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Conserved domains on  [gi|675886812|ref|XP_009028908|]
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hypothetical protein HELRODRAFT_95885 [Helobdella robusta]

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, ...
 879-947 1.75e-41

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


:

Pssm-ID: 439074  Cd Length: 69  Bit Score: 146.11  E-value: 1.75e-41
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 675886812 879 CLYKISSYTSFPMHDFYRCRTCNTTDRNAICVNCIKTCHAGHVVEFIRHDRFFCDCGAGTLNNQCHLQG 947
Cdd:cd19676    1 CLYKISSYTSFPMHDFYRCLTCNTTDRNAICVNCIKKCHEGHDVEFIRHDRFFCDCGAGTLSNDCQLAG 69
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 708-861 2.93e-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: 2.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  708 SGVQIRTGSCPVIKRNKIWGGQNGGILVYNGGLGVIENNEIFDNAMAGVWIKTDSNPTLRHNKIHDGRDGGVCIFNGGKG 787
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675886812  788 ILESNEIFRNTQAGVLISNQSHPTLINNRIYDGMAAGIEITNN-ATATLEGNKIFNNKFGGLCLASGVHPFTKDN 861
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSsNNVTISNNTVTNNKGAGILIVGGSSNNTVEN 155
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 570-723 1.28e-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: 109.80  E-value: 1.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  570 AGIWVTSNSDPTIRRNEIFNGHQGGVYIFGEGRGLIEYNDIHGNALAGIQIRTGSNPIVRHNKIHHGQHGGIYVHEKGQG 649
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675886812  650 LIEENEVYSNTLAGVWITTNSQPILRKNRIHSGKQVGVYFYDNGHG-TLEDNDIFNHLYSGVQIRTGSCPVIKRN 723
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNvTISNNTVTNNKGAGILIVGGSSNNTVEN 155
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 478-633 1.61e-24

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


:

Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 100.56  E-value: 1.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  478 AGVWVKNHANPIMRNNHIHHGRDVGIFTFDNGLGYFEGNEIHDNRIAGFEVKAGANPTVVKCHIHHGQTGGIYVHENGRG 557
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 675886812  558 QFMENKIHSNNFAGIWVTSNSDPTIRRNEIFNGHQGGVYIF-GEGRGLIEYNDIHGNALAGIQI-RTGSNPIVRHNKI 633
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEdSSNNVTISNNTVTNNKGAGILIvGGSSNNTVENNTF 158
F-box_SF super family cl45894
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 153-197 1.51e-21

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.


The actual alignment was detected with superfamily member cd22091:

Pssm-ID: 459239  Cd Length: 45  Bit Score: 88.25  E-value: 1.51e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 675886812 153 QNELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKLY 197
Cdd:cd22091    1 QEELPDEVLLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWKRLY 45
PemB super family cl30602
Pectin methylesterase and related acyl-CoA thioesterases [Carbohydrate transport and ...
 328-366 7.04e-03

Pectin methylesterase and related acyl-CoA thioesterases [Carbohydrate transport and metabolism, Lipid transport and metabolism];


The actual alignment was detected with superfamily member COG4677:

Pssm-ID: 443713 [Multi-domain]  Cd Length: 307  Bit Score: 39.82  E-value: 7.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 675886812 328 KRPTIIFIHPGTYSKRLSITS---NVILIGAGPgnvaDHVII 366
Cdd:COG4677   44 TERTTIYIKNGVYREKLVIPSnkpNITLIGEDR----DKTII 81
 
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, ...
 879-947 1.75e-41

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


Pssm-ID: 439074  Cd Length: 69  Bit Score: 146.11  E-value: 1.75e-41
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 675886812 879 CLYKISSYTSFPMHDFYRCRTCNTTDRNAICVNCIKTCHAGHVVEFIRHDRFFCDCGAGTLNNQCHLQG 947
Cdd:cd19676    1 CLYKISSYTSFPMHDFYRCLTCNTTDRNAICVNCIKKCHEGHDVEFIRHDRFFCDCGAGTLSNDCQLAG 69
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 708-861 2.93e-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: 2.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  708 SGVQIRTGSCPVIKRNKIWGGQNGGILVYNGGLGVIENNEIFDNAMAGVWIKTDSNPTLRHNKIHDGRDGGVCIFNGGKG 787
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675886812  788 ILESNEIFRNTQAGVLISNQSHPTLINNRIYDGMAAGIEITNN-ATATLEGNKIFNNKFGGLCLASGVHPFTKDN 861
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSsNNVTISNNTVTNNKGAGILIVGGSSNNTVEN 155
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 570-723 1.28e-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: 109.80  E-value: 1.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  570 AGIWVTSNSDPTIRRNEIFNGHQGGVYIFGEGRGLIEYNDIHGNALAGIQIRTGSNPIVRHNKIHHGQHGGIYVHEKGQG 649
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675886812  650 LIEENEVYSNTLAGVWITTNSQPILRKNRIHSGKQVGVYFYDNGHG-TLEDNDIFNHLYSGVQIRTGSCPVIKRN 723
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNvTISNNTVTNNKGAGILIVGGSSNNTVEN 155
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 478-633 1.61e-24

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


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 100.56  E-value: 1.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  478 AGVWVKNHANPIMRNNHIHHGRDVGIFTFDNGLGYFEGNEIHDNRIAGFEVKAGANPTVVKCHIHHGQTGGIYVHENGRG 557
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 675886812  558 QFMENKIHSNNFAGIWVTSNSDPTIRRNEIFNGHQGGVYIF-GEGRGLIEYNDIHGNALAGIQI-RTGSNPIVRHNKI 633
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEdSSNNVTISNNTVTNNKGAGILIvGGSSNNTVENNTF 158
F-box_FBXO11 cd22091
F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called ...
 153-197 1.51e-21

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: 88.25  E-value: 1.51e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 675886812 153 QNELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKLY 197
Cdd:cd22091    1 QEELPDEVLLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWKRLY 45
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 616-847 5.73e-18

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: 86.51  E-value: 5.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 616 AGIQIRTGSNPIVRHNKIHHGQHGgIYVHEKGQGLIEENEVYSNtlagvwittnsqpilRKNRIHSGkqVGVYFYDNGHG 695
Cdd:COG3420   99 AGIYVRGADNAVIENNRIENNLFG-IYLEGSDNNVIRNNTISGN---------------RDLRADRG--NGIHLWNSPGN 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 696 TLEDNDIFNHlYSGVQIRTGSCPVIKRNKIWGGQNGgILVYNGGLGVIENNEIFDNAmAGVWIKTDSNPTLRHNKIHDGR 775
Cdd:COG3420  161 VIEGNTISGG-RDGIYLEFSDNNVIRNNTIRNLRYG-IHYMYSNDNLVEGNTFRDNG-AGIALMYSKGNTVRGNTILGNS 237

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 675886812 776 DGGVCIFNGGKGILESNEIFRNTQaGVLISNQSHPTLINNRIYDGmAAGIEITNNAtatlEGNKIFNNKFGG 847
Cdd:COG3420  238 GYGILLKESSDSVIEGNTISGNGK-GIFIYNSNRNTIRGNLFAGN-GIGIHLTAGS----EGNRIYGNNFIG 303
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 154-197 1.39e-15

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 71.36  E-value: 1.39e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 675886812  154 NELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKLY 197
Cdd:pfam12937   2 SSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 331-663 4.26e-11

