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Conserved domains on  [gi|442615440|ref|NP_001259317|]
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Ubr3 ubiquitin ligase, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 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. ...
 1722-2202 3.00e-66

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: 232.16  E-value: 3.00e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  1722 LFIFVTSIARTNLEAEIIQRGGSLCTANATRYKP--KRECIVPLLHVLSVHVRVLVEwplwsswaSLAGLPVTATEPLPA 1799
Cdd:pfam18995   26 SDLLWDSLAYTISSIEIAQRGVGKPGGTLLGKLPeqQLTLLRILSETVSSYASVGFL--------RSGGTNEEGRELIRR 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  1800 HCL--------------ELIPSILA-DPIALLLKFILLAPLQLDQDyFTCMVKVMYNLLYYQIVVqlcvtltdlecdHIV 1864
Cdd:pfam18995   98 GILrlllqlfprisslgEASPPLLLrDPFGLLVELALCLPSLFLED-ILHLLRLCYLAEIVQVVL------------TLS 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  1865 KVYGSTSVGSDNSAAESQQQESAAGTTNNRrragqqqqsssqlgKAMALVLSQTNDLVHLRRDCIpstsssaaasaagss 1944
Cdd:pfam18995  165 RNLSKTLRWAEGLETRSPSDESEDALRDFR--------------EFVGSVLRHSGVFADLDNDGF--------------- 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  1945 sttstnhgasaatassattievNLKSMELQLQALCLPFLRVAALLRQHLYRHEMPEISAP---GLEFVRLVYYLELVtdS 2021
Cdd:pfam18995  216 ----------------------DDERLYKLVRKYALPFLRKAAILLHVLYGVPFPSPLSSdpeGDELERLCKYLRLP--S 271

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  2022 MDWDCFNASKGLCFIPGTettlpqfWCQQ-LMEVRPPADTVRELVLINQHSLwqqPRLLELPREYERLFTYYHERPCLNC 2100
Cdd:pfam18995  272 LDELCQSNQDTLRSLVSG-------WCRHpAVFGHLSASPLNPSILLSHPGI---FELVGLPKDYDTLIEEASKRRCPTC 341

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  2101 YKVPKESSICLLCGTIVCLKQNCCAENDC-CEAVRHTLSCGGGIGIFLVVTSTYIIVIRGRRACLWGSLYLDDFDEEDRD 2179
Cdd:pfam18995  342 GTDPTDPALCLFCGTILCSQSYCCQEELNvGECNQHMRKCGGGVGIFLLIRKCTILLLHGGNGSFWPAPYLDAHGETDPG 421

                          490       500
                   ....*....|....*....|...
gi 442615440  2180 LKRGKPLYLSKDRFNLLESQWLS 2202
Cdd:pfam18995  422 LRRGRPLYLNQKRYDELRRLWLS 444
UBR-box_UBR3 cd19673
UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3. ...
 224-292 9.14e-39

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: 139.25  E-value: 9.14e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442615440  224 CGLVWVPHVVAYRCRTCGISPCMSICRDCFKKGNHTNHDFNMFLSQAGGACDCGDTSVMKAEGFCSDHG 292
Cdd:cd19673     4 CGRVWKAGDIAYRCRTCGLDPTCVICADCFQAGDHEGHDYSMYRSSAGGCCDCGDPEAWKPSGFCSRHR 72
RING-H2_UBR3 cd16483
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar ...
 1601-1651 2.08e-24

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: 98.23  E-value: 2.08e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442615440 1601 GVHVQSCGHHVHLSCLEAYLKTLYTTQ---RQPVQDRGEFYCPVCRQLSNSVLP 1651
Cdd:cd16483    10 GVHVQTCGHYIHIDCHKSYLESLRQDQvglQLLSVRRGEFTCPLCRQLSNSVLP 63
FliJ pfam02050
Flagellar FliJ protein;
1410-1477 3.37e-05

Flagellar FliJ protein;


:

Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 45.35  E-value: 3.37e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442615440  1410 FIGNLLRKIAKQDEQCAQSIDDIRARL--WpnqREKQAEAKARE---AKEKEERRKKARERQQKMMQDFANKQ 1477
Cdd:pfam02050   53 FISQLDEAIAQQQQELAQAEAQVEKAReeW---QEARQERKSLEklrEREKKEERKEQNRREQKQLDELAARL 122
 
