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Conserved domains on  [gi|189526006|ref|XP_696134|]
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F-box only protein 11 isoform X1 [Danio rerio]

Protein Classification

F-box only protein 11( domain architecture ID 17778243)

F-box only protein 11 (FBXO11) functions as the substrate recognition component of an 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

CATH:  1.20.1280.50|2.160.20.10
Gene Symbol:  FBXO11
Gene Ontology:  GO:0006511|GO:0019005|GO:0005515|GO:0008270|GO:0016567
PubMed:  31898225|11178263|27492310
SCOP:  4001927|4006721|3001746

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, ...
 787-855 3.85e-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: 150.35  E-value: 3.85e-43
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189526006 787 CLYKISSYTSYPMHDFYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGAGTLSNPCTLAG 855
Cdd:cd19676    1 CLYKISSYTSFPMHDFYRCLTCNTTDRNAICVNCIKKCHEGHDVEFIRHDRFFCDCGAGTLSNDCQLAG 69
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 616-771 2.00e-31

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: 120.20  E-value: 2.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  616 SGVQIRTGSNPKIRRNKIWGGQNGGILVYNSGLGFIEDNEIFDNAMAGVWIKTDSNPTLRRNKIHDGRDGGICIFNGGRG 695
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189526006  696 LLEENDIFRNAQAGVLISTNSHPVLRKNRIFDGFAAGIEIT-NHATATLEGNQIFNNRFGGLFLASGV-NVTMKDNKI 771
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEdSSNNVTISNNTVTNNKGAGILIVGGSsNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 478-633 9.14e-29

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: 112.89  E-value: 9.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  478 AGVWITSNSDPTIRGNAIFNGNQGGVYIFGDGRGLIEGNDIYGNALAGIQIRTNSCPIVRHNKIHDGQHGGIYVHEKGQG 557
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189526006  558 VIEENEVYSNTLAGVWVTTGSTPVLRRNRIHSGKQVGVYFYDNGHGV-LEDNDIYNHMYSGVQI-RTGSNPKIRRNKI 633
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIvGGSSNNTVENNTF 158
F-box_FBXO11 cd22091
F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called ...
 108-152 1.98e-24

F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called FBX11, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1), is the substrate-recognition component of an 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. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


:

Pssm-ID: 438863  Cd Length: 45  Bit Score: 96.34  E-value: 1.98e-24
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 189526006 108 QEKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRLY 152
Cdd:cd22091    1 QEELPDEVLLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWKRLY 45
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 386-541 7.01e-24

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: 98.63  E-value: 7.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  386 AGIWVKNHGNPIIRRNHIHHGRDVGVFTFDHGMGYFESCNIHRNRIAGFEVKAYANPTVVRCEIHHGQTGGIYVHEKGRG 465
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189526006  466 QFIENKIYANNFAGVWITSNSDPTIRGNAIFNGNQGGVYIF-GDGRGLIEGNDIYGNALAGIQIRTNSC-PIVRHNKI 541
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEdSSNNVTISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 283-449 5.73e-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: 73.21  E-value: 5.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  283 VFMEGSEDAYVGYMTIrfnpddksaqHHNAHHCLEITVNCSPNIDHCVIRSTCtvGSAVCVSGqGAGPTIKHCNISDCEN 362
Cdd:pfam13229   3 ILLNGSSNATIKNNTI----------SNNGGYGIYLRGSSNATIENNTITNNG--GDGIEISG-SSNNTISNNTISNNGG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  363 VGLYITDHAQGIYEDNEISNNALAGIWVKNHGNPIIRRNHIHHGRDVGVFTFDHGMG-YFESCNIHRNRIAGFEV-KAYA 440
Cdd:pfam13229  70 GGIALRGSSNNLIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNvTISNNTVTNNKGAGILIvGGSS 149


                  ....*....
gi 189526006  441 NPTVVRCEI 449
Cdd:pfam13229 150 NNTVENNTF 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, ...
 787-855 3.85e-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: 150.35  E-value: 3.85e-43
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189526006 787 CLYKISSYTSYPMHDFYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGAGTLSNPCTLAG 855
Cdd:cd19676    1 CLYKISSYTSFPMHDFYRCLTCNTTDRNAICVNCIKKCHEGHDVEFIRHDRFFCDCGAGTLSNDCQLAG 69
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 616-771 2.00e-31

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: 120.20  E-value: 2.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  616 SGVQIRTGSNPKIRRNKIWGGQNGGILVYNSGLGFIEDNEIFDNAMAGVWIKTDSNPTLRRNKIHDGRDGGICIFNGGRG 695
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189526006  696 LLEENDIFRNAQAGVLISTNSHPVLRKNRIFDGFAAGIEIT-NHATATLEGNQIFNNRFGGLFLASGV-NVTMKDNKI 771
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEdSSNNVTISNNTVTNNKGAGILIVGGSsNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 478-633 9.14e-29

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: 112.89  E-value: 9.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  478 AGVWITSNSDPTIRGNAIFNGNQGGVYIFGDGRGLIEGNDIYGNALAGIQIRTNSCPIVRHNKIHDGQHGGIYVHEKGQG 557
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189526006  558 VIEENEVYSNTLAGVWVTTGSTPVLRRNRIHSGKQVGVYFYDNGHGV-LEDNDIYNHMYSGVQI-RTGSNPKIRRNKI 633
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIvGGSSNNTVENNTF 158
F-box_FBXO11 cd22091
F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called ...
 108-152 1.98e-24

F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called FBX11, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1), is the substrate-recognition component of an 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. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438863  Cd Length: 45  Bit Score: 96.34  E-value: 1.98e-24
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 189526006 108 QEKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRLY 152
Cdd:cd22091    1 QEELPDEVLLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWKRLY 45
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 386-541 7.01e-24

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: 98.63  E-value: 7.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  386 AGIWVKNHGNPIIRRNHIHHGRDVGVFTFDHGMGYFESCNIHRNRIAGFEVKAYANPTVVRCEIHHGQTGGIYVHEKGRG 465
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189526006  466 QFIENKIYANNFAGVWITSNSDPTIRGNAIFNGNQGGVYIF-GDGRGLIEGNDIYGNALAGIQIRTNSC-PIVRHNKI 541
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEdSSNNVTISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 489-779 1.05e-20

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: 94.60  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 489 TIRGnaifngnQGGVYIFGDGRG---LIEGNDIygnALAGIQIRtNScpivrhNKIHDGQHGGIYVHEKGQGVIEENEVy 565
Cdd:COG3420   55 TLIG-------EGGAVIDGGGKGtviTITADNV---TVRGLTIT-GS------GDSLTDDDAGIYVRGADNAVIENNRI- 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 566 SNTLAGVWVTTGSTPVLRRNRIHSGKQV------GVYFYDNGHGVLEDNDIYNHmYSGVQIRTGSNPKIRRNKIWGGQNG 639
Cdd:COG3420  117 ENNLFGIYLEGSDNNVIRNNTISGNRDLradrgnGIHLWNSPGNVIEGNTISGG-RDGIYLEFSDNNVIRNNTIRNLRYG 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 640 gILVYNSGLGFIEDNEIFDNAmAGVWIKTDSNPTLRRNKIHDGRDGGICIFNGGRGLLEENDIFRNAQagvlistnshpv 719
Cdd:COG3420  196 -IHYMYSNDNLVEGNTFRDNG-AGIALMYSKGNTVRGNTILGNSGYGILLKESSDSVIEGNTISGNGK------------ 261

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 720 lrknrifdgfaaGIEITNHATATLEGNQIFNNRFGGLFLASGVNVTMKDNKIMNNQDAIE 779
Cdd:COG3420  262 ------------GIFIYNSNRNTIRGNLFAGNGIGIHLTAGSEGNRIYGNNFIGNRTQVK 309
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 109-152 1.49e-17

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 76.75  E-value: 1.49e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 189526006  109 EKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRLY 152
Cdd:pfam12937   2 SSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 480-706 5.38e-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: 83.43  E-value: 5.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 480 VWITSnSDPTIRGNAIFN------GNQGGVYIFGDGRGLIEGNDIYGNaLAGIQIRTNSCPIVRHNKIHDGQHG------ 547
Cdd:COG3420   73 ITITA-DNVTVRGLTITGsgdsltDDDAGIYVRGADNAVIENNRIENN-LFGIYLEGSDNNVIRNNTISGNRDLradrgn 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 548 GIYVHEKGQGVIEENEVYSNTlAGVWVTTGSTPVLRRNRIHSGKqVGVYFYDNGHGVLEDNDIYNHmYSGVQIRTGSNPK 627
Cdd:COG3420  151 GIHLWNSPGNVIEGNTISGGR-DGIYLEFSDNNVIRNNTIRNLR-YGIHYMYSNDNLVEGNTFRDN-GAGIALMYSKGNT 227

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189526006 628 IRRNKIWGGQNGGILVYNSGLGFIEDNEIFDNAmAGVWIKTDSNPTLRRNKIHDGrDGGICIfnggRGLLEENDIFRNA 706
Cdd:COG3420  228 VRGNTILGNSGYGILLKESSDSVIEGNTISGNG-KGIFIYNSNRNTIRGNLFAGN-GIGIHL----TAGSEGNRIYGNN 300
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 283-449 5.73e-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: 73.21  E-value: 5.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  283 VFMEGSEDAYVGYMTIrfnpddksaqHHNAHHCLEITVNCSPNIDHCVIRSTCtvGSAVCVSGqGAGPTIKHCNISDCEN 362
Cdd:pfam13229   3 ILLNGSSNATIKNNTI----------SNNGGYGIYLRGSSNATIENNTITNNG--GDGIEISG-SSNNTISNNTISNNGG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  363 VGLYITDHAQGIYEDNEISNNALAGIWVKNHGNPIIRRNHIHHGRDVGVFTFDHGMG-YFESCNIHRNRIAGFEV-KAYA 440
Cdd:pfam13229  70 GGIALRGSSNNLIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNvTISNNTVTNNKGAGILIvGGSS 149


                  ....*....
gi 189526006  441 NPTVVRCEI 449
Cdd:pfam13229 150 NNTVENNTF 158
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 337-571 1.65e-12

