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Conserved domains on  [gi|6323052|ref|NP_013124|]
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putative ubiquitin-protein ligase UBR2 [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRT6_C super family cl40993
Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. ...
 1434-1842 7.60e-25

Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. Proteolysis 6 (PRT6) encodes a ubiquitin E3 ligase belonging to the N-end rule pathway of targeted protein degradation, which is a specialized subset of the ubiquitin proteasome system. In Arabidopsis, at least two N-recognins (E3 ubiquitin ligases) with different substrate specificities exist, namely PROTEOLYSIS1 (PRT1) and PRT6.


The actual alignment was detected with superfamily member pfam18995:

Pssm-ID: 465944  Cd Length: 444  Bit Score: 110.05  E-value: 7.60e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323052    1434 NTISNTELRLRSHKKEGKIVnMERISSQCILTLHLVCELKSFIYKKFVNSKTFSSEISRKIWnwnefliKGNNVNLLLym 1513
Cdd:pfam18995   35 YTISSIEIAQRGVGKPGGTL-LGKLPEQQLTLLRILSETVSSYASVGFLRSGGTNEEGRELI-------RRGILRLLL-- 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323052    1514 sQNFDNIDGGKTPQPP-------------NLCIYEMFKRRFH------------QLLLLLARDMMRVNfykdcrnkIKIS 1568
Cdd:pfam18995  105 -QLFPRISSLGEASPPlllrdpfgllvelALCLPSLFLEDILhllrlcylaeivQVVLTLSRNLSKTL--------RWAE 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323052    1569 SNGSEEPSTSFSYLFNTFKKY---VDLFKPDDVRFDFTSLEK--IKDFICSLLLeslsIFCRRTFLLFNIQYDDDGDGDN 1643
Cdd:pfam18995  176 GLETRSPSDESEDALRDFREFvgsVLRHSGVFADLDNDGFDDerLYKLVRKYAL----PFLRKAAILLHVLYGVPFPSPL 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323052    1644 NNnrsnnfmDVKQREIELIFRYFKLPNLTHFLKDffYNELTQN-IERYNDgndnlriQQVIYDMVQNINTRAYPSPEH-- 1720
Cdd:pfam18995  252 SS-------DPEGDELERLCKYLRLPSLDELCQS--NQDTLRSlVSGWCR-------HPAVFGHLSASPLNPSILLSHpg 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323052    1721 -IQLIELPLNLSkfSLDNDEISNKCDKY-----EIAVCLLCGQKCHIQKSIALQGYLQGECTDHMRNgCeiTSAYGVFLM 1794
Cdd:pfam18995  316 iFELVGLPKDYD--TLIEEASKRRCPTCgtdptDPALCLFCGTILCSQSYCCQEELNVGECNQHMRK-C--GGGVGIFLL 390

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 6323052    1795 TGTNAIYLSYGKRGTFYAAPYLSKYGETNEDYKFGTPVYLNRARYANL 1842
Cdd:pfam18995  391 IRKCTILLLHGGNGSFWPAPYLDAHGETDPGLRRGRPLYLNQKRYDEL 438
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 96-171 6.65e-24

Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain is involved in recognition of N-end rule substrates in yeast Ubr1p


:

Pssm-ID: 197698  Cd Length: 71  Bit Score: 96.74  E-value: 6.65e-24
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323052       96 TACTRLCFPSETIYYCFTCSTNPLYEICELCFDKEKHVNHSYVAKVVMRPegRICHCGDPFAfndPSDAFKCKNEL 171
Cdd:smart00396    1 DVCGYKFTGGEVIYRCKTCGLDPTCVLCSDCFRPSCHKGHDVSLKTSRGS--GICDCGDKEA---WNEDLKCKAHE 71
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
 1319-1369 2.89e-04

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; 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 different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. 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. RING finger/U-box-containing proteins are 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 enable efficient transfer of ubiquitin from E2 to the substrates.


