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Conserved domains on  [gi|1972288612|ref|NP_001379860|]
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F-box protein dre-1 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UBR-box_UBR6_FBXO11 cd19676
UBR-box found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11 (also called UBR6, ...
 845-913 1.35e-38

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: 137.64  E-value: 1.35e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972288612 845 CLFKVSSNNSFPMHNFYRCTTCNTTERNAICTNCIRTCHRGHSVELVRFDRFFCDCGAGTLERHCHLQN 913
Cdd:cd19676     1 CLYKISSYTSFPMHDFYRCLTCNTTDRNAICVNCIKKCHEGHDVEFIRHDRFFCDCGAGTLSNDCQLAG 69
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 674-829 2.90e-30

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: 117.12  E-value: 2.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 674 SGVQIRTGSNPKITRNKIWGGQNGGVLVYNGGKGCLEDNEIFDNAMAGVWIKTDSEPTLRRNKIYDGRDGGVCIFNRGKG 753
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972288612 754 LLEDNEIFRNAQAGVLISTESNPTLRRNRVFDGKSAGIEITNG-ATATLEENQLFRNKYGGLCVATGVTPVQ-RGNRI 829
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSsNNVTISNNTVTNNKGAGILIVGGSSNNTvENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 490-645 1.67e-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: 109.42  E-value: 1.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 490 SGIEVKNSANPVVIRCEVHHGYTGGIYVHERGRGQFMENRIYANAYAGIWITSHSDPTIRKNEIFTGQQGGVYIFGEGRG 569
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972288612 570 LIEQNNIYGNALAGIQIRSQSDPIVRLNKIHDGLHGGIYV-HEKGRGLIEENEVYGNTLAGIWVTTGSS-PILRKNRI 645
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIeDSSNNVTISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 398-553 2.04e-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: 97.48  E-value: 2.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 398 AAVCVKKSAAPKFKYCTVLDCENVGIYITDNATGHYEHCEIARNTLAGVWVKNHANPYFRKCTIHSGKDVGVFTFEHGQG 477
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972288612 478 YFEKCNIHSNRISGIEVKNSANPVVIRCEVHHGYTGGIYV-HERGRGQFMENRIYANAYAGIWITSHSD-PTIRKNEI 553
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIeDSSNNVTISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 162-206 3.67e-13

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


:

Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 64.43  E-value: 3.67e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972288612 162 INRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKELY 206
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
 
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, ...
 845-913 1.35e-38

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: 137.64  E-value: 1.35e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972288612 845 CLFKVSSNNSFPMHNFYRCTTCNTTERNAICTNCIRTCHRGHSVELVRFDRFFCDCGAGTLERHCHLQN 913
Cdd:cd19676     1 CLYKISSYTSFPMHDFYRCLTCNTTDRNAICVNCIKKCHEGHDVEFIRHDRFFCDCGAGTLSNDCQLAG 69
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 674-829 2.90e-30

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: 117.12  E-value: 2.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 674 SGVQIRTGSNPKITRNKIWGGQNGGVLVYNGGKGCLEDNEIFDNAMAGVWIKTDSEPTLRRNKIYDGRDGGVCIFNRGKG 753
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972288612 754 LLEDNEIFRNAQAGVLISTESNPTLRRNRVFDGKSAGIEITNG-ATATLEENQLFRNKYGGLCVATGVTPVQ-RGNRI 829
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSsNNVTISNNTVTNNKGAGILIVGGSSNNTvENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 490-645 1.67e-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: 109.42  E-value: 1.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 490 SGIEVKNSANPVVIRCEVHHGYTGGIYVHERGRGQFMENRIYANAYAGIWITSHSDPTIRKNEIFTGQQGGVYIFGEGRG 569
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972288612 570 LIEQNNIYGNALAGIQIRSQSDPIVRLNKIHDGLHGGIYV-HEKGRGLIEENEVYGNTLAGIWVTTGSS-PILRKNRI 645
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIeDSSNNVTISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 582-737 3.45e-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: 105.57  E-value: 3.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 582 AGIQIRSQSDPIVRLNKIHDGLHGGIYVHEKGRGLIEENEVYGNTLAGIWVTTGSSPILRKNRIHSGKQVGVYFYDQGHG 661
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972288612 662 LLEENDIFNHLYSGVQIRTGSNPKITRNKIWGGQNGGVLVYNGGKGC-LEDNEIFDNAMAGVWI-KTDSEPTLRRNKI 737
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIvGGSSNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 398-553 2.04e-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: 97.48  E-value: 2.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 398 AAVCVKKSAAPKFKYCTVLDCENVGIYITDNATGHYEHCEIARNTLAGVWVKNHANPYFRKCTIHSGKDVGVFTFEHGQG 477
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972288612 478 YFEKCNIHSNRISGIEVKNSANPVVIRCEVHHGYTGGIYV-HERGRGQFMENRIYANAYAGIWITSHSD-PTIRKNEI 553
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIeDSSNNVTISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 538-764 1.53e-15

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: 79.19  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 538 IWITShSDPTIRKNEI------FTGQQGGVYIFGEGRGLIEQNNIYGNaLAGIQIRSQSDPIVRLNKIHD-----GLHG- 605
Cdd:COG3420    73 ITITA-DNVTVRGLTItgsgdsLTDDDAGIYVRGADNAVIENNRIENN-LFGIYLEGSDNNVIRNNTISGnrdlrADRGn 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 606 GIYVHEKGRGLIEENEVYGNTlAGIWVTTGSSPILRKNRIHSGKqVGVYFYDQGHGLLEENDIFNHlYSGVQIRTGSNPK 685
Cdd:COG3420   151 GIHLWNSPGNVIEGNTISGGR-DGIYLEFSDNNVIRNNTIRNLR-YGIHYMYSNDNLVEGNTFRDN-GAGIALMYSKGNT 227

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972288612 686 ITRNKIWGGQNGGVLVYNGGKGCLEDNEIFDNAmAGVWIKTDSEPTLRRNKIYDGrDGGVcifnRGKGLLEDNEIFRNA 764
Cdd:COG3420   228 VRGNTILGNSGYGILLKESSDSVIEGNTISGNG-KGIFIYNSNRNTIRGNLFAGN-GIGI----HLTAGSEGNRIYGNN 300
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 162-206 3.67e-13

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 64.43  E-value: 3.67e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972288612 162 INRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKELY 206
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
F-box_FBXO15 cd22093
F-box domain found in F-box only protein 15 (FBXO15) and similar proteins; FBXO15, also called ...
 162-206 1.47e-11