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: 69.56  E-value: 1.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 337 VGSAVcVSGQGAGP---------TIKHCNISdceNVGLYITDHAQGIY---------EDNEISNNaLAGIWVKNHGNPII 398
Cdd:COG3420   59 EGGAV-IDGGGKGTvititadnvTVRGLTIT---GSGDSLTDDDAGIYvrgadnaviENNRIENN-LFGIYLEGSDNNVI 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 399 RRNHIHHGRDVGVftfDHGMG-YFESCN---IHRNRIA----GFEVKAYANPTVVRCEIHHGQTGgIYVHEKGRGQFIEN 470
Cdd:COG3420  134 RNNTISGNRDLRA---DRGNGiHLWNSPgnvIEGNTISggrdGIYLEFSDNNVIRNNTIRNLRYG-IHYMYSNDNLVEGN 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 471 KIYaNNFAGVWITSNSDPTIRGNAIFNGNQGGVYIFGDGRGLIEGNDIYGNALaGIQIRTNSCPIVRHNKIHDGQHgGIY 550
Cdd:COG3420  210 TFR-DNGAGIALMYSKGNTVRGNTILGNSGYGILLKESSDSVIEGNTISGNGK-GIFIYNSNRNTIRGNLFAGNGI-GIH 286

                        250       260
                 ....*....|....*....|.
gi 189526006 551 VHekgqGVIEENEVYSNTLAG 571
Cdd:COG3420  287 LT----AGSEGNRIYGNNFIG 303
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 802-843 4.22e-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: 56.68  E-value: 4.22e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 189526006   802 FYRCHTCNTTDRNAICVNC-IKKCHQGHDVEFIRHDR-FFCDCG 843
Cdd:smart00396  13 IYRCKTCGLDPTCVLCSDCfRPSCHKGHDVSLKTSRGsGICDCG 56
zf-UBR pfam02207
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ...
 802-843 3.98e-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: 53.45  E-value: 3.98e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 189526006  802 FYRCHTCNTTDRNAICVNCIKKC-HQGHDVEFIRHDR-FFCDCG 843
Cdd:pfam02207  11 VYRCLTCSLDPTCVICYSCFINCdHEGHDYELFTSRGgGCCDCG 54
FBOX smart00256
A Receptor for Ubiquitination Targets;
111-151 1.01e-07

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 48.59  E-value: 1.01e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 189526006   111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRL 151
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41
CASH smart00722
Domain present in carbohydrate binding proteins and sugar hydrolses;
417-506 1.12e-05

Domain present in carbohydrate binding proteins and sugar hydrolses;


Pssm-ID: 214788  Cd Length: 153  Bit Score: 46.35  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006   417 GMGYFESCNIHRNRIAGFEVKAYANPTVVRCEIHHGqtGGIYVHEKGRGQFIENKIYANNFA---GVWITSNSDPTIRGN 493
Cdd:smart00722  63 GIYVSASGDPVIQNDGTGKNLIIDNVTFNGTEINSG--AGIVVTAGSEGLFIGNRIIGNYVAtgdGNYLSDSSGGDLIGN 140

                           90
                   ....*....|...
gi 189526006   494 AIFNGNQGGVYIF 506
Cdd:smart00722 141 RIYDNNRDGIAVV 153
CASH smart00722
Domain present in carbohydrate binding proteins and sugar hydrolses;
566-690 8.53e-05

Domain present in carbohydrate binding proteins and sugar hydrolses;


Pssm-ID: 214788  Cd Length: 153  Bit Score: 43.65  E-value: 8.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006   566 SNTLAGVWVTTGSTPVLRRNRIHS--GKQVGVYFYD-----NGHGVLEDNDIYNHMYSGVQIRTGSNPKIRRNKIWGGqn 638
Cdd:smart00722  21 DIGGSGGAVIDMGSGRGSNITINSndVRVDGVTIGGdgnavTGIYVSASGDPVIQNDGTGKNLIIDNVTFNGTEINSG-- 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 189526006   639 GGILVYNSGLGFIEDNEIFDNAMA---GVWIKTDSNPTLRRNKIHDGRDGGICIF 690
Cdd:smart00722  99 AGIVVTAGSEGLFIGNRIIGNYVAtgdGNYLSDSSGGDLIGNRIYDNNRDGIAVV 153
para_beta_helix TIGR03804
parallel beta-helix repeat (two copies); This model represents a tandem pair of an ...
 479-521 2.15e-03

parallel beta-helix repeat (two copies); This model represents a tandem pair of an approximately 22-amino acid (each) repeat homologous to the beta-strand repeats that stack in a right-handed parallel beta-helix in the periplasmic C-5 mannuronan epimerase, AlgA, of Pseudomonas aeruginosa. A homology domain consisting of a longer tandem array of these repeats is described in the SMART database as CASH (SM00722), and is found in many carbohydrate-binding proteins and sugar hydrolases. A single repeat is represented by SM00710. This TIGRFAMs model represents a flavor of the parallel beta-helix-forming repeat based on prokaryotic sequences only in its seed alignment, although it also finds many eukaryotic sequences.


Pssm-ID: 274795 [Multi-domain]  Cd Length: 44  Bit Score: 36.72  E-value: 2.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 189526006  479 GVWITSNSDPTIRGNaIFNGNQGGVYIFGDGRGLIEGNDIYGN 521
Cdd:TIGR03804   1 GIYLESSSNNTLSNN-TASNNSYGIYLYDSSNNTLSNNTASNN 42
 
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, ...
 787-855 3.85e-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: 150.35  E-value: 3.85e-43
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189526006 787 CLYKISSYTSYPMHDFYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGAGTLSNPCTLAG 855
Cdd:cd19676    1 CLYKISSYTSFPMHDFYRCLTCNTTDRNAICVNCIKKCHEGHDVEFIRHDRFFCDCGAGTLSNDCQLAG 69
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 616-771 2.00e-31

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: 120.20  E-value: 2.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  616 SGVQIRTGSNPKIRRNKIWGGQNGGILVYNSGLGFIEDNEIFDNAMAGVWIKTDSNPTLRRNKIHDGRDGGICIFNGGRG 695
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189526006  696 LLEENDIFRNAQAGVLISTNSHPVLRKNRIFDGFAAGIEIT-NHATATLEGNQIFNNRFGGLFLASGV-NVTMKDNKI 771
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEdSSNNVTISNNTVTNNKGAGILIVGGSsNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 478-633 9.14e-29

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: 112.89  E-value: 9.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  478 AGVWITSNSDPTIRGNAIFNGNQGGVYIFGDGRGLIEGNDIYGNALAGIQIRTNSCPIVRHNKIHDGQHGGIYVHEKGQG 557
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189526006  558 VIEENEVYSNTLAGVWVTTGSTPVLRRNRIHSGKQVGVYFYDNGHGV-LEDNDIYNHMYSGVQI-RTGSNPKIRRNKI 633
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIvGGSSNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 432-587 9.59e-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: 107.11  E-value: 9.59e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  432 AGFEVKAYANPTVVRCEIHHGQTGGIYVHEKGRGQFIENKIYANNFAGVWITSNSDPTIRGNAIFNGNQGGVYIFGDGRG 511
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189526006  512 LIEGNDIYGNALAGIQIRTNSCPIVRHNKIHDGQHGGIYVHEKGQGV-IEENEVYSNTLAGVWVTTGSTPV-LRRNRI 587
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIVGGSSNNtVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 524-679 1.02e-26

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: 106.72  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  524 AGIQIRTNSCPIVRHNKIHDGQHGGIYVHEKGQGVIEENEVYSNTLAGVWVTTGSTPVLRRNRIHSGKQVGVYFYDNGHG 603
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189526006  604 VLEDNDIYNHMYSGVQIRTGSNPKIRRNKIWGGQNGGILVYNSGLGF-IEDNEIFDNAMAGVWI-KTDSNPTLRRNKI 679
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIvGGSSNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 570-717 3.43e-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: 102.49  E-value: 3.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  570 AGVWVTTGSTPVLRRNRIHSGKQVGVYFYDNGHGVLEDNDIYNHMYSGVQIRTGSNPKIRRNKIWGGQNGGILVYNSGLG 649
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189526006  650 FIEDNEIFDNAMAGVWIKTDSNPTLRRNKIHDGRDGGICIFNGGRGL-LEENDIFRNAQAGVLISTNSH 717
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIVGGSS 149
F-box_FBXO11 cd22091
F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called ...
 108-152 1.98e-24

F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called FBX11, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1), is the substrate-recognition component of an 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. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438863  Cd Length: 45  Bit Score: 96.34  E-value: 1.98e-24
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 189526006 108 QEKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRLY 152
Cdd:cd22091    1 QEELPDEVLLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWKRLY 45
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 386-541 7.01e-24

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: 98.63  E-value: 7.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  386 AGIWVKNHGNPIIRRNHIHHGRDVGVFTFDHGMGYFESCNIHRNRIAGFEVKAYANPTVVRCEIHHGQTGGIYVHEKGRG 465
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189526006  466 QFIENKIYANNFAGVWITSNSDPTIRGNAIFNGNQGGVYIF-GDGRGLIEGNDIYGNALAGIQIRTNSC-PIVRHNKI 541
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEdSSNNVTISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 339-495 1.51e-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: 97.86  E-value: 1.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  339 SAVCVSGQGaGPTIKHCNISDCENVGLYITDHAQGIYEDNEISNNALAGIWVKNHGNPIIRRNHIHHGRDVGVFTFDHGM 418
Cdd:pfam13229   1 SGILLNGSS-NATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSN 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189526006  419 GYFESCNIHRNRIAGFEVKAYANPTVVRCEIHHGQTGGIYV-HEKGRGQFIENKIYANNFAGVWITSNSD-PTIRGNAI 495
Cdd:pfam13229  80 NLIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIeDSSNNVTISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
UBR-box_UBR4_5_6_7 cd19671
UBR-box found in UBR4, UBR5, UBR6/FBOX11, UBR7 and similar proteins; This family includes UBR4 ...
 790-853 3.19e-21

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: 87.90  E-value: 3.19e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189526006 790 KISSYTSYPMHDFYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGAGTlSNPCTL 853
Cdd:cd19671    3 FEKTGRKYIKQPWYHCYTCGLIDGLGVCEACARKCHKGHDLVYIGYSNFYCDCGSSG-PGKCKC 65
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 489-779 1.05e-20

