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Conserved domains on  [gi|1063706929|ref|NP_001324262|]
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U-box domain-containing protein [Arabidopsis thaliana]

Protein Classification

argininosuccinate synthase; FAD synthase( domain architecture ID 10113151)

argininosuccinate synthase reversibly catalyzes the ATP-dependent condensation of a citrulline with an aspartate to give argininosuccinate| FAD (Flavin adenine dinucleotide) synthase catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
USP_STK_Ubox_N cd01989
N-terminal USP domain of serine threonine kinases (STK) and U-box domain proteins; This model ...
 15-144 4.58e-47

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: 157.45  E-value: 4.58e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706929  15 KIYVAVGSDLGN-KSTLVWAIQN--TGGKEFCIVHVHQPL----------------------YRK-EKEKTQKILDKYLQ 68
Cdd:cd01989     1 KVAVAVDGDDKKsKSALKWALDNlaPRGAKIVLVHVHPPVtmiptpsgkvppiqlreeevsaYRKqEREKTEKMLLPYLD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063706929  69 KCRQMQVCAEMIHIKMESVEKGIIQLISERNVKKLVMGAASDTRYSMRmaDLLSTKAIYIRQEAPATCCIWFTCKG 144
Cdd:cd01989    81 MCSRKKVQAEKVVIESDDVAKGIVELISQHGITKLVMGAASDNHFSMK--LKKSDVASSVMKAAPDFCTVWVVCKG 154
PTZ00121 super family cl31754
MAEBL; Provisional
 192-376 6.88e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 6.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706929  192 VYQLAVFEAEKSKKEASLEafKHQEVVKEKNEAIKRGKEWESAYLEELK-----QRKETEMELKKVRE--KLEKMRYISE 264
Cdd:PTZ00121  1635 VEQLKKKEAEEKKKAEELK--KAEEENKIKAAEEAKKAEEDKKKAEEAKkaeedEKKAAEALKKEAEEakKAEELKKKEA 1712

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706929  265 NRITESYMLVQKLQDKYNLATKVLRKAKEERDlliKGRDIAIIEVEELRKEVSRSDEHREAPQYFICPISLVNKKVNMER 344
Cdd:PTZ00121  1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKK---KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1063706929  345 NRRLYRISSQIKTFVFNVSGSDEGSTTSSRWI 376
Cdd:PTZ00121  1790 EKRRMEVDKKIKDIFDNFANIIEGGKEGNLVI 1821
 
Name Accession Description Interval E-value
USP_STK_Ubox_N cd01989
N-terminal USP domain of serine threonine kinases (STK) and U-box domain proteins; This model ...
 15-144 4.58e-47

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: 157.45  E-value: 4.58e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706929  15 KIYVAVGSDLGN-KSTLVWAIQN--TGGKEFCIVHVHQPL----------------------YRK-EKEKTQKILDKYLQ 68
Cdd:cd01989     1 KVAVAVDGDDKKsKSALKWALDNlaPRGAKIVLVHVHPPVtmiptpsgkvppiqlreeevsaYRKqEREKTEKMLLPYLD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063706929  69 KCRQMQVCAEMIHIKMESVEKGIIQLISERNVKKLVMGAASDTRYSMRmaDLLSTKAIYIRQEAPATCCIWFTCKG 144
Cdd:cd01989    81 MCSRKKVQAEKVVIESDDVAKGIVELISQHGITKLVMGAASDNHFSMK--LKKSDVASSVMKAAPDFCTVWVVCKG 154
PTZ00121 PTZ00121
MAEBL; Provisional
 192-376 6.88e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 6.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706929  192 VYQLAVFEAEKSKKEASLEafKHQEVVKEKNEAIKRGKEWESAYLEELK-----QRKETEMELKKVRE--KLEKMRYISE 264
Cdd:PTZ00121  1635 VEQLKKKEAEEKKKAEELK--KAEEENKIKAAEEAKKAEEDKKKAEEAKkaeedEKKAAEALKKEAEEakKAEELKKKEA 1712

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706929  265 NRITESYMLVQKLQDKYNLATKVLRKAKEERDlliKGRDIAIIEVEELRKEVSRSDEHREAPQYFICPISLVNKKVNMER 344
Cdd:PTZ00121  1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKK---KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1063706929  345 NRRLYRISSQIKTFVFNVSGSDEGSTTSSRWI 376
Cdd:PTZ00121  1790 EKRRMEVDKKIKDIFDNFANIIEGGKEGNLVI 1821
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 194-316 8.21e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.60  E-value: 8.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706929 194 QLAVFEAEKSKKEASLEAFKhqEVVKEKNEAIKRgKEWESAYLEELKQRKETEM-ELKKVRE---------KLEKMRYIS 263
Cdd:COG1579    32 ELAELEDELAALEARLEAAK--TELEDLEKEIKR-LELEIEEVEARIKKYEEQLgNVRNNKEyealqkeieSLKRRISDL 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063706929 264 ENRITESYMLVQKLQDKYNLATKVLRKAKEERDLLIKGRDIAIIEVEELRKEV 316
Cdd:COG1579   109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
 