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: 59.96  E-value: 1.47e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972288612 162 INRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKELY 206
Cdd:cd22093     1 IERLPSEILLKILSYLDASSLLCISCVNKLFYQLANDNALWRKLY 45
FBOX smart00256
A Receptor for Ubiquitination Targets;
165-205 2.49e-10

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 56.29  E-value: 2.49e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1972288612  165 LPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKEL 205
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 626-812 9.53e-10

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: 61.47  E-value: 9.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 626 TLAGIWVT-TGSSpilrknriHSGKQVGVYFYDQGHGLLEENDIFNHLYsGVQIRTGSNPKITRNKIWGGQNG------G 698
Cdd:COG3420    81 TVRGLTITgSGDS--------LTDDDAGIYVRGADNAVIENNRIENNLF-GIYLEGSDNNVIRNNTISGNRDLradrgnG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 699 VLVYNGGKGCLEDNEIFDNAmAGVWIKTDSEPTLRRNKIYDGRDGgVCIFNRGKGLLEDNEIFRNAqAGVLISTESNPTL 778
Cdd:COG3420   152 IHLWNSPGNVIEGNTISGGR-DGIYLEFSDNNVIRNNTIRNLRYG-IHYMYSNDNLVEGNTFRDNG-AGIALMYSKGNTV 228

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1972288612 779 RRNRVFDGKSAGIEITNGATATLEENQLFRNKYG 812
Cdd:COG3420   229 RGNTILGNSGYGILLKESSDSVIEGNTISGNGKG 262
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 860-901 3.41e-09

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: 53.98  E-value: 3.41e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1972288612  860 FYRCTTCNTTERNAICTNC-IRTCHRGHSVEL-VRFDRFFCDCG 901
Cdd:smart00396  13 IYRCKTCGLDPTCVLCSDCfRPSCHKGHDVSLkTSRGSGICDCG 56
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 416-646 5.83e-09

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: 58.77  E-value: 5.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 416 LDCENVGIYItDNATGHY-EHCEIaRNTLAGVWVKNHANPYFRKCTIHSGKDVGVftfEHGQG-YFEKCN---IHSNRIS 490
Cdd:COG3420    94 LTDDDAGIYV-RGADNAViENNRI-ENNLFGIYLEGSDNNVIRNNTISGNRDLRA---DRGNGiHLWNSPgnvIEGNTIS 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 491 ----GIEVKNSANPVVIRCEVHHGYTGgIYVHERGRGQFMENRIYANaYAGIWITSHSDPTIRKNEIFTGQQGGVYIFGE 566
Cdd:COG3420   169 ggrdGIYLEFSDNNVIRNNTIRNLRYG-IHYMYSNDNLVEGNTFRDN-GAGIALMYSKGNTVRGNTILGNSGYGILLKES 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 567 GRGLIEQNNIYGNALagiqirsqsdpivrlnkihdglhgGIYVHEKGRGLIEENEVYGNTLaGIWVTTGSSpilrKNRIH 646
Cdd:COG3420   247 SDSVIEGNTISGNGK------------------------GIFIYNSNRNTIRGNLFAGNGI-GIHLTAGSE----GNRIY 297
NosD_copper_fam TIGR04247
nitrous oxide reductase family maturation protein NosD; Members of this family include NosD, a ...
 558-811 2.40e-04

nitrous oxide reductase family maturation protein NosD; Members of this family include NosD, a repetitive periplasmic protein required for the maturation of the copper-containing enzyme nitrous-oxide reductase. NosD appears to be part of a complex with NosF (an ABC transporter family ATP-binding protein) and NosY (a six-helix transmembrane protein in the ABC-2 permease family). However, NosDFY-like complexes appear to occur also in species whose copper requiring enzymes are something other than nitrous-oxide reductase.


Pssm-ID: 275079 [Multi-domain]  Cd Length: 377  Bit Score: 44.49  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 558 QGGVYIFGEGRG---LIEQNNIygnALAGIQIR-SQSDpivrlnkiHDGLHGGIYVHEKGRGLIEENEVYGNtLAGIWVT 633
Cdd:TIGR04247  36 EGGAVIDGEGKGtviTIKAPDV---TIEGLTVRnSGTS--------LTEDDAGIKVEKADRAVIENNRLEDN-LFGIYLQ 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 634 TGSSPILRKNRIHSGKQV-------GVYFYDQGHGLLEENDIFNHlYSGVQIRTGSNPKITRNKiwgGQNG--GVLVYNG 704
Cdd:TIGR04247 104 EAHDSLIENNRITGKPDLrsndrgnGIHLWNSPGNVIEGNTVRGG-RDGIYIEFSHHNLIRNNT---SHNLryGLHFMYS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 705 GKGCLEDNEIFDNAmAGVWIKTDSEPTLRRNKIYDGRDggvcifNRGKGLL---------EDNEIFRNAQaGVLIStESN 775
Cdd:TIGR04247 180 NDNLVEDNVFRGNS-VGYALMYSKRLTVRGNVFLNNWG------DAGYGILlkeindseiEGNTVLGNTK-GLFID-NSP 250

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1972288612 776 PTLRRNRVFDGKSAGIEItngaTATLEENQLFRNKY 811
Cdd:TIGR04247 251 RNVFRDNDFEYNGIGIHF----TAGSERNRFEGNAF 282
CASH smart00722
Domain present in carbohydrate binding proteins and sugar hydrolses;
606-748 4.55e-04

Domain present in carbohydrate binding proteins and sugar hydrolses;


Pssm-ID: 214788  Cd Length: 153  Bit Score: 41.72  E-value: 4.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612  606 GIYVhEKGRGLIEENEVYGNTLAGIWVTTGSSPILRKNRIHS--GKQVGVYFYDQ-----GHGLLEENDIFNHLYSGVQI 678
Cdd:smart00722   4 GTVL-ELLRGAVHYMYTSDIGGSGGAVIDMGSGRGSNITINSndVRVDGVTIGGDgnavtGIYVSASGDPVIQNDGTGKN 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972288612  679 RTGSNpkITRNKIWGGQNGGVLVYNGGKGCLEDNEIFDNAMA---GVWIKTDSEPTLRRNKIYDGRDGGVCIF 748
Cdd:smart00722  83 LIIDN--VTFNGTEINSGAGIVVTAGSEGLFIGNRIIGNYVAtgdGNYLSDSSGGDLIGNRIYDNNRDGIAVV 153
beta_helix_1 TIGR03805
parallel beta-helix repeat-containing protein; Members of this protein family contain a tandem ...
 554-786 6.24e-03

parallel beta-helix repeat-containing protein; Members of this protein family contain a tandem pair of beta-helix repeats (see TIGR03804). Each repeat is expected to consist of three beta strands that form a single turn as they form a right-handed helix of stacked beta-structure. Member proteinsa occur regularly in two-gene pairs along with another uncharacterized protein family; both protein families exhibit either lipoprotein or regular signal peptides, suggesting transit through the plasma membrane, and the two may be fused. The function of the pair is unknown. [Unknown function, General]


