplasmic ...
8-141 8.00e-36

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: 120.21  E-value: 8.00e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383   8 ILVAVDGSDQSKEAIHEAVAIAKRNKTSLFVLHVKDETRLRGTPYALAINLDDLETESKEII---AEVEVLINDEVEFEV 84
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAELILLHVIDPPPSGAASLADESAEEEELELELAEAealAAAAAAEAGGVKVEV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1522592383  85 HAFTGNPKKEIINFAKQFELDLIVVGSNGKGLLDRMLVGSTTSYVVNHAPCNVMVVK 141
Cdd:pfam00582  81 VVVVGDPAEEILEVAEEEDADLIVMGSRGRSGLSRLLLGSVAEYVLRHAPCPVLVVR 137
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
6-141 9.17e-30

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: 105.01  E-value: 9.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383   6 KKILVAVDGSDQSKEAIHEAVAIAKRNKTSLFVLHVKDETRLRGTPYALAINL-----DDLETESKEIIAEVEVLINDE- 79
Cdd:cd23659     1 RKVLIAVDGSEESEYALEWALENLHRPGDEVVLLHVIEPPSLPAASLGSGSEEwealeEEAREKAEKLLEKYEKKLKEEk 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1522592383  80 -VEFEVHAFTGNPKKEIINFAKQFELDLIVVGSNGKGLLDRMLVGSTTSYVVNHAPCNVMVVK 141
Cdd:cd23659    81 gIKVKVEVVAGDPGEVICKAAEELKADLIVMGSRGLGALKRTLLGSVSDYVVHHSPCPVLVVR 143
USP-A-like cd23657
universal stress protein A and similar proteins; The universal stress protein UspA is a small ...
5-141 2.98e-18

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: 75.42  E-value: 2.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383   5 YKKILVAVDGSDQSKEAIHEAVAIAKRNKTSLFVLHVKDETRLRGTPYaLAINLDDLETESKEIIAEVEVLINDEVEFEV 84
Cdd:cd23657     1 YKHILVAVDLSPESQSLVDKAVEIARENDAKLSLIHVDEDISEYYTGL-IDVDIAALQDLESTMLEEALKNLSELAGYPV 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383  85 HAF---TGNPKKEIINFAKQFELDLIVVGSNGKGLLDRMlvGSTTSYVVNHAPCNVMVVK 141
Cdd:cd23657    80 DHTfigYGDLKEEILEVAKKHNVDLIVCGHHGDFGLSLL--GSSARAVLNSAPCDVLIVP 137
USP_Rv2623_repeat1 cd23944
universal stress protein Rv2623 and similar proteins, USP repeat 1; Mycobacterium tuberculosis ...
8-140 5.56e-15

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: 67.04  E-value: 5.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383   8 ILVAVDGSDQSKEAIHEAVAIAKRNKTSLFVLHVKDETRLRGTPYALAIN-LDDLETESKEIIAEV-----EVLIND-EV 80
Cdd:cd23944     2 IIVGVDGSPASDAAVRWAAREAQLRQIPLTLVHVVPPVVVSWPEGPRPAEvLDWQQDEARQVIEQArkvaeEASGEGpPV 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383  81 EFEVHAFTGNPKKEIINFAKQFELdlIVVGSNGKGLLDRMLVGSTTSYVVNHAPCNVMVV 140
Cdd:cd23944    82 KVETEIVPGSPVPTLVEASRDATM--VVVGSRGIGALAGLLLGSVSTSLVRHAHCPVAVI 139
USP_Rv2623_repeat2 cd23661
universal stress protein Rv2623 and similar proteins, USP repeat 2; Mycobacterium tuberculosis ...
8-141 1.28e-13

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: 63.30  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383   8 ILVAVDGSDQSKEAIHEAVAIAKRNKTSLFVLHVKDETRLRGTPyalAINLDDLETESKEIIAE-VEVLINDEVEFEVHA 86
Cdd:cd23661     2 VVVGVDGSPASELATEIAFDEASRRGVDLVALHAWSDMGPGGFL---GIDWRESEQDQERMLAErLAGWQERYPDVHVHK 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1522592383  87 FT--GNPKKEIINFAKQfeLDLIVVGSNGKGLLDRMLVGSTTSYVVNHAPCNVMVVK 141
Cdd:cd23661    79 VVvrDRPARVLLEASER--AQLVVVGSHGRGGFAGMLLGSVSRAVLHSAPCPVIVVR 133
PRK15005 PRK15005
universal stress protein UspF;
5-141 1.32e-10

universal stress protein UspF;


Pssm-ID: 184967 [Multi-domain]  Cd Length: 144  Bit Score: 55.58  E-value: 1.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383   5 YKKILVAVDGSDQS--KEAIHEAVAIAKRNKTSLFVLHVkdetrLRGTPYALAINL---------DDLETESKEIIAEVE 73
Cdd:PRK15005    2 NRTILVPIDISDSEltQRVISHVEAEAKIDDAEVHFLTV-----IPSLPYYASLGLaysaelpamDDLKAEAKSQLEEII 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1522592383  74 VLIN-DEVEFEVHAFTGNPKKEIINFAKQFELDLIVVGSNGKGlLDRMLVGSTTSYVVNHAPCNVMVVK 141
Cdd:PRK15005   77 KKFKlPTDRVHVHVEEGSPKDRILELAKKIPADMIIIASHRPD-ITTYLLGSNAAAVVRHAECSVLVVR 144
USP-E_repeat2 cd23660
Universal stress protein E, repeat 2; UspE is a tandem-type USP that consists of two USP ...
7-141 1.60e-08

