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Conserved domains on  [gi|2217376746|ref|XP_047279177|]
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F-box only protein 10 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F-box_FBXO10 cd22090
F-box domain found in F-box only protein 10 (FBXO10) and similar proteins; FBXO10, also called ...
 2-51 4.28e-28

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


:

Pssm-ID: 438862  Cd Length: 50  Bit Score: 107.05  E-value: 4.28e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217376746   2 EAGGLPLELWRMILAYLHLPDLGRCSLVCRAWYELILSLDSTRWRQLCLG 51
Cdd:cd22090     1 EVTGLPLELWRLILAYLPVRDLCRCCQVCRAWYELILSLDSTRWKQLYLG 50
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 464-610 1.78e-22

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


:

Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 94.78  E-value: 1.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 464 YAVRCIHNSKIIMLRNDIYRCRASGIFLRLEGGGLIAGNNIYHNAEAGVDIRKKSNPLILCNQIHHGLRSGIVVLGNGKG 543
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217376746 544 IIRNNQIFSNKEAGIYILYHGNPVVSGNHIFKGRAAGIAVNENGKGL-ITENVIRENQWGGVDIRRGG 610
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIVGGS 148
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 602-797 6.73e-15

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


:

Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 73.21  E-value: 6.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 602 GGVDIRRGGIPVLRSNLICFGYSDGVVVGDEGKGLIEGNTIYANKGCGVWMMSSSLPHVTSNHVSYNGLYGVAVFsqkdG 681
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALR----G 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 682 SSELprghraqenfsedgdailwetelekeddplrrpitiaLVESNSINHNGASGLYVQSSEALHVITNVIHANGDRGIT 761
Cdd:pfam13229  77 SSNN-------------------------------------LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIV 119

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2217376746 762 VAQSSQPTRVANNSISCNRQSGVKVEAQC-KVELRGN 797
Cdd:pfam13229 120 IEDSSNNVTISNNTVTNNKGAGILIVGGSsNNTVENN 156
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 735-893 1.75e-14

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


:

Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 72.05  E-value: 1.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 735 SGLYVQSSEALHVITNVIHANGDRGITVAQSSQPTrVANNSISCNRQSGVKVEAQCKVELRGNGIYDNRGHGI-ITKGDS 813
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNAT-IENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIaLRGSSN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 814 TIVIENDIIGNRGSGLQLLPRSDTKVIKNRIHSFRAYGIAV-RGRAKALVQENIIFQGKtsKTIFQQISNNRECIMQNNK 892
Cdd:pfam13229  80 NLIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIeDSSNNVTISNNTVTNNK--GAGILIVGGSSNNTVENNT 157


                  .
gi 2217376746 893 F 893
Cdd:pfam13229 158 F 158
 
Name Accession Description Interval E-value
F-box_FBXO10 cd22090
F-box domain found in F-box only protein 10 (FBXO10) and similar proteins; FBXO10, also called ...
 2-51 4.28e-28

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


Pssm-ID: 438862  Cd Length: 50  Bit Score: 107.05  E-value: 4.28e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217376746   2 EAGGLPLELWRMILAYLHLPDLGRCSLVCRAWYELILSLDSTRWRQLCLG 51
Cdd:cd22090     1 EVTGLPLELWRLILAYLPVRDLCRCCQVCRAWYELILSLDSTRWKQLYLG 50
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 464-610 1.78e-22

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


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 94.78  E-value: 1.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 464 YAVRCIHNSKIIMLRNDIYRCRASGIFLRLEGGGLIAGNNIYHNAEAGVDIRKKSNPLILCNQIHHGLRSGIVVLGNGKG 543
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217376746 544 IIRNNQIFSNKEAGIYILYHGNPVVSGNHIFKGRAAGIAVNENGKGL-ITENVIRENQWGGVDIRRGG 610
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIVGGS 148
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 602-797 6.73e-15

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


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 73.21  E-value: 6.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 602 GGVDIRRGGIPVLRSNLICFGYSDGVVVGDEGKGLIEGNTIYANKGCGVWMMSSSLPHVTSNHVSYNGLYGVAVFsqkdG 681
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALR----G 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 682 SSELprghraqenfsedgdailwetelekeddplrrpitiaLVESNSINHNGASGLYVQSSEALHVITNVIHANGDRGIT 761
Cdd:pfam13229  77 SSNN-------------------------------------LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIV 119