Name Accession Description Interval E-value
USP_STK_Ubox_N cd01989
N-terminal USP domain of serine threonine kinases (STK) and U-box domain proteins; This model ...
 15-144 4.58e-47

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: 157.45  E-value: 4.58e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706929  15 KIYVAVGSDLGN-KSTLVWAIQN--TGGKEFCIVHVHQPL----------------------YRK-EKEKTQKILDKYLQ 68
Cdd:cd01989     1 KVAVAVDGDDKKsKSALKWALDNlaPRGAKIVLVHVHPPVtmiptpsgkvppiqlreeevsaYRKqEREKTEKMLLPYLD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063706929  69 KCRQMQVCAEMIHIKMESVEKGIIQLISERNVKKLVMGAASDTRYSMRmaDLLSTKAIYIRQEAPATCCIWFTCKG 144
Cdd:cd01989    81 MCSRKKVQAEKVVIESDDVAKGIVELISQHGITKLVMGAASDNHFSMK--LKKSDVASSVMKAAPDFCTVWVVCKG 154
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
 15-106 6.81e-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: 36.83  E-value: 6.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706929  15 KIYVAV-GSDLGnKSTLVWAIQN--TGGKEFCIVHVHQP-----------------LYRKEKEKTQKILDKYLQKCRQMQ 74
Cdd:cd23659     2 KVLIAVdGSEES-EYALEWALENlhRPGDEVVLLHVIEPpslpaaslgsgseeweaLEEEAREKAEKLLEKYEKKLKEEK 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1063706929  75 VCAEMIHIKMESVEKGIIQLISERNVKKLVMG 106
Cdd:cd23659    81 GIKVKVEVVAGDPGEVICKAAEELKADLIVMG 112
PTZ00121 PTZ00121
MAEBL; Provisional
 192-376 6.88e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 6.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706929  192 VYQLAVFEAEKSKKEASLEafKHQEVVKEKNEAIKRGKEWESAYLEELK-----QRKETEMELKKVRE--KLEKMRYISE 264
Cdd:PTZ00121  1635 VEQLKKKEAEEKKKAEELK--KAEEENKIKAAEEAKKAEEDKKKAEEAKkaeedEKKAAEALKKEAEEakKAEELKKKEA 1712

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706929  265 NRITESYMLVQKLQDKYNLATKVLRKAKEERDlliKGRDIAIIEVEELRKEVSRSDEHREAPQYFICPISLVNKKVNMER 344
Cdd:PTZ00121  1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKK---KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1063706929  345 NRRLYRISSQIKTFVFNVSGSDEGSTTSSRWI 376
Cdd:PTZ00121  1790 EKRRMEVDKKIKDIFDNFANIIEGGKEGNLVI 1821
USP-like cd00293
universal stress protein (USP) and similar proteins; The universal stress protein (USP) is a ...
 15-107 8.16e-03

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: 36.17  E-value: 8.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706929  15 KIYVAV-GSDLGNKStLVWAIQN--TGGKEFCIVHVHQP------------LYRKEKEKTQKILDKYLQKCRQMQVCAEm 79
Cdd:cd00293     1 KILVAVdGSEESERA-LEWALELakRPGAELTLLHVVDPppssslsggleeLADELKEEAEELLEEAKKLAEEAGVEVE- 78

                          90       100
                  ....*....|....*....|....*...
gi 1063706929  80 IHIKMESVEKGIIQLISERNVKKLVMGA 107
Cdd:cd00293    79 TIVVEGDPAEAILEEAKELGADLIVMGS 106
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 194-316 8.21e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.60  E-value: 8.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706929 194 QLAVFEAEKSKKEASLEAFKhqEVVKEKNEAIKRgKEWESAYLEELKQRKETEM-ELKKVRE---------KLEKMRYIS 263
Cdd:COG1579    32 ELAELEDELAALEARLEAAK--TELEDLEKEIKR-LELEIEEVEARIKKYEEQLgNVRNNKEyealqkeieSLKRRISDL 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063706929 264 ENRITESYMLVQKLQDKYNLATKVLRKAKEERDLLIKGRDIAIIEVEELRKEV 316
Cdd:COG1579   109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
 
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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