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Conserved domains on  [gi|75180094|sp|Q9LQ92|]
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RecName: Full=U-box domain-containing protein 54; AltName: Full=Plant U-box protein 54; AltName: Full=RING-type E3 ubiquitin transferase PUB54

Protein Classification

U-box domain-containing protein; RING finger protein( domain architecture ID 11549902)

U-box domain-containing protein contains a modified RING finger and functions as an E3 ubiquitin ligase that mediates 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| RING finger protein may function as an E3 ubiquitin protein ligase that mediates 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; similar to Homo sapiens E3 ubiquitin-protein ligase RNF10

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 ...
 5-153 4.61e-54

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: 173.24  E-value: 4.61e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75180094   5 IYVAVNQDVRESKKTLLWALKNLQ--VKKIFLLHVHLPFSLTTS------SSRLEQSEIDAIQDSELNTSVNSLYKYRDI 76
Cdd:cd01989   2 VAVAVDGDDKKSKSALKWALDNLAprGAKIVLVHVHPPVTMIPTpsgkvpPIQLREEEVSAYRKQEREKTEKMLLPYLDM 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75180094  77 CINKGVNEKDVdtsMISGHDVGEGIVELIYQNIITNLVMGAAADPHYSRgMSITSRKAEYVSQHAPHSCKIWFICKG 153
Cdd:cd01989  82 CSRKKVQAEKV---VIESDDVAKGIVELISQHGITKLVMGAASDNHFSM-KLKKSDVASSVMKAAPDFCTVWVVCKG 154
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 235-289 2.25e-25

U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins; WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis.


:

Pssm-ID: 438317 [Multi-domain]  Cd Length: 55  Bit Score: 95.65  E-value: 2.25e-25
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75180094 235 EDFKCPISMEIMRDPHVAADGFTYEAEEFRKWLRSgGRTSPKTNKPLENHNLVPN 289
Cdd:cd16655   2 DEFLCPITQELMRDPVVAADGHTYERSAIEEWLET-HNTSPMTRLPLSSTDLVPN 55
 
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 ...
 5-153 4.61e-54

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: 173.24  E-value: 4.61e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75180094   5 IYVAVNQDVRESKKTLLWALKNLQ--VKKIFLLHVHLPFSLTTS------SSRLEQSEIDAIQDSELNTSVNSLYKYRDI 76
Cdd:cd01989   2 VAVAVDGDDKKSKSALKWALDNLAprGAKIVLVHVHPPVTMIPTpsgkvpPIQLREEEVSAYRKQEREKTEKMLLPYLDM 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75180094  77 CINKGVNEKDVdtsMISGHDVGEGIVELIYQNIITNLVMGAAADPHYSRgMSITSRKAEYVSQHAPHSCKIWFICKG 153
Cdd:cd01989  82 CSRKKVQAEKV---VIESDDVAKGIVELISQHGITKLVMGAASDNHFSM-KLKKSDVASSVMKAAPDFCTVWVVCKG 154
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 235-289 2.25e-25

U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins; WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis.


Pssm-ID: 438317 [Multi-domain]  Cd Length: 55  Bit Score: 95.65  E-value: 2.25e-25
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75180094 235 EDFKCPISMEIMRDPHVAADGFTYEAEEFRKWLRSgGRTSPKTNKPLENHNLVPN 289
Cdd:cd16655   2 DEFLCPITQELMRDPVVAADGHTYERSAIEEWLET-HNTSPMTRLPLSSTDLVPN 55
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 236-299 3.47e-21

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 84.98  E-value: 3.47e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75180094    236 DFKCPISMEIMRDPHVAADGFTYEAEEFRKWLRSGGrTSPKTNKPLENHNLVPNHTLRIIIKDW 299
Cdd:smart00504   1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLLSHG-TDPVTGQPLTHEDLIPNLALKSAIQEW 63
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 235-303 5.59e-16

U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues.