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


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 65.71  E-value: 4.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 331 TIIFIHPGTYSKRLSITSNVILIGAGpgnvadhviierqseSAVLFSEGAKQAylgyVTIKfspsAPssvphhkhyslEV 410
Cdd:COG3420   35 DTIEVPPGTYEGNIVIDKPLTLIGEG---------------GAVIDGGGKGTV----ITIT----AD-----------NV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 411 TdnsspiVDHCTV----KSFSVVGAAVCVSGSGaDPHIKHCNISDCenvglfitdhaqgtydyneicrnaLAGVWVKNHA 486
Cdd:COG3420   81 T------VRGLTItgsgDSLTDDDAGIYVRGAD-NAVIENNRIENN------------------------LFGIYLEGSD 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 487 NPIMRNNHIHhGRDVGIFTFDNG--LGYFEGNEIHDNRIA----GFEVKAGANPTVVKCHIHHGQTGgiyVHengrgqFM 560
Cdd:COG3420  130 NNVIRNNTIS-GNRDLRADRGNGihLWNSPGNVIEGNTISggrdGIYLEFSDNNVIRNNTIRNLRYG---IH------YM 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 561 ---ENKIHSNNF----AGIWVTSNSDPTIRRNEIFNGHQGGVYIFGEGRGLIEYNDIHGNALaGIQIRTGSNPIVRHNKI 633
Cdd:COG3420  200 ysnDNLVEGNTFrdngAGIALMYSKGNTVRGNTILGNSGYGILLKESSDSVIEGNTISGNGK-GIFIYNSNRNTIRGNLF 278

                        330       340       350
                 ....*....|....*....|....*....|
gi 675886812 634 HHGQHgGIYVHekgqGLIEENEVYSNTLAG 663
Cdd:COG3420  279 AGNGI-GIHLT----AGSEGNRIYGNNFIG 303
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 882-935 2.69e-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: 54.37  E-value: 2.69e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 675886812   882 KISSYTSFPMHDFYRCRTCNTTDRNAICVNC-IKTCHAGHVVEFIRHDR-FFCDCG 935
Cdd:smart00396   1 DVCGYKFTGGEVIYRCKTCGLDPTCVLCSDCfRPSCHKGHDVSLKTSRGsGICDCG 56
FBOX smart00256
A Receptor for Ubiquitination Targets;
156-196 5.39e-08

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 49.74  E-value: 5.39e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 675886812   156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKL 196
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41
zf-UBR pfam02207
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ...
 894-935 5.67e-08

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: 50.37  E-value: 5.67e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 675886812  894 FYRCRTCNTTDRNAICVNCIKTC-HAGHVVEFIRHDR-FFCDCG 935
Cdd:pfam02207  11 VYRCLTCSLDPTCVICYSCFINCdHEGHDYELFTSRGgGCCDCG 54
CASH smart00722
Domain present in carbohydrate binding proteins and sugar hydrolses;
467-598 2.63e-05

Domain present in carbohydrate binding proteins and sugar hydrolses;


Pssm-ID: 214788  Cd Length: 153  Bit Score: 45.19  E-value: 2.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812   467 YDYNEICRNALAGVWVKNHANPiMRNNHIHHGRDV--------GIFTFDNGLGYFEGNEIHDNRIAGFEVKAGANPTVVK 538
Cdd:smart00722  14 VHYMYTSDIGGSGGAVIDMGSG-RGSNITINSNDVrvdgvtigGDGNAVTGIYVSASGDPVIQNDGTGKNLIIDNVTFNG 92

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 675886812   539 CHIHHGqtGGIYVHENGRGQFMENKIHSNNFA---GIWVTSNSDPTIRRNEIFNGHQGGVYIF 598
Cdd:smart00722  93 TEINSG--AGIVVTAGSEGLFIGNRIIGNYVAtgdGNYLSDSSGGDLIGNRIYDNNRDGIAVV 153
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 448-613 3.59e-05

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


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 47.22  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 448 NISDCENVGLFITDHAQGTYDYNEICRNAlAGVWVKNHANPIMRNNHIHHGRDVGIFTFDNGLGYFEGNEIHDNRIagfe 527
Cdd:COG3420  187 NTIRNLRYGIHYMYSNDNLVEGNTFRDNG-AGIALMYSKGNTVRGNTILGNSGYGILLKESSDSVIEGNTISGNGK---- 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 528 vkaganptvvkchihhgqtgGIYVHENGRGQFMENKIhSNNFAGIWVTSNS-DPTIRRNE-IFNGHQggvyIFGEGRGLI 605
Cdd:COG3420  262 --------------------GIFIYNSNRNTIRGNLF-AGNGIGIHLTAGSeGNRIYGNNfIGNRTQ----VKYVGGRDN 316


                 ....*....
gi 675886812 606 EYN-DIHGN 613
Cdd:COG3420  317 EWSaDGRGN 325
CASH smart00722
Domain present in carbohydrate binding proteins and sugar hydrolses;
685-827 7.40e-04

Domain present in carbohydrate binding proteins and sugar hydrolses;


Pssm-ID: 214788  Cd Length: 153  Bit Score: 40.95  E-value: 7.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812   685 VGVYFYDNGHGTLEDNDIFNHLYSGVQIRTGSCPVI------KRNKIWGGQNGGILVYNGGLGVIENNEIFDNAMAGVWI 758
Cdd:smart00722   3 NGTVLELLRGAVHYMYTSDIGGSGGAVIDMGSGRGSnitinsNDVRVDGVTIGGDGNAVTGIYVSASGDPVIQNDGTGKN 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 675886812   759 KTDSNPTlrHNKIHDGRDGGVCIFNGGKGILESNEIFRNTQA---GVLISNQSHPTLINNRIYDGMAAGIEI 827
Cdd:smart00722  83 LIIDNVT--FNGTEINSGAGIVVTAGSEGLFIGNRIIGNYVAtgdGNYLSDSSGGDLIGNRIYDNNRDGIAV 152
PemB COG4677
Pectin methylesterase and related acyl-CoA thioesterases [Carbohydrate transport and ...
 328-366 7.04e-03

Pectin methylesterase and related acyl-CoA thioesterases [Carbohydrate transport and metabolism, Lipid transport and metabolism];


Pssm-ID: 443713 [Multi-domain]  Cd Length: 307  Bit Score: 39.82  E-value: 7.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 675886812 328 KRPTIIFIHPGTYSKRLSITS---NVILIGAGPgnvaDHVII 366
Cdd:COG4677   44 TERTTIYIKNGVYREKLVIPSnkpNITLIGEDR----DKTII 81
 
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, ...
 879-947 1.75e-41

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


Pssm-ID: 439074  Cd Length: 69  Bit Score: 146.11  E-value: 1.75e-41
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 675886812 879 CLYKISSYTSFPMHDFYRCRTCNTTDRNAICVNCIKTCHAGHVVEFIRHDRFFCDCGAGTLNNQCHLQG 947
Cdd:cd19676    1 CLYKISSYTSFPMHDFYRCLTCNTTDRNAICVNCIKKCHEGHDVEFIRHDRFFCDCGAGTLSNDCQLAG 69
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 708-861 2.93e-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: 2.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  708 SGVQIRTGSCPVIKRNKIWGGQNGGILVYNGGLGVIENNEIFDNAMAGVWIKTDSNPTLRHNKIHDGRDGGVCIFNGGKG 787
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675886812  788 ILESNEIFRNTQAGVLISNQSHPTLINNRIYDGMAAGIEITNN-ATATLEGNKIFNNKFGGLCLASGVHPFTKDN 861
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSsNNVTISNNTVTNNKGAGILIVGGSSNNTVEN 155
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 570-723 1.28e-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: 109.80  E-value: 1.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  570 AGIWVTSNSDPTIRRNEIFNGHQGGVYIFGEGRGLIEYNDIHGNALAGIQIRTGSNPIVRHNKIHHGQHGGIYVHEKGQG 649
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675886812  650 LIEENEVYSNTLAGVWITTNSQPILRKNRIHSGKQVGVYFYDNGHG-TLEDNDIFNHLYSGVQIRTGSCPVIKRN 723
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNvTISNNTVTNNKGAGILIVGGSSNNTVEN 155
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 524-670 5.34e-27

