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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409190  44 RRIIVVVDSCSEAKNALLWTLSHCAQPQDSILLLHFLKAKTSQSGDLANkEEGEDESCDKPTTSRADKKVSALKTMCELK 123
Cdd:cd23659   1 RKVLIAVDGSEESEYALEWALENLHRPGDEVVLLHVIEPPSLPAASLGS-GSEEWEALEEEAREKAEKLLEKYEKKLKEE 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18409190 124 RpEVKTEVVFVKGDeKGPTIVKEAREREASLLVLGQKKQHATWRLLM--VwaSqarpvtkhdfvEYCINNSPC 194
Cdd:cd23659  80 K-GIKVKVEVVAGD-PGEVICKAAEELKADLIVMGSRGLGALKRTLLgsV--S-----------DYVVHHSPC 137

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409190  44 RRIIVVVDSCSEAKNALLWTLSHCAQPQDSILLLHFLKAKTSQSGDLANkEEGEDESCDKPTTSRADKKVSALKTMCELK 123
Cdd:cd23659   1 RKVLIAVDGSEESEYALEWALENLHRPGDEVVLLHVIEPPSLPAASLGS-GSEEWEALEEEAREKAEKLLEKYEKKLKEE 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18409190 124 RpEVKTEVVFVKGDeKGPTIVKEAREREASLLVLGQKKQHATWRLLM--VwaSqarpvtkhdfvEYCINNSPC 194
Cdd:cd23659  80 K-GIKVKVEVVAGD-PGEVICKAAEELKADLIVMGSRGLGALKRTLLgsV--S-----------DYVVHHSPC 137

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409190  44 RRIIVVVDSCSEAKNALLWTLSHCAQPQDSILLLHFLKAKTSQSGDLANKEEGEDEscdkpttsRADKKVSALKTMCELK 123
Cdd:COG0589   3 KRILVPTDGSEEAERALEYAAELAKALGAELHLLHVVDPPPSAAAGPEELEEELRE--------EAEEALEEAAERLEEA 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18409190 124 RPEVKTEVVFvkgDEKGPTIVKEAREREASLLVLGQKKQHATWRLLM 170
Cdd:COG0589  75 GVEVETVVRE---GDPAEAILEAAEELDADLIVMGSRGRSGLRRLLL 118

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409190  44 RRIIVVVDSCSEAKNALLWTLSHCAQPQDSILLLHFLKAKTSQSGDLANkEEGEDESCDKPTTSRADKKVSALKTMCELK 123
Cdd:cd23659   1 RKVLIAVDGSEESEYALEWALENLHRPGDEVVLLHVIEPPSLPAASLGS-GSEEWEALEEEAREKAEKLLEKYEKKLKEE 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18409190 124 RpEVKTEVVFVKGDeKGPTIVKEAREREASLLVLGQKKQHATWRLLM--VwaSqarpvtkhdfvEYCINNSPC 194
Cdd:cd23659  80 K-GIKVKVEVVAGD-PGEVICKAAEELKADLIVMGSRGLGALKRTLLgsV--S-----------DYVVHHSPC 137

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409190    46 IIVVVDSCSEAKNALLWTLSHCAQPQDSILLLHFLKAKTSQSGDLANKEEGEDESCDKpttsRADKKVSALKTMCELKRP 125
Cdd:pfam00582   1 ILVAVDGSEESKRALEWAAELAKARGAELILLHVIDPPPSGAASLADESAEEEELELE----LAEAEALAAAAAAEAGGV 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18409190   126 EVKTEVVFVKGDEkgpTIVKEAREREASLLVLGQKKQHATWRLLMvwASQArpvtkhdfvEYCINNSPCMAIAVR 200
Cdd:pfam00582  77 KVEVVVVVGDPAE---EILEVAEEEDADLIVMGSRGRSGLSRLLL--GSVA---------EYVLRHAPCPVLVVR 137

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409190  45 RIIVVVDSCS-EAKNALLWTLSHCAQPQDSILLLH-FLKAKT--SQSGDLANKEEGEDE--SCDKPTTSRADKKVSALKT 118
Cdd:cd01989   1 KVAVAVDGDDkKSKSALKWALDNLAPRGAKIVLVHvHPPVTMipTPSGKVPPIQLREEEvsAYRKQEREKTEKMLLPYLD 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 18409190 119 MCElkRPEVKTEVVFVKGDEKGPTIVKEAREREASLLVLG 158
Cdd:cd01989  81 MCS--RKKVQAEKVVIESDDVAKGIVELISQHGITKLVMG 118