The actual alignment was detected with superfamily member cd16483:

Pssm-ID: 473075  Cd Length: 63  Bit Score: 40.84  E-value: 2.89e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6323052  1319 CGHGSHTKCLSGHMKSIRGIQNQTTKnipLSYGSGLIYCPVCNSLSNSFLP 1369
Cdd:cd16483   16 CGHYIHIDCHKSYLESLRQDQVGLQL---LSVRRGEFTCPLCRQLSNSVLP 63
 
Name Accession Description Interval E-value
PRT6_C pfam18995
Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. ...
 1434-1842 7.60e-25

Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. Proteolysis 6 (PRT6) encodes a ubiquitin E3 ligase belonging to the N-end rule pathway of targeted protein degradation, which is a specialized subset of the ubiquitin proteasome system. In Arabidopsis, at least two N-recognins (E3 ubiquitin ligases) with different substrate specificities exist, namely PROTEOLYSIS1 (PRT1) and PRT6.


Pssm-ID: 465944  Cd Length: 444  Bit Score: 110.05  E-value: 7.60e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323052    1434 NTISNTELRLRSHKKEGKIVnMERISSQCILTLHLVCELKSFIYKKFVNSKTFSSEISRKIWnwnefliKGNNVNLLLym 1513
Cdd:pfam18995   35 YTISSIEIAQRGVGKPGGTL-LGKLPEQQLTLLRILSETVSSYASVGFLRSGGTNEEGRELI-------RRGILRLLL-- 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323052    1514 sQNFDNIDGGKTPQPP-------------NLCIYEMFKRRFH------------QLLLLLARDMMRVNfykdcrnkIKIS 1568
Cdd:pfam18995  105 -QLFPRISSLGEASPPlllrdpfgllvelALCLPSLFLEDILhllrlcylaeivQVVLTLSRNLSKTL--------RWAE 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323052    1569 SNGSEEPSTSFSYLFNTFKKY---VDLFKPDDVRFDFTSLEK--IKDFICSLLLeslsIFCRRTFLLFNIQYDDDGDGDN 1643
Cdd:pfam18995  176 GLETRSPSDESEDALRDFREFvgsVLRHSGVFADLDNDGFDDerLYKLVRKYAL----PFLRKAAILLHVLYGVPFPSPL 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323052    1644 NNnrsnnfmDVKQREIELIFRYFKLPNLTHFLKDffYNELTQN-IERYNDgndnlriQQVIYDMVQNINTRAYPSPEH-- 1720
Cdd:pfam18995  252 SS-------DPEGDELERLCKYLRLPSLDELCQS--NQDTLRSlVSGWCR-------HPAVFGHLSASPLNPSILLSHpg 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323052    1721 -IQLIELPLNLSkfSLDNDEISNKCDKY-----EIAVCLLCGQKCHIQKSIALQGYLQGECTDHMRNgCeiTSAYGVFLM 1794
Cdd:pfam18995  316 iFELVGLPKDYD--TLIEEASKRRCPTCgtdptDPALCLFCGTILCSQSYCCQEELNVGECNQHMRK-C--GGGVGIFLL 390

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 6323052    1795 TGTNAIYLSYGKRGTFYAAPYLSKYGETNEDYKFGTPVYLNRARYANL 1842
Cdd:pfam18995  391 IRKCTILLLHGGNGSFWPAPYLDAHGETDPGLRRGRPLYLNQKRYDEL 438
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 96-171 6.65e-24

Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain is involved in recognition of N-end rule substrates in yeast Ubr1p


Pssm-ID: 197698  Cd Length: 71  Bit Score: 96.74  E-value: 6.65e-24
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323052       96 TACTRLCFPSETIYYCFTCSTNPLYEICELCFDKEKHVNHSYVAKVVMRPegRICHCGDPFAfndPSDAFKCKNEL 171
Cdd:smart00396    1 DVCGYKFTGGEVIYRCKTCGLDPTCVLCSDCFRPSCHKGHDVSLKTSRGS--GICDCGDKEA---WNEDLKCKAHE 71
UBR-box_UBR1_2_3 cd19670
UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), E3-alpha-3 ...
 98-169 1.98e-18

UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), E3-alpha-3 (UBR3) and similar proteins; This family includes UBR1, UBR2, and UBR3 (all belonging to EC 2.3.2.27). Both UBR1 (also called E3alpha-I or N-recognin-1) and UBR2 (also called E3-alpha-II or N-recognin-2), are RING-type E3 ubiquitin ligases of the Arg/N-end rule degradation pathway. They recognize and bind to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Deficiency of UBR1 causes Johanson-Blizzard syndrome. UBR2 is associated with chromatin and controls chromatin dynamics and gene expression in both germ cells and somatic cells. It plays an important role in spermatogenesis. UBR3, also called ubiquitin-protein ligase E3-alpha-III (E3alpha-III), or N-recognin-3, or zinc finger protein 650, is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. It negatively regulates the mono-ubiquitination of non-muscle Myosin II, a protein associated with hearing loss in humans. It acts as a positive regulator of Hedgehog (Hh) signaling in Drosophila and vertebrates. It also plays an important role for genome stability by controlling cellular levels of the essential DNA repair protein APE1.


Pssm-ID: 439068  Cd Length: 69  Bit Score: 80.87  E-value: 1.98e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323052    98 CTRLCFPSETIYYCFTCSTNPLYEICELCFDKEKHVNHSYVAKVVmrPEGRICHCGDPFAFNdpsDAFKCKN 169
Cdd:cd19670    1 CGKSLKKGELYYRCLDCSLDPSSCICEECFLNGNHEGHNYSLRTS--SGGGVCDCGDSEAWK---PSGFCSK 67
zf-UBR pfam02207
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ...
 98-169 2.70e-15

Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases that recognize N-recognins.


Pssm-ID: 460491  Cd Length: 68  Bit Score: 71.94  E-value: 2.70e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323052      98 CTRLCFPSETIYYCFTCSTNPLYEICELCFDKEKHVNHSYvaKVVMRPEGRICHCGDPFAFNDPSdafKCKN 169
Cdd:pfam02207    1 CGYVFKKGQPVYRCLTCSLDPTCVICYSCFINCDHEGHDY--ELFTSRGGGCCDCGDPEAWKEEG---FCKL 67
RING-H2_UBR3 cd16483
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar ...
 1319-1369 2.89e-04

RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3, also known as N-recognin-3, E3alpha-III, or zinc finger protein 650, is an E3 ubiquitin-protein ligase targeting the essential DNA repair protein APE1, also known as Ref-1, for ubiquitylation. It regulates cellular levels of APE1 and is required for genome stability. It also plays a regulatory role in sensory pathways, including olfaction. In Drosophila, UBR3 also regulates apoptosis by controlling the activity of Drosophila inhibitor of apoptosis protein 1 (DIAP1), which is required to prevent caspase activation. UBR3 contains an N-terminal ubiquitin-recognin (UBR) box, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain.


Pssm-ID: 438146  Cd Length: 63  Bit Score: 40.84  E-value: 2.89e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6323052  1319 CGHGSHTKCLSGHMKSIRGIQNQTTKnipLSYGSGLIYCPVCNSLSNSFLP 1369
Cdd:cd16483   16 CGHYIHIDCHKSYLESLRQDQVGLQL---LSVRRGEFTCPLCRQLSNSVLP 63
 
Name Accession Description Interval E-value
PRT6_C pfam18995
Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. ...
 1434-1842 7.60e-25

Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. Proteolysis 6 (PRT6) encodes a ubiquitin E3 ligase belonging to the N-end rule pathway of targeted protein degradation, which is a specialized subset of the ubiquitin proteasome system. In Arabidopsis, at least two N-recognins (E3 ubiquitin ligases) with different substrate specificities exist, namely PROTEOLYSIS1 (PRT1) and PRT6.