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


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 107.88  E-value: 5.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  524 AGFEVKAGANPTVVKCHIHHGQTGGIYVHENGRGQFMENKIHSNNFAGIWVTSNSDPTIRRNEIFNGHQGGVYIFGEGRG 603
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 675886812  604 LIEYNDIHGNALAGIQIRTGSNPIVRHNKIHHGQHGGIYVHEKGQGL-IEENEVYSNTLAGVWITTNS 670
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIVGGS 148
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 616-771 1.35e-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: 103.64  E-value: 1.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  616 AGIQIRTGSNPIVRHNKIHHGQHGGIYVHEKGQGLIEENEVYSNTLAGVWITTNSQPILRKNRIHSGKQVGVYFYDNGHG 695
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 675886812  696 TLEDNDIFNHLYSGVQIRTGSCPVIKRNKIWGGQNGGILVYNGGLGV-IENNEIFDNAMAGVWI-KTDSNPTLRHNKI 771
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIvGGSSNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 478-633 1.61e-24

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


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 100.56  E-value: 1.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  478 AGVWVKNHANPIMRNNHIHHGRDVGIFTFDNGLGYFEGNEIHDNRIAGFEVKAGANPTVVKCHIHHGQTGGIYVHENGRG 557
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 675886812  558 QFMENKIHSNNFAGIWVTSNSDPTIRRNEIFNGHQGGVYIF-GEGRGLIEYNDIHGNALAGIQI-RTGSNPIVRHNKI 633
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEdSSNNVTISNNTVTNNKGAGILIvGGSSNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 662-815 5.38e-24

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


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 99.40  E-value: 5.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  662 AGVWITTNSQPILRKNRIHSGKQVGVYFYDNGHGTLEDNDIFNHLYSGVQIRTGSCPVIKRNKIWGGQNGGILVYNGGLG 741
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675886812  742 VIENNEIFDNAMAGVWIKTDSNPTLRHNKIHDGRDGGVCIFNGGKGI-LESNEIFRNTQAGVLISNQSHPTLINN 815
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIVGGSSNNTVEN 155
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 431-587 1.34e-21

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: 92.47  E-value: 1.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  431 AAVCVSGSGaDPHIKHCNISDCENVGLFITDHAQGTYDYNEICRNALAGVWVKNHANPIMRNNHIHHGRDVGIFTFDNGL 510
Cdd:pfam13229   1 SGILLNGSS-NATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSN 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 675886812  511 GYFEGNEIHDNRIAGFEVKAGANPTVVKCHIHHGQTGGIYVHENG-RGQFMENKIHSNNFAGIWVTSNSD-PTIRRNEI 587
Cdd:pfam13229  80 NLIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSnNVTISNNTVTNNKGAGILIVGGSSnNTVENNTF 158
F-box_FBXO11 cd22091
F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called ...
 153-197 1.51e-21

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: 88.25  E-value: 1.51e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 675886812 153 QNELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKLY 197
Cdd:cd22091    1 QEELPDEVLLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWKRLY 45
UBR-box_UBR4_5_6_7 cd19671
UBR-box found in UBR4, UBR5, UBR6/FBOX11, UBR7 and similar proteins; This family includes UBR4 ...
 882-946 1.84e-19

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: 82.89  E-value: 1.84e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675886812 882 KISSYTSFPMHDFYRCRTCNTTDRNAICVNCIKTCHAGHVVEFIRHDRFFCDCGAGTlNNQCHLQ 946
Cdd:cd19671    3 FEKTGRKYIKQPWYHCYTCGLIDGLGVCEACARKCHKGHDLVYIGYSNFYCDCGSSG-PGKCKCE 66
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 616-847 5.73e-18

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: 86.51  E-value: 5.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 616 AGIQIRTGSNPIVRHNKIHHGQHGgIYVHEKGQGLIEENEVYSNtlagvwittnsqpilRKNRIHSGkqVGVYFYDNGHG 695
Cdd:COG3420   99 AGIYVRGADNAVIENNRIENNLFG-IYLEGSDNNVIRNNTISGN---------------RDLRADRG--NGIHLWNSPGN 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 696 TLEDNDIFNHlYSGVQIRTGSCPVIKRNKIWGGQNGgILVYNGGLGVIENNEIFDNAmAGVWIKTDSNPTLRHNKIHDGR 775
Cdd:COG3420  161 VIEGNTISGG-RDGIYLEFSDNNVIRNNTIRNLRYG-IHYMYSNDNLVEGNTFRDNG-AGIALMYSKGNTVRGNTILGNS 237

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 675886812 776 DGGVCIFNGGKGILESNEIFRNTQaGVLISNQSHPTLINNRIYDGmAAGIEITNNAtatlEGNKIFNNKFGG 847
Cdd:COG3420  238 GYGILLKESSDSVIEGNTISGNGK-GIFIYNSNRNTIRGNLFAGN-GIGIHLTAGS----EGNRIYGNNFIG 303
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 456-615 1.06e-17

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


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 81.30  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  456 GLFITDHAQGTYDYNEICRNALAGVWVKNHANPIMRNNHIHHGRDVGIFTFDNGLGYFEGNEIHDNRIAGFEVKAGANPT 535
Cdd:pfam13229   2 GILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNNL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  536 VVKCHIHHGQTGGIYVHENGRGQFMENKIHSNNFAGIWVTSNSD-PTIRRNEIFNGHQGGVYIFGEGRglieYNDIHGNA 614
Cdd:pfam13229  82 IENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNnVTISNNTVTNNKGAGILIVGGSS----NNTVENNT 157


                  .
gi 675886812  615 L 615
Cdd:pfam13229 158 F 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 754-866 2.78e-17

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


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 80.14  E-value: 2.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  754 AGVWIKTDSNPTLRHNKIHDGRDGGVCIFNGGKGILESNEIFRNTQAGVLISNQSHPTLINNRIYDGMAAGIEITNNATA 833
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 675886812  834 TLEGNKIFNNKFGGLCLASGVHPFTKDNVIYDN 866
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNN 113
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 154-197 1.39e-15

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 71.36  E-value: 1.39e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 675886812  154 NELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKLY 197
Cdd:pfam12937   2 SSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
UBR-box cd19669
UBR-box found in UBR family of E3 ubiquitin ligases (UBR1-7) and similar proteins; The UBR-box ...
 894-941 1.49e-14

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


Pssm-ID: 439067  Cd Length: 66  Bit Score: 69.08  E-value: 1.49e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 675886812 894 FYRCRTCNTTDRNAICVNCIKTCHAGHVVEFIRHDRFFCDCGAGTLNN 941
Cdd:cd19669   12 MYHCLTCSLDDNSGICEECAKKCHEGHDVVYIGSGSGFCDCGDSSAKS 59
UBR-box_UBR4_like cd19674
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3. ...
 877-944 6.32e-14

UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3.2.27; also called 600 kDa retinoblastoma protein-associated factor, N-recognin-4, retinoblastoma-associated factor of 600 kDa, RBAF600, p600, or zinc finger UBR1-type protein 1) is a RING-type E3 ubiquitin ligase of the Arg/N-end rule degradation pathway. It recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR4 acts as a multifunctional protein with roles in anoikis, viral transformation, and protein degradation, as well as in neurogenesis, neuronal migration, neuronal signaling, and survival. 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: 67.37  E-value: 6.32e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 675886812 877 GQCLYKISSyTSFPMHDFYRCRTCNTTDRNAICVNCIKTCHAGHVVEFIRHDRFFCDCGAGTLNNQCH 944
Cdd:cd19674    1 NVCTFASTG-KNYARQHWYECYTCFLNGNEGVCEVCARVCHKGHDLVYSKTSSFFCDCGAGGGPSKCK 67
UBR-box_BIG_like cd19681
UBR-box found in Arabidopsis thaliana auxin transport protein BIG and similar proteins; BIG ...
 879-938 1.13e-13

