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Conserved domains on  [gi|398366351|ref|NP_010552|]
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E3 ubiquitin-protein ligase HEL2 [Saccharomyces cerevisiae S288C]

Protein Classification

zinc finger family protein( domain architecture ID 11474179)

zinc finger family protein may be involved in transcriptional regulation; similar to Schizosaccharomyces pombe E3 ubiquitin-protein ligase hel2, which that plays a key role in the ribosome quality control (RQC), and Homo sapiens histone H4 transcription factor

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
1-507 0e+00

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


:

Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 749.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351   1 MSESVKENVTPTRNFRRTQGPQNNTKPHNDRKNFRRKQKKNNLSAEPNLTTSSADDTDEENELCVICARKLTYVSLTPCH 80
Cdd:COG5236    1 MSESVKENVTPTRNFRRTQGPQNNTKPHNDRKNFRRKQKKNNLSAEPNLTTSSADDTDEENMNCQICAGSTTYSARYPCG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351  81 HKTCHICGFRQRALYNKKSCLICRTENEEVMFTDRIDGDISDKYNFCEKNEKYGINFTSEEVATETLNLLKFFCPLSKDE 160
Cdd:COG5236   81 HQICHACAVRLRALYMQKGCPLCRTETEAVVFTASSPADITDRRQWKGREEKVGIFYEGEDVRDEMEDLLSFKCPKSKCH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351 161 QVCDFgsFKKYNEHLKSEHNRMICLICATHKHAFPCELEIFTQNQLRNHQTKGNSE-GFKGHPMCAFCSgKRFYSDDELY 239
Cdd:COG5236  161 RRCGS--LKELKKHYKAQHGFVLCSECIGNKKDFWNEIRLFRSSTLRDHKNGGLEEeGFKGHPLCIFCK-IYFYDDDELR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351 240 IHMRNQHEKCHICDKMNPASPQYFKDYNQLFDHFKHSHYVCTVQTCLDNKFVVFKDELELQAHILQEHGNILKGKPKFFQ 319
Cdd:COG5236  238 RHCRLRHEACHICDMVGPIRYQYFKSYEDLEAHFRNAHYCCTFQTCRVGKCYVFPYHTELLEHLTRFHKVNARLSEIPRP 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351 320 SELSTFISAPsrVIRERDDYDLPSISSLPGSSSGSRTDVRSASSPEESRLRLAERAKYYLENSKEDFNKfssyneDYSKG 399
Cdd:COG5236  318 GRCSIPVMDP--FKRKKAPARVSVIDPSGGNARAPMAHRGGSRQDTASPSTEAELPKYLNRNILEEERR------KLQKR 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351 400 RLSAEKLLESYKLLFTKPNADVYLLIHNLAETFPKNSSKYNNLNAIYEQREQTLARQTslpsLSSDSSLSMSIGRGHWGG 479
Cdd:COG5236  390 RLVIDRICKAEGNEIEEIINEFLGDSIDVTEAFNRISKVTGDAAALKLFESAPFGPKQ----SVVEGSIKALRKRVMFPK 465
                        490       500
                 ....*....|....*....|....*...
gi 398366351 480 TNDGGSAGAALGVRNIKNLPTLKSPSAS 507
Cdd:COG5236  466 FVPSEPVRYREPERKGPGFTVIDLHKRK 493
 
Name Accession Description Interval E-value
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
1-507 0e+00