Pssm-ID: 465944  Cd Length: 444  Bit Score: 110.05  E-value: 7.60e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323052    1434 NTISNTELRLRSHKKEGKIVnMERISSQCILTLHLVCELKSFIYKKFVNSKTFSSEISRKIWnwnefliKGNNVNLLLym 1513
Cdd:pfam18995   35 YTISSIEIAQRGVGKPGGTL-LGKLPEQQLTLLRILSETVSSYASVGFLRSGGTNEEGRELI-------RRGILRLLL-- 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323052    1514 sQNFDNIDGGKTPQPP-------------NLCIYEMFKRRFH------------QLLLLLARDMMRVNfykdcrnkIKIS 1568
Cdd:pfam18995  105 -QLFPRISSLGEASPPlllrdpfgllvelALCLPSLFLEDILhllrlcylaeivQVVLTLSRNLSKTL--------RWAE 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323052    1569 SNGSEEPSTSFSYLFNTFKKY---VDLFKPDDVRFDFTSLEK--IKDFICSLLLeslsIFCRRTFLLFNIQYDDDGDGDN 1643
Cdd:pfam18995  176 GLETRSPSDESEDALRDFREFvgsVLRHSGVFADLDNDGFDDerLYKLVRKYAL----PFLRKAAILLHVLYGVPFPSPL 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323052    1644 NNnrsnnfmDVKQREIELIFRYFKLPNLTHFLKDffYNELTQN-IERYNDgndnlriQQVIYDMVQNINTRAYPSPEH-- 1720
Cdd:pfam18995  252 SS-------DPEGDELERLCKYLRLPSLDELCQS--NQDTLRSlVSGWCR-------HPAVFGHLSASPLNPSILLSHpg 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323052    1721 -IQLIELPLNLSkfSLDNDEISNKCDKY-----EIAVCLLCGQKCHIQKSIALQGYLQGECTDHMRNgCeiTSAYGVFLM 1794
Cdd:pfam18995  316 iFELVGLPKDYD--TLIEEASKRRCPTCgtdptDPALCLFCGTILCSQSYCCQEELNVGECNQHMRK-C--GGGVGIFLL 390

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 6323052    1795 TGTNAIYLSYGKRGTFYAAPYLSKYGETNEDYKFGTPVYLNRARYANL 1842
Cdd:pfam18995  391 IRKCTILLLHGGNGSFWPAPYLDAHGETDPGLRRGRPLYLNQKRYDEL 438
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 96-171 6.65e-24

Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain is involved in recognition of N-end rule substrates in yeast Ubr1p


Pssm-ID: 197698  Cd Length: 71  Bit Score: 96.74  E-value: 6.65e-24
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323052       96 TACTRLCFPSETIYYCFTCSTNPLYEICELCFDKEKHVNHSYVAKVVMRPegRICHCGDPFAfndPSDAFKCKNEL 171
Cdd:smart00396    1 DVCGYKFTGGEVIYRCKTCGLDPTCVLCSDCFRPSCHKGHDVSLKTSRGS--GICDCGDKEA---WNEDLKCKAHE 71
UBR-box_UBR1_2_3 cd19670
UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), E3-alpha-3 ...
 98-169 1.98e-18

UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), E3-alpha-3 (UBR3) and similar proteins; This family includes UBR1, UBR2, and UBR3 (all belonging to EC 2.3.2.27). Both UBR1 (also called E3alpha-I or N-recognin-1) and UBR2 (also called E3-alpha-II or N-recognin-2), are RING-type E3 ubiquitin ligases of the Arg/N-end rule degradation pathway. They recognize and bind to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Deficiency of UBR1 causes Johanson-Blizzard syndrome. UBR2 is associated with chromatin and controls chromatin dynamics and gene expression in both germ cells and somatic cells. It plays an important role in spermatogenesis. UBR3, also called ubiquitin-protein ligase E3-alpha-III (E3alpha-III), or N-recognin-3, or zinc finger protein 650, is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. It negatively regulates the mono-ubiquitination of non-muscle Myosin II, a protein associated with hearing loss in humans. It acts as a positive regulator of Hedgehog (Hh) signaling in Drosophila and vertebrates. It also plays an important role for genome stability by controlling cellular levels of the essential DNA repair protein APE1.


Pssm-ID: 439068  Cd Length: 69  Bit Score: 80.87  E-value: 1.98e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323052    98 CTRLCFPSETIYYCFTCSTNPLYEICELCFDKEKHVNHSYVAKVVmrPEGRICHCGDPFAFNdpsDAFKCKN 169
Cdd:cd19670    1 CGKSLKKGELYYRCLDCSLDPSSCICEECFLNGNHEGHNYSLRTS--SGGGVCDCGDSEAWK---PSGFCSK 67
zf-UBR pfam02207
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ...
 98-169 2.70e-15

Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases that recognize N-recognins.