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: 67.05  E-value: 1.13e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 879 CLYkISSYTSFPMHDFYRCRTCNTTDRNAICVNCIKTCHAGHVVEFIRHDRFFCDCGAGT 938
Cdd:cd19681    3 CTY-VSSGSNFMEQHWYFCYTCGLVDSKGCCSVCAKVCHRGHDVVYSRYSRFFCDCGAGG 61
F-box_unchar cd22139
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 ...
 156-196 5.50e-13

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


Pssm-ID: 438911  Cd Length: 45  Bit Score: 63.80  E-value: 5.50e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKL 196
Cdd:cd22139    4 LPDELWLHIFSFLSPKDLCQVALVCRRFNRLASDESLWKQI 44
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 708-866 1.41e-12

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


Pssm-ID: 428281 [Multi-domain]  Cd Length: 215  Bit Score: 67.83  E-value: 1.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  708 SGVQIRTGSCPVIKRNKIWGGQNGGILVYNGGlGVIENNEIFDNaMAGVWIKTDSNPTLRHNKIHDGRDGgVCIFNGGKG 787
Cdd:pfam05048  20 NGIQLWNTEGNVISNNDIINSRDGIYLDASNN-NTITGNRISNL-RYGIHLMNSNDNTISDNVFSGNTAG-IALMSSSNN 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 675886812  788 ILESNEIFRNTQAGVLISNQSHPTLINNRIYDGMAAGIEITNNATATLEGNKIFNNKFGGLCLASGvhpftKDNVIYDN 866
Cdd:pfam05048  97 TLENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRITSNGIGIHFLAGS-----NGNTIYNN 170
UBR-box_UBR4 cd19680
UBR-box found in RING-type E3 ubiquitin-protein ligase UBR4 and similar proteins; UBR4 (EC 2.3. ...
 882-936 1.40e-11

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: 60.93  E-value: 1.40e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 675886812 882 KISSYT----SFPMHDFYRCRTCNTTDRNAICVNCIKTCHAGHVVEFIRHDRFFCDCGA 936
Cdd:cd19680    1 KLCTFTitqkEFMNQHWYHCHTCKMVDGVGVCSVCAKVCHKDHDLSYAKYGSFFCDCGA 59
F-box_FBXO15 cd22093
F-box domain found in F-box only protein 15 (FBXO15) and similar proteins; FBXO15, also called ...
 156-197 2.50e-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: 59.19  E-value: 2.50e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKLY 197
Cdd:cd22093    4 LPSEILLKILSYLDASSLLCISCVNKLFYQLANDNALWRKLY 45
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 660-866 3.56e-11

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


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 65.71  E-value: 3.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 660 TLAGVWITtNSqpilrkNRIHSGKQVGVYFYDNGHGTLEDNDIFNHLYsGVQIRTGSCPVIKRNKIWGGQNG------GI 733
Cdd:COG3420   81 TVRGLTIT-GS------GDSLTDDDAGIYVRGADNAVIENNRIENNLF-GIYLEGSDNNVIRNNTISGNRDLradrgnGI 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 734 LVYNGGLGVIENNEIFDNAmAGVWIKTDSNPTLRHNKIHDGRDGgVCIFNGGKGILESNeIFRNTQAGVLISNQSHPTLI 813
Cdd:COG3420  153 HLWNSPGNVIEGNTISGGR-DGIYLEFSDNNVIRNNTIRNLRYG-IHYMYSNDNLVEGN-TFRDNGAGIALMYSKGNTVR 229

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 675886812 814 NNRIYDGMAAGIEITNNATATLEGNKIFNNKFgGLCLASGVHPFTKDNVIYDN 866
Cdd:COG3420  230 GNTILGNSGYGILLKESSDSVIEGNTISGNGK-GIFIYNSNRNTIRGNLFAGN 281
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 331-663 4.26e-11

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


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 65.71  E-value: 4.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 331 TIIFIHPGTYSKRLSITSNVILIGAGpgnvadhviierqseSAVLFSEGAKQAylgyVTIKfspsAPssvphhkhyslEV 410
Cdd:COG3420   35 DTIEVPPGTYEGNIVIDKPLTLIGEG---------------GAVIDGGGKGTV----ITIT----AD-----------NV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 411 TdnsspiVDHCTV----KSFSVVGAAVCVSGSGaDPHIKHCNISDCenvglfitdhaqgtydyneicrnaLAGVWVKNHA 486
Cdd:COG3420   81 T------VRGLTItgsgDSLTDDDAGIYVRGAD-NAVIENNRIENN------------------------LFGIYLEGSD 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 487 NPIMRNNHIHhGRDVGIFTFDNG--LGYFEGNEIHDNRIA----GFEVKAGANPTVVKCHIHHGQTGgiyVHengrgqFM 560
Cdd:COG3420  130 NNVIRNNTIS-GNRDLRADRGNGihLWNSPGNVIEGNTISggrdGIYLEFSDNNVIRNNTIRNLRYG---IH------YM 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 561 ---ENKIHSNNF----AGIWVTSNSDPTIRRNEIFNGHQGGVYIFGEGRGLIEYNDIHGNALaGIQIRTGSNPIVRHNKI 633
Cdd:COG3420  200 ysnDNLVEGNTFrdngAGIALMYSKGNTVRGNTILGNSGYGILLKESSDSVIEGNTISGNGK-GIFIYNSNRNTIRGNLF 278

                        330       340       350
                 ....*....|....*....|....*....|
gi 675886812 634 HHGQHgGIYVHekgqGLIEENEVYSNTLAG 663
Cdd:COG3420  279 AGNGI-GIHLT----AGSEGNRIYGNNFIG 303
F-box_FBXO3 cd22084
F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called ...
 154-201 1.91e-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: 56.88  E-value: 1.91e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 675886812 154 NELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKLYQNVF 201
Cdd:cd22084    2 DDLPSDPLLNILSFLDYRDLISCSQVCRRLNQLCSHDPLWKRLCKKYW 49
F-box_FBXW5 cd22132
F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, ...
 156-198 5.28e-10

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


Pssm-ID: 438904 [Multi-domain]  Cd Length: 46  Bit Score: 55.70  E-value: 5.28e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKLYQ 198
Cdd:cd22132    4 LPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLWKELFY 46
F-box_FBXL1 cd22114
F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also ...
 154-193 6.56e-10