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: 94.60  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 489 TIRGnaifngnQGGVYIFGDGRG---LIEGNDIygnALAGIQIRtNScpivrhNKIHDGQHGGIYVHEKGQGVIEENEVy 565
Cdd:COG3420   55 TLIG-------EGGAVIDGGGKGtviTITADNV---TVRGLTIT-GS------GDSLTDDDAGIYVRGADNAVIENNRI- 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 566 SNTLAGVWVTTGSTPVLRRNRIHSGKQV------GVYFYDNGHGVLEDNDIYNHmYSGVQIRTGSNPKIRRNKIWGGQNG 639
Cdd:COG3420  117 ENNLFGIYLEGSDNNVIRNNTISGNRDLradrgnGIHLWNSPGNVIEGNTISGG-RDGIYLEFSDNNVIRNNTIRNLRYG 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 640 gILVYNSGLGFIEDNEIFDNAmAGVWIKTDSNPTLRRNKIHDGRDGGICIFNGGRGLLEENDIFRNAQagvlistnshpv 719
Cdd:COG3420  196 -IHYMYSNDNLVEGNTFRDNG-AGIALMYSKGNTVRGNTILGNSGYGILLKESSDSVIEGNTISGNGK------------ 261

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 720 lrknrifdgfaaGIEITNHATATLEGNQIFNNRFGGLFLASGVNVTMKDNKIMNNQDAIE 779
Cdd:COG3420  262 ------------GIFIYNSNRNTIRGNLFAGNGIGIHLTAGSEGNRIYGNNFIGNRTQVK 309
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 594-748 1.26e-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: 89.39  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  594 GVYFYDNGHGVLEDNDIYNHMYSGVQIRTGSNPKIRRNKIWGGQNGGILVYNSGLGFIEDNEIFDNAMAGVWIKTDSNPT 673
Cdd:pfam13229   2 GILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNNL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189526006  674 LRRNKIHDGRDGGICIFNGGRGLLEENDIFRNAQAGVLISTNSHPV-LRKNRIFDGFAAGIEITNHAT-ATLEGNQI 748
Cdd:pfam13229  82 IENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 109-152 1.49e-17

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 76.75  E-value: 1.49e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 189526006  109 EKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRLY 152
Cdd:pfam12937   2 SSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 480-706 5.38e-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: 83.43  E-value: 5.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 480 VWITSnSDPTIRGNAIFN------GNQGGVYIFGDGRGLIEGNDIYGNaLAGIQIRTNSCPIVRHNKIHDGQHG------ 547
Cdd:COG3420   73 ITITA-DNVTVRGLTITGsgdsltDDDAGIYVRGADNAVIENNRIENN-LFGIYLEGSDNNVIRNNTISGNRDLradrgn 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 548 GIYVHEKGQGVIEENEVYSNTlAGVWVTTGSTPVLRRNRIHSGKqVGVYFYDNGHGVLEDNDIYNHmYSGVQIRTGSNPK 627
Cdd:COG3420  151 GIHLWNSPGNVIEGNTISGGR-DGIYLEFSDNNVIRNNTIRNLR-YGIHYMYSNDNLVEGNTFRDN-GAGIALMYSKGNT 227

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189526006 628 IRRNKIWGGQNGGILVYNSGLGFIEDNEIFDNAmAGVWIKTDSNPTLRRNKIHDGrDGGICIfnggRGLLEENDIFRNA 706
Cdd:COG3420  228 VRGNTILGNSGYGILLKESSDSVIEGNTISGNG-KGIFIYNSNRNTIRGNLFAGN-GIGIHL----TAGSEGNRIYGNN 300
UBR-box cd19669
UBR-box found in UBR family of E3 ubiquitin ligases (UBR1-7) and similar proteins; The UBR-box ...
 802-849 9.88e-17

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: 75.24  E-value: 9.88e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 189526006 802 FYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGAGTLSN 849
Cdd:cd19669   12 MYHCLTCSLDDNSGICEECAKKCHEGHDVVYIGSGSGFCDCGDSSAKS 59
UBR-box_UBR4_like cd19674
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3. ...
 785-851 3.44e-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: 70.84  E-value: 3.44e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189526006 785 GQCLYKISSyTSYPMHDFYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGAGTLSNPC 851
Cdd:cd19674    1 NVCTFASTG-KNYARQHWYECYTCFLNGNEGVCEVCARVCHKGHDLVYSKTSSFFCDCGAGGGPSKC 66
UBR-box_BIG_like cd19681
UBR-box found in Arabidopsis thaliana auxin transport protein BIG and similar proteins; BIG ...
 787-851 3.58e-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: 70.90  E-value: 3.58e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189526006 787 CLYkISSYTSYPMHDFYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGAGTLS--NPC 851
Cdd:cd19681    3 CTY-VSSGSNFMEQHWYFCYTCGLVDSKGCCSVCAKVCHRGHDVVYSRYSRFFCDCGAGGAKrgRPC 68
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 283-449 5.73e-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: 73.21  E-value: 5.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  283 VFMEGSEDAYVGYMTIrfnpddksaqHHNAHHCLEITVNCSPNIDHCVIRSTCtvGSAVCVSGqGAGPTIKHCNISDCEN 362
Cdd:pfam13229   3 ILLNGSSNATIKNNTI----------SNNGGYGIYLRGSSNATIENNTITNNG--GDGIEISG-SSNNTISNNTISNNGG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  363 VGLYITDHAQGIYEDNEISNNALAGIWVKNHGNPIIRRNHIHHGRDVGVFTFDHGMG-YFESCNIHRNRIAGFEV-KAYA 440
Cdd:pfam13229  70 GGIALRGSSNNLIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNvTISNNTVTNNKGAGILIvGGSS 149


                  ....*....
gi 189526006  441 NPTVVRCEI 449
Cdd:pfam13229 150 NNTVENNTF 158
UBR-box_UBR4 cd19680
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3. ...
 803-844 6.81e-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: 67.10  E-value: 6.81e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 189526006 803 YRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGA 844
Cdd:cd19680   18 YHCHTCKMVDGVGVCSVCAKVCHKDHDLSYAKYGSFFCDCGA 59
F-box_FBXO15 cd22093
F-box domain found in F-box only protein 15 (FBXO15) and similar proteins; FBXO15, also called ...
 109-153 2.10e-13

F-box domain found in F-box only protein 15 (FBXO15) and similar proteins; FBXO15, also called FBX15, has a novel dual molecular function by controlling transcriptional repression and being part of SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligases, which is essential for stress response, gliotoxin production and virulence in the opportunistic human pathogen Aspergillus fumigatus. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438865  Cd Length: 46  Bit Score: 64.97  E-value: 2.10e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 189526006 109 EKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRLYM 153
Cdd:cd22093    2 ERLPSEILLKILSYLDASSLLCISCVNKLFYQLANDNALWRKLYS 46
F-box_unchar cd22139
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 ...
 111-151 3.47e-13

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 (FBXO3); This subfamily corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 3 (FBXO3). FBXO3, also called FBX3, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex, that mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. It also promotes ubiquitylation and transcriptional activity of AIRE (autoimmune regulator). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438911  Cd Length: 45  Bit Score: 64.57  E-value: 3.47e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRL 151
Cdd:cd22139    4 LPDELWLHIFSFLSPKDLCQVALVCRRFNRLASDESLWKQI 44
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 337-571 1.65e-12

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: 69.56  E-value: 1.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 337 VGSAVcVSGQGAGP---------TIKHCNISdceNVGLYITDHAQGIY---------EDNEISNNaLAGIWVKNHGNPII 398
Cdd:COG3420   59 EGGAV-IDGGGKGTvititadnvTVRGLTIT---GSGDSLTDDDAGIYvrgadnaviENNRIENN-LFGIYLEGSDNNVI 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 399 RRNHIHHGRDVGVftfDHGMG-YFESCN---IHRNRIA----GFEVKAYANPTVVRCEIHHGQTGgIYVHEKGRGQFIEN 470
Cdd:COG3420  134 RNNTISGNRDLRA---DRGNGiHLWNSPgnvIEGNTISggrdGIYLEFSDNNVIRNNTIRNLRYG-IHYMYSNDNLVEGN 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006 471 KIYaNNFAGVWITSNSDPTIRGNAIFNGNQGGVYIFGDGRGLIEGNDIYGNALaGIQIRTNSCPIVRHNKIHDGQHgGIY 550
Cdd:COG3420  210 TFR-DNGAGIALMYSKGNTVRGNTILGNSGYGILLKESSDSVIEGNTISGNGK-GIFIYNSNRNTIRGNLFAGNGI-GIH 286

                        250       260
                 ....*....|....*....|.
gi 189526006 551 VHekgqGVIEENEVYSNTLAG 571
Cdd:COG3420  287 LT----AGSEGNRIYGNNFIG 303
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 548-705 2.51e-12

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: 67.06  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  548 GIYVHEKGQGVIEENEVySNTLAGVWVTTGSTPVLRRNRIHSGKQvGVYFYDNGHGVLEDNDIYNhMYSGVQIRTGSNPK 627
Cdd:pfam05048  21 GIQLWNTEGNVISNNDI-INSRDGIYLDASNNNTITGNRISNLRY-GIHLMNSNDNTISDNVFSG-NTAGIALMSSSNNT 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189526006  628 IRRNKIWGGQNGGILVYNSGLGFIEDNEIFDNAMAGVWIKTDSNPTLRRNKIhDGRDGGICIFNGGrgllEENDIFRN 705
Cdd:pfam05048  98 LENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRI-TSNGIGIHFLAGS----NGNTIYNN 170
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 486-681 5.10e-12

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: 66.29  E-value: 5.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  486 SDPTIRGNAIFNGNQG----GVYIFGDGRGLIEGNDIYGNAlAGIQIRTNSCPIVRHNKIHDGqHGGIYVHEKGQGVIEE 561
Cdd:pfam05048   1 VNNAISGDTIGIYNGLsrgnGIQLWNTEGNVISNNDIINSR-DGIYLDASNNNTITGNRISNL-RYGIHLMNSNDNTISD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  562 NEVYSNTlagvwvttgstpvlrrnrihsgkqVGVYFYDNGHGVLEDNDIYNHMYSGVQIRTGSNPKIRRNKIWGGQNGGI 641
Cdd:pfam05048  79 NVFSGNT------------------------AGIALMSSSNNTLENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGI 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 189526006  642 LVYNSGLGFIEDNEIFDNAmAGVWIKTDSNptlrRNKIHD 681
Cdd:pfam05048 135 FLYNSDYNTITGNRITSNG-IGIHFLAGSN----GNTIYN 169
F-box_FBXL5 cd22118
F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also ...
 110-148 1.55e-11

F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also called F-box and leucine-rich repeat protein 5, F-box protein FBL4/FBL5, or p45SKP2-like protein, is the substrate-recognition component of an SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438890  Cd Length: 41  Bit Score: 59.66  E-value: 1.55e-11
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 189526006 110 KLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILW 148
Cdd:cd22118    3 SLPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 593-775 2.22e-11

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: 64.36  E-value: 2.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  593 VGVYFYDNGHGVLEDNDIYNhmysGVQIRTGSNPKIRRNKIWGGQNGGILVYNSGLGfIEDNEIFDNaMAGVWIKTDSNP 672
Cdd:pfam05048   1 VNNAISGDTIGIYNGLSRGN----GIQLWNTEGNVISNNDIINSRDGIYLDASNNNT-ITGNRISNL-RYGIHLMNSNDN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  673 TLRRNKIHDGRDGgICIFNGGRGLLEENDIFRNAQAGVLISTNSHPVLRKNRIFDGFAAGIEITNHATATLEGNQIFNNR 752
Cdd:pfam05048  75 TISDNVFSGNTAG-IALMSSSNNTLENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRITSNG 153

                         170       180
                  ....*....|....*....|...
gi 189526006  753 FGGLFLASGVNVTMKDNKIMNNQ 775
Cdd:pfam05048 154 IGIHFLAGSNGNTIYNNYFINNS 176
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 109-143 4.06e-11

F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.