Pssm-ID: 163517 [Multi-domain]  Cd Length: 314  Bit Score: 39.66  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 554 FTGQQGGVYIFgegrgLIEQNNIYGNALA-------GIQIRSQSDPIVRL--------NKIHDGLHGgIYVHEKGRGLIE 618
Cdd:TIGR03805  48 FSGQVGGAEGL-----LVTSDDVTLSDLAventkgdGVKVKGSDGIIIRRlrvewtggPKSSNGAYG-IYPVESTNVLVE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 619 ENEVYGNTLAGIWVTTGSSPILRKNRIHsgKQVGvyfydqghGLLEENDIFNHLYsgvqirtgsNPKITRNkiwggqNGG 698
Cdd:TIGR03805 122 DSYVRGASDAGIYVGQSQNIVVRNNVAE--ENVA--------GIEIENSQNADVY---------NNIATNN------TGG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 699 VLVYN--------GGKGCLEDNEIFDN-----AMAGvwiktdseptlrrnkiydgrdGGVCIFNRGKGLL----EDNEIF 761
Cdd:TIGR03805 177 ILVFDlpglpqpgGSNVRVFDNIIFDNntpnfAPAG---------------------SIVASVPAGTGVVvmanRDVEIF 235

                         250       260       270
                  ....*....|....*....|....*....|
gi 1972288612 762 RNA-----QAGVLISTESNPTLRRNRVFDG 786
Cdd:TIGR03805 236 GNVisnndTANVLISSYHSTGLPDQPPDDG 265
 
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, ...
 845-913 1.35e-38

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: 137.64  E-value: 1.35e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972288612 845 CLFKVSSNNSFPMHNFYRCTTCNTTERNAICTNCIRTCHRGHSVELVRFDRFFCDCGAGTLERHCHLQN 913
Cdd:cd19676     1 CLYKISSYTSFPMHDFYRCLTCNTTDRNAICVNCIKKCHEGHDVEFIRHDRFFCDCGAGTLSNDCQLAG 69
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 674-829 2.90e-30

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: 117.12  E-value: 2.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 674 SGVQIRTGSNPKITRNKIWGGQNGGVLVYNGGKGCLEDNEIFDNAMAGVWIKTDSEPTLRRNKIYDGRDGGVCIFNRGKG 753
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972288612 754 LLEDNEIFRNAQAGVLISTESNPTLRRNRVFDGKSAGIEITNG-ATATLEENQLFRNKYGGLCVATGVTPVQ-RGNRI 829
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSsNNVTISNNTVTNNKGAGILIVGGSSNNTvENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 490-645 1.67e-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: 109.42  E-value: 1.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 490 SGIEVKNSANPVVIRCEVHHGYTGGIYVHERGRGQFMENRIYANAYAGIWITSHSDPTIRKNEIFTGQQGGVYIFGEGRG 569
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972288612 570 LIEQNNIYGNALAGIQIRSQSDPIVRLNKIHDGLHGGIYV-HEKGRGLIEENEVYGNTLAGIWVTTGSS-PILRKNRI 645
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIeDSSNNVTISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 536-691 3.32e-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: 108.26  E-value: 3.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 536 AGIWITSHSDPTIRKNEIFTGQQGGVYIFGEGRGLIEQNNIYGNALAGIQIRSQSDPIVRLNKIHDGLHGGIYVHEKGRG 615
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972288612 616 LIEENEVYGNTLAGIWVTTGSSPILRKNRIHSGKQVGVYFYDQGHGL-LEENDIFNHLYSGVQI-RTGSNPKITRNKI 691
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIvGGSSNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 582-737 3.45e-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: 105.57  E-value: 3.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 582 AGIQIRSQSDPIVRLNKIHDGLHGGIYVHEKGRGLIEENEVYGNTLAGIWVTTGSSPILRKNRIHSGKQVGVYFYDQGHG 661
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972288612 662 LLEENDIFNHLYSGVQIRTGSNPKITRNKIWGGQNGGVLVYNGGKGC-LEDNEIFDNAMAGVWI-KTDSEPTLRRNKI 737
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIvGGSSNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 444-599 3.65e-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: 3.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 444 AGVWVKNHANPYFRKCTIHSGKDVGVFTFEHGQGYFEKCNIHSNRISGIEVKNSANPVVIRCEVHHGYTGGIYVHERGRG 523
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972288612 524 QFMENRIYANAYAGIWITSHSDPTIRKNEIFTGQQGGVYIF-GEGRGLIEQNNIYGNALAGIQIRSQSD-PIVRLNKI 599
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEdSSNNVTISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 628-783 1.45e-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: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 628 AGIWVTTGSSPILRKNRIHSGKQVGVYFYDQGHGLLEENDIFNHLYSGVQIRTGSNPKITRNKIWGGQNGGVLVYNGGKG 707
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972288612 708 CLEDNEIFDNAMAGVWIKTDSEPTLRRNKIYDGRDGGVCIFNRGKGL-LEDNEIFRNAQAGVLI-STESNPTLRRNRV 783
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIvGGSSNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 398-553 2.04e-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: 97.48  E-value: 2.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 398 AAVCVKKSAAPKFKYCTVLDCENVGIYITDNATGHYEHCEIARNTLAGVWVKNHANPYFRKCTIHSGKDVGVFTFEHGQG 477
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972288612 478 YFEKCNIHSNRISGIEVKNSANPVVIRCEVHHGYTGGIYV-HERGRGQFMENRIYANAYAGIWITSHSD-PTIRKNEI 553
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIeDSSNNVTISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
UBR-box_UBR4_5_6_7 cd19671
UBR-box found in UBR4, UBR5, UBR6/FBOX11, UBR7 and similar proteins; This family includes UBR4 ...
 845-913 2.74e-17