Pssm-ID: 460491  Cd Length: 68  Bit Score: 71.94  E-value: 2.70e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323052      98 CTRLCFPSETIYYCFTCSTNPLYEICELCFDKEKHVNHSYvaKVVMRPEGRICHCGDPFAFNDPSdafKCKN 169
Cdd:pfam02207    1 CGYVFKKGQPVYRCLTCSLDPTCVICYSCFINCDHEGHDY--ELFTSRGGGCCDCGDPEAWKEEG---FCKL 67
UBR-box_UBR1_like cd19672
UBR-box found in ubiquitin-protein ligases, E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), and similar ...
 98-162 2.32e-13

UBR-box found in ubiquitin-protein ligases, E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), and similar proteins; This family includes UBR1 and UBR2 (both EC 2.3.2.27). Both UBR1 (also called E3alpha-I or N-recognin-1) and UBR2 (also called E3-alpha-II or N-recognin-2), are RING-type E3 ubiquitin ligases of the Arg/N-end rule degradation pathway. They recognize and bind to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Deficiency of UBR1 causes Johanson-Blizzard syndrome. UBR2 is associated with chromatin and controls chromatin dynamics and gene expression in both germ cells and somatic cells. It plays an important role in spermatogenesis.


Pssm-ID: 439070  Cd Length: 70  Bit Score: 66.51  E-value: 2.32e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323052    98 CTRLCFPSETIYYCFTCSTNPLYEICELCFDKEKHVNHSYvaKVVMRPEGRICHCGDPFAFNDPS 162
Cdd:cd19672    2 CGRVFKPGEPTYSCLDCGVDPTCVLCEDCFLNSEHVNHNY--KMSISSGGGCCDCGDPEAWKSHS 64
UBR-box cd19669
UBR-box found in UBR family of E3 ubiquitin ligases (UBR1-7) and similar proteins; The UBR-box ...
 98-169 1.98e-10

UBR-box found in UBR family of E3 ubiquitin ligases (UBR1-7) and similar proteins; The UBR-box is a 70-residue zinc finger domain present in the UBR family of E3 ubiquitin ligases (UBR1-7, also called N-recognins) that directly binds N-terminal degradation signals (N-degrons) in substrate proteins to facilitate substrate ubiquitination and proteasomal degradation via the ubiquitin-proteasome system (UPS). UBR1 and UBR2 bind all type-1 and type-2 N-degrons. They mediate ubiquitination and proteolysis of short-lived regulators and misfolded proteins. UBR4 binds both type-1 and type-2 N-degrons and is involved in proteome-wide turnover of cell surface proteins. UBR5 preferentially binds type-1 N-degrons and mediates ubiquitination of short-lived proteins. UBR3, UBR6 (also called FBXO11), and UBR7 may not bind efficiently to N-degrons. UBR3 is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. UBR6 is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. It does not bind N-terminal signals. UBR7 is a RING-type E3 ubiquitin ligase that may play an important role in spermiogenesis and fertilization.


Pssm-ID: 439067  Cd Length: 66  Bit Score: 58.30  E-value: 1.98e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323052    98 CTRLCF-PSETIYYCFTCSTNPLYEICELCFDKeKHVNHSYVAKvvmRPEGRICHCGDPFAFNdpsdaFKCKN 169
Cdd:cd19669    1 CTFSITgINQVMYHCLTCSLDDNSGICEECAKK-CHEGHDVVYI---GSGSGFCDCGDSSAKS-----GFCKC 64
UBR-box_UBR3 cd19673
UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3. ...
 95-159 4.40e-08

UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3.2.27), also called ubiquitin-protein ligase E3-alpha-III (E3alpha-III), or N-recognin-3, or zinc finger protein 650, is a RING-type E3 ubiquitin ligase with a function in olfactory and other sensory systems. It negatively regulates the mono-ubiquitination of non-muscle Myosin II, a protein associated with hearing loss in humans. It acts as a positive regulator of Hedgehog (Hh) signaling in Drosophila and vertebrates. It also plays an important role for genome stability by controlling cellular levels of the essential DNA repair protein APE1.