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. ...
 1722-2202 3.00e-66

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: 232.16  E-value: 3.00e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  1722 LFIFVTSIARTNLEAEIIQRGGSLCTANATRYKP--KRECIVPLLHVLSVHVRVLVEwplwsswaSLAGLPVTATEPLPA 1799
Cdd:pfam18995   26 SDLLWDSLAYTISSIEIAQRGVGKPGGTLLGKLPeqQLTLLRILSETVSSYASVGFL--------RSGGTNEEGRELIRR 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  1800 HCL--------------ELIPSILA-DPIALLLKFILLAPLQLDQDyFTCMVKVMYNLLYYQIVVqlcvtltdlecdHIV 1864
Cdd:pfam18995   98 GILrlllqlfprisslgEASPPLLLrDPFGLLVELALCLPSLFLED-ILHLLRLCYLAEIVQVVL------------TLS 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  1865 KVYGSTSVGSDNSAAESQQQESAAGTTNNRrragqqqqsssqlgKAMALVLSQTNDLVHLRRDCIpstsssaaasaagss 1944
Cdd:pfam18995  165 RNLSKTLRWAEGLETRSPSDESEDALRDFR--------------EFVGSVLRHSGVFADLDNDGF--------------- 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  1945 sttstnhgasaatassattievNLKSMELQLQALCLPFLRVAALLRQHLYRHEMPEISAP---GLEFVRLVYYLELVtdS 2021
Cdd:pfam18995  216 ----------------------DDERLYKLVRKYALPFLRKAAILLHVLYGVPFPSPLSSdpeGDELERLCKYLRLP--S 271

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  2022 MDWDCFNASKGLCFIPGTettlpqfWCQQ-LMEVRPPADTVRELVLINQHSLwqqPRLLELPREYERLFTYYHERPCLNC 2100
Cdd:pfam18995  272 LDELCQSNQDTLRSLVSG-------WCRHpAVFGHLSASPLNPSILLSHPGI---FELVGLPKDYDTLIEEASKRRCPTC 341

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  2101 YKVPKESSICLLCGTIVCLKQNCCAENDC-CEAVRHTLSCGGGIGIFLVVTSTYIIVIRGRRACLWGSLYLDDFDEEDRD 2179
Cdd:pfam18995  342 GTDPTDPALCLFCGTILCSQSYCCQEELNvGECNQHMRKCGGGVGIFLLIRKCTILLLHGGNGSFWPAPYLDAHGETDPG 421

                          490       500
                   ....*....|....*....|...
gi 442615440  2180 LKRGKPLYLSKDRFNLLESQWLS 2202
Cdd:pfam18995  422 LRRGRPLYLNQKRYDELRRLWLS 444
UBR-box_UBR3 cd19673
UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3. ...
 224-292 9.14e-39

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: 139.25  E-value: 9.14e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442615440  224 CGLVWVPHVVAYRCRTCGISPCMSICRDCFKKGNHTNHDFNMFLSQAGGACDCGDTSVMKAEGFCSDHG 292
Cdd:cd19673     4 CGRVWKAGDIAYRCRTCGLDPTCVICADCFQAGDHEGHDYSMYRSSAGGCCDCGDPEAWKPSGFCSRHR 72
zf-UBR pfam02207
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ...
 224-291 4.92e-28

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: 108.53  E-value: 4.92e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442615440   224 CGLVWVPHVVAYRCRTCGISPCMSICRDCFKKGNHTNHDFNMFLSQAGGACDCGDTSVMKAEGFCSDH 291
Cdd:pfam02207    1 CGYVFKKGQPVYRCLTCSLDPTCVICYSCFINCDHEGHDYELFTSRGGGCCDCGDPEAWKEEGFCKLH 68
RING-H2_UBR3 cd16483
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar ...
 1601-1651 2.08e-24

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: 98.23  E-value: 2.08e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442615440 1601 GVHVQSCGHHVHLSCLEAYLKTLYTTQ---RQPVQDRGEFYCPVCRQLSNSVLP 1651
Cdd:cd16483    10 GVHVQTCGHYIHIDCHKSYLESLRQDQvglQLLSVRRGEFTCPLCRQLSNSVLP 63
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 223-292 3.41e-18