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2217376746 762 VAQSSQPTRVANNSISCNRQSGVKVEAQC-KVELRGN 797
Cdd:pfam13229 120 IEDSSNNVTISNNTVTNNKGAGILIVGGSsNNTVENN 156
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 735-893 1.75e-14

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


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 72.05  E-value: 1.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 735 SGLYVQSSEALHVITNVIHANGDRGITVAQSSQPTrVANNSISCNRQSGVKVEAQCKVELRGNGIYDNRGHGI-ITKGDS 813
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNAT-IENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIaLRGSSN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 814 TIVIENDIIGNRGSGLQLLPRSDTKVIKNRIHSFRAYGIAV-RGRAKALVQENIIFQGKtsKTIFQQISNNRECIMQNNK 892
Cdd:pfam13229  80 NLIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIeDSSNNVTISNNTVTNNK--GAGILIVGGSSNNTVENNT 157


                  .
gi 2217376746 893 F 893
Cdd:pfam13229 158 F 158
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 528-781 2.54e-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: 66.09  E-value: 2.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 528 HHGLRSGIVVLGNGKGIIRNNQIFSNkEAGIYILYHGNPVVSGNHIfKGRAAGIAVNENG-------KGLITENVIRENQ 600
Cdd:COG3420    94 LTDDDAGIYVRGADNAVIENNRIENN-LFGIYLEGSDNNVIRNNTI-SGNRDLRADRGNGihlwnspGNVIEGNTISGGR 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 601 WgGVDIRRGGIPVLRSNL-------ICFGYSDGVvvgdegkgLIEGNTIYANkGCGVWMMSSSLPHVTSNHVSYNGLYGV 673
Cdd:COG3420   172 D-GIYLEFSDNNVIRNNTirnlrygIHYMYSNDN--------LVEGNTFRDN-GAGIALMYSKGNTVRGNTILGNSGYGI 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 674 AVfsqKDGSSelprghraqenfsedgdailwetelekeddplrrpitiALVESNSINHNGaSGLYVQSSEALHVITNVIH 753
Cdd:COG3420   242 LL---KESSD--------------------------------------SVIEGNTISGNG-KGIFIYNSNRNTIRGNLFA 279

                         250       260
                  ....*....|....*....|....*...
gi 2217376746 754 ANGdRGITVAQSSQPTRVANNSISCNRQ 781
Cdd:COG3420   280 GNG-IGIHLTAGSEGNRIYGNNFIGNRT 306
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 6-49 4.12e-11

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 58.65  E-value: 4.12e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWYELIlsLDSTRWRQLC 49
Cdd:pfam12937   4 LPDEILLQIFSYLDPKDLLRLALVCRRWRELA--SDDSLWRRLC 45
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 439-668 8.19e-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: 64.55  E-value: 8.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 439 DGKGGVFVCSHGRAKMEGNIFRNLTYAVRCIHNSKIIMLRNDIYR------CRASGIFLRLEGGGLIAGNNIYHNAEaGV 512
Cdd:COG3420    96 DDDAGIYVRGADNAVIENNRIENNLFGIYLEGSDNNVIRNNTISGnrdlraDRGNGIHLWNSPGNVIEGNTISGGRD-GI 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 513 DIRKKSNPLILCNQIHHgLRSGIVVLGNGKGIIRNNQIFSNkEAGIYILYHGNPVVSGNHIFKGRAAGIAVNENGKGLIT 592
Cdd:COG3420   175 YLEFSDNNVIRNNTIRN-LRYGIHYMYSNDNLVEGNTFRDN-GAGIALMYSKGNTVRGNTILGNSGYGILLKESSDSVIE 252

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217376746 593 ENVIRENqwggvdirRGGIPVLRSNlicfgysdgvvvgdegKGLIEGNTIYANkGCGVWMMSSSlphvTSNHVSYN 668
Cdd:COG3420   253 GNTISGN--------GKGIFIYNSN----------------RNTIRGNLFAGN-GIGIHLTAGS----EGNRIYGN 299
FBOX smart00256
A Receptor for Ubiquitination Targets;
6-42 1.95e-07

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 48.20  E-value: 1.95e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2217376746    6 LPLELWRMILAYLHLPDLGRCSLVCRAWYELILSLDS 42
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDF 37
CASH smart00722
Domain present in carbohydrate binding proteins and sugar hydrolses;
455-584 1.57e-03