Pssm-ID: 438852  Cd Length: 35  Bit Score: 58.22  E-value: 4.06e-11
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 189526006 109 EKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELAN 143
Cdd:cd09917    1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35
F-box_FBXL7 cd22120
F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also ...
 109-148 1.13e-10

F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also called F-box and leucine-rich repeat protein 7, or F-box protein FBL6/FBL7, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of Aurora kinase A (AURKA) during mitosis, causing mitotic arrest. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438892  Cd Length: 44  Bit Score: 57.39  E-value: 1.13e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 189526006 109 EKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILW 148
Cdd:cd22120    2 DRLPDDVILQIFSHLPTNQLCRCARVCRRWYNLAWDPRLW 41
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 802-843 4.22e-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: 56.68  E-value: 4.22e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 189526006   802 FYRCHTCNTTDRNAICVNC-IKKCHQGHDVEFIRHDR-FFCDCG 843
Cdd:smart00396  13 IYRCKTCGLDPTCVLCSDCfRPSCHKGHDVSLKTSRGsGICDCG 56
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 449-635 4.80e-10

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: 60.51  E-value: 4.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  449 IHHGQTGGIYVHEKGRGQF-IENKIYANNFAGVWITSNSDPTIRGNAIFNGNqGGVYIFGDGRGLIEGNDIYGNalagiq 527
Cdd:pfam05048  12 IYNGLSRGNGIQLWNTEGNvISNNDIINSRDGIYLDASNNNTITGNRISNLR-YGIHLMNSNDNTISDNVFSGN------ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  528 irtnscpivrhnkihdgqHGGIYVHEKGQGVIEENEVYSNTLAGVWVTTGSTPVLRRNRIHSGKQVGVYFYDNGHGVLED 607
Cdd:pfam05048  85 ------------------TAGIALMSSSNNTLENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITG 146

                         170       180
                  ....*....|....*....|....*...
gi 189526006  608 NDIYNHmYSGVQIRTGSNpkirRNKIWG 635
Cdd:pfam05048 147 NRITSN-GIGIHFLAGSN----GNTIYN 169
F-box_FBXW5 cd22132
F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, ...
 111-152 8.10e-10

F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, also called F-box and WD-40 domain-containing protein 5, is the substrate-recognition component of both SCF (SKP1-CUL1-F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438904 [Multi-domain]  Cd Length: 46  Bit Score: 54.93  E-value: 8.10e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRLY 152
Cdd:cd22132    4 LPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLWKELF 45
F-box_SpPof1-like cd22147
F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar ...
 111-151 8.25e-10

F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar proteins; SpPof1, also called F-box/WD repeat-containing protein pof1, probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It is required for the inactivation of zip1 via ubiquitination. This subfamily also includes Saccharomyces cerevisiae methionine-requiring protein 30 (ScMET30, also called E3 ubiquitin ligase complex SCF(Met30) subunit MET30), Aspergillus niger sulfur controller B (AnSCONB, also called sulfur metabolite repression control protein B) and Neurospora crassa sulfur controller 2 (NcSCON2, also called sulfur metabolite repression control protein 2). ScMET30 acts as a transcriptional inhibitor that negatively regulates the expression of sulfur amino acid biosynthesis genes. It controls cell cycle function (being required for the G1/S transition and M-phase but not the S-phase), sulfur metabolism, and methionine biosynthesis as part of the E3 ubiquitin ligase complex SCF(Met30). AnSCONB and NcSCON2 are components of the SCF (sconB/scon-2) E3 ubiquitin ligase complexes involved in the regulation of sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438918  Cd Length: 46  Bit Score: 55.01  E-value: 8.25e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRL 151
Cdd:cd22147    5 LPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELWKRM 45
F-box_FBXL4 cd22117
F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also ...
 109-152 8.40e-10

F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also called F-box and leucine-rich repeat protein 4, or F-box protein FBL4/FBL5, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It serves as a clock output molecule that regulates sleep through promotion of rhythmic degradation of the GABA(A) receptor. Biallelic pathogenic variants in FBXL4 are associated with an encephalopathic mtDNA maintenance defect syndrome that is a multi-system disease characterized by lactic acidemia, developmental delay, and hypotonia. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438889  Cd Length: 47  Bit Score: 54.94  E-value: 8.40e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 189526006 109 EKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRLY 152
Cdd:cd22117    2 DLLPYELIQLILSYLDLPSLCRLSQTCKLFRKHCYDPLLWKELN 45
F-box_JHDM cd22122
F-box domain found in the JmjC domain-containing histone demethylation protein (JHDM) family; ...
 111-150 9.24e-10

F-box domain found in the JmjC domain-containing histone demethylation protein (JHDM) family; The JHDM family includes F-box/LRR-repeat proteins FBXL10, FBXL11 and FBXL19. FBXL10 is also called lysine-specific demethylase 2B (KDM2B), CXXC-type zinc finger protein 2 (CXXC2), F-box and leucine-rich repeat protein 10 (FBL10), JmjC domain-containing histone demethylation protein 1B (JHDM1B), Jumonji domain-containing EMSY-interactor methyltransferase motif protein, protein JEMMA, protein-containing CXXC domain 2, [Histone-H3]-lysine-36 demethylase 1B, or NDY1. It is a histone demethylase that catalyzes the demethylation of H3K4me3 and H3K36me2, thereby playing a central role in the histone code. It preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation. FBXL10 may also serve as the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. FBXL11, also called KDM2A, CXXC8, F-box and leucine-rich repeat protein 11, F-box protein FBL7, F-box protein Lilina, JmjC domain-containing histone demethylation protein 1A (JHDM1A), or [Histone-H3]-lysine-36 demethylase 1A, is a histone H3 lysine 36 (H3K36) demethylase that regulates epithelial mesenchymal transition (EMT) and the metastasis of ovarian cancer. It plays an essential role in embryonic development and homeostasis by regulating cell proliferation and survival. FBXL11 may also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. It associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. It is required to sustain centromeric integrity and genomic stability, particularly during mitosis. FBXL19, also called F-box and leucine-rich repeat protein 19, is the substrate-recognition component of an SCF-type E3 ubiquitin ligase complex. It acts as a CpG island-binding protein in mouse embryonic stem (ES) cells and has been shown to associate with the CDK-Mediator complex. It promotes H2Bub1 at the promoters of CpG island-containing genes by interacting with RNF20. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438894  Cd Length: 43  Bit Score: 54.59  E-value: 9.24e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKR 150
Cdd:cd22122    4 LPREVWLPVFQYLSPKDLCVCMRVCKTWNRWCCDPSLWKR 43
F-box_DmSKP2-like cd22149
F-box domain found in Drosophila melanogaster S-phase kinase-associated protein 2 (DmSKP2) and ...
 109-150 9.33e-10

F-box domain found in Drosophila melanogaster S-phase kinase-associated protein 2 (DmSKP2) and similar proteins; DmSKP2 is a Drosophila F-box protein that regulates cell proliferation by targeting Dacapo (Dap) for ubiquitination and proteasome-mediated degradation. It plays a role in maintaining diploidy of mitotic cells during development. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438920  Cd Length: 43  Bit Score: 54.69  E-value: 9.33e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 189526006 109 EKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKR 150
Cdd:cd22149    2 ERLSDEIILSIFKWLPKKTLARCARVCRRWKRLCFDESLWRR 43
F-box_FBXO3 cd22084
F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called ...
 111-151 1.32e-09

F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called FBX3, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. It also promotes ubiquitylation and transcriptional activity of AIRE (autoimmune regulator). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438856  Cd Length: 49  Bit Score: 54.19  E-value: 1.32e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRL 151
Cdd:cd22084    4 LPSDPLLNILSFLDYRDLISCSQVCRRLNQLCSHDPLWKRL 44
F-box_AtGID2-like cd22151
F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, ...
 110-152 1.87e-09

F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, also called protein SLEEPY 1, is an essential component of the SCF-type E3 ligase complex, SCF(GID2), a complex that positively regulates the gibberellin signaling pathway. Upon gibberellin treatment, the SCF(GID2) complex mediates the ubiquitination and subsequent degradation of DELLA proteins (GAI, RGA and RGL2), some repressors of the gibberellin pathway, leading to the activation of the pathway. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438922  Cd Length: 44  Bit Score: 53.86  E-value: 1.87e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 189526006 110 KLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRLY 152
Cdd:cd22151    2 KLPDDLLQEIFKRLDPKSLARAACVCRRWRAAARSESLWENAC 44
F-box_FBXL12 cd22123
F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also ...
 109-149 3.09e-09

F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also called F-box and leucine-rich repeat protein 12, or F-box protein FBL12, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It mediates the polyubiquitination and proteasomal degradation of calcium/calmodulin dependent protein kinase I (CAMK1) leading to disruption of cyclin D1/CDK4 complex assembly, which results in G1 cell cycle arrest in lung epithelia. It regulates T-cell differentiation in a cell-autonomous manner. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438895  Cd Length: 42  Bit Score: 53.12  E-value: 3.09e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 189526006 109 EKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWK 149
Cdd:cd22123    2 DQLPENVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLWR 42
zf-UBR pfam02207
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ...
 802-843 3.98e-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: 53.45  E-value: 3.98e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 189526006  802 FYRCHTCNTTDRNAICVNCIKKC-HQGHDVEFIRHDR-FFCDCG 843
Cdd:pfam02207  11 VYRCLTCSLDPTCVICYSCFINCdHEGHDYELFTSRGgGCCDCG 54
F-box_unchar cd22138
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 ...
 110-151 6.79e-09