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: 55.11  E-value: 6.56e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 675886812 154 NELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELW 193
Cdd:cd22114    2 DSLPDELLLGIFSCLCLPDLLKVSQVCKRWYRLASDESLW 41
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 154-188 2.01e-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: 53.60  E-value: 2.01e-09
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 675886812 154 NELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVAN 188
Cdd:cd09917    1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35
ZnF_UBR1 smart00396
Putative zinc finger in N-recognin, a recognition component of the N-end rule pathway; Domain ...
 882-935 2.69e-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: 54.37  E-value: 2.69e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 675886812   882 KISSYTSFPMHDFYRCRTCNTTDRNAICVNC-IKTCHAGHVVEFIRHDR-FFCDCG 935
Cdd:smart00396   1 DVCGYKFTGGEVIYRCKTCGLDPTCVLCSDCfRPSCHKGHDVSLKTSRGsGICDCG 56
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 617-773 5.42e-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: 57.43  E-value: 5.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  617 GIQIRTGSNPIVRHNKIHHGqHGGIYVHEKGQGLIEENeVYSNTLAGVWITTNSQPILRKNRIhSGKQVGVYFYDNGHGT 696
Cdd:pfam05048  21 GIQLWNTEGNVISNNDIINS-RDGIYLDASNNNTITGN-RISNLRYGIHLMNSNDNTISDNVF-SGNTAGIALMSSSNNT 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 675886812  697 LEDNDIFNHLYSGVQIRTGSCPVIKRNKIWGGQNGGILVYNGGLGVIENNEIFDNAmAGVWIKTDSNptlrHNKIHD 773
Cdd:pfam05048  98 LENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRITSNG-IGIHFLAGSN----GNTIYN 169
F-box_FBXW12 cd22137
F-box domain found in F-box/WD repeat-containing protein 12 (FBXW12) and similar proteins; ...
 155-196 6.12e-09

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: 52.38  E-value: 6.12e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 675886812 155 ELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKL 196
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. ...
 895-946 9.93e-09

UBR-box found in RING-type E3 ubiquitin-protein ligase UBR7 and similar proteins; UBR7 (EC 2.3.2.27; also called N-recognin-7) is a RING-type E3 ubiquitin ligase of the Arg/N-end rule degradation pathway. It recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR7 may play an important role in spermiogenesis and fertilization.


Pssm-ID: 439075  Cd Length: 71  Bit Score: 52.70  E-value: 9.93e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 675886812 895 YRCRTCN---TTDRNAICVNCIKTCHAGH-VVEFIRHDRFFCDCG-AGTLNNQCHLQ 946
Cdd:cd19677   14 YACLTCTpagADQPAGICLACSLSCHEGHeLEELYTKRNFRCDCGnSKFPSNPCKLF 70
F-box_FBXL5 cd22118
F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also ...
 156-193 2.25e-08

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: 50.80  E-value: 2.25e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELW 193
Cdd:cd22118    4 LPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41
F-box_FBXO13 cd22092
F-box domain found in F-box only protein 13 (FBXO13) and similar proteins; FBXO13, also called ...
 153-196 4.70e-08

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


Pssm-ID: 438864  Cd Length: 49  Bit Score: 50.11  E-value: 4.70e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 675886812 153 QNELPDEVLLKIFSYL-LEFDLSNVATVCKRFNAVANDSELWKKL 196
Cdd:cd22092    2 INQLPDSILLKIFSYLsLQERCLSASLVCKYWRDLCLDSQFWKQI 46
F-box_FBXL12 cd22123
F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also ...
 154-194 4.94e-08

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: 49.66  E-value: 4.94e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 675886812 154 NELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWK 194
Cdd:cd22123    2 DQLPENVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLWR 42
FBOX smart00256
A Receptor for Ubiquitination Targets;
156-196 5.39e-08

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 49.74  E-value: 5.39e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 675886812   156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKL 196
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41
zf-UBR pfam02207
Putative zinc finger in N-recognin (UBR box); This region is found in E3 ubiquitin ligases ...
 894-935 5.67e-08

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: 50.37  E-value: 5.67e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 675886812  894 FYRCRTCNTTDRNAICVNCIKTC-HAGHVVEFIRHDR-FFCDCG 935
Cdd:pfam02207  11 VYRCLTCSLDPTCVICYSCFINCdHEGHDYELFTSRGgGCCDCG 54
F-box_FBXO7 cd22087
F-box domain found in F-box only protein 7 (FBXO7) and similar proteins; FBXO7, also called ...
 156-197 1.10e-07

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: 48.83  E-value: 1.10e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKLY 197
Cdd:cd22087    4 LPPEIKLRILSLLDVRSLLSLSQVCRDLNSATNDQLLWRFLL 45
F-box_DmSKP2-like cd22149
F-box domain found in Drosophila melanogaster S-phase kinase-associated protein 2 (DmSKP2) and ...
 156-195 1.73e-07

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: 48.52  E-value: 1.73e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKK 195
Cdd:cd22149    4 LSDEIILSIFKWLPKKTLARCARVCRRWKRLCFDESLWRR 43
F-box_FBXO36 cd22106
F-box domain found in F-box only protein 36 (FBXO36) and similar proteins; FBXO36, also called ...
 156-198 2.41e-07

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: 47.96  E-value: 2.41e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 675886812 156 LPDEVLLKIFSYL-LEfDLSNVATVCKRFNAVANDSELWKKLYQ 198
Cdd:cd22106    4 LPDKLLLYIISYLdLE-DIARLSQTSKRFKKLCNSDELWEKIYM 46
F-box_FBXO21 cd22096
F-box domain found in F-box only protein 21 (FBXO21) and similar proteins; FBXO21, also called ...
 154-198 2.63e-07

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


Pssm-ID: 438868  Cd Length: 48  Bit Score: 48.07  E-value: 2.63e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 675886812 154 NELPDEVLLKIFSYLL--EFDLSNVATVCKRFNAVANDSELWKKLYQ 198
Cdd:cd22096    2 LELPDELLEYILCSDNldHHDIIRLSCTCRRLREVCQSGKVWREKFF 48
F-box_AtSKIP31-like cd22166
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 31 (AtSKIP31) and similar ...
 156-197 3.44e-07

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: 47.45  E-value: 3.44e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKLY 197
Cdd:cd22166    4 LPPELFRHILKFLSPEDLTSCATVCRFLRGAASDESLWRRLY 45
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 155-195 4.45e-07

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: 47.15  E-value: 4.45e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 675886812  155 ELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKK 195
Cdd:pfam00646   3 DLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWKK 43
F-box_FBXO31 cd22102
F-box domain found in F-box only protein 31 (FBXO31) and similar proteins; FBXO31, also called ...
 155-195 5.14e-07

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: 47.04  E-value: 5.14e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 675886812 155 ELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKK 195
Cdd:cd22102    3 DLPPELLVEIFSSLPGTDLPSLAQVCKKFREILNTDTIWQR 43
F-box_SpPof1-like cd22147
F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar ...
 156-196 9.46e-07

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: 9.46e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKL 196
Cdd:cd22147    5 LPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELWKRM 45
UBR-box_UBR1_2_3 cd19670
UBR-box found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), E3-alpha-3 ...
 894-935 1.20e-06

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: 46.59  E-value: 1.20e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 675886812 894 FYRCRTCNTTDRNAICVNC-IKTCHAGH-VVEFIRHDRFFCDCG 935
Cdd:cd19670   11 YYRCLDCSLDPSSCICEECfLNGNHEGHnYSLRTSSGGGVCDCG 54
F-box_FBXO9 cd22089
F-box domain found in F-box only protein 9 (FBXO9) and similar proteins; FBXO9, also called ...
 156-197 1.25e-06

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: 46.07  E-value: 1.25e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 675886812 156 LPDEVLLKIFSYLLEFD----LSNVATVCKRFNAVANDSELWKKLY 197
Cdd:cd22089    6 LPSEILLYILRWVVSDLdlrsLEQLSLVCRKFYLLARDPSIWRLAC 51
F-box_FBXL4 cd22117
F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also ...
 156-197 1.38e-06

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: 45.69  E-value: 1.38e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKLY 197
Cdd:cd22117    4 LPYELIQLILSYLDLPSLCRLSQTCKLFRKHCYDPLLWKELN 45
F-box_DdgacFF-like cd22148
F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) ...
 156-194 1.43e-06

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


Pssm-ID: 438919  Cd Length: 44  Bit Score: 45.74  E-value: 1.43e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWK 194
Cdd:cd22148    5 LPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELWK 43
F-box_FBXO18 cd22095
F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called ...
 154-196 1.77e-06