Domain present in carbohydrate binding proteins and sugar hydrolses;


Pssm-ID: 214788  Cd Length: 153  Bit Score: 40.18  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746  455 EGNIFRNLTYAVRCIHNSKIIMLRN---DIYRCRASGI-----------FLRLEGGGLIAGNNIYHNAEAGVDIRKKSNP 520
Cdd:smart00722   3 NGTVLELLRGAVHYMYTSDIGGSGGaviDMGSGRGSNItinsndvrvdgVTIGGDGNAVTGIYVSASGDPVIQNDGTGKN 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217376746  521 LILCNQIHHGLR----SGIVVLGNGKGIIRNNQIFSNKEA---GIYILYHGNPVVSGNHIFKGRAAGIAVN 584
Cdd:smart00722  83 LIIDNVTFNGTEinsgAGIVVTAGSEGLFIGNRIIGNYVAtgdGNYLSDSSGGDLIGNRIYDNNRDGIAVV 153
 
Name Accession Description Interval E-value
F-box_FBXO10 cd22090
F-box domain found in F-box only protein 10 (FBXO10) and similar proteins; FBXO10, also called ...
 2-51 4.28e-28

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


Pssm-ID: 438862  Cd Length: 50  Bit Score: 107.05  E-value: 4.28e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217376746   2 EAGGLPLELWRMILAYLHLPDLGRCSLVCRAWYELILSLDSTRWRQLCLG 51
Cdd:cd22090     1 EVTGLPLELWRLILAYLPVRDLCRCCQVCRAWYELILSLDSTRWKQLYLG 50
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 464-610 1.78e-22

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


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 94.78  E-value: 1.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 464 YAVRCIHNSKIIMLRNDIYRCRASGIFLRLEGGGLIAGNNIYHNAEAGVDIRKKSNPLILCNQIHHGLRSGIVVLGNGKG 543
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217376746 544 IIRNNQIFSNKEAGIYILYHGNPVVSGNHIFKGRAAGIAVNENGKGL-ITENVIRENQWGGVDIRRGG 610
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIVGGS 148
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 533-681 3.50e-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: 91.31  E-value: 3.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 533 SGIVVLGNGKGIIRNNQIFSNKEAGIYILYHGNPVVSGNHIFKGRAAGIAVNENGKGLITENVIRENQWGGVDIRRGGIP 612
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 613 VLRSNLICFGYSDGVVVGDEGKGLIEGNTIYANKGCGVWMMSSSL-PHVTSNHVSYNGLYGVAVFSQKDG 681
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNnVTISNNTVTNNKGAGILIVGGSSN 150
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 510-663 6.19e-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: 90.54  E-value: 6.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 510 AGVDIRKKSNPLILCNQIHHGLRSGIVVLGNGKGIIRNNQIFSNKEAGIYILYHGNPVVSGNHIFKGRAAGIAVNENGKG 589
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217376746 590 LITENVIRENQWGGVDIRRGGIPVLRSNLICFGYSDGVVVGDEGKGL-IEGNTIYANKGCGVW-MMSSSLPHVTSN 663
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILiVGGSSNNTVENN 156
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 423-571 3.79e-19

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: 85.15  E-value: 3.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 423 LANSVQGCLIRKCLFRD-GKGGVFVCSHGRAKMEGNIFRNLTY-AVRCIHNSKIIMLRNDIYRCRASGIFLRLEGGGLIA 500
Cdd:pfam13229   4 LLNGSSNATIKNNTISNnGGYGIYLRGSSNATIENNTITNNGGdGIEISGSSNNTISNNTISNNGGGGIALRGSSNNLIE 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217376746 501 GNNIYHNAEAGVDIRKKSNPLILCNQIHHGLRSGIVVLGNGKGI-IRNNQIFSNKEAGIYILYHG-NPVVSGN 571
Cdd:pfam13229  84 NNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDSSNNVtISNNTVTNNKGAGILIVGGSsNNTVENN 156
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 442-600 1.76e-18

