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Conserved domains on  [gi|33243977|gb|AAH55343|]
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Fbxo11 protein, partial [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UBR-box_UBR6_FBXO11 cd19676
UBR-box found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11 (also called UBR6, ...
 429-497 6.98e-43

UBR-box found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11 (also called UBR6, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1)) is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. FBXO11 is a substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. FBXO11 does not bind N-terminal signals.


:

Pssm-ID: 439074  Cd Length: 69  Bit Score: 146.88  E-value: 6.98e-43
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33243977 429 CLYKISSYTSYPMHDFYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGAGTLSNPCTLAG 497
Cdd:cd19676   1 CLYKISSYTSFPMHDFYRCLTCNTTDRNAICVNCIKKCHEGHDVEFIRHDRFFCDCGAGTLSNDCQLAG 69
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 258-413 6.83e-27

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


:

Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 106.34  E-value: 6.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977   258 SGVQIRTGSNPKIRRNKIWGGQNGGILVYNSGLGCIEDNEIFDNAMAGVWIKTDSNPTLRRNKIHDGRDGGICIFNGGRG 337
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33243977   338 LLEENDIFRNAQAGVLISTNSHPVLRKNRIFDGFAAGIEIT-NHATATLEGNQIFNNRFGGLFLASGV-NVTMKDNKI 413
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEdSSNNVTISNNTVTNNKGAGILIVGGSsNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 120-275 9.07e-25

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


:

Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 100.17  E-value: 9.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977   120 AGVWITSNSDPTIRGNSIFNGNQGGVYIFGDGRGLIEGNDIYGNALAGIQIRTNSCPIVRHNKIHDGQHGGIYVHEKGQG 199
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33243977   200 VIEENEVYSNTLAGVWVTTGSTPVLRRNRIHSGKQVGVYFYDNGHGV-LEDNDIYNHMYSGVQI-RTGSNPKIRRNKI 275
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIvGGSSNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 28-183 3.76e-20

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


:

Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 87.08  E-value: 3.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977    28 AGIWVKNHGNPIIRRNHIHHGRDVGVFTFDHGMGYFESCNIHRNRIAGFEVKAYANPTVVRCEIHHGQTGGIYVHEKGRG 107
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33243977   108 QFIENKIYANNFAGVWITSNSDPTIRGNSIFNGNQGGVYIF-GDGRGLIEGNDIYGNALAGIQIRTNSC-PIVRHNKI 183
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEdSSNNVTISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
 
Name Accession Description Interval E-value
UBR-box_UBR6_FBXO11 cd19676
UBR-box found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11 (also called UBR6, ...
 429-497 6.98e-43

UBR-box found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11 (also called UBR6, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1)) is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. FBXO11 is a substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. FBXO11 does not bind N-terminal signals.


Pssm-ID: 439074  Cd Length: 69  Bit Score: 146.88  E-value: 6.98e-43
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33243977 429 CLYKISSYTSYPMHDFYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGAGTLSNPCTLAG 497
Cdd:cd19676   1 CLYKISSYTSFPMHDFYRCLTCNTTDRNAICVNCIKKCHEGHDVEFIRHDRFFCDCGAGTLSNDCQLAG 69
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 258-413 6.83e-27

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 106.34  E-value: 6.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977   258 SGVQIRTGSNPKIRRNKIWGGQNGGILVYNSGLGCIEDNEIFDNAMAGVWIKTDSNPTLRRNKIHDGRDGGICIFNGGRG 337
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33243977   338 LLEENDIFRNAQAGVLISTNSHPVLRKNRIFDGFAAGIEIT-NHATATLEGNQIFNNRFGGLFLASGV-NVTMKDNKI 413
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEdSSNNVTISNNTVTNNKGAGILIVGGSsNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 120-275 9.07e-25

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 100.17  E-value: 9.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977   120 AGVWITSNSDPTIRGNSIFNGNQGGVYIFGDGRGLIEGNDIYGNALAGIQIRTNSCPIVRHNKIHDGQHGGIYVHEKGQG 199
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33243977   200 VIEENEVYSNTLAGVWVTTGSTPVLRRNRIHSGKQVGVYFYDNGHGV-LEDNDIYNHMYSGVQI-RTGSNPKIRRNKI 275
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIvGGSSNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 28-183 3.76e-20

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 87.08  E-value: 3.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977    28 AGIWVKNHGNPIIRRNHIHHGRDVGVFTFDHGMGYFESCNIHRNRIAGFEVKAYANPTVVRCEIHHGQTGGIYVHEKGRG 107
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33243977   108 QFIENKIYANNFAGVWITSNSDPTIRGNSIFNGNQGGVYIF-GDGRGLIEGNDIYGNALAGIQIRTNSC-PIVRHNKI 183
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEdSSNNVTISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 131-421 7.57e-17

Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion transport and metabolism];


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 81.89  E-value: 7.57e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977 131 TIRGnsifngnQGGVYIFGDGRG---LIEGNDIygnALAGIQIRtNScpivrhNKIHDGQHGGIYVHEKGQGVIEENEVy 207
Cdd:COG3420  55 TLIG-------EGGAVIDGGGKGtviTITADNV---TVRGLTIT-GS------GDSLTDDDAGIYVRGADNAVIENNRI- 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977 208 SNTLAGVWVTTGSTPVLRRNRIHSGKQV------GVYFYDNGHGVLEDNDIYNHmYSGVQIRTGSNPKIRRNKIWGGQNG 281
Cdd:COG3420 117 ENNLFGIYLEGSDNNVIRNNTISGNRDLradrgnGIHLWNSPGNVIEGNTISGG-RDGIYLEFSDNNVIRNNTIRNLRYG 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977 282 gILVYNSGLGCIEDNEIFDNAmAGVWIKTDSNPTLRRNKIHDGRDGGICIFNGGRGLLEENDIFRNAQagvlistnshpv 361
Cdd:COG3420 196 -IHYMYSNDNLVEGNTFRDNG-AGIALMYSKGNTVRGNTILGNSGYGILLKESSDSVIEGNTISGNGK------------ 261

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977 362 lrknrifdgfaaGIEITNHATATLEGNQIFNNRFGGLFLASGVNVTMKDNKIMNNQDAIE 421
Cdd:COG3420 262 ------------GIFIYNSNRNTIRGNLFAGNGIGIHLTAGSEGNRIYGNNFIGNRTQVK 309
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 92-305 1.34e-14

Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion transport and metabolism];


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 74.95  E-value: 1.34e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977  92 HHGQTGGIYVhEKGRGQFIENKIYANNFAGVWITSNSDPTIRGNSIFNGNQG------GVYIFGDGRGLIEGNDIYGNAl 165
Cdd:COG3420  94 LTDDDAGIYV-RGADNAVIENNRIENNLFGIYLEGSDNNVIRNNTISGNRDLradrgnGIHLWNSPGNVIEGNTISGGR- 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977 166 AGIQIRTNSCPIVRHNKIHDGQHgGIYVHEKGQGVIEENEVYSNTlAGVWVTTGSTPVLRRNRIHSGKQVGVYFYDNGHG 245
Cdd:COG3420 172 DGIYLEFSDNNVIRNNTIRNLRY-GIHYMYSNDNLVEGNTFRDNG-AGIALMYSKGNTVRGNTILGNSGYGILLKESSDS 249

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977 246 VLEDNDIYNHMYsGVQIRTGSNPKIRRNKIWGGQNGGILVYNSglgciEDNEIFDNAMAG 305
Cdd:COG3420 250 VIEGNTISGNGK-GIFIYNSNRNTIRGNLFAGNGIGIHLTAGS-----EGNRIYGNNFIG 303
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 444-485 6.53e-10

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: 55.14  E-value: 6.53e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 33243977    444 FYRCHTCNTTDRNAICVNC-IKKCHQGHDVEFIRHDR-FFCDCG 485
Cdd:smart00396  13 IYRCKTCGLDPTCVLCSDCfRPSCHKGHDVSLKTSRGsGICDCG 56
zf-UBR pfam02207
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ...
 444-485 6.68e-09

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: 52.29  E-value: 6.68e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 33243977   444 FYRCHTCNTTDRNAICVNCIKKC-HQGHDVEFIRHDR-FFCDCG 485
Cdd:pfam02207  11 VYRCLTCSLDPTCVICYSCFINCdHEGHDYELFTSRGgGCCDCG 54
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 17-163 6.78e-05

Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion transport and metabolism];


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 44.91  E-value: 6.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977  17 YEDNEISNNAlAGIWVKNHGNPIIRRNHIHHGRDVGVFTFDhgmgyfescnIHRNRIAGfevkayaNpTVVRCEIhhgqt 96
Cdd:COG3420 206 VEGNTFRDNG-AGIALMYSKGNTVRGNTILGNSGYGILLKE----------SSDSVIEG-------N-TISGNGK----- 261

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33243977  97 gGIYVHEKGRGQFIENKIyANNFAGVWITSNS-DPTIRGNSiFNGNQGGVYiFGDGRGLIEGNDIYGN 163
Cdd:COG3420 262 -GIFIYNSNRNTIRGNLF-AGNGIGIHLTAGSeGNRIYGNN-FIGNRTQVK-YVGGRDNEWSADGRGN 325
CASH smart00722
Domain present in carbohydrate binding proteins and sugar hydrolses;
59-148 6.93e-03