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: 76.73  E-value: 2.74e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972288612 845 CLFKVSSNNSFPMHnFYRCTTCNTTERNAICTNCIRTCHRGHSVELVRFDRFFCDCGAGTLErHCHLQN 913
Cdd:cd19671     1 CTFEKTGRKYIKQP-WYHCYTCGLIDGLGVCEACARKCHKGHDLVYIGYSNFYCDCGSSGPG-KCKCES 67
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 720-832 3.93e-16

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


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 76.68  E-value: 3.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 720 AGVWIKTDSEPTLRRNKIYDGRDGGVCIFNRGKGLLEDNEIFRNAQAGVLISTESNPTLRRNRVFDGKSAGIEITNGATA 799
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1972288612 800 TLEENQLFRNKYGGLCVATGVTPVQRGNRIYDN 832
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNN 113
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 538-764 1.53e-15

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: 79.19  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 538 IWITShSDPTIRKNEI------FTGQQGGVYIFGEGRGLIEQNNIYGNaLAGIQIRSQSDPIVRLNKIHD-----GLHG- 605
Cdd:COG3420    73 ITITA-DNVTVRGLTItgsgdsLTDDDAGIYVRGADNAVIENNRIENN-LFGIYLEGSDNNVIRNNTISGnrdlrADRGn 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 606 GIYVHEKGRGLIEENEVYGNTlAGIWVTTGSSPILRKNRIHSGKqVGVYFYDQGHGLLEENDIFNHlYSGVQIRTGSNPK 685
Cdd:COG3420   151 GIHLWNSPGNVIEGNTISGGR-DGIYLEFSDNNVIRNNTIRNLR-YGIHYMYSNDNLVEGNTFRDN-GAGIALMYSKGNT 227

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972288612 686 ITRNKIWGGQNGGVLVYNGGKGCLEDNEIFDNAmAGVWIKTDSEPTLRRNKIYDGrDGGVcifnRGKGLLEDNEIFRNA 764
Cdd:COG3420   228 VRGNTILGNSGYGILLKESSDSVIEGNTISGNG-KGIFIYNSNRNTIRGNLFAGN-GIGI----HLTAGSEGNRIYGNN 300
UBR-box_BIG_like cd19681
UBR-box found in Arabidopsis thaliana auxin transport protein BIG and similar proteins; BIG ...
 843-908 2.49e-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: 71.67  E-value: 2.49e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972288612 843 GLCLFkVSSNNSFPMHNFYRCTTCNTTERNAICTNCIRTCHRGHSVELVRFDRFFCDCGAGTLERH 908
Cdd:cd19681     1 KVCTY-VSSGSNFMEQHWYFCYTCGLVDSKGCCSVCAKVCHRGHDVVYSRYSRFFCDCGAGGAKRG 65
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 385-528 1.10e-14

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


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 72.44  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 385 IERCDITSKVGNGaaVCVKKSAAPKFKYCTVLDCENVGIYITDNATGHYEHCEIARNTLAGVWVKNHANPYFRKCTIHSG 464
Cdd:pfam13229  13 IKNNTISNNGGYG--IYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNNLIENNTISNN 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972288612 465 KDVGVFTFEHGQGYFEKCNIHSNRISGIEVKNSANPVVIR-CEVHHGYTGGIYVHERGRGQFMEN 528
Cdd:pfam13229  91 GGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVTISnNTVTNNKGAGILIVGGSSNNTVEN 155
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 162-206 3.67e-13

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 64.43  E-value: 3.67e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972288612 162 INRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKELY 206
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
UBR-box_UBR4_like cd19674
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3. ...
 843-910 5.42e-13

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: 64.67  E-value: 5.42e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972288612 843 GLCLFKVSSNNsFPMHNFYRCTTCNTTERNAICTNCIRTCHRGHSVELVRFDRFFCDCGAGTLERHCH 910
Cdd:cd19674     1 NVCTFASTGKN-YARQHWYECYTCFLNGNEGVCEVCARVCHKGHDLVYSKTSSFFCDCGAGGGPSKCK 67
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 674-832 6.30e-13

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: 68.98  E-value: 6.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 674 SGVQIRTGSNPKITRNKIWGGQNGGVLVYNGGKGcLEDNEIFDNaMAGVWIKTDSEPTLRRNKIYDGRDGgVCIFNRGKG 753
Cdd:pfam05048  20 NGIQLWNTEGNVISNNDIINSRDGIYLDASNNNT-ITGNRISNL-RYGIHLMNSNDNTISDNVFSGNTAG-IALMSSSNN 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972288612 754 LLEDNEIFRNAQAGVLISTESNPTLRRNRVFDGKSAGIEITNGATATLEENQLFRNKYGGLCVATGvtpvqRGNRIYDN 832
Cdd:pfam05048  97 TLENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRITSNGIGIHFLAGS-----NGNTIYNN 170
UBR-box cd19669
UBR-box found in UBR family of E3 ubiquitin ligases (UBR1-7) and similar proteins; The UBR-box ...
 860-913 6.59e-13

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: 64.46  E-value: 6.59e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1972288612 860 FYRCTTCNTTERNAICTNCIRTCHRGHSVELVRFDRFFCDCGAGTLER-HCHLQN 913
Cdd:cd19669    12 MYHCLTCSLDDNSGICEECAKKCHEGHDVVYIGSGSGFCDCGDSSAKSgFCKCHS 66
UBR-box_UBR4 cd19680
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3. ...
 843-902 1.75e-12

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: 63.25  E-value: 1.75e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 843 GLCLFKVSsNNSFPMHNFYRCTTCNTTERNAICTNCIRTCHRGHSVELVRFDRFFCDCGA 902
Cdd:cd19680     1 KLCTFTIT-QKEFMNQHWYHCHTCKMVDGVGVCSVCAKVCHKDHDLSYAKYGSFFCDCGA 59
F-box_FBXO15 cd22093
F-box domain found in F-box only protein 15 (FBXO15) and similar proteins; FBXO15, also called ...
 162-206 1.47e-11

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: 59.96  E-value: 1.47e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972288612 162 INRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKELY 206
Cdd:cd22093     1 IERLPSEILLKILSYLDASSLLCISCVNKLFYQLANDNALWRKLY 45
FBOX smart00256
A Receptor for Ubiquitination Targets;
165-205 2.49e-10

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 56.29  E-value: 2.49e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1972288612  165 LPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKEL 205
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41
F-box_FBXO3 cd22084
F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called ...
 162-210 9.15e-10

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: 54.96  E-value: 9.15e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1972288612 162 INRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKElYCNLY 210
Cdd:cd22084     1 LDDLPSDPLLNILSFLDYRDLISCSQVCRRLNQLCSHDPLWKR-LCKKY 48
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 626-812 9.53e-10