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: 83.23  E-value: 1.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 442 GGVFVCSHGRAKMEGNIFRNL-TYAVRCIHNSKIIMLRNDIYRCRASGIFLRLEGGGLIAGNNIYHNAEAGVDIRKKSNP 520
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNgGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 521 LILCNQIHHGLRSGIVVLGNGKGIIRNNQIFSNKEAGIYILY-HGNPVVSGNHIFKGRAAGIAVNENGkgliTENVIREN 599
Cdd:pfam13229  81 LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIEDsSNNVTISNNTVTNNKGAGILIVGGS----SNNTVENN 156


                  .
gi 2217376746 600 Q 600
Cdd:pfam13229 157 T 157
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 602-797 6.73e-15

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


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 73.21  E-value: 6.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 602 GGVDIRRGGIPVLRSNLICFGYSDGVVVGDEGKGLIEGNTIYANKGCGVWMMSSSLPHVTSNHVSYNGLYGVAVFsqkdG 681
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALR----G 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 682 SSELprghraqenfsedgdailwetelekeddplrrpitiaLVESNSINHNGASGLYVQSSEALHVITNVIHANGDRGIT 761
Cdd:pfam13229  77 SSNN-------------------------------------LIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIV 119

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2217376746 762 VAQSSQPTRVANNSISCNRQSGVKVEAQC-KVELRGN 797
Cdd:pfam13229 120 IEDSSNNVTISNNTVTNNKGAGILIVGGSsNNTVENN 156
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 735-893 1.75e-14

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


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 72.05  E-value: 1.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 735 SGLYVQSSEALHVITNVIHANGDRGITVAQSSQPTrVANNSISCNRQSGVKVEAQCKVELRGNGIYDNRGHGI-ITKGDS 813
Cdd:pfam13229   1 SGILLNGSSNATIKNNTISNNGGYGIYLRGSSNAT-IENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIaLRGSSN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 814 TIVIENDIIGNRGSGLQLLPRSDTKVIKNRIHSFRAYGIAV-RGRAKALVQENIIFQGKtsKTIFQQISNNRECIMQNNK 892
Cdd:pfam13229  80 NLIENNTISNNGGAGIYLSDSSNNTIENNIIHNNGGSGIVIeDSSNNVTISNNTVTNNK--GAGILIVGGSSNNTVENNT 157


                  .
gi 2217376746 893 F 893
Cdd:pfam13229 158 F 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 722-867 1.94e-14

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


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 71.67  E-value: 1.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 722 ALVESNSINHNGASGLYVQSSEALHVITNVIHANGDRGITVAQSSQPTrVANNSISCNRQSGVKVEAQCKVELRGNGIYD 801
Cdd:pfam13229  11 ATIKNNTISNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNT-ISNNTISNNGGGGIALRGSSNNLIENNTISN 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217376746 802 NRGHGIITKGDSTIVIENDII-GNRGSGLQLLPRSDT-KVIKNRIHSFRAYGIAV-RGRAKALVQENII 867
Cdd:pfam13229  90 NGGAGIYLSDSSNNTIENNIIhNNGGSGIVIEDSSNNvTISNNTVTNNKGAGILIvGGSSNNTVENNTF 158
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
 720-842 1.20e-13

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: 69.36  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 720 TIALVESNSINHNGASGLYVQSSEALHVITNVIHANGDRGITVAQSSQPTrVANNSISCNRQSGVKVEAQCKVELRGNGI 799
Cdd:pfam13229  32 SNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIALRGSSNNL-IENNTISNNGGAGIYLSDSSNNTIENNII 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2217376746 800 YDNRGHGI-ITKGDSTIVIENDII-GNRGSGLQLLPRSDTKVIKN 842
Cdd:pfam13229 111 HNNGGSGIvIEDSSNNVTISNNTVtNNKGAGILIVGGSSNNTVEN 155
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 528-781 2.54e-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: 66.09  E-value: 2.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 528 HHGLRSGIVVLGNGKGIIRNNQIFSNkEAGIYILYHGNPVVSGNHIfKGRAAGIAVNENG-------KGLITENVIRENQ 600
Cdd:COG3420    94 LTDDDAGIYVRGADNAVIENNRIENN-LFGIYLEGSDNNVIRNNTI-SGNRDLRADRGNGihlwnspGNVIEGNTISGGR 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 601 WgGVDIRRGGIPVLRSNL-------ICFGYSDGVvvgdegkgLIEGNTIYANkGCGVWMMSSSLPHVTSNHVSYNGLYGV 673
Cdd:COG3420   172 D-GIYLEFSDNNVIRNNTirnlrygIHYMYSNDN--------LVEGNTFRDN-GAGIALMYSKGNTVRGNTILGNSGYGI 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 674 AVfsqKDGSSelprghraqenfsedgdailwetelekeddplrrpitiALVESNSINHNGaSGLYVQSSEALHVITNVIH 753
Cdd:COG3420   242 LL---KESSD--------------------------------------SVIEGNTISGNG-KGIFIYNSNRNTIRGNLFA 279