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 (FBXO13); The family corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 13 (FBXO13). FBXO13, also called FBX13, or F-box/LRR-repeat protein 17 (FBL17), or F-box and leucine-rich repeat protein 17 (FBXL17), is the substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438910  Cd Length: 45  Bit Score: 52.33  E-value: 6.79e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 189526006 110 KLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRL 151
Cdd:cd22138    3 SLPVECQLKIFSFLSEVDKCLAATVCRSWSELIRSPRLWRTV 44
UBR-box_UBR7 cd19677
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR7 and similar proteins; UBR7 (EC 2.3. ...
 803-853 9.69e-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: 52.70  E-value: 9.69e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189526006 803 YRCHTCN---TTDRNAICVNCIKKCHQGHDVEFIRHDRFF-CDCG-AGTLSNPCTL 853
Cdd:cd19677   14 YACLTCTpagADQPAGICLACSLSCHEGHELEELYTKRNFrCDCGnSKFPSNPCKL 69
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 640-778 1.35e-08

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: 55.89  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  640 GILVYNSGLGFIEDNEIfDNAMAGVWIKTDSNPTLRRNKIHDGRdGGICIFNGGRGLLEENDIFRNaQAGVLISTNSHPV 719
Cdd:pfam05048  21 GIQLWNTEGNVISNNDI-INSRDGIYLDASNNNTITGNRISNLR-YGIHLMNSNDNTISDNVFSGN-TAGIALMSSSNNT 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 189526006  720 LRKNRIFDGFAAGIEITNHATATLEGNQIFNNRFGGLFLASGVNVTMKDNKIMNNQDAI 778
Cdd:pfam05048  98 LENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRITSNGIGI 156
F-box_FBXL1 cd22114
F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also ...
 110-148 1.52e-08

F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also called S-phase kinase-associated protein 2, cyclin-A/CDK2-associated protein p45, F-box protein Skp2, or p45skp2, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. It specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438886  Cd Length: 41  Bit Score: 51.26  E-value: 1.52e-08
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 189526006 110 KLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILW 148
Cdd:cd22114    3 SLPDELLLGIFSCLCLPDLLKVSQVCKRWYRLASDESLW 41
F-box_FBXO8 cd22088
F-box domain found in F-box only protein 8 (FBXO8) and similar proteins; FBXO8, also called ...
 109-151 2.17e-08

F-box domain found in F-box only protein 8 (FBXO8) and similar proteins; FBXO8, also called FBX8, or F-box/SEC7 protein FBS, is a novel component of F-box proteins which contains an F-box domain and a putative Sec7 domain. FBX8 was originally identified as a Skp1-binding protein. It is involved in the ubiquitin-dependent proteolytic pathway. It acts as a metastasis suppressor that functions through mTOR signaling pathway. FBXO8 may promote the activation of ADP-ribosylation factor (ARF) through replacement of GDP with GTP. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438860  Cd Length: 46  Bit Score: 50.79  E-value: 2.17e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 189526006 109 EKLPDEVVLKIFSYLLEQDLCQAACVckrFSELANDPILWKRL 151
Cdd:cd22088    5 EELPPELSLTVLSHLNATDLCLASCV---WQDLANDELLWQGL 44
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 109-150 2.28e-08

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 425796  Cd Length: 43  Bit Score: 50.62  E-value: 2.28e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 189526006  109 EKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKR 150
Cdd:pfam00646   2 LDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWKK 43
F-box_FBXO9 cd22089
F-box domain found in F-box only protein 9 (FBXO9) and similar proteins; FBXO9, also called ...
 110-153 2.45e-08

F-box domain found in F-box only protein 9 (FBXO9) and similar proteins; FBXO9, also called FBX9, cross-immune reaction antigen 1, renal carcinoma antigen NY-REN-57, or VCIA1, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. FBXO9 acts as an E3 ubiquitin ligase that regulates the stability and activity of peroxisome proliferator-activated receptor gamma (PPARgamma) through ubiquitination. It is also required for adipocyte differentiation. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438861  Cd Length: 53  Bit Score: 51.07  E-value: 2.45e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 189526006 110 KLPDEVVLKIFSYLLEQD----LCQAACVCKRFSELANDPILWKRLYM 153
Cdd:cd22089    5 ALPSEILLYILRWVVSDLdlrsLEQLSLVCRKFYLLARDPSIWRLACE 52
F-box_FBXW4 cd20090
F-box domain found in F-box/WD repeat-containing protein 4 (FBXW4) and similar proteins; FBXW4, ...
 111-151 6.22e-08

F-box domain found in F-box/WD repeat-containing protein 4 (FBXW4) and similar proteins; FBXW4, also called dactylin, or F-box and WD-40 domain-containing protein 4, probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It is likely to be involved in key signaling pathways crucial for normal limb development. It may participate in Wnt signaling and act as a novel tumor suppressor that regulates important cellular processes. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438853  Cd Length: 47  Bit Score: 49.52  E-value: 6.22e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRL 151
Cdd:cd20090    5 LPDDLLFLIFSYLDPASLGRLSQVCRRLYRLISRDAVWRRI 45
F-box_FBXO36 cd22106
F-box domain found in F-box only protein 36 (FBXO36) and similar proteins; FBXO36, also called ...
 109-153 6.74e-08

F-box domain found in F-box only protein 36 (FBXO36) and similar proteins; FBXO36, also called FBX36, likely functions as the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438878  Cd Length: 46  Bit Score: 49.50  E-value: 6.74e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 189526006 109 EKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRLYM 153
Cdd:cd22106    2 VRLPDKLLLYIISYLDLEDIARLSQTSKRFKKLCNSDELWEKIYM 46
F-box_FBXO13 cd22092
F-box domain found in F-box only protein 13 (FBXO13) and similar proteins; FBXO13, also called ...
 108-151 8.96e-08

F-box domain found in F-box only protein 13 (FBXO13) and similar proteins; FBXO13, also called FBX13, F-box/LRR-repeat protein 17 (FBL17), or F-box and leucine-rich repeat protein 17 (FBXL17), is the substrate-recognition component of SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438864  Cd Length: 49  Bit Score: 49.34  E-value: 8.96e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 189526006 108 QEKLPDEVVLKIFSYLLEQDLCQAAC-VCKRFSELANDPILWKRL 151
Cdd:cd22092    2 INQLPDSILLKIFSYLSLQERCLSASlVCKYWRDLCLDSQFWKQI 46
UBR-box_UBR1_2_3 cd19670
UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), E3-alpha-3 ...
 802-843 8.99e-08

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: 49.67  E-value: 8.99e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 189526006 802 FYRCHTCNTTDRNAICVNC-IKKCHQGHDVEFIR-HDRFFCDCG 843
Cdd:cd19670   11 YYRCLDCSLDPSSCICEECfLNGNHEGHNYSLRTsSGGGVCDCG 54
F-box_FBXW12 cd22137
F-box domain found in F-box/WD repeat-containing protein 12 (FBXW12) and similar proteins; ...
 111-151 9.77e-08

F-box domain found in F-box/WD repeat-containing protein 12 (FBXW12) and similar proteins; FBXW12, also called F-box and WD-40 domain-containing protein 12, or F-box only protein 35 (FBXO35), is the substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It functions as an epithelial growth suppressor. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438909  Cd Length: 44  Bit Score: 48.91  E-value: 9.77e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRL 151
Cdd:cd22137    3 LPDLPMLRIFSFLDAFSLLQAAQVNKQWNKVADSDYLWRNL 43
FBOX smart00256
A Receptor for Ubiquitination Targets;
111-151 1.01e-07

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 48.59  E-value: 1.01e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 189526006   111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRL 151
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41
F-box_FBXO4 cd22085
F-box domain found in F-box only protein 4 (FBXO4) and similar proteins; FBXO4, also called ...
 110-151 3.37e-07

F-box domain found in F-box only protein 4 (FBXO4) and similar proteins; FBXO4, also called FBX4, is a specific substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that catalyzes the ubiquitination and subsequent degradation of cyclin D1 and Trx1. It recognizes TERF1 and promotes its ubiquitination together with UBE2D1. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438857  Cd Length: 50  Bit Score: 47.79  E-value: 3.37e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 189526006 110 KLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRL 151
Cdd:cd22085    5 HLPIDLQLYILSFLSPHDLCQLGLTSHYWHTLVRDPLLWRYF 46
F-box_FBXL2-like cd22115
F-box domain found in F-box/LRR-repeat protein 2 (FBXL2), F-box/LRR-repeat protein 20 (FBXL20) ...
 107-149 5.25e-07

F-box domain found in F-box/LRR-repeat protein 2 (FBXL2), F-box/LRR-repeat protein 20 (FBXL20) and similar proteins; The family includes FBXL2 and FBXL30. FBXL2, also called F-box and leucine-rich repeat protein 2, or F-box protein FBL2/FBL3, is a calcium-activated substrate-recognition component of an SCF (SKP1-cullin-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Unlike many F-box proteins, FBXL2 does not seem to target phosphodegron within its substrates but rather calmodulin-binding motifs and is thereby antagonized by calmodulin. FBXL20, also called SCRAPPER, F-box and leucine-rich repeat protein 20, or F-box/LRR-repeat protein 2-like, is a component of a synapse-localized SCF-type E3 ubiquitin ligase which regulates neural transmission. It is widely expressed in the central nervous system and plays an important role in the ubiquitin-dependent degradation of regulating synaptic membrane exocytosis 1 (RIM1), which is an important factor in the release of synaptic vesicles. It may also mediate the ubiquitin degradation of E-cadherin resulting in an increased invasive ability of malignant cells. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438887  Cd Length: 45  Bit Score: 47.03  E-value: 5.25e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 189526006 107 LQEKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWK 149
Cdd:cd22115    3 INKKLPKELLLRIFSFLDVVTLCRCAQVSKYWNVLALDGSNWQ 45
F-box_FBXO41 cd22109
F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called ...
 108-152 7.20e-07