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: 61.47  E-value: 9.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 626 TLAGIWVT-TGSSpilrknriHSGKQVGVYFYDQGHGLLEENDIFNHLYsGVQIRTGSNPKITRNKIWGGQNG------G 698
Cdd:COG3420    81 TVRGLTITgSGDS--------LTDDDAGIYVRGADNAVIENNRIENNLF-GIYLEGSDNNVIRNNTISGNRDLradrgnG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 699 VLVYNGGKGCLEDNEIFDNAmAGVWIKTDSEPTLRRNKIYDGRDGgVCIFNRGKGLLEDNEIFRNAqAGVLISTESNPTL 778
Cdd:COG3420   152 IHLWNSPGNVIEGNTISGGR-DGIYLEFSDNNVIRNNTIRNLRYG-IHYMYSNDNLVEGNTFRDNG-AGIALMYSKGNTV 228

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1972288612 779 RRNRVFDGKSAGIEITNGATATLEENQLFRNKYG 812
Cdd:COG3420   229 RGNTILGNSGYGILLKESSDSVIEGNTISGNGKG 262
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 162-203 1.42e-09

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: 54.08  E-value: 1.42e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972288612 162 INRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWK 203
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWK 42
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 860-901 3.41e-09

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: 53.98  E-value: 3.41e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1972288612  860 FYRCTTCNTTERNAICTNC-IRTCHRGHSVEL-VRFDRFFCDCG 901
Cdd:smart00396  13 IYRCKTCGLDPTCVLCSDCfRPSCHKGHDVSLkTSRGSGICDCG 56
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 163-197 4.63e-09

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: 52.45  E-value: 4.63e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1972288612 163 NRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISN 197
Cdd:cd09917     1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 416-646 5.83e-09

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: 58.77  E-value: 5.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 416 LDCENVGIYItDNATGHY-EHCEIaRNTLAGVWVKNHANPYFRKCTIHSGKDVGVftfEHGQG-YFEKCN---IHSNRIS 490
Cdd:COG3420    94 LTDDDAGIYV-RGADNAViENNRI-ENNLFGIYLEGSDNNVIRNNTISGNRDLRA---DRGNGiHLWNSPgnvIEGNTIS 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 491 ----GIEVKNSANPVVIRCEVHHGYTGgIYVHERGRGQFMENRIYANaYAGIWITSHSDPTIRKNEIFTGQQGGVYIFGE 566
Cdd:COG3420   169 ggrdGIYLEFSDNNVIRNNTIRNLRYG-IHYMYSNDNLVEGNTFRDN-GAGIALMYSKGNTVRGNTILGNSGYGILLKES 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 567 GRGLIEQNNIYGNALagiqirsqsdpivrlnkihdglhgGIYVHEKGRGLIEENEVYGNTLaGIWVTTGSSpilrKNRIH 646
Cdd:COG3420   247 SDSVIEGNTISGNGK------------------------GIFIYNSNRNTIRGNLFAGNGI-GIHLTAGSE----GNRIY 297
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 618-763 8.38e-09

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


Pssm-ID: 428281 [Multi-domain]  Cd Length: 215  Bit Score: 56.66  E-value: 8.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 618 EENEVYGNTL----AGIWVTTGSSPILRKNRIHSGKQvGVYFYDQGHGLLEENdIFNHLYSGVQIRTGSNPKITRNKIWG 693
Cdd:pfam05048  28 EGNVISNNDIinsrDGIYLDASNNNTITGNRISNLRY-GIHLMNSNDNTISDN-VFSGNTAGIALMSSSNNTLENNTISG 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 694 GQNGGVLVYNGGKGCLEDNEIFDNAMAGVWIKTDSEPTLRRNKIYDgRDGGVCIFNRGkgllEDNEIFRN 763
Cdd:pfam05048 106 NTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRITS-NGIGIHFLAGS----NGNTIYNN 170
F-box_FBXO11 cd22091
F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called ...
 165-206 1.57e-08

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: 51.27  E-value: 1.57e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972288612 165 LPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKELY 206
Cdd:cd22091     4 LPDEVLLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWKRLY 45
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 537-693 1.67e-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: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 537 GIWITSHSDPTIRKNEIFTGQQGgVYIFGEGRGLIEQNNIYGNAlAGIQIRSQSDPIVRLNKIhDGLHGGIYVHEKGRGL 616
Cdd:pfam05048  21 GIQLWNTEGNVISNNDIINSRDG-IYLDASNNNTITGNRISNLR-YGIHLMNSNDNTISDNVF-SGNTAGIALMSSSNNT 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1972288612 617 IEENEVYGNTLAGIWVTTGSSPILRKNRIHSGKQVGVYFYDQGHGLLEENDIFNHlYSGVQIRTGSNpkitRNKIWG 693
Cdd:pfam05048  98 LENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRITSN-GIGIHFLAGSN----GNTIYN 169
F-box_DdgacFF-like cd22148
F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) ...
 165-204 5.33e-08

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: 49.59  E-value: 5.33e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1972288612 165 LPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKE 204
Cdd:cd22148     5 LPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELWKA 44
F-box_unchar cd22139
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 ...
 165-205 1.09e-07

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: 48.78  E-value: 1.09e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1972288612 165 LPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKEL 205
Cdd:cd22139     4 LPDELWLHIFSFLSPKDLCQVALVCRRFNRLASDESLWKQI 44
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 651-809 1.05e-06

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


Pssm-ID: 428281 [Multi-domain]  Cd Length: 215  Bit Score: 50.49  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 651 VGVYFYDQGHGLLEENDIFNhLYSGVQIRTGSNPKITRNKIWGGQNGgVLVYNGGKGCLEDNEIFDNAMaGVWIKTDSEP 730
Cdd:pfam05048  20 NGIQLWNTEGNVISNNDIIN-SRDGIYLDASNNNTITGNRISNLRYG-IHLMNSNDNTISDNVFSGNTA-GIALMSSSNN 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972288612 731 TLRRNKIYDGRDGGVCIFNRGKGLLEDNEIFRNAQAGVLISTESNPTLRRNRvFDGKSAGIEITNGAtatlEENQLFRN 809
Cdd:pfam05048  97 TLENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNR-ITSNGIGIHFLAGS----NGNTIYNN 170
F-box_SpPof1-like cd22147
F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar ...
 162-205 1.10e-06

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: 46.15  E-value: 1.10e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1972288612 162 INRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKEL 205
Cdd:cd22147     2 LSALPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELWKRM 45
zf-UBR pfam02207
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ...
 860-912 1.91e-06