Pssm-ID: 439071  Cd Length: 72  Bit Score: 51.81  E-value: 4.40e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323052    95 GTACTRLCFPSETIYYCFTCSTNPLYEICELCFDKEKHVNHSYvaKVVMRPEGRICHCGDPFAFN 159
Cdd:cd19673    1 SGVCGRVWKAGDIAYRCRTCGLDPTCVICADCFQAGDHEGHDY--SMYRSSAGGCCDCGDPEAWK 63
UBR-box_UBR1 cd19678
UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1) and similar proteins; UBR1 (EC 2.3. ...
 98-154 6.04e-05

UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1) and similar proteins; UBR1 (EC 2.3.2.27), also called ubiquitin-protein ligase E3-alpha-I (E3alpha-I), or N-recognin-1, is a RING-type E3 ubiquitin ligase of the Arg/N-end rule degradation pathway. It recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Deficiency of UBR1 causes Johanson-Blizzard syndrome.


Pssm-ID: 439076  Cd Length: 71  Bit Score: 42.97  E-value: 6.04e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6323052    98 CTRLCFPSETIYYCFTCSTNPLYEICELCFDKEKHVNHSYvaKVVMRPEGRICHCGD 154
Cdd:cd19678    2 CGRVFKGGETTYSCRDCAIDPTCVLCMDCFQNSVHKNHRY--KMHSSTGGGFCDCGD 56
RING-H2_UBR3 cd16483
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar ...
 1319-1369 2.89e-04

RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3, also known as N-recognin-3, E3alpha-III, or zinc finger protein 650, is an E3 ubiquitin-protein ligase targeting the essential DNA repair protein APE1, also known as Ref-1, for ubiquitylation. It regulates cellular levels of APE1 and is required for genome stability. It also plays a regulatory role in sensory pathways, including olfaction. In Drosophila, UBR3 also regulates apoptosis by controlling the activity of Drosophila inhibitor of apoptosis protein 1 (DIAP1), which is required to prevent caspase activation. UBR3 contains an N-terminal ubiquitin-recognin (UBR) box, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain.


Pssm-ID: 438146  Cd Length: 63  Bit Score: 40.84  E-value: 2.89e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6323052  1319 CGHGSHTKCLSGHMKSIRGIQNQTTKnipLSYGSGLIYCPVCNSLSNSFLP 1369
Cdd:cd16483   16 CGHYIHIDCHKSYLESLRQDQVGLQL---LSVRRGEFTCPLCRQLSNSVLP 63
RING-H2_UBR1-like cd16482
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 ...
 1318-1369 1.99e-03

RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), and similar proteins; Two UBR family members, UBR1 and UBR2, are major N-recognin ubiquitin ligases that both function in the N-end rule degradation pathway. They can recognize substrate proteins with type-1 (basic) and type-2 (bulky hydrophobic) N-terminal residues as part of N-degrons and an internal lysine residue for ubiquitin conjugation. They also function in a quality control pathway for degradation of unfolded cytosolic proteins. Their action is stimulated by Hsp70. Moreover, UBR1 and UBR2 are negative regulators of the leucine-mTOR signaling pathway. Leucine might activate this pathway in part through inhibition of their ubiquitin ligase activity. In yeast, only one E3, encoded by UBR1, mediates the recognition of substrates by the N-end rule pathway. Saccharomyces cerevisiae UBR1 also functions as an additional E3 ligase in the endoplasmic reticulum-associated protein degradation (ERAD). It can provide ubiquitin ligation activity for the ERAD substrate mutated Ste6 (sterile). Schizosaccharomyces pombe UBR1 is a critical regulator that influences the oxidative stress response via degradation of active Pap1 basic leucine zipper (bZIP) transcription factor in the nucleus. Both UBR1 and UBR2 contain an N-terminal ubiquitin-recognin (UBR) box involved in binding type-1 (basic) N-end rule substrate, an N-domain (also known as ClpS domain) required for type-2 (bulky hydrophobic) N-end rule substrate recognition, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain.


Pssm-ID: 438145  Cd Length: 67  Bit Score: 38.48  E-value: 1.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6323052  1318 ACGHGSHTKCLSGHMKSIRGIQNQTT---KNIPLSYGSGLIYCPVCNSLSNSFLP 1369
Cdd:cd16482   13 SCGHVMHYDCWQRYFDSVRLREQRRPafrRHHSEDVSKGEFLCPLCKSLSNTVLP 67
 
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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