Domain present in carbohydrate binding proteins and sugar hydrolses;


Pssm-ID: 214788  Cd Length: 153  Bit Score: 37.49  E-value: 6.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977     59 GMGYFESCNIHRNRIAGFEVKAYANPTVVRCEIHHGqtGGIYVHEKGRGQFIENKIYANNFA---GVWITSNSDPTIRGN 135
Cdd:smart00722  63 GIYVSASGDPVIQNDGTGKNLIIDNVTFNGTEINSG--AGIVVTAGSEGLFIGNRIIGNYVAtgdGNYLSDSSGGDLIGN 140

                           90
                   ....*....|...
gi 33243977    136 SIFNGNQGGVYIF 148
Cdd:smart00722 141 RIYDNNRDGIAVV 153
 
Name Accession Description Interval E-value
UBR-box_UBR6_FBXO11 cd19676
UBR-box found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11 (also called UBR6, ...
 429-497 6.98e-43

UBR-box found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11 (also called UBR6, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1)) is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. FBXO11 is a substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. FBXO11 does not bind N-terminal signals.


Pssm-ID: 439074  Cd Length: 69  Bit Score: 146.88  E-value: 6.98e-43
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33243977 429 CLYKISSYTSYPMHDFYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGAGTLSNPCTLAG 497
Cdd:cd19676   1 CLYKISSYTSFPMHDFYRCLTCNTTDRNAICVNCIKKCHEGHDVEFIRHDRFFCDCGAGTLSNDCQLAG 69
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 258-413 6.83e-27

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 106.34  E-value: 6.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977   258 SGVQIRTGSNPKIRRNKIWGGQNGGILVYNSGLGCIEDNEIFDNAMAGVWIKTDSNPTLRRNKIHDGRDGGICIFNGGRG 337
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33243977   338 LLEENDIFRNAQAGVLISTNSHPVLRKNRIFDGFAAGIEIT-NHATATLEGNQIFNNRFGGLFLASGV-NVTMKDNKI 413
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEdSSNNVTISNNTVTNNKGAGILIVGGSsNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 120-275 9.07e-25

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 100.17  E-value: 9.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977   120 AGVWITSNSDPTIRGNSIFNGNQGGVYIFGDGRGLIEGNDIYGNALAGIQIRTNSCPIVRHNKIHDGQHGGIYVHEKGQG 199
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33243977   200 VIEENEVYSNTLAGVWVTTGSTPVLRRNRIHSGKQVGVYFYDNGHGV-LEDNDIYNHMYSGVQI-RTGSNPKIRRNKI 275
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIvGGSSNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 74-221 5.64e-23

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 95.17  E-value: 5.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977    74 AGFEVKAYANPTVVRCEIHHGQTGGIYVHEKGRGQFIENKIYANNFAGVWITSNSDPTIRGNSIFNGNQGGVYIFGDGRG 153
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33243977   154 LIEGNDIYGNALAGIQIRTNSCPIVRHNKIHDGQHGGIYVHEKGQGV-IEENEVYSNTLAGVWVTTGST 221
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIVGGSS 149
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 166-321 3.32e-22

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 93.24  E-value: 3.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977   166 AGIQIRTNSCPIVRHNKIHDGQHGGIYVHEKGQGVIEENEVYSNTLAGVWVTTGSTPVLRRNRIHSGKQVGVYFYDNGHG 245
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33243977   246 VLEDNDIYNHMYSGVQIRTGSNPKIRRNKIWGGQNGGILVYNSGLGC-IEDNEIFDNAMAGVWI-KTDSNPTLRRNKI 321
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIvGGSSNNTVENNTF 158
UBR-box_UBR4_5_6_7 cd19671
UBR-box found in UBR4, UBR5, UBR6/FBOX11, UBR7 and similar proteins; This family includes UBR4 ...
 432-495 1.17e-20

UBR-box found in UBR4, UBR5, UBR6/FBOX11, UBR7 and similar proteins; This family includes UBR4 (EC 2.3.2.27), UBR5 (EC 2.3.2.26), UBR6/FBOX11 and UBR7 (EC 2.3.2.27). Both UBR4 (also called 600 kDa retinoblastoma protein-associated factor, or N-recognin-4, or retinoblastoma-associated factor of 600 kDa, or RBAF600, or p600, or zinc finger UBR1-type protein 1) and UBR7 (also called N-recognin-7) 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. UBR5 (also called E3 ubiquitin-protein ligase, HECT domain-containing 1, E3 ligase identified by differential display (EDD), hyperplastic discs protein homolog (HYD), progestin-induced protein, or N-recognin-5) is a HECT (homologous to E6-AP C-terminus)-type E3 ubiquitin-protein ligase that acts as a key regulator of the ubiquitin proteasome system in both cancer and developmental biology. It is required for Wnt signal responses in Drosophila and human cell lines downstream of activated Armadillo/beta-catenin. It also plays a key role in ciliogenesis by regulating centriolar satellite stability and primary cilia. UBR6 (also called FBOX11, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1)), is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. UBR6 is a substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. UBR6 does not bind N-terminal signals.