Pssm-ID: 398320 [Multi-domain]  Cd Length: 73  Bit Score: 71.19  E-value: 5.59e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75180094   235 EDFKCPISMEIMRDPHVAADGFTYEAEEFRKWLRSGGRTSPKTNKPLENHNLVPNHTLRIIIKDWLEKN 303
Cdd:pfam04564   3 DEFLDPITFELMTDPVILPSGITYDRSTIERHLLSVDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEK 71
 
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 ...
 5-153 4.61e-54

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: 173.24  E-value: 4.61e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75180094   5 IYVAVNQDVRESKKTLLWALKNLQ--VKKIFLLHVHLPFSLTTS------SSRLEQSEIDAIQDSELNTSVNSLYKYRDI 76
Cdd:cd01989   2 VAVAVDGDDKKSKSALKWALDNLAprGAKIVLVHVHPPVTMIPTpsgkvpPIQLREEEVSAYRKQEREKTEKMLLPYLDM 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75180094  77 CINKGVNEKDVdtsMISGHDVGEGIVELIYQNIITNLVMGAAADPHYSRgMSITSRKAEYVSQHAPHSCKIWFICKG 153
Cdd:cd01989  82 CSRKKVQAEKV---VIESDDVAKGIVELISQHGITKLVMGAASDNHFSM-KLKKSDVASSVMKAAPDFCTVWVVCKG 154
RING-Ubox_WDSUB1-like cd16655
U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing ...
 235-289 2.25e-25

U-box domain, a modified RING finger, found in WD repeat, SAM and U-box domain-containing protein 1 (WDSUB1) and similar proteins; WDSUB1 is an uncharacterized protein containing seven WD40 repeats and a SAM domain in addition to the U-box. Its biological role remains unclear. This subfamily also includes many uncharacterized kinase domain-containing U-box (AtPUB) proteins and several MIF4G motif-containing AtPUB proteins from Arabidopsis.


Pssm-ID: 438317 [Multi-domain]  Cd Length: 55  Bit Score: 95.65  E-value: 2.25e-25
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75180094 235 EDFKCPISMEIMRDPHVAADGFTYEAEEFRKWLRSgGRTSPKTNKPLENHNLVPN 289
Cdd:cd16655   2 DEFLCPITQELMRDPVVAADGHTYERSAIEEWLET-HNTSPMTRLPLSSTDLVPN 55
Ubox smart00504
Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2 ...
 236-299 3.47e-21

Modified RING finger domain; Modified RING finger domain, without the full complement of Zn2+-binding ligands. Probable involvement in E2-dependent ubiquitination.


Pssm-ID: 128780 [Multi-domain]  Cd Length: 63  Bit Score: 84.98  E-value: 3.47e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75180094    236 DFKCPISMEIMRDPHVAADGFTYEAEEFRKWLRSGGrTSPKTNKPLENHNLVPNHTLRIIIKDW 299
Cdd:smart00504   1 EFLCPISLEVMKDPVILPSGQTYERSAIEKWLLSHG-TDPVTGQPLTHEDLIPNLALKSAIQEW 63
U-box pfam04564
U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast ...
 235-303 5.59e-16

U-box domain; The U-box is a domain of ~70 amino acids that is present in proteins from yeast to human. It consists of the beta-beta-alpha-beta-alpha- fold typical of U-box and RING domains. The central alpha helix is flanked by two prominent surface-exposed loop regions. This domain is one class of E3 ligases, involved in the ubiquitination process. This domain is related to the Ring finger pfam00097 but lacks the zinc binding residues.


Pssm-ID: 398320 [Multi-domain]  Cd Length: 73  Bit Score: 71.19  E-value: 5.59e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75180094   235 EDFKCPISMEIMRDPHVAADGFTYEAEEFRKWLRSGGRTSPKTNKPLENHNLVPNHTLRIIIKDWLEKN 303
Cdd:pfam04564   3 DEFLDPITFELMTDPVILPSGITYDRSTIERHLLSVDPTDPFTREPLTHDQLIPNLELKAKIDAWLEEK 71
RING-Ubox_PUB cd16664
U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and ...
 235-283 1.97e-15