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: 80.56  E-value: 3.41e-18
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440    223 KCGLVWVPHVVAYRCRTCGISPCMSICRDCFKKGNHTNHDFNMFLSQAGGACDCGDTSVMKAEGFCSDHG 292
Cdd:smart00396    2 VCGYKFTGGEVIYRCKTCGLDPTCVLCSDCFRPSCHKGHDVSLKTSRGSGICDCGDKEAWNEDLKCKAHE 71
FliJ pfam02050
Flagellar FliJ protein;
1410-1477 3.37e-05

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 45.35  E-value: 3.37e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442615440  1410 FIGNLLRKIAKQDEQCAQSIDDIRARL--WpnqREKQAEAKARE---AKEKEERRKKARERQQKMMQDFANKQ 1477
Cdd:pfam02050   53 FISQLDEAIAQQQQELAQAEAQVEKAReeW---QEARQERKSLEklrEREKKEERKEQNRREQKQLDELAARL 122
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
1410-1477 6.11e-04

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 442129 [Multi-domain]  Cd Length: 142  Bit Score: 42.20  E-value: 6.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442615440 1410 FIGNLLRKIAKQD---EQCAQSIDDIRARLwpnqREKQAEAKA----REAKEKEERRKKAReRQQKMMQDFANKQ 1477
Cdd:COG2882    72 FIARLDEAIEQQQqqvAQAEQQVEQARQAW----LEARQERKAleklKERRREEERQEENR-REQKELDELASRR 141
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 1411-1477 3.88e-03

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 39.99  E-value: 3.88e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442615440  1411 IGNLLRKIAKQDEQCaqsiDDIRARLWPNQREKQAEAKAREAKEKEERRKKAReRQQKMMQDFANKQ 1477
Cdd:TIGR02473   77 IQQQQQELALLQQEV----EAKRERLLEARRELKALEKLKEKKQKEYRAEEAK-REQKEMDELATQR 138
 
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. ...
 1722-2202 3.00e-66

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: 232.16  E-value: 3.00e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  1722 LFIFVTSIARTNLEAEIIQRGGSLCTANATRYKP--KRECIVPLLHVLSVHVRVLVEwplwsswaSLAGLPVTATEPLPA 1799
Cdd:pfam18995   26 SDLLWDSLAYTISSIEIAQRGVGKPGGTLLGKLPeqQLTLLRILSETVSSYASVGFL--------RSGGTNEEGRELIRR 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  1800 HCL--------------ELIPSILA-DPIALLLKFILLAPLQLDQDyFTCMVKVMYNLLYYQIVVqlcvtltdlecdHIV 1864
Cdd:pfam18995   98 GILrlllqlfprisslgEASPPLLLrDPFGLLVELALCLPSLFLED-ILHLLRLCYLAEIVQVVL------------TLS 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  1865 KVYGSTSVGSDNSAAESQQQESAAGTTNNRrragqqqqsssqlgKAMALVLSQTNDLVHLRRDCIpstsssaaasaagss 1944
Cdd:pfam18995  165 RNLSKTLRWAEGLETRSPSDESEDALRDFR--------------EFVGSVLRHSGVFADLDNDGF--------------- 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  1945 sttstnhgasaatassattievNLKSMELQLQALCLPFLRVAALLRQHLYRHEMPEISAP---GLEFVRLVYYLELVtdS 2021
Cdd:pfam18995  216 ----------------------DDERLYKLVRKYALPFLRKAAILLHVLYGVPFPSPLSSdpeGDELERLCKYLRLP--S 271

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  2022 MDWDCFNASKGLCFIPGTettlpqfWCQQ-LMEVRPPADTVRELVLINQHSLwqqPRLLELPREYERLFTYYHERPCLNC 2100
Cdd:pfam18995  272 LDELCQSNQDTLRSLVSG-------WCRHpAVFGHLSASPLNPSILLSHPGI---FELVGLPKDYDTLIEEASKRRCPTC 341

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  2101 YKVPKESSICLLCGTIVCLKQNCCAENDC-CEAVRHTLSCGGGIGIFLVVTSTYIIVIRGRRACLWGSLYLDDFDEEDRD 2179
Cdd:pfam18995  342 GTDPTDPALCLFCGTILCSQSYCCQEELNvGECNQHMRKCGGGVGIFLLIRKCTILLLHGGNGSFWPAPYLDAHGETDPG 421