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


Pssm-ID: 438867  Cd Length: 48  Bit Score: 45.73  E-value: 1.77e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 675886812 154 NELPDEVLLKIFSYLLEFDL-SNVATVCKRFNAVANDSE--LWKKL 196
Cdd:cd22095    3 QQLPEELLRNIFAFLPAEDLyQNISLVCRHWRDIVSDPLfiPWKKL 48
F-box_FBXW4 cd20090
F-box domain found in F-box/WD repeat-containing protein 4 (FBXW4) and similar proteins; FBXW4, ...
 155-196 2.30e-06

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: 45.28  E-value: 2.30e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 675886812 155 ELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKL 196
Cdd:cd20090    4 DLPDDLLFLIFSYLDPASLGRLSQVCRRLYRLISRDAVWRRI 45
F-box_AtSKIP5-like cd22163
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 5 (AtSKIP5) and similar ...
 154-193 3.84e-06

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


Pssm-ID: 438934  Cd Length: 46  Bit Score: 44.64  E-value: 3.84e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 675886812 154 NELPDEVLLKIFSYLLEF-DLSNVATVCKRFNAVANDSELW 193
Cdd:cd22163    2 NDLDDDCLMHIFSFLTPLpDRFNAARVCKRWRALALDPRSW 42
F-box_FBXO28 cd22100
F-box domain found in F-box only protein 28 (FBXO28) and similar proteins; FBXO28, also called ...
 154-189 4.02e-06

F-box domain found in F-box only protein 28 (FBXO28) and similar proteins; FBXO28, also called FBX28, 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 promotes mitotic progression and regulates topoisomerase IIalpha-dependent DNA decatenation. FBXO28 plays a crucial role in the pathogenesis of the 1q41q42 microdeletion syndrome. 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: 438872  Cd Length: 45  Bit Score: 44.46  E-value: 4.02e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 675886812 154 NELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVAND 189
Cdd:cd22100    2 LELPDEIIEKILSYLSYDEISKLRLVCRRFNEVCQR 37
F-box_JHDM cd22122
F-box domain found in the JmjC domain-containing histone demethylation protein (JHDM) family; ...
 156-194 6.63e-06

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: 43.80  E-value: 6.63e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWK 194
Cdd:cd22122    4 LPREVWLPVFQYLSPKDLCVCMRVCKTWNRWCCDPSLWK 42
F-box_ScMFB1-like cd22146
F-box domain found in Saccharomyces cerevisiae mitochondrial F-box protein MFB1 (ScMFB1) and ...
 155-194 6.77e-06

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


Pssm-ID: 438917  Cd Length: 42  Bit Score: 43.78  E-value: 6.77e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 675886812 155 ELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWK 194
Cdd:cd22146    3 GLPLEILFEILIYLDIPDILNLSKTCRFLYVLLNDEILWR 42
F-box_FBXO41 cd22109
F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called ...
 158-197 8.55e-06

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: 43.47  E-value: 8.55e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 675886812 158 DEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKLY 197
Cdd:cd22109    8 RDALFCVFSYLDTKSLLRCAEVCREWRDVSRHPALWQRVC 47
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
 154-186 1.28e-05

F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), coronatine-insensitive protein 1 (COI1) and similar proteins; TIR1, also called F-box/LRR-repeat protein 1 (FBL1), is part of an SCF (SKP1-cullin-F-box) protein ligase complex that promotes the ubiquitin-dependent proteolysis of a family of transcriptional regulators known as Aux/IAAs in an auxin-dependent manner. TIR1 is an auxin receptor that plays a potential role in plant hormone signaling. COI1, also called F-box/LRR-repeat protein 2 (FBL2), is the substrate-recruiting module of an SCF ubiquitin E3 ligase complex. It mediates jasmonate signalling by promoting hormone-dependent ubiquitylation and degradation of transcriptional repressor JASMONATE ZIM-domain (JAZ) family proteins. This subfamily also includes Arabidopsis thaliana EIN3-binding F-box protein 1 (EBF1). EBF1, also called F-box/LRR-repeat protein 6 (FBL6), is a component of the SCF(EBF1) E3 ubiquitin ligase complex, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (probably including EIN3 and EIL1). 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: 438930  Cd Length: 40  Bit Score: 42.84  E-value: 1.28e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 675886812 154 NELPDEVLLKIFSYLLE-FDLSNVATVCKRFNAV 186
Cdd:cd22159    2 DLLPDEILELIFSYLSDpWDRNSCSLVCKRWYRL 35
F-box_AtGID2-like cd22151
F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, ...
 156-197 1.81e-05

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


Pssm-ID: 438922  Cd Length: 44  Bit Score: 42.69  E-value: 1.81e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKLY 197
Cdd:cd22151    3 LPDDLLQEIFKRLDPKSLARAACVCRRWRAAARSESLWENAC 44
F-box_ScCDC4-like cd22141
F-box domain found in Saccharomyces cerevisiae cell division control protein 4 (ScCDC4) and ...
 156-196 2.36e-05

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: 42.55  E-value: 2.36e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKL 196
Cdd:cd22141    4 LPFEISLKIFNYLQFEDLLNSLGVSKKWNKIIRNTALWKKL 44
CASH smart00722
Domain present in carbohydrate binding proteins and sugar hydrolses;
467-598 2.63e-05

Domain present in carbohydrate binding proteins and sugar hydrolses;


Pssm-ID: 214788  Cd Length: 153  Bit Score: 45.19  E-value: 2.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812   467 YDYNEICRNALAGVWVKNHANPiMRNNHIHHGRDV--------GIFTFDNGLGYFEGNEIHDNRIAGFEVKAGANPTVVK 538
Cdd:smart00722  14 VHYMYTSDIGGSGGAVIDMGSG-RGSNITINSNDVrvdgvtigGDGNAVTGIYVSASGDPVIQNDGTGKNLIIDNVTFNG 92

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 675886812   539 CHIHHGqtGGIYVHENGRGQFMENKIHSNNFA---GIWVTSNSDPTIRRNEIFNGHQGGVYIF 598
Cdd:smart00722  93 TEINSG--AGIVVTAGSEGLFIGNRIIGNYVAtgdGNYLSDSSGGDLIGNRIYDNNRDGIAVV 153
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 448-613 3.59e-05

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


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 47.22  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 448 NISDCENVGLFITDHAQGTYDYNEICRNAlAGVWVKNHANPIMRNNHIHHGRDVGIFTFDNGLGYFEGNEIHDNRIagfe 527
Cdd:COG3420  187 NTIRNLRYGIHYMYSNDNLVEGNTFRDNG-AGIALMYSKGNTVRGNTILGNSGYGILLKESSDSVIEGNTISGNGK---- 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812 528 vkaganptvvkchihhgqtgGIYVHENGRGQFMENKIhSNNFAGIWVTSNS-DPTIRRNE-IFNGHQggvyIFGEGRGLI 605
Cdd:COG3420  262 --------------------GIFIYNSNRNTIRGNLF-AGNGIGIHLTAGSeGNRIYGNNfIGNRTQ----VKYVGGRDN 316


                 ....*....
gi 675886812 606 EYN-DIHGN 613
Cdd:COG3420  317 EWSaDGRGN 325
F-box_AtSKIP22-like cd22165
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 22 (AtSKIP22) and similar ...
 156-197 4.30e-05

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


Pssm-ID: 438936  Cd Length: 46  Bit Score: 41.49  E-value: 4.30e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKLY 197
Cdd:cd22165    5 LPTELKLKILELLPGVDLARMACVCSELRFLASNDDLWKQKF 46
F-box_FBXO42 cd22110
F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called ...
 154-189 4.39e-05