U-box domain, a modified RING finger, found in Arabidopsis plant U-box proteins (AtPUB) and similar proteins; The plant PUB proteins, also known as U-box domain-containing proteins, are much more numerous in Arabidopsis which has 62 in comparison with the typical 6 in most animals. The majority of AtPUBs in this subfamily are known as ARM domain-containing PUB proteins, containing a C-terminally-located, tandem ARM (armadillo) repeat protein-interaction region in addition to the U-box domain. They have been implicated in the regulation of cell death and defense. They also play important roles in other plant-specific pathways, such as controlling both self-incompatibility and pseudo-self-incompatibility, as well as acting in abiotic stress. A subgroup of ARM domain-containing PUB proteins harbors a plant-specific U-box N-terminal domain.


Pssm-ID: 438326 [Multi-domain]  Cd Length: 53  Bit Score: 69.13  E-value: 1.97e-15
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 75180094 235 EDFKCPISMEIMRDPHVAADGFTYEAEEFRKWLRSGGRTSPKTNKPLEN 283
Cdd:cd16664   2 EEFICPISLELMKDPVILATGQTYERAAIEKWLDSGNNTCPITGQPLTH 50
RING-Ubox_CHIP cd16654
U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein ...
 237-303 2.74e-14

U-box domain, a modified RING finger, found in carboxyl terminus of HSP70-interacting protein (CHIP) and similar proteins; CHIP, also known as STIP1 homology and U box-containing protein 1 (STUB1), CLL-associated antigen KW-8, or Antigen NY-CO-7, is a multifunctional protein that functions both as a co-chaperone and an E3 ubiquitin-protein ligase. It couples protein folding and proteasome mediated degradation by interacting with heat shock proteins (e.g. HSC70) and ubiquitinating their misfolded client proteins, thereby targeting them for proteasomal degradation. It is also important for cellular differentiation and survival (or apoptosis), as well as susceptibility to stress. It targets a wide range of proteins, such as expanded ataxin-1, ataxin-3, huntingtin, and androgen receptor, which play roles in glucocorticoid response, tau degradation, and both p53 and cAMP signaling. CHIP contains an N-terminal tetratricopeptide repeat (TPR) domain responsible for protein-protein interaction, a highly charged middle coiled-coil (CC), and a C-terminal RING-like U-box domain acting as an ubiquitin ligase.


Pssm-ID: 438316 [Multi-domain]  Cd Length: 71  Bit Score: 66.45  E-value: 2.74e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75180094 237 FKCPISMEIMRDPHVAADGFTYEAEEFRKWLRSGGRTSPKTNKPLENHNLVPNHTLRIIIKDWLEKN 303
Cdd:cd16654   5 LCCKISFELMRDPVITPSGITYERKDIEEHLQRVGHFDPITREPLTQDQLIPNLALKEAIEAFLEEN 71
RING-Ubox_LubX-like_rpt2 cd23150
second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein ...
 237-302 2.83e-12

second U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the second one.


Pssm-ID: 438512 [Multi-domain]  Cd Length: 69  Bit Score: 60.94  E-value: 2.83e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75180094 237 FKCPISMEIMRDPHVAADGFTYEAEEFRKWLRSGGrTSPKTNKPLENHNLVPNHTLRIIIKDWLEK 302
Cdd:cd23150   4 FLCPISKTLIKTPVITAQGKVYDQEALSNFLIATG-NKDETGKKLSIDDVVVFDELYQQIKVYNFY 68
RING-Ubox cd16453
U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that ...
 237-281 3.48e-11

U-box domain, a modified RING finger; The U-box protein family is a family of E3 enzymes that also includes the HECT family and the RING finger family. The E3 enzyme is ubiquitin-protein ligase that cooperates with a ubiquitin-activating enzyme (E1) and a ubiquitin-conjugating enzyme (E2), and plays a central role in determining the specificity of the ubiquitination system. It removes the ubiquitin molecule from the E2 enzyme and attaches it to the target substrate, forming a covalent bond between ubiquitin and the target. U-box proteins are characterized by the presence of a U-box domain of approximately 70 amino acids. The U-box is a modified form of the RING finger domain that lacks metal chelating cysteines and histidines. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms.