                          490       500
                   ....*....|....*....|...
gi 442615440  2180 LKRGKPLYLSKDRFNLLESQWLS 2202
Cdd:pfam18995  422 LRRGRPLYLNQKRYDELRRLWLS 444
UBR-box_UBR3 cd19673
UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3. ...
 224-292 9.14e-39

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: 139.25  E-value: 9.14e-39
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442615440  224 CGLVWVPHVVAYRCRTCGISPCMSICRDCFKKGNHTNHDFNMFLSQAGGACDCGDTSVMKAEGFCSDHG 292
Cdd:cd19673     4 CGRVWKAGDIAYRCRTCGLDPTCVICADCFQAGDHEGHDYSMYRSSAGGCCDCGDPEAWKPSGFCSRHR 72
zf-UBR pfam02207
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ...
 224-291 4.92e-28

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: 108.53  E-value: 4.92e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442615440   224 CGLVWVPHVVAYRCRTCGISPCMSICRDCFKKGNHTNHDFNMFLSQAGGACDCGDTSVMKAEGFCSDH 291
Cdd:pfam02207    1 CGYVFKKGQPVYRCLTCSLDPTCVICYSCFINCDHEGHDYELFTSRGGGCCDCGDPEAWKEEGFCKLH 68
UBR-box_UBR1_2_3 cd19670
UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), E3-alpha-3 ...
 224-291 4.61e-26

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: 102.83  E-value: 4.61e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442615440  224 CGLVWVPHVVAYRCRTCGISPCMSICRDCFKKGNHTNHDFNMFLSQAGGACDCGDTSVMKAEGFCSDH 291
Cdd:cd19670     1 CGKSLKKGELYYRCLDCSLDPSSCICEECFLNGNHEGHNYSLRTSSGGGVCDCGDSEAWKPSGFCSKH 68
RING-H2_UBR3 cd16483
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar ...
 1601-1651 2.08e-24

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: 98.23  E-value: 2.08e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442615440 1601 GVHVQSCGHHVHLSCLEAYLKTLYTTQ---RQPVQDRGEFYCPVCRQLSNSVLP 1651
Cdd:cd16483    10 GVHVQTCGHYIHIDCHKSYLESLRQDQvglQLLSVRRGEFTCPLCRQLSNSVLP 63
UBR-box_UBR1_like cd19672
UBR-box found in ubiquitin-protein ligases, E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), and similar ...
 223-292 1.88e-19

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: 84.23  E-value: 1.88e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440  223 KCGLVWVPHVVAYRCRTCGISPCMSICRDCFKKGNHTNHDFNMFLSQAGGACDCGDTSVMKAEGFCSDHG 292
Cdd:cd19672     1 VCGRVFKPGEPTYSCLDCGVDPTCVLCEDCFLNSEHVNHNYKMSISSGGGCCDCGDPEAWKSHSFCSKHG 70
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 223-292 3.41e-18

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: 80.56  E-value: 3.41e-18
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440    223 KCGLVWVPHVVAYRCRTCGISPCMSICRDCFKKGNHTNHDFNMFLSQAGGACDCGDTSVMKAEGFCSDHG 292
Cdd:smart00396    2 VCGYKFTGGEVIYRCKTCGLDPTCVLCSDCFRPSCHKGHDVSLKTSRGSGICDCGDKEAWNEDLKCKAHE 71
UBR-box_UBR1 cd19678
UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1) and similar proteins; UBR1 (EC 2.3. ...
 224-291 6.82e-16

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: 74.18  E-value: 6.82e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442615440  224 CGLVWVPHVVAYRCRTCGISPCMSICRDCFKKGNHTNHDFNMFLSQAGGACDCGDTSVMKAEGFCSDH 291
Cdd:cd19678     2 CGRVFKGGETTYSCRDCAIDPTCVLCMDCFQNSVHKNHRYKMHSSTGGGFCDCGDTEAWKTGPFCVKH 69
UBR-box cd19669
UBR-box found in UBR family of E3 ubiquitin ligases (UBR1-7) and similar proteins; The UBR-box ...
 224-291 2.03e-14