Pssm-ID: 439069  Cd Length: 67  Bit Score: 85.59  E-value: 1.17e-20
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33243977 432 KISSYTSYPMHDFYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGAGTlSNPCTL 495
Cdd:cd19671   3 FEKTGRKYIKQPWYHCYTCGLIDGLGVCEACARKCHKGHDLVYIGYSNFYCDCGSSG-PGKCKC 65
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 212-359 2.25e-20

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 87.85  E-value: 2.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977   212 AGVWVTTGSTPVLRRNRIHSGKQVGVYFYDNGHGVLEDNDIYNHMYSGVQIRTGSNPKIRRNKIWGGQNGGILVYNSGLG 291
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33243977   292 CIEDNEIFDNAMAGVWIKTDSNPTLRRNKIHDGRDGGICIFNGGRGL-LEENDIFRNAQAGVLISTNSH 359
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIVGGSS 149
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 28-183 3.76e-20

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 87.08  E-value: 3.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977    28 AGIWVKNHGNPIIRRNHIHHGRDVGVFTFDHGMGYFESCNIHRNRIAGFEVKAYANPTVVRCEIHHGQTGGIYVHEKGRG 107
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33243977   108 QFIENKIYANNFAGVWITSNSDPTIRGNSIFNGNQGGVYIF-GDGRGLIEGNDIYGNALAGIQIRTNSC-PIVRHNKI 183
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEdSSNNVTISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 236-390 6.64e-17

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 77.83  E-value: 6.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977   236 GVYFYDNGHGVLEDNDIYNHMYSGVQIRTGSNPKIRRNKIWGGQNGGILVYNSGLGCIEDNEIFDNAMAGVWIKTDSNPT 315
Cdd:pfam13229   2 GILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNNL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33243977   316 LRRNKIHDGRDGGICIFNGGRGLLEENDIFRNAQAGVLISTNSHPV-LRKNRIFDGFAAGIEITNHAT-ATLEGNQI 390
Cdd:pfam13229  82 IENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 131-421 7.57e-17

Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion transport and metabolism];


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 81.89  E-value: 7.57e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977 131 TIRGnsifngnQGGVYIFGDGRG---LIEGNDIygnALAGIQIRtNScpivrhNKIHDGQHGGIYVHEKGQGVIEENEVy 207
Cdd:COG3420  55 TLIG-------EGGAVIDGGGKGtviTITADNV---TVRGLTIT-GS------GDSLTDDDAGIYVRGADNAVIENNRI- 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977 208 SNTLAGVWVTTGSTPVLRRNRIHSGKQV------GVYFYDNGHGVLEDNDIYNHmYSGVQIRTGSNPKIRRNKIWGGQNG 281
Cdd:COG3420 117 ENNLFGIYLEGSDNNVIRNNTISGNRDLradrgnGIHLWNSPGNVIEGNTISGG-RDGIYLEFSDNNVIRNNTIRNLRYG 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977 282 gILVYNSGLGCIEDNEIFDNAmAGVWIKTDSNPTLRRNKIHDGRDGGICIFNGGRGLLEENDIFRNAQagvlistnshpv 361
Cdd:COG3420 196 -IHYMYSNDNLVEGNTFRDNG-AGIALMYSKGNTVRGNTILGNSGYGILLKESSDSVIEGNTISGNGK------------ 261

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977 362 lrknrifdgfaaGIEITNHATATLEGNQIFNNRFGGLFLASGVNVTMKDNKIMNNQDAIE 421
Cdd:COG3420 262 ------------GIFIYNSNRNTIRGNLFAGNGIGIHLTAGSEGNRIYGNNFIGNRTQVK 309
UBR-box cd19669
UBR-box found in UBR family of E3 ubiquitin ligases (UBR1-7) and similar proteins; The UBR-box ...
 444-491 3.30e-16

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: 72.93  E-value: 3.30e-16
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 33243977 444 FYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGAGTLSN 491
Cdd:cd19669  12 MYHCLTCSLDDNSGICEECAKKCHEGHDVVYIGSGSGFCDCGDSSAKS 59
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 1-137 3.67e-16