F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called FBX41, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a novel central nervous system (CNS)-specific F-box protein that localizes to the centrosome and the cytoplasm of neurons and promotes neuronal migration. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438881  Cd Length: 47  Bit Score: 46.55  E-value: 7.20e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 189526006 108 QEKLPDEVVLK-IFSYLLEQDLCQAACVCKRFSELANDPILWKRLY 152
Cdd:cd22109    2 LESLRRRDALFcVFSYLDTKSLLRCAEVCREWRDVSRHPALWQRVC 47
F-box_FBXW8 cd22134
F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, ...
 111-151 1.06e-06

F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, also called F-box and WD-40 domain-containing protein 8, or F-box only protein 29 (FBXO29), is the substrate-recognition component of a Cul7-RING ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as GORASP1, IRS1, MAP4K1/HPK1. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438906  Cd Length: 48  Bit Score: 46.22  E-value: 1.06e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRL 151
Cdd:cd22134    7 LPRELALKIFQYLSVTDLCRCAQVSKSWKSLAEDELLWYRI 47
F-box_FBXO48 cd22113
F-box domain found in F-box only protein 48 (FBXO48) and similar proteins; FBXO48, also called ...
 109-149 1.71e-06

F-box domain found in F-box only protein 48 (FBXO48) and similar proteins; FBXO48, also called FBX48, is one of the paralogs of the F-box only protein 7 (FBXO7), which is the causative gene for PARK15 (also known as Parkinsonian-pyramidal disease, PPD). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438885  Cd Length: 46  Bit Score: 45.38  E-value: 1.71e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 189526006 109 EKLPDEVVLKIFSYLLEQDLCQAACVCKRFSEL-ANDPILWK 149
Cdd:cd22113    2 ELLPPEMSLRIFSQLDVQSLCRASQTCKTWNDLiENSDYLWR 43
F-box_FBXO18 cd22095
F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called ...
 109-151 2.08e-06

F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called FBX18, or F-box DNA helicase 1 (FBH1), is a 3'-5' DNA helicase and the substrate-recognition component of the SCF(FBH1) E3 ubiquitin ligase complex that plays a key role in response to stalled/damaged replication forks. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438867  Cd Length: 48  Bit Score: 45.34  E-value: 2.08e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 189526006 109 EKLPDEVVLKIFSYLLEQDLCQAAC-VCKRFSELANDP--ILWKRL 151
Cdd:cd22095    3 QQLPEELLRNIFAFLPAEDLYQNISlVCRHWRDIVSDPlfIPWKKL 48
F-box_FBXO21 cd22096
F-box domain found in F-box only protein 21 (FBXO21) and similar proteins; FBXO21, also called ...
 111-152 2.34e-06

F-box domain found in F-box only protein 21 (FBXO21) and similar proteins; FBXO21, also called FBX21, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It facilitates Lys29-linkage and activation of ASK1 (apoptosis signal-regulating kinase 1) and promotes type I interferon production upon viral infection. It also polyubiquitylates EP300-interacting inhibitor of differentiation 1 (EID1) and is required for the efficient degradation of EID1 in both cycling and quiescent cells. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438868  Cd Length: 48  Bit Score: 44.99  E-value: 2.34e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 189526006 111 LPDEVVLKIFSYLL--EQDLCQAACVCKRFSELANDPILWKRLY 152
Cdd:cd22096    4 LPDELLEYILCSDNldHHDIIRLSCTCRRLREVCQSGKVWREKF 47
F-box_DdgacFF-like cd22148
F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) ...
 111-150 4.17e-06

F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) and similar proteins; DdgacFF, also called GTPase activating factor for raC protein FF, is a Rho GTPase-activating protein involved in the signal transduction pathway. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438919  Cd Length: 44  Bit Score: 44.19  E-value: 4.17e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKR 150
Cdd:cd22148    5 LPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELWKA 44
F-box_FBXL6 cd22119
F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also ...
 109-149 6.51e-06

F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also called F-box and leucine-rich repeat protein 6, or F-box protein FBL6 (FBL6A), is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438891  Cd Length: 47  Bit Score: 43.78  E-value: 6.51e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 189526006 109 EKLPDEVVLKIFSYLLEQD-----LCQAACVCKRFSELANDPILWK 149
Cdd:cd22119    2 QRLPPEILVKIFQFAVATEgavplLCRLSRVCRLWREVALDPSLWT 47
F-box_FBXO10 cd22090
F-box domain found in F-box only protein 10 (FBXO10) and similar proteins; FBXO10, also called ...
 111-153 6.93e-06

F-box domain found in F-box only protein 10 (FBXO10) and similar proteins; FBXO10, also called FBX10, or PRMT11, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The SCF(FBXO10) complex mediates ubiquitination and degradation of BCL2, an anti-apoptotic protein, thereby playing a role in apoptosis by controlling the stability of BCL2. It also associates with the receptor for advanced glycation end products (RAGE) to mediate its ubiquitination and degradation. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438862  Cd Length: 50  Bit Score: 43.88  E-value: 6.93e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSEL--ANDPILWKRLYM 153
Cdd:cd22090    5 LPLELWRLILAYLPVRDLCRCCQVCRAWYELilSLDSTRWKQLYL 49
F-box_FBXO7 cd22087
F-box domain found in F-box only protein 7 (FBXO7) and similar proteins; FBXO7, also called ...
 111-152 1.01e-05

F-box domain found in F-box only protein 7 (FBXO7) and similar proteins; FBXO7, also called FBX7, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It recognizes BIRC2 and DLGAP5. FBXO7 plays a role downstream of PINK1 in the clearance of damaged mitochondria via selective autophagy (mitophagy) by targeting PRKN to dysfunctional depolarized mitochondria. It promotes MFN1 ubiquitination. FBXO7 acts as a cell cycle regulator by enhancing cyclin D/cyclin-dependent kinase 6 (Cdk6) complex formation and stabilizing levels of p27, a cyclin-dependent kinase inhibitor. Mutations in the FBXO7 (PARK15) gene have been implicated in a juvenile form of parkinsonism called parkinsonian pyramidal syndrome (PPS), characterized by Parkinsonian symptoms and pyramidal tract signs. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438859  Cd Length: 45  Bit Score: 43.44  E-value: 1.01e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRLY 152
Cdd:cd22087    4 LPPEIKLRILSLLDVRSLLSLSQVCRDLNSATNDQLLWRFLL 45
CASH smart00722
Domain present in carbohydrate binding proteins and sugar hydrolses;
417-506 1.12e-05

Domain present in carbohydrate binding proteins and sugar hydrolses;


Pssm-ID: 214788  Cd Length: 153  Bit Score: 46.35  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006   417 GMGYFESCNIHRNRIAGFEVKAYANPTVVRCEIHHGqtGGIYVHEKGRGQFIENKIYANNFA---GVWITSNSDPTIRGN 493
Cdd:smart00722  63 GIYVSASGDPVIQNDGTGKNLIIDNVTFNGTEINSG--AGIVVTAGSEGLFIGNRIIGNYVAtgdGNYLSDSSGGDLIGN 140

                           90
                   ....*....|...
gi 189526006   494 AIFNGNQGGVYIF 506
Cdd:smart00722 141 RIYDNNRDGIAVV 153
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 354-528 1.19e-05

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: 47.41  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  354 HCNISDCENVGLYITDHAQGIY----EDNEISNNAL----AGIWVKNHGNPIIRRNHIHHGRdVGVFTFDHGMGYFESCN 425
Cdd:pfam05048   2 NNAISGDTIGIYNGLSRGNGIQlwntEGNVISNNDIinsrDGIYLDASNNNTITGNRISNLR-YGIHLMNSNDNTISDNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006  426 IHRNRiAGFEVKAYANPTVVRCEIHHGQTGGIYVHEKGRGQFIENKIYANNFAGVWITSNSDPTIRGNAIfNGNQGGVYI 505
Cdd:pfam05048  81 FSGNT-AGIALMSSSNNTLENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRI-TSNGIGIHF 158

                         170       180
                  ....*....|....*....|...
gi 189526006  506 FGDGrgliEGNDIYGNALAGIQI 528
Cdd:pfam05048 159 LAGS----NGNTIYNNYFINNSE 177
F-box_AtSKIP3-like cd22162
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 3 (AtSKIP3) and similar ...
 109-152 1.45e-05

F-box domain found in Arabidopsis thaliana SKP1-interacting partner 3 (AtSKIP3) and similar proteins; AtSKIP3, also called F-box protein SKIP3, F-box protein PP2-B9, or protein PHLOEM PROTEIN 2-LIKE B9, is a component of SCF (SKP1-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It interacts with SKP1A/ASK1. This subfamily also includes many other Arabidopsis thaliana protein PHLOEM PROTEIN 2-LIKE proteins. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438933  Cd Length: 46  Bit Score: 42.95  E-value: 1.45e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 189526006 109 EKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRLY 152
Cdd:cd22162    2 EDLPEDCIALILSFTSPRDVCRLSAVSKTFRSAAESDVVWERFL 45
UBR-box_UBR3 cd19673
UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3. ...
 802-843 1.49e-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: 43.72  E-value: 1.49e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 189526006 802 FYRCHTCNTTDRNAICVNCIKKC-HQGHDVEFIRHDRF-FCDCG 843
Cdd:cd19673   14 AYRCRTCGLDPTCVICADCFQAGdHEGHDYSMYRSSAGgCCDCG 57
F-box_FBXO42 cd22110
F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called ...
 109-144 1.64e-05

F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called FBX42, or just one F-box and Kelch domain-containing protein (JFK), is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It specifically recognizes p53/TP53, promoting its ubiquitination and degradation. FBXO42 is also involved in the ubiquitin-proteasome system that may play a role in the pathogenesis of Parkinson's disease (PD). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438882  Cd Length: 38  Bit Score: 42.32  E-value: 1.64e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 189526006 109 EKLPDEVVLKIFSYL-LEQDLCQAACVCKRFSELAND 144
Cdd:cd22110    2 NDLPEEILEYILSYLsPYGDLKSAALVCKRWHRIIKG 38
F-box_AtSKIP31-like cd22166
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 31 (AtSKIP31) and similar ...
 110-152 3.71e-05

F-box domain found in Arabidopsis thaliana SKP1-interacting partner 31 (AtSKIP31) and similar proteins; AtSKIP31, also called F-box protein SKIP31, is a component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It interacts with SKP1A/ASK1 and SPK1B/ASK2. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438937  Cd Length: 46  Bit Score: 41.67  E-value: 3.71e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 189526006 110 KLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRLY 152
Cdd:cd22166    3 KLPPELFRHILKFLSPEDLTSCATVCRFLRGAASDESLWRRLY 45
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
 109-151 5.89e-05