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: 49.96  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383   7 KILVAVDGSDQSKEA-------IHEAVAIAKRNKTSLFVLHVKDETrlrgtPYALAINLDDLETESKEIIAEVEVLINDE 79
Cdd:cd23660     3 RILVAVDPSNEEEYHedlnlrlIELAYSLAAQLKAELHLVSAWPVT-----PENIAIELPEFDPTEYVDAIRGRHLEAMK 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383  80 --------VEFEVHAFTGNPKKEIINFAKQFELDLIVVGSNGKGLLDRMLVGSTTSYVVNHAPCNVMVVK 141
Cdd:cd23660    78 alrqkfgiDEEQTHVLEGLPEEVIPDFAEELDADIVVLGTVARTGLSGALIGNTAEHVLDHLNCDLLALK 147
USP_KdpD-like cd01987
USP domain of the osmosensitive K+ channel histidine kinase family; The KdpDE two component ...
7-134 1.87e-07

USP domain of the osmosensitive K+ channel histidine kinase family; The KdpDE two component system is widespread in bacteria and archaea; it controls potassium homeostasis and virulence by regulating the transcription of multiple genes, including a kdpFABC operon, which encodes a high-affinity P-type ATPase transporter. The KdpD histidine kinase (HK, EC:2.7.13.3) contain an N-terminal sensory cytoplasmic region (NTR) composed of KdpD' and universal stress protein (USP) domains, a canonical transmembrane domain, and a cytoplasmic C-terminal region with a transmitter GAF domain and an EnvZ-like catalytic HK domain. Proteins containing the USP domain are induced by many environmental stressors such as nutrient starvation, drought, extreme temperatures, high salinity, and the presence of uncouplers, antibiotics, and metals. It enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity.


Pssm-ID: 467491 [Multi-domain]  Cd Length: 124  Bit Score: 46.86  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383   7 KILVAVDGSDQSKEAIHEAVAIAKRNKTSLFVLHVKDETRLRGTPYALAiNLDDLETESKEIIAEVEVLINDEVefevha 86
Cdd:cd01987     1 RILVCISSSPTSEKLIRRAARLAERLNGELTAVYVETPEESRLDEESQR-RLLTNLKLAEELGAEVVSVEGDDV------ 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1522592383  87 ftgnpKKEIINFAKQFELDLIVVGSNGKGLLDRMLVGSTTSYVVNHAP 134
Cdd:cd01987    74 -----AEAIVEFARERNVTQIVLGQSRRRRWRRLFKGSLVDRLLREAP 116
USP_NhaS5_C cd01988
C-terminal USP domain(s) of Na(+)/H(+) antiporter NhaS5 and similar proteins; Na(+)/H(+) ...
8-139 1.11e-05

C-terminal USP domain(s) of Na(+)/H(+) antiporter NhaS5 and similar proteins; Na(+)/H(+) exchange proteins eject protons from cells, effectively eliminating excess acid from actively metabolizing cells. Na(+)/H(+) exchange activity is also crucial for the regulation of cell volume, and for the reabsorption of NaCl across renal, intestinal, and other epithelia. These antiporters exchange Na(+) for H(+) in an electroneutral manner, and this activity is carried out by a family of Na(+)/H(+) exchangers, or NHEs, which are known to be present in both prokaryotic and eukaryotic cells. These exchangers are highly-regulated (glyco)phosphoproteins, which, based on their primary structure, appear to contain 10-12 membrane-spanning regions (M) at the N-terminus and a large cytoplasmic region at the C-terminus. The transmembrane regions M3-M12 share identity with other members of the family. The M6 and M7 regions are highly conserved. This is thought to be the region that is involved in the transport of sodium and hydrogen ions. The C-terminal region contains one or two domains that show homology with universal stress protein (USP), 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: 467492  Cd Length: 125  Bit Score: 42.10  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1522592383   8 ILVAVDGSDQSKEAIHEAVAIAkRNKTSLFV--LHVK--DETRLRGTPYALAINLDDLETESKeIIAEVEVLINDEVefe 83
Cdd:cd01988     2 VLVPTANPPTAKLLLEFAAALA-EDEKGAIVplLYVGspNHMDDKELEQAEQRFEELMELLNG-VNVHPIVRISHSV--- 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1522592383  84 vhaftgnPKKEIINFAKQFElDLIVVGSNGKGLLDRMLvGSTTSYVVNHAPCNVMV 139
Cdd:cd01988    77 -------AARVTAREAKSFA-DLIVMGWRRTFLGNVLL-GSTIDKVLMKAPTDVAV 123
PRK15456 PRK15456
universal stress protein UspG; Provisional
78-141 8.09e-03

universal stress protein UspG; Provisional


Pssm-ID: 185353  Cd Length: 142  Bit Score: 34.53  E-value: 8.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1522592383  78 DEVEFEVHAFTGNPKKEIINFAKQFELDLIVVGSNGKGLLDRMLvGSTTSYVVNHAPCNVMVVK 141
Cdd:PRK15456   80 DPSRIKQHVRFGSVRDEVNELAEELGADVVVIGSRNPSISTHLL-GSNASSVIRHANLPVLVVR 142
 
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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