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 749.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351   1 MSESVKENVTPTRNFRRTQGPQNNTKPHNDRKNFRRKQKKNNLSAEPNLTTSSADDTDEENELCVICARKLTYVSLTPCH 80
Cdd:COG5236    1 MSESVKENVTPTRNFRRTQGPQNNTKPHNDRKNFRRKQKKNNLSAEPNLTTSSADDTDEENMNCQICAGSTTYSARYPCG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351  81 HKTCHICGFRQRALYNKKSCLICRTENEEVMFTDRIDGDISDKYNFCEKNEKYGINFTSEEVATETLNLLKFFCPLSKDE 160
Cdd:COG5236   81 HQICHACAVRLRALYMQKGCPLCRTETEAVVFTASSPADITDRRQWKGREEKVGIFYEGEDVRDEMEDLLSFKCPKSKCH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351 161 QVCDFgsFKKYNEHLKSEHNRMICLICATHKHAFPCELEIFTQNQLRNHQTKGNSE-GFKGHPMCAFCSgKRFYSDDELY 239
Cdd:COG5236  161 RRCGS--LKELKKHYKAQHGFVLCSECIGNKKDFWNEIRLFRSSTLRDHKNGGLEEeGFKGHPLCIFCK-IYFYDDDELR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351 240 IHMRNQHEKCHICDKMNPASPQYFKDYNQLFDHFKHSHYVCTVQTCLDNKFVVFKDELELQAHILQEHGNILKGKPKFFQ 319
Cdd:COG5236  238 RHCRLRHEACHICDMVGPIRYQYFKSYEDLEAHFRNAHYCCTFQTCRVGKCYVFPYHTELLEHLTRFHKVNARLSEIPRP 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351 320 SELSTFISAPsrVIRERDDYDLPSISSLPGSSSGSRTDVRSASSPEESRLRLAERAKYYLENSKEDFNKfssyneDYSKG 399
Cdd:COG5236  318 GRCSIPVMDP--FKRKKAPARVSVIDPSGGNARAPMAHRGGSRQDTASPSTEAELPKYLNRNILEEERR------KLQKR 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351 400 RLSAEKLLESYKLLFTKPNADVYLLIHNLAETFPKNSSKYNNLNAIYEQREQTLARQTslpsLSSDSSLSMSIGRGHWGG 479
Cdd:COG5236  390 RLVIDRICKAEGNEIEEIINEFLGDSIDVTEAFNRISKVTGDAAALKLFESAPFGPKQ----SVVEGSIKALRKRVMFPK 465
                        490       500
                 ....*....|....*....|....*...
gi 398366351 480 TNDGGSAGAALGVRNIKNLPTLKSPSAS 507
Cdd:COG5236  466 FVPSEPVRYREPERKGPGFTVIDLHKRK 493
RING-HC_ZNF598 cd16615
RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ...
62-112 4.69e-21

RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ZNF598 associates with eukaryotic initiation factor 4E (eIF4E) homologous protein from mammals (m4EHP) by binding to Grb10-interacting GYF protein 2 (GIGYF2). The m4EHP-GIGYF2 complex functions as a translational repressor and is essential for normal embryonic development of mammalian. ZNF598 harbors a C3HC4-type RING-HC finger at its N-terminus.


Pssm-ID: 438277 [Multi-domain]  Cd Length: 51  Bit Score: 86.51  E-value: 4.69e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 398366351  62 ELCVICARKLTYVSLTPCHHKTCHICGFRQRALYNKKSCLICRTENEEVMF 112
Cdd:cd16615    1 ETCVICCEEIEYFAVGPCNHPVCYKCSLRMRVLYKDKYCPICRTELDKVIF 51
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
60-110 1.70e-06

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 45.06  E-value: 1.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 398366351   60 ENELCVICARKLTYVSLTPC-HHKTCHICgfRQRALYNKKSCLICRTENEEV 110
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLLPCgHLCLCEEC--AERLLRKKKKCPICRQPIESV 50
 
Name Accession Description Interval E-value
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
1-507 0e+00

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 749.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351   1 MSESVKENVTPTRNFRRTQGPQNNTKPHNDRKNFRRKQKKNNLSAEPNLTTSSADDTDEENELCVICARKLTYVSLTPCH 80
Cdd:COG5236    1 MSESVKENVTPTRNFRRTQGPQNNTKPHNDRKNFRRKQKKNNLSAEPNLTTSSADDTDEENMNCQICAGSTTYSARYPCG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351  81 HKTCHICGFRQRALYNKKSCLICRTENEEVMFTDRIDGDISDKYNFCEKNEKYGINFTSEEVATETLNLLKFFCPLSKDE 160
Cdd:COG5236   81 HQICHACAVRLRALYMQKGCPLCRTETEAVVFTASSPADITDRRQWKGREEKVGIFYEGEDVRDEMEDLLSFKCPKSKCH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351 161 QVCDFgsFKKYNEHLKSEHNRMICLICATHKHAFPCELEIFTQNQLRNHQTKGNSE-GFKGHPMCAFCSgKRFYSDDELY 239
Cdd:COG5236  161 RRCGS--LKELKKHYKAQHGFVLCSECIGNKKDFWNEIRLFRSSTLRDHKNGGLEEeGFKGHPLCIFCK-IYFYDDDELR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351 240 IHMRNQHEKCHICDKMNPASPQYFKDYNQLFDHFKHSHYVCTVQTCLDNKFVVFKDELELQAHILQEHGNILKGKPKFFQ 319
Cdd:COG5236  238 RHCRLRHEACHICDMVGPIRYQYFKSYEDLEAHFRNAHYCCTFQTCRVGKCYVFPYHTELLEHLTRFHKVNARLSEIPRP 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351 320 SELSTFISAPsrVIRERDDYDLPSISSLPGSSSGSRTDVRSASSPEESRLRLAERAKYYLENSKEDFNKfssyneDYSKG 399
Cdd:COG5236  318 GRCSIPVMDP--FKRKKAPARVSVIDPSGGNARAPMAHRGGSRQDTASPSTEAELPKYLNRNILEEERR------KLQKR 389
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366351 400 RLSAEKLLESYKLLFTKPNADVYLLIHNLAETFPKNSSKYNNLNAIYEQREQTLARQTslpsLSSDSSLSMSIGRGHWGG 479
Cdd:COG5236  390 RLVIDRICKAEGNEIEEIINEFLGDSIDVTEAFNRISKVTGDAAALKLFESAPFGPKQ----SVVEGSIKALRKRVMFPK 465
                        490       500
                 ....*....|....*....|....*...
gi 398366351 480 TNDGGSAGAALGVRNIKNLPTLKSPSAS 507
Cdd:COG5236  466 FVPSEPVRYREPERKGPGFTVIDLHKRK 493
RING-HC_ZNF598 cd16615
RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ...
62-112 4.69e-21

RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ZNF598 associates with eukaryotic initiation factor 4E (eIF4E) homologous protein from mammals (m4EHP) by binding to Grb10-interacting GYF protein 2 (GIGYF2). The m4EHP-GIGYF2 complex functions as a translational repressor and is essential for normal embryonic development of mammalian. ZNF598 harbors a C3HC4-type RING-HC finger at its N-terminus.


Pssm-ID: 438277 [Multi-domain]  Cd Length: 51  Bit Score: 86.51  E-value: 4.69e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 398366351  62 ELCVICARKLTYVSLTPCHHKTCHICGFRQRALYNKKSCLICRTENEEVMF 112
Cdd:cd16615    1 ETCVICCEEIEYFAVGPCNHPVCYKCSLRMRVLYKDKYCPICRTELDKVIF 51
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
60-110 1.70e-06

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 45.06  E-value: 1.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 398366351   60 ENELCVICARKLTYVSLTPC-HHKTCHICgfRQRALYNKKSCLICRTENEEV 110
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLLPCgHLCLCEEC--AERLLRKKKKCPICRQPIESV 50
RING-HC_RNF123 cd16541
RING finger, HC subclass, found in RING finger protein 123 (RNF123) and similar proteins; ...
62-106 2.05e-03

RING finger, HC subclass, found in RING finger protein 123 (RNF123) and similar proteins; RNF123, also known as Kip1 ubiquitination-promoting complex protein 1 (KPC1), is an E3 ubiquitin-protein ligase that mediates ubiquitination and proteasomal processing of the nuclear factor-kappaB 1 (NF-kappaB1) precursor p105 to the p50 active subunit that restricts tumor growth. It also regulates degradation of heterochromatin protein 1alpha (HP1alpha) and 1beta (HP1beta) in lamin A/C knock-down cells. Moreover, RNF123, together with Kip1 ubiquitylation-promoting complex 2 (KPC2), forms the Kip1 ubiquitination-promoting complex (KPC), acting as a cytoplasmic ubiquitin ligase that regulates degradation of the cyclin-dependent kinase inhibitor p27 (Kip1) at the G1 phase of the cell cycle. RNF123 may also function as a clinically relevant, peripheral state marker of depression. RNF123 contains a C3HC4-type RING-HC finger at the C-terminus.


Pssm-ID: 438203 [Multi-domain]  Cd Length: 44  Bit Score: 36.51  E-value: 2.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 398366351  62 ELCVICARKLTYVSLTPCHHKTCHICgfRQRALYNKKSCLICRTE 106
Cdd:cd16541    1 DLCPICYAHPIDAVFLPCGHKSCRSC--INRHLMNNKECFFCKAT 43
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
62-103 4.33e-03

HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to the HC subclass of RING (RING-HC) fingers that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC fingers can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438113 [Multi-domain]  Cd Length: 41  Bit Score: 35.54  E-value: 4.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 398366351  62 ELCVICARKLTYVSLTPCHHKTCHICgFRQRALYNKKSCLIC 103
Cdd:cd16449    1 LECPICLERLKDPVLLPCGHVFCREC-IRRLLESGSIKCPIC 41
 
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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