                         250       260
                  ....*....|....*....|....*...
gi 2217376746 754 ANGdRGITVAQSSQPTRVANNSISCNRQ 781
Cdd:COG3420   280 GNG-IGIHLTAGSEGNRIYGNNFIGNRT 306
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 6-49 4.12e-11

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 58.65  E-value: 4.12e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWYELIlsLDSTRWRQLC 49
Cdd:pfam12937   4 LPDEILLQIFSYLDPKDLLRLALVCRRWRELA--SDDSLWRRLC 45
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 439-668 8.19e-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: 64.55  E-value: 8.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 439 DGKGGVFVCSHGRAKMEGNIFRNLTYAVRCIHNSKIIMLRNDIYR------CRASGIFLRLEGGGLIAGNNIYHNAEaGV 512
Cdd:COG3420    96 DDDAGIYVRGADNAVIENNRIENNLFGIYLEGSDNNVIRNNTISGnrdlraDRGNGIHLWNSPGNVIEGNTISGGRD-GI 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 513 DIRKKSNPLILCNQIHHgLRSGIVVLGNGKGIIRNNQIFSNkEAGIYILYHGNPVVSGNHIFKGRAAGIAVNENGKGLIT 592
Cdd:COG3420   175 YLEFSDNNVIRNNTIRN-LRYGIHYMYSNDNLVEGNTFRDN-GAGIALMYSKGNTVRGNTILGNSGYGILLKESSDSVIE 252

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217376746 593 ENVIRENqwggvdirRGGIPVLRSNlicfgysdgvvvgdegKGLIEGNTIYANkGCGVWMMSSSlphvTSNHVSYN 668
Cdd:COG3420   253 GNTISGN--------GKGIFIYNSN----------------RNTIRGNLFAGN-GIGIHLTAGS----EGNRIYGN 299
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 485-668 6.63e-10

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


Pssm-ID: 428281 [Multi-domain]  Cd Length: 215  Bit Score: 60.12  E-value: 6.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 485 RASGIFLRLEGGGLIAGNNIYhNAEAGVDIRKKSNPLILCNQIHhGLRSGIVVLGNGKGIIRNNQIFSNkEAGIYILYHG 564
Cdd:pfam05048  18 RGNGIQLWNTEGNVISNNDII-NSRDGIYLDASNNNTITGNRIS-NLRYGIHLMNSNDNTISDNVFSGN-TAGIALMSSS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 565 NPVVSGNHIFKGRAAGIAVNENGKGLITENVIRENQwggvdirrggipvlrsnlicfgySDGVVVGDEGKGLIEGNTIYA 644
Cdd:pfam05048  95 NNTLENNTISGNTNYGILLSDSSNNTISNNTISNNN-----------------------GKGIFLYNSDYNTITGNRITS 151

                         170       180
                  ....*....|....*....|....
gi 2217376746 645 NkGCGVWMMSSSlphvTSNHVSYN 668
Cdd:pfam05048 152 N-GIGIHFLAGS----NGNTIYNN 170
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 6-37 1.55e-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: 53.99  E-value: 1.55e-09
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWYELI 37
Cdd:cd09917     3 LPDEILLKILSYLDPRDLLRLSLVCKRWRELA 34
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 423-602 2.71e-09

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


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 59.93  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 423 LANSvQGCLIRKCLFRDGKGGVFVCSHGRAKMEGNIFRNLTYAVrCIHNSkiimlrndiyrcrasgiflrleGGGLIAGN 502
Cdd:COG3420   154 LWNS-PGNVIEGNTISGGRDGIYLEFSDNNVIRNNTIRNLRYGI-HYMYS----------------------NDNLVEGN 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 503 NIYHNaeagvdirkksnplilcnqihhglRSGIVVLGNGKGIIRNNQIFSNKEAGIYILYHGNPVVSGNHIfKGRAAGIA 582
Cdd:COG3420   210 TFRDN------------------------GAGIALMYSKGNTVRGNTILGNSGYGILLKESSDSVIEGNTI-SGNGKGIF 264