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: 69.85  E-value: 2.03e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442615440  224 CGLVW-VPHVVAYRCRTCGISPCMSICRDCFKKgNHTNHDFNMFLSQaGGACDCGDTSVmkAEGFCSDH 291
Cdd:cd19669     1 CTFSItGINQVMYHCLTCSLDDNSGICEECAKK-CHEGHDVVYIGSG-SGFCDCGDSSA--KSGFCKCH 65
UBR-box_UBR2 cd19679
UBR-box found in ubiquitin-protein ligase E3-alpha-2 (UBR2) and similar proteins; UBR2 (EC 2.3. ...
 224-291 1.38e-11

UBR-box found in ubiquitin-protein ligase E3-alpha-2 (UBR2) and similar proteins; UBR2 (EC 2.3.2.27), also called ubiquitin-protein ligase E3-alpha-II (E3alpha-II), or N-recognin-2, 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. 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: 439077  Cd Length: 70  Bit Score: 61.86  E-value: 1.38e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442615440  224 CGLVWVPHVVAYRCRTCGISPCMSICRDCFKKGNHTNHDFNMFLSQAGGACDCGDTSVMKAEGFCSDH 291
Cdd:cd19679     2 CGRVFKVGEPTYSCRDCAVDPTCVLCMECFLGSIHRDHRYRMTTSGGGGFCDCGDTEAWKEGPYCQKH 69
RING-H2_UBR1-like cd16482
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 ...
 1601-1651 1.57e-11

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: 61.59  E-value: 1.57e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440 1601 GVHVQSCGHHVHLSCLEAYL-KTLYTTQRQPVQ--------DRGEFYCPVCRQLSNSVLP 1651
Cdd:cd16482     8 GLHISSCGHVMHYDCWQRYFdSVRLREQRRPAFrrhhsedvSKGEFLCPLCKSLSNTVLP 67
RING-H2_UBR1 cd16685
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1) and similar ...
 1591-1654 2.04e-07

RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1) and similar proteins; UBR1, also known as N-recognin-1 or E3alpha-I, is an E3 ubiquitin-protein ligase component of the N-end rule pathway. It also promotes degradation of proteins via distinct mechanism that detects a misfolded conformation. UBR1 associates with the RAD6-encoded E2 enzyme to form an E2-E3 complex that catalyzes the synthesis of a substrate-linked multi-ubiquitin chain and may also mediate the delivery of substrates to the 26S proteasome. Moreover, UBR1 promotes the degradation of misfolded proteins in the cytosol. It promotes protein kinase quality control and sensitizes cells to heat shock protein 90 (Hsp90) inhibition. Furthermore, UBR1 functions as a polyubiquitylation-enhancing component of the UBR1-UFD4 complex in its targeting of ubiquitin-fusion degradation (UFD) substrates. UBR1 harbors at least three distinct substrate-binding sites and functions in association with Ubc2/Rad6 and also Ubc4. It contains 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. A missense mutation in UBR1 is responsible for Johanson-Blizzard syndrome leads to UBR box unfolding and loss of function.


Pssm-ID: 438346  Cd Length: 120  Bit Score: 51.79  E-value: 2.04e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442615440 1591 YLSNNMAYdnGVHVQSCGHHVHLSCLEAYLKTLYTTQRQPVQ-------DRGEFYCPVCRQLSNSVLPLSP 1654
Cdd:cd16685    52 FMNPDLAY--GTHTGSCGHVMHAVCWQKYFEAVQNSTRQRLHvelifdlENGEYLCPLCKSLCNTVIPIIP 120
RING-H2_UBR2 cd16686
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-2 (UBR2) and similar ...
 1559-1651 6.81e-07

RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-2 (UBR2) and similar proteins; UBR2, also known as N-recognin-2 or E3alpha-II, is an E3 ubiquitin-protein ligase that plays an important role in maintaining genome integrity and in homologous recombination repair. It regulates the level of the transcription factor Rpn4 (also known as Son1 and Ufd5) through ubiquitylation. The ubiquitin-conjugating enzyme Rad6, another binding partner of URB2, and an additional factor Mub1, are required for the ubiquitin-dependent degradation of Rpn4. UBR2 associates with Mub1 to form a Mub1/Ubr2 complex that regulates the conserved Dsn1 kinetochore protein levels, which is a part of a quality control system that monitors kinetochore integrity, thus ensuring genomic stability. As the recognition component of a major cellular proteolytic system, UBR2 is associated with chromatin and controls chromatin dynamics and gene expression in both spermatocytes and somatic cells. UBR2 also mediates transcriptional silencing during spermatogenesis via histone ubiquitination. It functions as a scaffold E3 promoting HR6B/UbcH2-dependent ubiquitylation of H2A and H2B, but not H3 and H4. It also binds to Tex19.1, also known as Tex19, a germ cell-specific protein, and metabolically stabilizes it during spermatogenesis. Furthermore, UBR2 is involved in skeletal muscle (SKM) atrophy. Its expression can be modulated by the mouse ether-a-gogo-related gene 1a (MERG1a) potassium channel. In addition, UBR2 up-regulation in cachectic muscle is mediated by the p38beta-CCAAT/enhancer binding protein (C/EBP)-beta signaling pathway responsible for the bulk of tumor-induced muscle proteolysis. UBR2 contains 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: 438347  Cd Length: 116  Bit Score: 50.01  E-value: 6.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442615440 1559 EDESRLAHTTRLAAEFNRRTELLSlkfGDESWYLSNNMAYDN---------GVHVQSCGHHVHLSCLEAYLKTLYTTQRQ 1629
Cdd:cd16686     8 EQEIKVDNKAMVLAAFVQRSTVMS---KNRSRVIHDPEKYDPlfmhpdlscGTHTGSCGHIMHAHCWQRYFDAVQAKEQR 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 442615440 1630 PVQ----------DRGEFYCPVCRQLSNSVLP 1651
Cdd:cd16686    85 RQQrlrvhtsydvENGEFLCPLCECLSNTVIP 116
FliJ pfam02050
Flagellar FliJ protein;
1410-1477 3.37e-05

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 45.35  E-value: 3.37e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442615440  1410 FIGNLLRKIAKQDEQCAQSIDDIRARL--WpnqREKQAEAKARE---AKEKEERRKKARERQQKMMQDFANKQ 1477
Cdd:pfam02050   53 FISQLDEAIAQQQQELAQAEAQVEKAReeW---QEARQERKSLEklrEREKKEERKEQNRREQKQLDELAARL 122
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1414-1484 1.25e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.45  E-value: 1.25e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442615440  1414 LLRKIAKQDEQcaqsiDDIRARLWPNQREKQAEAKAREAKEKEERR----KKARERQ----QKMMQDFANKQKLFMQSA 1484
Cdd:pfam13868  193 QEKAQDEKAER-----DELRAKLYQEEQERKERQKEREEAEKKARQrqelQQAREEQielkERRLAEEAEREEEEFERM 266
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
1410-1477 6.11e-04

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 442129 [Multi-domain]  Cd Length: 142  Bit Score: 42.20  E-value: 6.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442615440 1410 FIGNLLRKIAKQD---EQCAQSIDDIRARLwpnqREKQAEAKA----REAKEKEERRKKAReRQQKMMQDFANKQ 1477
Cdd:COG2882    72 FIARLDEAIEQQQqqvAQAEQQVEQARQAW----LEARQERKAleklKERRREEERQEENR-REQKELDELASRR 141
Nexin_C pfam08628
Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the ...
 1421-1471 3.86e-03

Sorting nexin C terminal; This region is found a the C terminal of proteins belonging to the sorting nexin family. It is found on proteins which also contain pfam00787.


Pssm-ID: 462541  Cd Length: 111  Bit Score: 39.13  E-value: 3.86e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 442615440  1421 QDEQCAQSIDDIRARLWPNQREKQaEAKAREAKEKEERRKKARerqQKMMQ 1471
Cdd:pfam08628   35 SEEQVASYIRLLRDALWPGGLLAE-PPPERTEEEKLRTRKEAR---KLLLS 81
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
 1411-1477 3.88e-03

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 39.99  E-value: 3.88e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442615440  1411 IGNLLRKIAKQDEQCaqsiDDIRARLWPNQREKQAEAKAREAKEKEERRKKAReRQQKMMQDFANKQ 1477
Cdd:TIGR02473   77 IQQQQQELALLQQEV----EAKRERLLEARRELKALEKLKEKKQKEYRAEEAK-REQKEMDELATQR 138
 
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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