Pssm-ID: 438117 [Multi-domain]  Cd Length: 44  Bit Score: 57.18  E-value: 3.48e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 75180094 237 FKCPISMEIMRDPHVAADGFTYEAEEFRKWLRSGGrTSPKTNKPL 281
Cdd:cd16453   1 FLCPISGELMKDPVITPSGITYDRSAIERWLLSDN-TDPFTREPL 44
RING-Ubox_LubX-like_rpt1 cd23149
first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX ...
 237-292 1.55e-09

first U-box domain, a modified RING finger, found in Legionella pneumophila U-box protein LubX and similar proteins; LubX, also called RING-type E3 ubiquitin transferase LubX, is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. LubX acts as an E3 ubiquitin-protein ligase (EC 2.3.2.27) that interferes with the host's ubiquitination pathway. LubX contains two RING-like U-box domains. U-box 1 is critical to the ubiquitin ligase activity, and U-box 2 mediates interaction with host target. This model corresponds to the first one.


Pssm-ID: 438511 [Multi-domain]  Cd Length: 55  Bit Score: 52.87  E-value: 1.55e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75180094 237 FKCPISMEIMRDPHVAADGFTYEAEEFRKWLRsGGRTSPKTNKPLENHNLVPNHTL 292
Cdd:cd23149   1 FTCPITSGFMEDPVITPSGFSYERSAIERWLE-TKPEDPQTREPLTAKDLQPNREL 55
USP_At3g01520-like cd23659
universal stress protein At3g01520 and similar proteins; This subfamily includes plant and ...
 7-142 1.97e-09

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: 55.32  E-value: 1.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75180094   7 VAVNQDVrESKKTLLWALKNLQVK--KIFLLHVHLPFSLTTSSSRLEQSEIDAIQDSELNTSVNSLYKYRDICInkgvNE 84
Cdd:cd23659   5 IAVDGSE-ESEYALEWALENLHRPgdEVVLLHVIEPPSLPAASLGSGSEEWEALEEEAREKAEKLLEKYEKKLK----EE 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75180094  85 KDVDTSMISGH-DVGEGIVELIYQNIITNLVMGaaadphySRGMSITSR-----KAEYVSQHAP 142
Cdd:cd23659  80 KGIKVKVEVVAgDPGEVICKAAEELKADLIVMG-------SRGLGALKRtllgsVSDYVVHHSP 136
SPL-RING_NSE2 cd16651
SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as ...
 237-297 1.70e-04

SPL-RING finger found in E3 SUMO-protein ligase NSE2 and similar proteins; NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress. Moreover, NSE2 together with its partner proteins SMC6 and SMC5 form a tight subcomplex of the structural maintenance of chromosomes SMC5-6 complex, which includes another two subcomplexes, NSE1-NSE3-NSE4 and NSE5-NSE6. SMC6 and NSE3 are sumoylated in an NSE2-dependent manner, but SMC5 and NSE1 are not. NSE2-dependent E3 SUMO ligase activity is required for efficient DNA repair, but not for SMC5-6 complex stability. NSE2 contains a RING variant known as a Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription)-like RING (SPL-RING) finger that is likely shared by the SP-RING type SUMO E3 ligases, such as PIAS family proteins. The SPL-RING finger is a variant of the RING finger, which lacks the second, fifth, and sixth zinc-binding residues of the consensus C3H2C3-/C3HC4-type RING fingers. It harbors only one Zn binding site and is required for the sumoylating activity.


Pssm-ID: 438313 [Multi-domain]  Cd Length: 67  Bit Score: 39.17  E-value: 1.70e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75180094 237 FKCPISMEIMRDPHVAAD-GFTYEAEEFRKWLRSGGRTS--PKT--NKPLENHNLVPNHTLRIIIK 297
Cdd:cd16651   1 LKCPITQQLMVDPVRNKKcGHTYEKAAILQYLQSRKKKAkcPVAgcRNTVSKSDLVPDPELKRRIE 66
 
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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