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


Pssm-ID: 438882  Cd Length: 38  Bit Score: 41.55  E-value: 4.39e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 675886812 154 NELPDEVLLKIFSYLLEF-DLSNVATVCKRFNAVAND 189
Cdd:cd22110    2 NDLPEEILEYILSYLSPYgDLKSAALVCKRWHRIIKG 38
F-box_FBXL2-like cd22115
F-box domain found in F-box/LRR-repeat protein 2 (FBXL2), F-box/LRR-repeat protein 20 (FBXL20) ...
 156-194 6.15e-05

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: 41.25  E-value: 6.15e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWK 194
Cdd:cd22115    7 LPKELLLRIFSFLDVVTLCRCAQVSKYWNVLALDGSNWQ 45
UBR-box_UBR3 cd19673
UBR-box found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3 (EC 2.3. ...
 894-935 6.62e-05

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


Pssm-ID: 439071  Cd Length: 72  Bit Score: 41.79  E-value: 6.62e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 675886812 894 FYRCRTCNTTDRNAICVNCIK-TCHAGHVVEFIRHDRF-FCDCG 935
Cdd:cd19673   14 AYRCRTCGLDPTCVICADCFQaGDHEGHDYSMYRSSAGgCCDCG 57
F-box_ScMDM30-like cd22143
F-box domain found in Saccharomyces cerevisiae mitochondrial distribution and morphology ...
 154-196 8.69e-05

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


Pssm-ID: 438915  Cd Length: 44  Bit Score: 40.67  E-value: 8.69e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 675886812 154 NELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANdSELWKKL 196
Cdd:cd22143    3 DSLPDEILSIIFSHLPQSDLYNLLFVNKHFYSLAL-PELWRSI 44
F-box_FBXL7 cd22120
F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also ...
 156-196 9.02e-05

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: 40.83  E-value: 9.02e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKL 196
Cdd:cd22120    4 LPDDVILQIFSHLPTNQLCRCARVCRRWYNLAWDPRLWTTI 44
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 479-634 1.08e-04

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: 44.72  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812  479 GVWVKNHANPIMRNNHIHHGRDvGIFTFDNGLGYFEGNEIHDNRiAGFEVKAGANPTVVKCHIHHGqTGGIYVHENGRGQ 558
Cdd:pfam05048  21 GIQLWNTEGNVISNNDIINSRD-GIYLDASNNNTITGNRISNLR-YGIHLMNSNDNTISDNVFSGN-TAGIALMSSSNNT 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 675886812  559 FMENKIHSNNFAGIWVTSNSDPTIRRNEIFNGHQGGVYIFGEGRGLIEYNDIHGNAlAGIQIRTGSNpivrHNKIH 634
Cdd:pfam05048  98 LENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRITSNG-IGIHFLAGSN----GNTIY 168
F-box_FBXL21 cd22179
F-box domain found in F-box/LRR-repeat protein 21 (FBXL21) and similar proteins; FBXL21, also ...
 156-193 1.48e-04

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


Pssm-ID: 438950  Cd Length: 43  Bit Score: 40.28  E-value: 1.48e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELW 193
Cdd:cd22179    6 LPHHVVLHIFQYLPLVDRARASSVCRRWNEVFHIPDLW 43
F-box_unchar cd22138
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 ...
 154-194 1.55e-04

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


Pssm-ID: 438910  Cd Length: 45  Bit Score: 40.01  E-value: 1.55e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 675886812 154 NELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWK 194
Cdd:cd22138    2 QSLPVECQLKIFSFLSEVDKCLAATVCRSWSELIRSPRLWR 42
F-box_FBXW9 cd22135
F-box domain found in F-box/WD repeat-containing protein 9 (FBXW9) and similar proteins; FBXW9, ...
 156-194 3.94e-04

F-box domain found in F-box/WD repeat-containing protein 9 (FBXW9) and similar proteins; FBXW9, also called F-box and WD-40 domain-containing protein 9, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438907  Cd Length: 45  Bit Score: 38.80  E-value: 3.94e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 675886812 156 LPDEVLLKIFSYL-LEFDLSNVATVCKRFNAVANDSELWK 194
Cdd:cd22135    4 LPPELLLHICSYLdARFVLHVLPLVCKTFRDILSDETTWR 43
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
 156-196 4.75e-04

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


Pssm-ID: 438876  Cd Length: 48  Bit Score: 38.78  E-value: 4.75e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKL 196
Cdd:cd22104    4 LPSVVLVHIFSYLPPRDRLRASSTCRRWREALFHPSLWRSL 44
F-box_FBXL6 cd22119
F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also ...
 154-194 5.23e-04

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


Pssm-ID: 438891  Cd Length: 47  Bit Score: 38.77  E-value: 5.23e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 675886812 154 NELPDEVLLKIFSYLLEFD-----LSNVATVCKRFNAVANDSELWK 194
Cdd:cd22119    2 QRLPPEILVKIFQFAVATEgavplLCRLSRVCRLWREVALDPSLWT 47
F-box_FBXO39 cd22108
F-box domain found in F-box only protein 39 (FBXO39) and similar proteins; FBXO39, also called ...
 155-194 5.60e-04

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


Pssm-ID: 438880  Cd Length: 44  Bit Score: 38.55  E-value: 5.60e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 675886812 155 ELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWK 194
Cdd:cd22108    3 NLPDVCLRHVFRWLGDRDRSRAALVCKRWNQAMYSPALWR 42
F-box_AtADO-like cd22154
F-box domain found in Arabidopsis thaliana Adagio proteins (AtADO1/2/3) and similar proteins; ...
 155-194 5.69e-04

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


Pssm-ID: 438925  Cd Length: 47  Bit Score: 38.62  E-value: 5.69e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 675886812 155 ELPDEVL-LKIFSYLLEFDLSNVATVCKRFNAVANDSELWK 194
Cdd:cd22154    4 QLSDEVLaQKILSRLTPRDVASVGSVCRRLYELTKNEDLWR 44
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 155-193 5.72e-04

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


Pssm-ID: 438896  Cd Length: 42  Bit Score: 38.47  E-value: 5.72e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 675886812 155 ELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELW 193
Cdd:cd22124    3 LLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLW 41
CASH smart00722
Domain present in carbohydrate binding proteins and sugar hydrolses;
685-827 7.40e-04

Domain present in carbohydrate binding proteins and sugar hydrolses;


Pssm-ID: 214788  Cd Length: 153  Bit Score: 40.95  E-value: 7.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812   685 VGVYFYDNGHGTLEDNDIFNHLYSGVQIRTGSCPVI------KRNKIWGGQNGGILVYNGGLGVIENNEIFDNAMAGVWI 758
Cdd:smart00722   3 NGTVLELLRGAVHYMYTSDIGGSGGAVIDMGSGRGSnitinsNDVRVDGVTIGGDGNAVTGIYVSASGDPVIQNDGTGKN 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 675886812   759 KTDSNPTlrHNKIHDGRDGGVCIFNGGKGILESNEIFRNTQA---GVLISNQSHPTLINNRIYDGMAAGIEI 827
Cdd:smart00722  83 LIIDNVT--FNGTEINSGAGIVVTAGSEGLFIGNRIIGNYVAtgdGNYLSDSSGGDLIGNRIYDNNRDGIAV 152
F-box_FBXL3 cd22178
F-box domain found in F-box/LRR-repeat protein 3 (FBXL3) and similar proteins; FBXL3, also ...
 155-193 8.48e-04