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 75.91  E-value: 3.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977     1 DCENVGLYITDHAQGIYEDNEISNNALAGIWVKNHGNPIIRRNHIHHGRDVGVFTFDHGMGYFESCNIHRNRIAGFEVKA 80
Cdd:pfam13229  20 NNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNNLIENNTISNNGGAGIYLSD 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 33243977    81 YANPTVVRCEIHHGQTGGIYV-HEKGRGQFIENKIYANNFAGVWITSNSD-PTIRGNSI 137
Cdd:pfam13229 100 SSNNTIENNIIHNNGGSGIVIeDSSNNVTISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
UBR-box_UBR4_like cd19674
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3. ...
 427-493 4.00e-15

UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3.2.27; also called 600 kDa retinoblastoma protein-associated factor, N-recognin-4, retinoblastoma-associated factor of 600 kDa, RBAF600, p600, or zinc finger UBR1-type protein 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. UBR4 acts as a multifunctional protein with roles in anoikis, viral transformation, and protein degradation, as well as in neurogenesis, neuronal migration, neuronal signaling, and survival. The family also includes Arabidopsis thaliana auxin transport protein BIG (also called protein attenuated shade avoidance 1, protein corymbosa1, protein dark over-expression of cab 1, protein low phosphate-resistant root 1, protein transport inhibitor response 3, or protein umbrella 1). It is a calossin-like protein required for auxin efflux and polar auxin transport (PAT) influencing auxin-mediated developmental responses in Arabidopsis.


Pssm-ID: 439072  Cd Length: 72  Bit Score: 70.07  E-value: 4.00e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33243977 427 GQCLYKISSyTSYPMHDFYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGAGTLSNPC 493
Cdd:cd19674   1 NVCTFASTG-KNYARQHWYECYTCFLNGNEGVCEVCARVCHKGHDLVYSKTSSFFCDCGAGGGPSKC 66
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 304-419 4.14e-15

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 72.82  E-value: 4.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977   304 AGVWIKTDSNPTLRRNKIHDGRDGGICIFNGGRGLLEENDIFRNAQAGVLISTNSHPVLRKNRIFDGFAAGIEITNHATA 383
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 33243977   384 TLEGNQIFNNRFGGLFLASGVNVTMKDNKIMNNQDA 419
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGS 116
UBR-box_BIG_like cd19681
UBR-box found in Arabidopsis thaliana auxin transport protein BIG and similar proteins; BIG ...
 429-493 5.52e-15

UBR-box found in Arabidopsis thaliana auxin transport protein BIG and similar proteins; BIG (also called protein attenuated shade avoidance 1, protein corymbosa1, protein dark over-expression of cab 1, protein low phosphate-resistant root 1, protein transport inhibitor response 3, or protein umbrella 1) is a calossin-like protein required for auxin efflux and polar auxin transport (PAT) influencing auxin-mediated developmental responses in Arabidopsis.


Pssm-ID: 439079  Cd Length: 74  Bit Score: 69.74  E-value: 5.52e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33243977 429 CLYkISSYTSYPMHDFYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGAGTLS--NPC 493
Cdd:cd19681   3 CTY-VSSGSNFMEQHWYFCYTCGLVDSKGCCSVCAKVCHRGHDVVYSRYSRFFCDCGAGGAKrgRPC 68
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 92-305 1.34e-14

Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion transport and metabolism];


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 74.95  E-value: 1.34e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977  92 HHGQTGGIYVhEKGRGQFIENKIYANNFAGVWITSNSDPTIRGNSIFNGNQG------GVYIFGDGRGLIEGNDIYGNAl 165
Cdd:COG3420  94 LTDDDAGIYV-RGADNAVIENNRIENNLFGIYLEGSDNNVIRNNTISGNRDLradrgnGIHLWNSPGNVIEGNTISGGR- 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977 166 AGIQIRTNSCPIVRHNKIHDGQHgGIYVHEKGQGVIEENEVYSNTlAGVWVTTGSTPVLRRNRIHSGKQVGVYFYDNGHG 245
Cdd:COG3420 172 DGIYLEFSDNNVIRNNTIRNLRY-GIHYMYSNDNLVEGNTFRDNG-AGIALMYSKGNTVRGNTILGNSGYGILLKESSDS 249

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977 246 VLEDNDIYNHMYsGVQIRTGSNPKIRRNKIWGGQNGGILVYNSglgciEDNEIFDNAMAG 305
Cdd:COG3420 250 VIEGNTISGNGK-GIFIYNSNRNTIRGNLFAGNGIGIHLTAGS-----EGNRIYGNNFIG 303
UBR-box_UBR4 cd19680
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3. ...
 445-486 7.34e-14

UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3.2.27; also called 600 kDa retinoblastoma protein-associated factor, N-recognin-4, retinoblastoma-associated factor of 600 kDa, RBAF600, p600, or zinc finger UBR1-type protein 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. UBR4 acts as a multifunctional protein with roles in anoikis, viral transformation, and protein degradation, as well as in neurogenesis, neuronal migration, neuronal signaling, and survival.