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: 46.13  E-value: 1.91e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1972288612 860 FYRCTTCNTTERNAICTNCIRTC-HRGHSVELVRFDR-FFCDCG---AGTLERHCHLQ 912
Cdd:pfam02207  11 VYRCLTCSLDPTCVICYSCFINCdHEGHDYELFTSRGgGCCDCGdpeAWKEEGFCKLH 68
F-box_FBXO36 cd22106
F-box domain found in F-box only protein 36 (FBXO36) and similar proteins; FBXO36, also called ...
 162-207 2.26e-06

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: 45.26  E-value: 2.26e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1972288612 162 INRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKELYC 207
Cdd:cd22106     1 LVRLPDKLLLYIISYLDLEDIARLSQTSKRFKKLCNSDELWEKIYM 46
F-box_FBXW12 cd22137
F-box domain found in F-box/WD repeat-containing protein 12 (FBXW12) and similar proteins; ...
 164-205 5.11e-06

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: 44.29  E-value: 5.11e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972288612 164 RLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKEL 205
Cdd:cd22137     2 QLPDLPMLRIFSFLDAFSLLQAAQVNKQWNKVADSDYLWRNL 43
UBR-box_UBR7 cd19677
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR7 and similar proteins; UBR7 (EC 2.3. ...
 861-901 8.81e-06

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: 44.22  E-value: 8.81e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972288612 861 YRCTTCN---TTERNAICTNCIRTCHRGHSV-ELVRFDRFFCDCG 901
Cdd:cd19677    14 YACLTCTpagADQPAGICLACSLSCHEGHELeELYTKRNFRCDCG 58
F-box_FBXL5 cd22118
F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also ...
 162-202 1.11e-05

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: 43.10  E-value: 1.11e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1972288612 162 INRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVW 202
Cdd:cd22118     1 ISSLPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41
UBR-box_UBR1_2_3 cd19670
UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), E3-alpha-3 ...
 860-901 1.38e-05

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: 43.89  E-value: 1.38e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1972288612 860 FYRCTTCNTTERNAICTNC-IRTCHRGHSVELVR-FDRFFCDCG 901
Cdd:cd19670    11 YYRCLDCSLDPSSCICEECfLNGNHEGHNYSLRTsSGGGVCDCG 54
F-box_JHDM cd22122
F-box domain found in the JmjC domain-containing histone demethylation protein (JHDM) family; ...
 163-204 1.79e-05

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: 42.65  E-value: 1.79e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972288612 163 NRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKE 204
Cdd:cd22122     2 HVLPREVWLPVFQYLSPKDLCVCMRVCKTWNRWCCDPSLWKR 43
F-box_FBXO31 cd22102
F-box domain found in F-box only protein 31 (FBXO31) and similar proteins; FBXO31, also called ...
 165-203 2.51e-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: 42.41  E-value: 2.51e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1972288612 165 LPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWK 203
Cdd:cd22102     4 LPPELLVEIFSSLPGTDLPSLAQVCKKFREILNTDTIWQ 42
F-box_FBXW5 cd22132
F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, ...
 165-207 2.57e-05

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: 42.21  E-value: 2.57e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972288612 165 LPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKELYC 207
Cdd:cd22132     4 LPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLWKELFY 46
F-box_FBXO16-like cd22094
F-box domain found in F-box only protein 16 (FBXO16), epithelial cell-transforming sequence 2 ...
 165-203 2.67e-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: 42.43  E-value: 2.67e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1972288612 165 LPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWK 203
Cdd:cd22094     6 LPRFLSLYIFSYLDPRSLCRAAQVSWYWKFLCESDELWL 44
F-box_ScMDM30-like cd22143
F-box domain found in Saccharomyces cerevisiae mitochondrial distribution and morphology ...
 162-205 3.13e-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: 41.83  E-value: 3.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1972288612 162 INRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNShEVWKEL 205
Cdd:cd22143     2 FDSLPDEILSIIFSHLPQSDLYNLLFVNKHFYSLALP-ELWRSI 44
F-box_FBXO24 cd22098
F-box domain found in F-box only protein 24 (FBXO24) and similar proteins; FBXO24, also called ...
 161-205 4.19e-05

F-box domain found in F-box only protein 24 (FBXO24) and similar proteins; FBXO24, also called FBX24, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It recognizes deacetylated nucleoside diphosphate kinase A (NDPK-A) to enhance its 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: 438870  Cd Length: 47  Bit Score: 41.54  E-value: 4.19e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972288612 161 HINRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKEL 205
Cdd:cd22098     1 SLLDLPPEILDRIISFLPVKDIVSLGQTCRYFHEVCNSEAVWRRL 45
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 483-601 4.33e-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: 45.87  E-value: 4.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 483 NIHSNRISGIEVKNSANPVVIRCEVHHGyTGGIYVHERGRGQFMENRIYANAYAGIWITSHSDPTIRKNEIFTGQQGGVY 562
Cdd:pfam05048  57 NRISNLRYGIHLMNSNDNTISDNVFSGN-TAGIALMSSSNNTLENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIF 135

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1972288612 563 IFGEGRGLIEQNNIYGNAlAGIQIRSQSDPivrlNKIHD 601
Cdd:pfam05048 136 LYNSDYNTITGNRITSNG-IGIHFLAGSNG----NTIYN 169
UBR-box_UBR5 cd19675
UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3. ...
 859-900 7.83e-05

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: 41.68  E-value: 7.83e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972288612 859 NFYRCTTCNTTERNAICTNCIRTCHRGHSVELVRFD-RFFCDC 900
Cdd:cd19675    22 DIFECRTCGLVGSLCCCTECARVCHKGHDCKLKRTSpTAYCDC 64
F-box_DmSKP2-like cd22149
F-box domain found in Drosophila melanogaster S-phase kinase-associated protein 2 (DmSKP2) and ...
 164-203 8.39e-05

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: 40.82  E-value: 8.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1972288612 164 RLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWK 203
Cdd:cd22149     3 RLSDEIILSIFKWLPKKTLARCARVCRRWKRLCFDESLWR 42
F-box_FBXL2-like cd22115
F-box domain found in F-box/LRR-repeat protein 2 (FBXL2), F-box/LRR-repeat protein 20 (FBXL20) ...
 162-196 1.03e-04

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: 40.48  E-value: 1.03e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1972288612 162 INRLPEELLLKVFSFLPDKSLLACSSVSYRFNQIS 196
Cdd:cd22115     4 NKKLPKELLLRIFSFLDVVTLCRCAQVSKYWNVLA 38
F-box_FBXO41 cd22109
F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called ...
 167-206 1.10e-04