F-box domain found in F-box/LRR-repeat protein 3 (FBXL3) and similar proteins; FBXL3, also called F-box and leucine-rich repeat protein 3A, or F-box/LRR-repeat protein 3A, is the substrate-recognition component of the SCF(FBXL3) E3 ubiquitin ligase complex that mainly acts in the nucleus and mediates ubiquitination and subsequent degradation of CRY1 and CRY2, and thus, is involved in circadian rhythm function. It plays a key role in the maintenance of both the speed and the robustness of the circadian clock oscillation. 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: 438949  Cd Length: 43  Bit Score: 37.96  E-value: 8.48e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 675886812 155 ELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELW 193
Cdd:cd22178    5 NLLQDIILQIFQYLPLLDRAHASQVCRNWNQVFHMPDLW 43
UBR-box_UBR5 cd19675
UBR-box found in HECT-type E3 ubiquitin-protein ligase UBR5 and similar proteins; UBR5 (EC 2.3. ...
 893-934 9.44e-04

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


Pssm-ID: 439073  Cd Length: 76  Bit Score: 38.99  E-value: 9.44e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 675886812 893 DFYRCRTCNTTDRNAICVNCIKTCHAGHVVEFIRHD-RFFCDC 934
Cdd:cd19675   22 DIFECRTCGLVGSLCCCTECARVCHKGHDCKLKRTSpTAYCDC 64
F-box_FBXW8 cd22134
F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, ...
 155-196 9.80e-04

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


Pssm-ID: 438906  Cd Length: 48  Bit Score: 37.74  E-value: 9.80e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 675886812 155 ELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKL 196
Cdd:cd22134    6 QLPRELALKIFQYLSVTDLCRCAQVSKSWKSLAEDELLWYRI 47
F-box_FBXO48 cd22113
F-box domain found in F-box only protein 48 (FBXO48) and similar proteins; FBXO48, also called ...
 154-196 1.37e-03

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: 37.30  E-value: 1.37e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 675886812 154 NELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSE-LWKKL 196
Cdd:cd22113    2 ELLPPEMSLRIFSQLDVQSLCRASQTCKTWNDLIENSDyLWRPH 45
F-box_FBXO6-like cd22168
F-box domain found in F-box only proteins FBXO6, FBXO44 and similar proteins; This subfamily ...
 154-220 1.44e-03

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


Pssm-ID: 438939 [Multi-domain]  Cd Length: 82  Bit Score: 38.42  E-value: 1.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 675886812 154 NELPDEVLLKIFSYLLEFDL-SNVATVCKRFNAVANDSELWKKLYQNVFEYDLPLTTSALEFGIFKFI 220
Cdd:cd22168    5 SDLPEDVLLEILSLVPARDLiLSCRLVCSRWRDLVDLPTLWKRKCQREGFILKDWDGPPKDWKIFYFL 72
F-box_D3-like cd22140
F-box domain found in Oryza sativa F-box/LRR-repeat Max2 homolog (D3) and similar proteins; D3 ...
 156-190 1.46e-03

F-box domain found in Oryza sativa F-box/LRR-repeat Max2 homolog (D3) and similar proteins; D3 is the ortholog of Arabidopsis MORE AXILLARY GROWTH2 (MAX2) and DWARF14 (AtD14) in rice. These proteins are essential signaling components to regulate strigolactone (SL)-repressed plant branching. In rice shoot branching inhibition, the SL-metabolizing alpha/beta hydrolase D14 interacts with the F-box protein D3 to ubiquitinate and degrade the transcription repressor D53. 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: 438912  Cd Length: 38  Bit Score: 36.96  E-value: 1.46e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDS 190
Cdd:cd22140    4 LPEDLLLHILSFLNLRDRLNLSLTCKRLRALAYSD 38
F-box_FBXO45 cd22111
F-box domain found in F-box only protein 45 (FBXO45) and similar proteins; FBXO45, also called ...
 156-188 2.76e-03

F-box domain found in F-box only protein 45 (FBXO45) and similar proteins; FBXO45, also called FBX45, or F-box/SPRY domain-containing protein 1, functions as the substrate-recognition component of E3 ubiquitin ligase complexes. It is critical for synaptogenesis, neuronal migration, and synaptic transmission. 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: 438883  Cd Length: 36  Bit Score: 36.11  E-value: 2.76e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVAN 188
Cdd:cd22111    4 LPSRVLEVIFSYLDLPDLRNCSLVCKSWYRLLN 36
F-box_FBXO34-like cd22105
F-box domain found in F-box only protein 34 (FBXO34), F-box only protein 46 (FBXO46) and ...
 156-192 4.55e-03

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


Pssm-ID: 438877  Cd Length: 47  Bit Score: 35.84  E-value: 4.55e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 675886812 156 LPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSEL 192
Cdd:cd22105    4 LPDHVLSKIFSHLPTRSLAALKCTCKDFKWLIEMFDV 40
F-box_FBXO1 cd22082
F-box domain found in F-box only protein 1 (FBXO1) and similar proteins; FBXO1, also called ...
 155-193 5.00e-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: 5.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 675886812 155 ELPDEVLLKIFSYLLEFDLSNVATVCKRF-NAVANDSELW 193
Cdd:cd22082    4 SLPEEVLLHILKGLPIKDLLNMRAVHSRFkDLIDSNPSLW 43
PemB COG4677
Pectin methylesterase and related acyl-CoA thioesterases [Carbohydrate transport and ...
 328-366 7.04e-03

Pectin methylesterase and related acyl-CoA thioesterases [Carbohydrate transport and metabolism, Lipid transport and metabolism];


Pssm-ID: 443713 [Multi-domain]  Cd Length: 307  Bit Score: 39.82  E-value: 7.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 675886812 328 KRPTIIFIHPGTYSKRLSITS---NVILIGAGPgnvaDHVII 366
Cdd:COG4677   44 TERTTIYIKNGVYREKLVIPSnkpNITLIGEDR----DKTII 81
CASH smart00722
Domain present in carbohydrate binding proteins and sugar hydrolses;
658-782 7.79e-03

Domain present in carbohydrate binding proteins and sugar hydrolses;


Pssm-ID: 214788  Cd Length: 153  Bit Score: 38.26  E-value: 7.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675886812   658 SNTLAGVWITTNSQPILRKNRIHS--GKQVGVYFYD-----NGHGTLEDNDIFNHLYSGVQIRTGSCPVIKRNKIWGGqn 730
Cdd:smart00722  21 DIGGSGGAVIDMGSGRGSNITINSndVRVDGVTIGGdgnavTGIYVSASGDPVIQNDGTGKNLIIDNVTFNGTEINSG-- 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 675886812   731 GGILVYNGGLGVIENNEIFDNAMA---GVWIKTDSNPTLRHNKIHDGRDGGVCIF 782
Cdd:smart00722  99 AGIVVTAGSEGLFIGNRIIGNYVAtgdGNYLSDSSGGDLIGNRIYDNNRDGIAVV 153
F-box_FBXO24 cd22098
F-box domain found in F-box only protein 24 (FBXO24) and similar proteins; FBXO24, also called ...
 155-196 8.51e-03

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: 35.38  E-value: 8.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 675886812 155 ELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWKKL 196
Cdd:cd22098    4 DLPPEILDRIISFLPVKDIVSLGQTCRYFHEVCNSEAVWRRL 45
F-box_FBXO16-like cd22094
F-box domain found in F-box only protein 16 (FBXO16), epithelial cell-transforming sequence 2 ...
 155-194 9.60e-03

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: 35.11  E-value: 9.60e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 675886812 155 ELPDEVLLKIFSYLLEFDLSNVATVCKRFNAVANDSELWK 194
Cdd:cd22094    5 VLPRFLSLYIFSYLDPRSLCRAAQVSWYWKFLCESDELWL 44
 
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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