Pssm-ID: 439078  Cd Length: 71  Bit Score: 66.33  E-value: 7.34e-14
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 33243977 445 YRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGA 486
Cdd:cd19680  18 YHCHTCKMVDGVGVCSVCAKVCHKDHDLSYAKYGSFFCDCGA 59
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 28-230 1.86e-11

Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion transport and metabolism];


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 65.32  E-value: 1.86e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977  28 AGIWVKNHGNPIIRRNHIhHGRDVGVFTFDHgmgyfESCNIHRNRIAGFEVKAYA-----------NPTVVRCEIHHGQt 96
Cdd:COG3420  99 AGIYVRGADNAVIENNRI-ENNLFGIYLEGS-----DNNVIRNNTISGNRDLRADrgngihlwnspGNVIEGNTISGGR- 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977  97 GGIYVHEKGRGQFIENKIyANNFAGVWITSNSDPTIRGNsIFNGNQGGVYIFGDGRGLIEGNDIYGNALAGIQIRTNSCP 176
Cdd:COG3420 172 DGIYLEFSDNNVIRNNTI-RNLRYGIHYMYSNDNLVEGN-TFRDNGAGIALMYSKGNTVRGNTILGNSGYGILLKESSDS 249

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 33243977 177 IVRHNKIHDGQHgGIYVHEKGQGVIEENEVYSNTLaGVWVTTGSTpvlrRNRIH 230
Cdd:COG3420 250 VIEGNTISGNGK-GIFIYNSNRNTIRGNLFAGNGI-GIHLTAGSE----GNRIY 297
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 444-485 6.53e-10

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: 55.14  E-value: 6.53e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 33243977    444 FYRCHTCNTTDRNAICVNC-IKKCHQGHDVEFIRHDR-FFCDCG 485
Cdd:smart00396  13 IYRCKTCGLDPTCVLCSDCfRPSCHKGHDVSLKTSRGsGICDCG 56
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 190-347 1.21e-09

Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to insert copper into the exported reductase apoenzyme (NosZ). This region forms a parallel beta helix domain.


Pssm-ID: 428281 [Multi-domain]  Cd Length: 215  Bit Score: 58.20  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977   190 GIYVHEKGQGVIEENEVySNTLAGVWVTTGSTPVLRRNRIHSGKQvGVYFYDNGHGVLEDNDIYNhMYSGVQIRTGSNPK 269
Cdd:pfam05048  21 GIQLWNTEGNVISNNDI-INSRDGIYLDASNNNTITGNRISNLRY-GIHLMNSNDNTISDNVFSG-NTAGIALMSSSNNT 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33243977   270 IRRNKIWGGQNGGILVYNSGLGCIEDNEIFDNAMAGVWIKTDSNPTLRRNKIhDGRDGGICIFNGGrgllEENDIFRN 347
Cdd:pfam05048  98 LENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRI-TSNGIGIHFLAGS----NGNTIYNN 170
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 128-323 4.53e-09

Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to insert copper into the exported reductase apoenzyme (NosZ). This region forms a parallel beta helix domain.


Pssm-ID: 428281 [Multi-domain]  Cd Length: 215  Bit Score: 56.66  E-value: 4.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977   128 SDPTIRGNSIFNGNQG----GVYIFGDGRGLIEGNDIYGNAlAGIQIRTNSCPIVRHNKIHDGqHGGIYVHEKGQGVIEE 203
Cdd:pfam05048   1 VNNAISGDTIGIYNGLsrgnGIQLWNTEGNVISNNDIINSR-DGIYLDASNNNTITGNRISNL-RYGIHLMNSNDNTISD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977   204 NEVYSNTlagvwvttgstpvlrrnrihsgkqVGVYFYDNGHGVLEDNDIYNHMYSGVQIRTGSNPKIRRNKIWGGQNGGI 283
Cdd:pfam05048  79 NVFSGNT------------------------AGIALMSSSNNTLENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGI 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 33243977   284 LVYNSGLGCIEDNEIFDNAmAGVWIKTDSNptlrRNKIHD 323
Cdd:pfam05048 135 FLYNSDYNTITGNRITSNG-IGIHFLAGSN----GNTIYN 169
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 235-417 5.63e-09

Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to insert copper into the exported reductase apoenzyme (NosZ). This region forms a parallel beta helix domain.