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: 40.39  E-value: 1.10e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1972288612 167 EELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKELY 206
Cdd:cd22109     8 RDALFCVFSYLDTKSLLRCAEVCREWRDVSRHPALWQRVC 47
F-box_FBXL12 cd22123
F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also ...
 162-203 1.18e-04

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: 40.41  E-value: 1.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972288612 162 INRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWK 203
Cdd:cd22123     1 LDQLPENVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLWR 42
F-box_FBXO7 cd22087
F-box domain found in F-box only protein 7 (FBXO7) and similar proteins; FBXO7, also called ...
 165-206 1.81e-04

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: 39.98  E-value: 1.81e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972288612 165 LPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKELY 206
Cdd:cd22087     4 LPPEIKLRILSLLDVRSLLSLSQVCRDLNSATNDQLLWRFLL 45
NosD_copper_fam TIGR04247
nitrous oxide reductase family maturation protein NosD; Members of this family include NosD, a ...
 558-811 2.40e-04

nitrous oxide reductase family maturation protein NosD; Members of this family include NosD, a repetitive periplasmic protein required for the maturation of the copper-containing enzyme nitrous-oxide reductase. NosD appears to be part of a complex with NosF (an ABC transporter family ATP-binding protein) and NosY (a six-helix transmembrane protein in the ABC-2 permease family). However, NosDFY-like complexes appear to occur also in species whose copper requiring enzymes are something other than nitrous-oxide reductase.


Pssm-ID: 275079 [Multi-domain]  Cd Length: 377  Bit Score: 44.49  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 558 QGGVYIFGEGRG---LIEQNNIygnALAGIQIR-SQSDpivrlnkiHDGLHGGIYVHEKGRGLIEENEVYGNtLAGIWVT 633
Cdd:TIGR04247  36 EGGAVIDGEGKGtviTIKAPDV---TIEGLTVRnSGTS--------LTEDDAGIKVEKADRAVIENNRLEDN-LFGIYLQ 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 634 TGSSPILRKNRIHSGKQV-------GVYFYDQGHGLLEENDIFNHlYSGVQIRTGSNPKITRNKiwgGQNG--GVLVYNG 704
Cdd:TIGR04247 104 EAHDSLIENNRITGKPDLrsndrgnGIHLWNSPGNVIEGNTVRGG-RDGIYIEFSHHNLIRNNT---SHNLryGLHFMYS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 705 GKGCLEDNEIFDNAmAGVWIKTDSEPTLRRNKIYDGRDggvcifNRGKGLL---------EDNEIFRNAQaGVLIStESN 775
Cdd:TIGR04247 180 NDNLVEDNVFRGNS-VGYALMYSKRLTVRGNVFLNNWG------DAGYGILlkeindseiEGNTVLGNTK-GLFID-NSP 250

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1972288612 776 PTLRRNRVFDGKSAGIEItngaTATLEENQLFRNKY 811
Cdd:TIGR04247 251 RNVFRDNDFEYNGIGIHF----TAGSERNRFEGNAF 282
F-box_FBXL1 cd22114
F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also ...
 165-202 2.75e-04

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: 39.32  E-value: 2.75e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1972288612 165 LPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVW 202
Cdd:cd22114     4 LPDELLLGIFSCLCLPDLLKVSQVCKRWYRLASDESLW 41
F-box_ScCDC4-like cd22141
F-box domain found in Saccharomyces cerevisiae cell division control protein 4 (ScCDC4) and ...
 162-205 4.27e-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: 38.70  E-value: 4.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1972288612 162 INRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKEL 205
Cdd:cd22141     1 IGNLPFEISLKIFNYLQFEDLLNSLGVSKKWNKIIRNTALWKKL 44
CASH smart00722
Domain present in carbohydrate binding proteins and sugar hydrolses;
606-748 4.55e-04

Domain present in carbohydrate binding proteins and sugar hydrolses;


Pssm-ID: 214788  Cd Length: 153  Bit Score: 41.72  E-value: 4.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612  606 GIYVhEKGRGLIEENEVYGNTLAGIWVTTGSSPILRKNRIHS--GKQVGVYFYDQ-----GHGLLEENDIFNHLYSGVQI 678
Cdd:smart00722   4 GTVL-ELLRGAVHYMYTSDIGGSGGAVIDMGSGRGSNITINSndVRVDGVTIGGDgnavtGIYVSASGDPVIQNDGTGKN 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972288612  679 RTGSNpkITRNKIWGGQNGGVLVYNGGKGCLEDNEIFDNAMA---GVWIKTDSEPTLRRNKIYDGRDGGVCIF 748
Cdd:smart00722  83 LIIDN--VTFNGTEINSGAGIVVTAGSEGLFIGNRIIGNYVAtgdGNYLSDSSGGDLIGNRIYDNNRDGIAVV 153
F-box_FBXO48 cd22113
F-box domain found in F-box only protein 48 (FBXO48) and similar proteins; FBXO48, also called ...
 162-203 8.41e-04

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: 38.07  E-value: 8.41e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972288612 162 INRLPEELLLKVFSFLPDKSLLACSSVSYRFNQ-ISNSHEVWK 203
Cdd:cd22113     1 IELLPPEMSLRIFSQLDVQSLCRASQTCKTWNDlIENSDYLWR 43
F-box_FBXO9 cd22089
F-box domain found in F-box only protein 9 (FBXO9) and similar proteins; FBXO9, also called ...
 161-206 1.50e-03

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: 37.59  E-value: 1.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1972288612 161 HINRLPEELLLKVF----SFLPDKSLLACSSVSYRFNQISNSHEVWKELY 206
Cdd:cd22089     2 HISALPSEILLYILrwvvSDLDLRSLEQLSLVCRKFYLLARDPSIWRLAC 51
F-box_FBXO16 cd22172
F-box domain found in F-box only protein 16 (FBXO16) and similar proteins; FBXO16, also called ...
 157-202 1.55e-03

F-box domain found in F-box only protein 16 (FBXO16) and similar proteins; 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. 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: 438943  Cd Length: 55  Bit Score: 37.65  E-value: 1.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1972288612 157 DQQDHINRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVW 202
Cdd:cd22172     1 EHIDFTRVLPRVLSLYIFSFLDPRSLCRCAQVCWYWKYLTELDQLW 46
F-box_AtSKIP31-like cd22166
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 31 (AtSKIP31) and similar ...
 164-207 1.85e-03