                         170       180
                  ....*....|....*....|
gi 2217376746 583 VNENGKGLITENVIRENQWG 602
Cdd:COG3420   265 IYNSNRNTIRGNLFAGNGIG 284
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 6-45 8.37e-09

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


Pssm-ID: 425796  Cd Length: 43  Bit Score: 52.16  E-value: 8.37e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWYELILSLDSTRW 45
Cdd:pfam00646   4 LPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWKK 43
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 479-602 3.21e-08

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


Pssm-ID: 428281 [Multi-domain]  Cd Length: 215  Bit Score: 55.12  E-value: 3.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 479 NDIYRCRaSGIFLRLEGGGLIAGNNIyHNAEAGVDIRKKSNPLILCNQIHHGlRSGIVVLGNGKGIIRNNQIFSNKEAGI 558
Cdd:pfam05048  35 NDIINSR-DGIYLDASNNNTITGNRI-SNLRYGIHLMNSNDNTISDNVFSGN-TAGIALMSSSNNTLENNTISGNTNYGI 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2217376746 559 YILYHGNPVVSGNHIFKGRAAGIAVNENGKGLITENVIRENQWG 602
Cdd:pfam05048 112 LLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRITSNGIG 155
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 722-844 6.53e-08

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


Pssm-ID: 428281 [Multi-domain]  Cd Length: 215  Bit Score: 54.35  E-value: 6.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 722 ALVESNSINhNGASGLYVQSSEALHVITNVIHaNGDRGITVAQSSQPTrVANNSISCNRqSGVKVEAQCKVELRGNGIYD 801
Cdd:pfam05048  30 NVISNNDII-NSRDGIYLDASNNNTITGNRIS-NLRYGIHLMNSNDNT-ISDNVFSGNT-AGIALMSSSNNTLENNTISG 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2217376746 802 NRGHGI-ITKGDSTIVIENDIIGNRGSGLQLLPRSDTKVIKNRI 844
Cdd:pfam05048 106 NTNYGIlLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRI 149
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 527-673 1.02e-07

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


Pssm-ID: 428281 [Multi-domain]  Cd Length: 215  Bit Score: 53.58  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 527 IHHGLRSGIVVLGNGKG--IIRNNQIfSNKEAGIYILYHGNPVVSGNHIFKGRAaGIAVNENGKGLITENVIRENqWGGV 604
Cdd:pfam05048  12 IYNGLSRGNGIQLWNTEgnVISNNDI-INSRDGIYLDASNNNTITGNRISNLRY-GIHLMNSNDNTISDNVFSGN-TAGI 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217376746 605 DIRRGGIPVLRSNLICFGYSDGVVVGDEGKGLIEGNTIYANKGCGVWMMSSSLPHVTSNHVSYNGlYGV 673
Cdd:pfam05048  89 ALMSSSNNTLENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRITSNG-IGI 156
FBOX smart00256
A Receptor for Ubiquitination Targets;
6-42 1.95e-07

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 48.20  E-value: 1.95e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2217376746    6 LPLELWRMILAYLHLPDLGRCSLVCRAWYELILSLDS 42
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDF 37
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
 626-844 2.28e-07

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: 53.77  E-value: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 626 GVVVGDEGKGLIEGNTIYaNKGCGVWMMSSSLPHVTSNHVSYNglygvavfsqkdgsselprghraQENFSEDGDAI-LW 704
Cdd:COG3420   100 GIYVRGADNAVIENNRIE-NNLFGIYLEGSDNNVIRNNTISGN-----------------------RDLRADRGNGIhLW 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 705 ETelekeddplrrpiTIALVESNSINHNGaSGLYVQSSEALHVITNVIHaNGDRGITVAQSSQpTRVANNSISCNRqSGV 784
Cdd:COG3420   156 NS-------------PGNVIEGNTISGGR-DGIYLEFSDNNVIRNNTIR-NLRYGIHYMYSND-NLVEGNTFRDNG-AGI 218