Pssm-ID: 428281 [Multi-domain]  Cd Length: 215  Bit Score: 56.27  E-value: 5.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977   235 VGVYFYDNGHGVLEDNDIYNhmysGVQIRTGSNPKIRRNKIWGGQNGGILVYNSGLGcIEDNEIFDNaMAGVWIKTDSNP 314
Cdd:pfam05048   1 VNNAISGDTIGIYNGLSRGN----GIQLWNTEGNVISNNDIINSRDGIYLDASNNNT-ITGNRISNL-RYGIHLMNSNDN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977   315 TLRRNKIHDGRDGgICIFNGGRGLLEENDIFRNAQAGVLISTNSHPVLRKNRIFDGFAAGIEITNHATATLEGNQIFNNR 394
Cdd:pfam05048  75 TISDNVFSGNTAG-IALMSSSNNTLENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRITSNG 153

                         170       180
                  ....*....|....*....|...
gi 33243977   395 FGGLFLASGVNVTMKDNKIMNNQ 417
Cdd:pfam05048 154 IGIHFLAGSNGNTIYNNYFINNS 176
zf-UBR pfam02207
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ...
 444-485 6.68e-09

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: 52.29  E-value: 6.68e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 33243977   444 FYRCHTCNTTDRNAICVNCIKKC-HQGHDVEFIRHDR-FFCDCG 485
Cdd:pfam02207  11 VYRCLTCSLDPTCVICYSCFINCdHEGHDYELFTSRGgGCCDCG 54
UBR-box_UBR7 cd19677
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR7 and similar proteins; UBR7 (EC 2.3. ...
 445-495 8.85e-09

UBR-box found in RING-type E3 ubiquitin-protein ligase UBR7 and similar proteins; UBR7 (EC 2.3.2.27; also called N-recognin-7) 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. UBR7 may play an important role in spermiogenesis and fertilization.


Pssm-ID: 439075  Cd Length: 71  Bit Score: 51.93  E-value: 8.85e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 33243977 445 YRCHTCN---TTDRNAICVNCIKKCHQGHDVEFIRHDRFF-CDCG-AGTLSNPCTL 495
Cdd:cd19677  14 YACLTCTpagADQPAGICLACSLSCHEGHELEELYTKRNFrCDCGnSKFPSNPCKL 69
UBR-box_UBR1_2_3 cd19670
UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), E3-alpha-3 ...
 444-485 1.78e-07

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: 48.13  E-value: 1.78e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 33243977 444 FYRCHTCNTTDRNAICVNC-IKKCHQGHDVEFIR-HDRFFCDCG 485
Cdd:cd19670  11 YYRCLDCSLDPSSCICEECfLNGNHEGHNYSLRTsSGGGVCDCG 54
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 91-277 3.50e-07

Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to insert copper into the exported reductase apoenzyme (NosZ). This region forms a parallel beta helix domain.


Pssm-ID: 428281 [Multi-domain]  Cd Length: 215  Bit Score: 50.88  E-value: 3.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977    91 IHHGQTGGIYVHEKGRGQF-IENKIYANNFAGVWITSNSDPTIRGNSIFNGNqGGVYIFGDGRGLIEGNDIYGNalagiq 169
Cdd:pfam05048  12 IYNGLSRGNGIQLWNTEGNvISNNDIINSRDGIYLDASNNNTITGNRISNLR-YGIHLMNSNDNTISDNVFSGN------ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977   170 irtnscpivrhnkihdgqHGGIYVHEKGQGVIEENEVYSNTLAGVWVTTGSTPVLRRNRIHSGKQVGVYFYDNGHGVLED 249
Cdd:pfam05048  85 ------------------TAGIALMSSSNNTLENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITG 146

                         170       180
                  ....*....|....*....|....*...
gi 33243977   250 NDIYNHmYSGVQIRTGSNpkirRNKIWG 277
Cdd:pfam05048 147 NRITSN-GIGIHFLAGSN----GNTIYN 169
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 282-420 1.09e-06

Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to insert copper into the exported reductase apoenzyme (NosZ). This region forms a parallel beta helix domain.