F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called FBX33, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It exerts similar functions as F-box involved in polyQ pathogenesis (FipoQ) in modulating the ubiquitination and solubility of expanded SCA3-polyQ proteins. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438876  Cd Length: 48  Bit Score: 41.09  E-value: 5.89e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 189526006 109 EKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRL 151
Cdd:cd22104    2 ANLPSVVLVHIFSYLPPRDRLRASSTCRRWREALFHPSLWRSL 44
F-box_FBXO31 cd22102
F-box domain found in F-box only protein 31 (FBXO31) and similar proteins; FBXO31, also called ...
 111-150 6.12e-05

F-box domain found in F-box only protein 31 (FBXO31) and similar proteins; FBXO31, also called FBX31, or FBXO14, is a component of an SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in G1 arrest following DNA damage. It specifically recognizes phosphorylated cyclin-D1 (CCND1), promoting its ubiquitination and degradation by the proteasome, resulting in G1 arrest. FBXO31 may act as a tumor suppressor. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438874  Cd Length: 48  Bit Score: 41.26  E-value: 6.12e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKR 150
Cdd:cd22102    4 LPPELLVEIFSSLPGTDLPSLAQVCKKFREILNTDTIWQR 43
CASH smart00722
Domain present in carbohydrate binding proteins and sugar hydrolses;
566-690 8.53e-05

Domain present in carbohydrate binding proteins and sugar hydrolses;


Pssm-ID: 214788  Cd Length: 153  Bit Score: 43.65  E-value: 8.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189526006   566 SNTLAGVWVTTGSTPVLRRNRIHS--GKQVGVYFYD-----NGHGVLEDNDIYNHMYSGVQIRTGSNPKIRRNKIWGGqn 638
Cdd:smart00722  21 DIGGSGGAVIDMGSGRGSNITINSndVRVDGVTIGGdgnavTGIYVSASGDPVIQNDGTGKNLIIDNVTFNGTEINSG-- 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 189526006   639 GGILVYNSGLGFIEDNEIFDNAMA---GVWIKTDSNPTLRRNKIHDGRDGGICIF 690
Cdd:smart00722  99 AGIVVTAGSEGLFIGNRIIGNYVAtgdGNYLSDSSGGDLIGNRIYDNNRDGIAVV 153
F-box_FBXO16-like cd22094
F-box domain found in F-box only protein 16 (FBXO16), epithelial cell-transforming sequence 2 ...
 110-149 8.57e-05

F-box domain found in F-box only protein 16 (FBXO16), epithelial cell-transforming sequence 2 oncogene-like (ECT2L) and similar proteins; This family includes FBXO16 and ECT2L. FBXO16, also called FBX16, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It functions as a tumor suppressor by attenuating nuclear beta-catenin function. ECT2L, also called lung-specific F-box and DH domain-containing protein, or putative guanine nucleotide exchange factor LFDH, may act as a guanine nucleotide exchange factor (GEF). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438866  Cd Length: 49  Bit Score: 40.89  E-value: 8.57e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 189526006 110 KLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWK 149
Cdd:cd22094    5 VLPRFLSLYIFSYLDPRSLCRAAQVSWYWKFLCESDELWL 44
F-box_ScMDM30-like cd22143
F-box domain found in Saccharomyces cerevisiae mitochondrial distribution and morphology ...
 109-151 9.66e-05

F-box domain found in Saccharomyces cerevisiae mitochondrial distribution and morphology protein 30 (ScMDM30) and similar proteins; ScMDM30 is an F-box protein required for maintenance of fusion-competent mitochondria in yeast. It is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. ScMDM30 recognizes FZO1 and regulates the amount of FZO1. It acts as a regulatory factor for the mitochondrial fusion machinery and is required for mitochondrial DNA maintenance. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438915  Cd Length: 44  Bit Score: 40.29  E-value: 9.66e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 189526006 109 EKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANdPILWKRL 151
Cdd:cd22143    3 DSLPDEILSIIFSHLPQSDLYNLLFVNKHFYSLAL-PELWRSI 44
F-box_FBXW7 cd22133
F-box domain found in F-box/WD repeat-containing protein 7 (FBXW7) and similar proteins; FBXW7, ...
 111-149 1.59e-04

F-box domain found in F-box/WD repeat-containing protein 7 (FBXW7) and similar proteins; FBXW7, also called Archipelago homolog (Ago), F-box and WD-40 domain-containing protein 7, F-box protein FBX30, SEL-10, or Cdc4, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as cyclin-E (CCNE1 or CCNE2), DISC1, JUN, MYC, NOTCH1 released notch intracellular domain (NICD), NOTCH2, MCL1, and probably PSEN1. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438905  Cd Length: 59  Bit Score: 40.49  E-value: 1.59e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWK 149
Cdd:cd22133   21 LPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 59
F-box_FBXO6-like cd22168
F-box domain found in F-box only proteins FBXO6, FBXO44 and similar proteins; This subfamily ...
 111-152 2.02e-04

F-box domain found in F-box only proteins FBXO6, FBXO44 and similar proteins; This subfamily includes FBXO6 and FBXO44. FBXO6, also called FBX6, F-box protein that recognizes sugar chains 2 (FBS2), or F-box/G-domain protein 2 (FBG2), is a substrate-recognition component of SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. It is involved in the endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins, by recognizing and binding sugar chains on unfolded glycoproteins that are retro-translocated into the cytosol and promoting their ubiquitination and subsequent degradation. FBXO6 can recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex-type oligosaccharides. It also recognizes sulfated glycans. FBXO6 is involved in DNA damage response by specifically recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting its ubiquitination and degradation. FBXO44, also called FBXO6A, FBX44, or F-box/G-domain protein 3 (FBG3), is a substrate-recognition component of an SCF-type E3 ubiquitin ligase complex. It interacts with SKP1 and CUL1. FBXO44 mediates BRCA1 ubiquitination and degradation. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438939 [Multi-domain]  Cd Length: 82  Bit Score: 40.73  E-value: 2.02e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 189526006 111 LPDEVVLKIFSYLLEQDL---CQAacVCKRFSELANDPILWKRLY 152
Cdd:cd22168    7 LPEDVLLEILSLVPARDLilsCRL--VCSRWRDLVDLPTLWKRKC 49
F-box_AtSKIP22-like cd22165
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 22 (AtSKIP22) and similar ...
 111-152 2.57e-04

F-box domain found in Arabidopsis thaliana SKP1-interacting partner 22 (AtSKIP22) and similar proteins; AtSKIP22, also called F-box protein SKIP22, is a component of SCF (SKP1/ASK-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It interacts with SKP1A/ASK1 and SPK1B/ASK2. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438936  Cd Length: 46  Bit Score: 39.18  E-value: 2.57e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRLY 152
Cdd:cd22165    5 LPTELKLKILELLPGVDLARMACVCSELRFLASNDDLWKQKF 46
F-box_FBXL21 cd22179
F-box domain found in F-box/LRR-repeat protein 21 (FBXL21) and similar proteins; FBXL21, also ...
 111-148 3.12e-04

F-box domain found in F-box/LRR-repeat protein 21 (FBXL21) and similar proteins; FBXL21, also called F-box and leucine-rich repeat protein 21, F-box and leucine-rich repeat protein 3B (FBXL3B), or F-box/LRR-repeat protein 3B, is the substrate-recognition component of the SCF(FBXL21) E3 ubiquitin ligase complex that mainly acts in the cytosol and mediates ubiquitination of CRY proteins (CRY1 and CRY2), leading to CRY protein stabilization, and thus, is involved in circadian rhythm function. It regulates the oscillation of the circadian clock through ubiquitination and stabilization of cryptochromes. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438950  Cd Length: 43  Bit Score: 39.12  E-value: 3.12e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILW 148
Cdd:cd22179    6 LPHHVVLHIFQYLPLVDRARASSVCRRWNEVFHIPDLW 43
F-box_AtSKIP5-like cd22163
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 5 (AtSKIP5) and similar ...
 111-150 4.41e-04

F-box domain found in Arabidopsis thaliana SKP1-interacting partner 5 (AtSKIP5) and similar proteins; AtSKIP5, also called F-box protein SKIP5, is a component of SCF (SKP1-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It interacts with SKP1A/ASK1. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438934  Cd Length: 46  Bit Score: 38.87  E-value: 4.41e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 189526006 111 LPDEVVLKIFSYLLE-QDLCQAACVCKRFSELANDPILWKR 150
Cdd:cd22163    4 LDDDCLMHIFSFLTPlPDRFNAARVCKRWRALALDPRSWLR 44
F-box_ScCDC4-like cd22141
F-box domain found in Saccharomyces cerevisiae cell division control protein 4 (ScCDC4) and ...
 111-151 6.05e-04

F-box domain found in Saccharomyces cerevisiae cell division control protein 4 (ScCDC4) and similar proteins; ScCDC4 is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It is essential for initiation of DNA replication and separation of the spindle pole bodies to form the poles of the mitotic spindle. It also plays a role in bud development, fusion of zygotic nuclei after conjugation and various aspects of sporulation. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438913  Cd Length: 47  Bit Score: 38.31  E-value: 6.05e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRL 151
Cdd:cd22141    4 LPFEISLKIFNYLQFEDLLNSLGVSKKWNKIIRNTALWKKL 44
F-box_ScMFB1-like cd22146
F-box domain found in Saccharomyces cerevisiae mitochondrial F-box protein MFB1 (ScMFB1) and ...
 111-149 6.47e-04

F-box domain found in Saccharomyces cerevisiae mitochondrial F-box protein MFB1 (ScMFB1) and similar proteins; ScMFB1 is a novel mitochondria-associated F-box protein that functions to increase mitochondrial connectivity in yeast. ScMFB1 acts as a key component of a Skp1-Cdc53/Cullin-F-box protein (SCF) ubiquitin ligase complex machinery that regulates mitochondrial dynamics throughout the yeast's entire life cycle. It interacts with Skp1p in an F-box-dependent manner. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438917  Cd Length: 42  Bit Score: 38.00  E-value: 6.47e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWK 149
Cdd:cd22146    4 LPLEILFEILIYLDIPDILNLSKTCRFLYVLLNDEILWR 42
UBR-box_UBR5 cd19675
UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3. ...
 801-842 6.67e-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: 38.99  E-value: 6.67e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 189526006 801 DFYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHD-RFFCDC 842
Cdd:cd19675   22 DIFECRTCGLVGSLCCCTECARVCHKGHDCKLKRTSpTAYCDC 64
F-box_FBXW1B cd22183
F-box domain found in F-box/WD repeat-containing protein 1B (FBXW1B) and similar proteins; ...
 107-150 6.91e-04