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217376746 785 KVEAQCKVELRGNGIYDNRGHGIITK-GDSTIVIENDIIGNrGSGLQLLPRSDTKVIKNRI 844
Cdd:COG3420   219 ALMYSKGNTVRGNTILGNSGYGILLKeSSDSVIEGNTISGN-GKGIFIYNSNRNTIRGNLF 278
F-box_FBXO45 cd22111
F-box domain found in F-box only protein 45 (FBXO45) and similar proteins; FBXO45, also called ...
 3-36 4.71e-07

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: 46.89  E-value: 4.71e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2217376746   3 AGGLPLELWRMILAYLHLPDLGRCSLVCRAWYEL 36
Cdd:cd22111     1 AARLPSRVLEVIFSYLDLPDLRNCSLVCKSWYRL 34
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 425-574 1.93e-06

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


Pssm-ID: 428281 [Multi-domain]  Cd Length: 215  Bit Score: 49.72  E-value: 1.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 425 NSVQGCLIRKCLFRDGKGGVFVCSHGRAKMEGNIFRNLTYAVRCIHNSKIIMLRNDIYRCRAsGIFLRLEGGGLIAGNNI 504
Cdd:pfam05048  25 WNTEGNVISNNDIINSRDGIYLDASNNNTITGNRISNLRYGIHLMNSNDNTISDNVFSGNTA-GIALMSSSNNTLENNTI 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 505 YHNAEAGVDIRKKSNPLILCNQIHHGLRSGIVVLGNGKGIIRNNQIFSNKEaGIYILYHGNpvvsGNHIF 574
Cdd:pfam05048 104 SGNTNYGILLSDSSNNTISNNTISNNNGKGIFLYNSDYNTITGNRITSNGI-GIHFLAGSN----GNTIY 168
F-box_unchar cd22139
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 ...
 6-49 2.40e-06

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: 45.31  E-value: 2.40e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWYEliLSLDSTRWRQLC 49
Cdd:cd22139     4 LPDELWLHIFSFLSPKDLCQVALVCRRFNR--LASDESLWKQIC 45
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 541-673 4.02e-06

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


Pssm-ID: 428281 [Multi-domain]  Cd Length: 215  Bit Score: 48.95  E-value: 4.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 541 GKGIIRNNQIFSNKeaGIYILYHGNPVVSGNHIFKGRAaGIAVNENGKGLITENVIRENQwGGVDIRRGGIPVLRSNlIC 620
Cdd:pfam05048   7 GDTIGIYNGLSRGN--GIQLWNTEGNVISNNDIINSRD-GIYLDASNNNTITGNRISNLR-YGIHLMNSNDNTISDN-VF 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217376746 621 FGYSDGVVVGDEGKGLIEGNTIYANKGCGVWMMSSSLPHVTSNHVSYNGLYGV 673
Cdd:pfam05048  82 SGNTAGIALMSSSNNTLENNTISGNTNYGILLSDSSNNTISNNTISNNNGKGI 134
F-box_FBXO9 cd22089
F-box domain found in F-box only protein 9 (FBXO9) and similar proteins; FBXO9, also called ...
 6-50 7.01e-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: 44.14  E-value: 7.01e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2217376746   6 LPLELWRMILAY----LHLPDLGRCSLVCRAWYelILSLDSTRWRQLCL 50
Cdd:cd22089     6 LPSEILLYILRWvvsdLDLRSLEQLSLVCRKFY--LLARDPSIWRLACE 52
F-box_FBXO41 cd22109
F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called ...
 9-49 2.04e-05

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: 42.70  E-value: 2.04e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217376746   9 ELWRMILAYLHLPDLGRCSLVCRAWYEliLSLDSTRWRQLC 49
Cdd:cd22109     9 DALFCVFSYLDTKSLLRCAEVCREWRD--VSRHPALWQRVC 47
F-box_FBXO48 cd22113
F-box domain found in F-box only protein 48 (FBXO48) and similar proteins; FBXO48, also called ...
 6-49 5.26e-05

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: 41.53  E-value: 5.26e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWYELILSLDSTrWRQLC 49
Cdd:cd22113     4 LPPEMSLRIFSQLDVQSLCRASQTCKTWNDLIENSDYL-WRPHC 46
F-box_SpPof1-like cd22147
F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar ...
 6-49 5.87e-05