Pssm-ID: 428281 [Multi-domain]  Cd Length: 215  Bit Score: 49.72  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977   282 GILVYNSGlGCIEDNEIFDNAMAGVWIKTDSNPTLRRNKIHDGRdGGICIFNGGRGLLEENDIFRNaQAGVLISTNSHPV 361
Cdd:pfam05048  21 GIQLWNTE-GNVISNNDIINSRDGIYLDASNNNTITGNRISNLR-YGIHLMNSNDNTISDNVFSGN-TAGIALMSSSNNT 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 33243977   362 LRKNRIFDGFAAGIEITNHATATLEGNQIFNNRFGGLFLASGVNVTMKDNKIMNNQDAI 420
Cdd:pfam05048  98 LENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRITSNGIGI 156
UBR-box_UBR3 cd19673
UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3. ...
 444-485 2.15e-05

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: 42.56  E-value: 2.15e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 33243977 444 FYRCHTCNTTDRNAICVNCIKKC-HQGHDVEFIRHDRF-FCDCG 485
Cdd:cd19673  14 AYRCRTCGLDPTCVICADCFQAGdHEGHDYSMYRSSAGgCCDCG 57
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 17-163 6.78e-05

Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion transport and metabolism];


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 44.91  E-value: 6.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977  17 YEDNEISNNAlAGIWVKNHGNPIIRRNHIHHGRDVGVFTFDhgmgyfescnIHRNRIAGfevkayaNpTVVRCEIhhgqt 96
Cdd:COG3420 206 VEGNTFRDNG-AGIALMYSKGNTVRGNTILGNSGYGILLKE----------SSDSVIEG-------N-TISGNGK----- 261

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33243977  97 gGIYVHEKGRGQFIENKIyANNFAGVWITSNS-DPTIRGNSiFNGNQGGVYiFGDGRGLIEGNDIYGN 163
Cdd:COG3420 262 -GIFIYNSNRNTIRGNLF-AGNGIGIHLTAGSeGNRIYGNN-FIGNRTQVK-YVGGRDNEWSADGRGN 325
UBR-box_UBR5 cd19675
UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3. ...
 443-484 5.72e-04

UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3.2.26; also called E3 ubiquitin-protein ligase, HECT domain-containing 1, E3 ligase identified by differential display (EDD), hyperplastic discs protein homolog (HYD), progestin-induced protein, or N-recognin-5) is a HECT (homologous to E6-AP C-terminus)-type E3 ubiquitin-protein ligase that acts as a key regulator of the ubiquitin proteasome system in both cancer and developmental biology. It is required for Wnt signal responses in Drosophila and human cell lines downstream of activated Armadillo/beta-catenin. It also plays a key role in ciliogenesis by regulating centriolar satellite stability and primary cilia.


Pssm-ID: 439073  Cd Length: 76  Bit Score: 38.60  E-value: 5.72e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 33243977 443 DFYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHD-RFFCDC 484
Cdd:cd19675  22 DIFECRTCGLVGSLCCCTECARVCHKGHDCKLKRTSpTAYCDC 64
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 6-170 2.24e-03

Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to insert copper into the exported reductase apoenzyme (NosZ). This region forms a parallel beta helix domain.


Pssm-ID: 428281 [Multi-domain]  Cd Length: 215  Bit Score: 39.71  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977     6 GLYITDHAQGIY-EDNEISNNAL----AGIWVKNHGNPIIRRNHIHHGRdVGVFTFDHGMGYFESCNIHRNRiAGFEVKA 80
Cdd:pfam05048  15 GLSRGNGIQLWNtEGNVISNNDIinsrDGIYLDASNNNTITGNRISNLR-YGIHLMNSNDNTISDNVFSGNT-AGIALMS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977    81 YANPTVVRCEIHHGQTGGIYVHEKGRGQFIENKIYANNFAGVWITSNSDPTIRGNSIfNGNQGGVYIFGDGrgliEGNDI 160
Cdd:pfam05048  93 SSNNTLENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRI-TSNGIGIHFLAGS----NGNTI 167

                         170
                  ....*....|
gi 33243977   161 YGNALAGIQI 170
Cdd:pfam05048 168 YNNYFINNSE 177
CASH smart00722
Domain present in carbohydrate binding proteins and sugar hydrolses;
59-148 6.93e-03

Domain present in carbohydrate binding proteins and sugar hydrolses;


Pssm-ID: 214788  Cd Length: 153  Bit Score: 37.49  E-value: 6.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33243977     59 GMGYFESCNIHRNRIAGFEVKAYANPTVVRCEIHHGqtGGIYVHEKGRGQFIENKIYANNFA---GVWITSNSDPTIRGN 135
Cdd:smart00722  63 GIYVSASGDPVIQNDGTGKNLIIDNVTFNGTEINSG--AGIVVTAGSEGLFIGNRIIGNYVAtgdGNYLSDSSGGDLIGN 140

                           90
                   ....*....|...
gi 33243977    136 SIFNGNQGGVYIF 148
Cdd:smart00722 141 RIYDNNRDGIAVV 153
 
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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