F-box domain found in F-box/WD repeat-containing protein 1B (FBXW1B) and similar proteins; FBXW1B, also called F-box/WD repeat-containing protein 11 (FBXW11), F-box and WD repeats protein beta-TrCP2, or homologous to Slimb protein (HOS), is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as IFNAR1, CEP68 and CDC25A, as well as phosphorylated CTNNB1, NFKBIA, PER1 and PER2. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438954  Cd Length: 51  Bit Score: 38.35  E-value: 6.91e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 189526006 107 LQEKLPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKR 150
Cdd:cd22183    8 LPAKGLDHIAENILSYLDAESLCAAELVCKEWQRVISEGMLWKK 51
F-box_FBXO34-like cd22105
F-box domain found in F-box only protein 34 (FBXO34), F-box only protein 46 (FBXO46) and ...
 111-144 7.34e-04

F-box domain found in F-box only protein 34 (FBXO34), F-box only protein 46 (FBXO46) and similar proteins; This family includes FBXO34 (also called FBX34) and FBXO46 (also called FBX46), both of which are substrate-recognition components of SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. The SCF(FBOX46) complex mediates degradation of the tumor suppressor FBXO31 and thereby prevents premature cellular senescence. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438877  Cd Length: 47  Bit Score: 38.15  E-value: 7.34e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELAND 144
Cdd:cd22105    4 LPDHVLSKIFSHLPTRSLAALKCTCKDFKWLIEM 37
F-box_EMI cd22086
F-box domain found in the early mitotic inhibitor (EMI) family of F-box proteins; The EMI ...
 107-151 1.08e-03

F-box domain found in the early mitotic inhibitor (EMI) family of F-box proteins; The EMI family includes FBX5 (EMI1) and FBX43 (EMI2), which are anaphase-promoting complex/cyclosome (APC/C) inhibitors that bind APC/C-CCD20 (Cell division cycle protein 20) and/or APC/C-CDH1 (CDC20 homologue 1) complexes. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438858  Cd Length: 48  Bit Score: 37.48  E-value: 1.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 189526006 107 LQEKLPDEVVLKIFSYLLEQDLCQAACVCKRFSE-LANDPILWKRL 151
Cdd:cd22086    3 LHKRNCPHILSKILSYLSPEDLCRVSCVSKTWRQiCLSDPKANRRR 48
F-box_FBXL10 cd22180
F-box domain found in F-box/LRR-repeat protein 10 (FBXL10) and similar proteins; FBXL10 is ...
 111-150 1.80e-03

F-box domain found in F-box/LRR-repeat protein 10 (FBXL10) and similar proteins; FBXL10 is also called lysine-specific demethylase 2B (KDM2B), CXXC-type zinc finger protein 2 (CXXC2), F-box and leucine-rich repeat protein 10, F-box protein FBL10, JmjC domain-containing histone demethylation protein 1B (JHDM1B), Jumonji domain-containing EMSY-interactor methyltransferase motif protein, protein JEMMA, protein-containing CXXC domain 2, [Histone-H3]-lysine-36 demethylase 1B, or NDY1. It is a histone demethylase that catalyzes the demethylation of H3K4me3 and H3K36me2, thereby playing a central role in the histone code. It preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation. FBXL10 may also serve as the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438951  Cd Length: 45  Bit Score: 36.84  E-value: 1.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKR 150
Cdd:cd22180    6 MQREVWMAVFSYLSHRDLCVCMRVCRTWNRWCCDKRLWTR 45
F-box_FBXW1A cd22182
F-box domain found in F-box/WD repeat-containing protein 1A (FBXW1A) and similar proteins; ...
 113-151 1.96e-03

F-box domain found in F-box/WD repeat-containing protein 1A (FBXW1A) and similar proteins; FBXW1A, also called E3RSIkappaB, epididymis tissue protein Li 2a, F-box and WD repeats protein beta-TrCP, or pIkappaBalpha-E3 receptor subunit, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as CTNNB1, NFKBIA, NFKBIB and NFKBIE, as well as phosphorylated NFKB1, ATF4, CDC25A, DLG1, FBXO5, PER1, SMAD3, SMAD4, SNAI1 and probably NFKB2. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438953  Cd Length: 60  Bit Score: 37.35  E-value: 1.96e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 189526006 113 DEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKRL 151
Cdd:cd22182   16 DHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 54
para_beta_helix TIGR03804
parallel beta-helix repeat (two copies); This model represents a tandem pair of an ...
 479-521 2.15e-03

parallel beta-helix repeat (two copies); This model represents a tandem pair of an approximately 22-amino acid (each) repeat homologous to the beta-strand repeats that stack in a right-handed parallel beta-helix in the periplasmic C-5 mannuronan epimerase, AlgA, of Pseudomonas aeruginosa. A homology domain consisting of a longer tandem array of these repeats is described in the SMART database as CASH (SM00722), and is found in many carbohydrate-binding proteins and sugar hydrolases. A single repeat is represented by SM00710. This TIGRFAMs model represents a flavor of the parallel beta-helix-forming repeat based on prokaryotic sequences only in its seed alignment, although it also finds many eukaryotic sequences.


Pssm-ID: 274795 [Multi-domain]  Cd Length: 44  Bit Score: 36.72  E-value: 2.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 189526006  479 GVWITSNSDPTIRGNaIFNGNQGGVYIFGDGRGLIEGNDIYGN 521
Cdd:TIGR03804   1 GIYLESSSNNTLSNN-TASNNSYGIYLYDSSNNTLSNNTASNN 42
F-box_AtADO-like cd22154
F-box domain found in Arabidopsis thaliana Adagio proteins (AtADO1/2/3) and similar proteins; ...
 110-151 2.57e-03

F-box domain found in Arabidopsis thaliana Adagio proteins (AtADO1/2/3) and similar proteins; This subfamily contains Arabidopsis thaliana Adagio proteins, including AtADO1, AtADO2 and AtADO3. They are components of E3 ubiquitin ligase complexes that play central roles in blue light-dependent circadian cycles. They act as blue light photoreceptors, due to the presence of FMN, that mediate light-regulated protein degradation of critical clock components by targeting them to the proteasome complex. AtADO1, also called clock-associated PAS protein ZTL, F-box only protein 2b (FBX2b), flavin-binding kelch repeat F-box protein 1-like protein 2 (FKL2), FKF1-like protein 2, LOV kelch protein 1 (LKP1), or protein ZEITLUPE, is a novel clock-associated PAS protein from Arabidopsis. Its circadian phase-specific degradation is mediated by the proteasome. AtADO2, also called F-box only protein 2c (FBX2c), flavin-binding kelch repeat F-box protein 1-like protein 1 (FKL1), FKF1-like protein 1, or LOV kelch protein 2 (LKP2), functions close to the circadian clock oscillator. AtADO3, also called F-box only protein 2a (FBX2a), or flavin-binding kelch repeat F-box protein 1 (FKF1), is essential for photoperiodic-specific light signaling and mediates cyclic degradation of a repressor of CONSTANS in Arabidopsis. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438925  Cd Length: 47  Bit Score: 36.69  E-value: 2.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 189526006 110 KLPDEVV-LKIFSYLLEQDLCQAACVCKRFSELANDPILWKRL 151
Cdd:cd22154    4 QLSDEVLaQKILSRLTPRDVASVGSVCRRLYELTKNEDLWRMV 46
F-box_FBXO39 cd22108
F-box domain found in F-box only protein 39 (FBXO39) and similar proteins; FBXO39, also called ...
 111-149 2.76e-03

F-box domain found in F-box only protein 39 (FBXO39) and similar proteins; FBXO39, also called FBX39, likely functions as the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a cancer/testis antigen from colon cancer patients by serological analysis of recombinant cDNA expression libraries (SEREX). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438880  Cd Length: 44  Bit Score: 36.24  E-value: 2.76e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWK 149
Cdd:cd22108    4 LPDVCLRHVFRWLGDRDRSRAALVCKRWNQAMYSPALWR 42
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 111-148 2.85e-03

F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6, is a component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. It is also the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438896  Cd Length: 42  Bit Score: 36.16  E-value: 2.85e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILW 148
Cdd:cd22124    4 LPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLW 41
F-box_FBXW1 cd22130
F-box domain found in F-box/WD repeat-containing proteins, FBXW1A, FBXW1B and similar proteins; ...
 113-150 6.74e-03

F-box domain found in F-box/WD repeat-containing proteins, FBXW1A, FBXW1B and similar proteins; FBXW1A, also called E3RSIkappaB, epididymis tissue protein Li 2a, F-box and WD repeats protein beta-TrCP, or pIkappaBalpha-E3 receptor subunit, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as CTNNB1, NFKBIA, NFKBIB and NFKBIE, as well as phosphorylated NFKB1, ATF4, CDC25A, DLG1, FBXO5, PER1, SMAD3, SMAD4, SNAI1 and probably NFKB2. FBXW1B, also called F-box/WD repeat-containing protein 11 (FBXW11), F-box and WD repeats protein beta-TrCP2, or homologous to Slimb protein (HOS), is the substrate-recognition component of an SCF E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as IFNAR1, CEP68 and CDC25A, as well as phosphorylated CTNNB1, NFKBIA, PER1 and PER2. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438902  Cd Length: 51  Bit Score: 35.53  E-value: 6.74e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 189526006 113 DEVVLKIFSYLLEQDLCQAACVCKRFSELANDPILWKR 150
Cdd:cd22130   14 DHIAENILSYLDAKSLCAAELVCKEWYRVIADGMLWKK 51
F-box_FBXO1 cd22082
F-box domain found in F-box only protein 1 (FBXO1) and similar proteins; FBXO1, also called ...
 111-150 6.90e-03

F-box domain found in F-box only protein 1 (FBXO1) and similar proteins; FBXO1, also called FBX1, or cyclin-F, is a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of CP110 during G2 phase, thereby acting as an inhibitor of centrosome reduplication. It is the largest among all cyclins and oscillates in the cell cycle like other cyclins. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438854  Cd Length: 52  Bit Score: 35.30  E-value: 6.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 189526006 111 LPDEVVLKIFSYLLEQDLCQAACVCKRFSELA-NDPILWKR 150
Cdd:cd22082    5 LPEEVLLHILKGLPIKDLLNMRAVHSRFKDLIdSNPSLWAN 45
 
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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