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: 37.05  E-value: 1.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1972288612 164 RLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKELYC 207
Cdd:cd22166     3 KLPPELFRHILKFLSPEDLTSCATVCRFLRGAASDESLWRRLYC 46
F-box_FBXO17-like cd22169
F-box domain found in F-box only protein 17 (FBXO17), F-box only protein 27 (FBXO27) and ...
 162-203 1.90e-03

F-box domain found in F-box only protein 17 (FBXO17), F-box only protein 27 (FBXO27) and similar proteins; This subfamily includes FBXO17 and FBXO27. FBXO17 is also called FBX17, F-box only protein 26 (FBX26/FBXO26), or FBG4, while FBXO27 is also called FBX27, or F-box/G-domain protein 5. FBXO17 and FBXO27 are the substrate-recognition components of SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. They can recognize and bind denatured glycoproteins, which are modified with complex-type oligosaccharides. FBXO17 also recognizes sulfated glycans but does not bind high-mannose glycoproteins. 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: 438940  Cd Length: 48  Bit Score: 37.02  E-value: 1.90e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972288612 162 INRLPEELLLKVFSFLPDKSLLA-CSSVSYRFNQISNSHEVWK 203
Cdd:cd22169     1 LSLLPEELLLLVLSHVPARTLVTrCRLVCRDWRDLVDGPTLWK 43
F-box_FBXW2 cd22131
F-box domain found in F-box/WD repeat-containing protein 2 (FBXW2) and similar proteins; FBXW2, ...
 160-198 2.46e-03

F-box domain found in F-box/WD repeat-containing protein 2 (FBXW2) and similar proteins; FBXW2, also called F-box and WD-40 domain-containing protein 2, or protein MD6, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a tumor suppressor by promoting SKP2 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: 438903  Cd Length: 40  Bit Score: 36.54  E-value: 2.46e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1972288612 160 DHINRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNS 198
Cdd:cd22131     1 DFLKLLPLELSFYLLSFLDPESLLTCCLVSKQWNKVISS 39
F-box_FBXL7 cd22120
F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also ...
 162-205 2.59e-03

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: 36.59  E-value: 2.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1972288612 162 INRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKEL 205
Cdd:cd22120     1 FDRLPDDVILQIFSHLPTNQLCRCARVCRRWYNLAWDPRLWTTI 44
F-box_FBXO13 cd22092
F-box domain found in F-box only protein 13 (FBXO13) and similar proteins; FBXO13, also called ...
 161-205 2.97e-03

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: 36.63  E-value: 2.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1972288612 161 HINRLPEELLLKVFSFLP--DKSLLACsSVSYRFNQISNSHEVWKEL 205
Cdd:cd22092     1 NINQLPDSILLKIFSYLSlqERCLSAS-LVCKYWRDLCLDSQFWKQI 46
F-box_FBXW4 cd20090
F-box domain found in F-box/WD repeat-containing protein 4 (FBXW4) and similar proteins; FBXW4, ...
 161-205 4.57e-03

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: 36.04  E-value: 4.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972288612 161 HINRLPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKEL 205
Cdd:cd20090     1 PLLDLPDDLLFLIFSYLDPASLGRLSQVCRRLYRLISRDAVWRRI 45
F-box_FBXO1 cd22082
F-box domain found in F-box only protein 1 (FBXO1) and similar proteins; FBXO1, also called ...
 165-202 5.06e-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: 36.07  E-value: 5.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1972288612 165 LPEELLLKVFSFLPDKSLLACSSVSYRFNQ-ISNSHEVW 202
Cdd:cd22082     5 LPEEVLLHILKGLPIKDLLNMRAVHSRFKDlIDSNPSLW 43
beta_helix_1 TIGR03805
parallel beta-helix repeat-containing protein; Members of this protein family contain a tandem ...
 554-786 6.24e-03

parallel beta-helix repeat-containing protein; Members of this protein family contain a tandem pair of beta-helix repeats (see TIGR03804). Each repeat is expected to consist of three beta strands that form a single turn as they form a right-handed helix of stacked beta-structure. Member proteinsa occur regularly in two-gene pairs along with another uncharacterized protein family; both protein families exhibit either lipoprotein or regular signal peptides, suggesting transit through the plasma membrane, and the two may be fused. The function of the pair is unknown. [Unknown function, General]


Pssm-ID: 163517 [Multi-domain]  Cd Length: 314  Bit Score: 39.66  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 554 FTGQQGGVYIFgegrgLIEQNNIYGNALA-------GIQIRSQSDPIVRL--------NKIHDGLHGgIYVHEKGRGLIE 618
Cdd:TIGR03805  48 FSGQVGGAEGL-----LVTSDDVTLSDLAventkgdGVKVKGSDGIIIRRlrvewtggPKSSNGAYG-IYPVESTNVLVE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 619 ENEVYGNTLAGIWVTTGSSPILRKNRIHsgKQVGvyfydqghGLLEENDIFNHLYsgvqirtgsNPKITRNkiwggqNGG 698
Cdd:TIGR03805 122 DSYVRGASDAGIYVGQSQNIVVRNNVAE--ENVA--------GIEIENSQNADVY---------NNIATNN------TGG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972288612 699 VLVYN--------GGKGCLEDNEIFDN-----AMAGvwiktdseptlrrnkiydgrdGGVCIFNRGKGLL----EDNEIF 761
Cdd:TIGR03805 177 ILVFDlpglpqpgGSNVRVFDNIIFDNntpnfAPAG---------------------SIVASVPAGTGVVvmanRDVEIF 235

                         250       260       270
                  ....*....|....*....|....*....|
gi 1972288612 762 RNA-----QAGVLISTESNPTLRRNRVFDG 786
Cdd:TIGR03805 236 GNVisnndTANVLISSYHSTGLPDQPPDDG 265
F-box_FBXO18 cd22095
F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called ...
 161-195 7.14e-03

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: 35.33  E-value: 7.14e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1972288612 161 HINRLPEELLLKVFSFLPDKSL-LACSSVSYRFNQI 195
Cdd:cd22095     1 HIQQLPEELLRNIFAFLPAEDLyQNISLVCRHWRDI 36
F-box_FBXL4 cd22117
F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also ...
 165-206 9.89e-03

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: 34.91  E-value: 9.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972288612 165 LPEELLLKVFSFLPDKSLLACSSVSYRFNQISNSHEVWKELY 206
Cdd:cd22117     4 LPYELIQLILSYLDLPSLCRLSQTCKLFRKHCYDPLLWKELN 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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