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: 41.14  E-value: 5.87e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWYELILSLDStrWRQLC 49
Cdd:cd22147     5 LPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDEL--WKRMC 46
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 723-825 7.03e-05

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


Pssm-ID: 428281 [Multi-domain]  Cd Length: 215  Bit Score: 45.10  E-value: 7.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 723 LVESNSINHNGAsGLYVQSSEALHVITNVIHANGDRGITVAQSSQpTRVANNSISCNRQSGVKVEAQCKVELRGNGIYDN 802
Cdd:pfam05048  75 TISDNVFSGNTA-GIALMSSSNNTLENNTISGNTNYGILLSDSSN-NTISNNTISNNNGKGIFLYNSDYNTITGNRITSN 152

                          90       100
                  ....*....|....*....|....*
gi 2217376746 803 rGHGI--ITKGDSTIVIENDIIGNR 825
Cdd:pfam05048 153 -GIGIhfLAGSNGNTIYNNYFINNS 176
F-box_FBXL1 cd22114
F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also ...
 6-45 7.30e-05

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: 40.86  E-value: 7.30e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWYelILSLDSTRW 45
Cdd:cd22114     4 LPDELLLGIFSCLCLPDLLKVSQVCKRWY--RLASDESLW 41
F-box_FBXO18 cd22095
F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called ...
 6-37 1.76e-04

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: 39.95  E-value: 1.76e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2217376746   6 LPLELWRMILAYLHLPDLGR-CSLVCRAWYELI 37
Cdd:cd22095     5 LPEELLRNIFAFLPAEDLYQnISLVCRHWRDIV 37
F-box_FBXW2 cd22131
F-box domain found in F-box/WD repeat-containing protein 2 (FBXW2) and similar proteins; FBXW2, ...
 6-40 3.44e-04

F-box domain found in F-box/WD repeat-containing protein 2 (FBXW2) and similar proteins; FBXW2, also called F-box and WD-40 domain-containing protein 2, or protein MD6, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a tumor suppressor by promoting SKP2 degradation. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438903  Cd Length: 40  Bit Score: 38.85  E-value: 3.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWYELILSL 40
Cdd:cd22131     6 LPLELSFYLLSFLDPESLLTCCLVSKQWNKVISSC 40
F-box_FBXO7 cd22087
F-box domain found in F-box only protein 7 (FBXO7) and similar proteins; FBXO7, also called ...
 6-49 4.39e-04

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


Pssm-ID: 438859  Cd Length: 45  Bit Score: 38.82  E-value: 4.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWYelILSLDSTRWRQLC 49
Cdd:cd22087     4 LPPEIKLRILSLLDVRSLLSLSQVCRDLN--SATNDQLLWRFLL 45
F-box_FBXL2-like cd22115
F-box domain found in F-box/LRR-repeat protein 2 (FBXL2), F-box/LRR-repeat protein 20 (FBXL20) ...
 6-46 5.12e-04

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


Pssm-ID: 438887  Cd Length: 45  Bit Score: 38.55  E-value: 5.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWYelILSLDSTRWR 46
Cdd:cd22115     7 LPKELLLRIFSFLDVVTLCRCAQVSKYWN--VLALDGSNWQ 45
F-box_FBXO42 cd22110
F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called ...
 6-38 6.77e-04

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: 38.09  E-value: 6.77e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2217376746   6 LPLELWRMILAYLHL-PDLGRCSLVCRAWYELIL 38
Cdd:cd22110     4 LPEEILEYILSYLSPyGDLKSAALVCKRWHRIIK 37
F-box_FBXW8 cd22134
F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, ...
 6-49 7.77e-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: 38.13  E-value: 7.77e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWYelILSLDSTRWRQLC 49
Cdd:cd22134     7 LPRELALKIFQYLSVTDLCRCAQVSKSWK--SLAEDELLWYRIC 48
F-box_FBXO3 cd22084
F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called ...
 6-49 8.30e-04

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: 38.01  E-value: 8.30e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWYEliLSLDSTRWRQLC 49
Cdd:cd22084     4 LPSDPLLNILSFLDYRDLISCSQVCRRLNQ--LCSHDPLWKRLC 45
F-box_FBXL13 cd22124
F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also ...
 6-45 8.43e-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: 37.70  E-value: 8.43e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWyeLILSLDSTRW 45
Cdd:cd22124     4 LPRKAALKIFSYLDLRDLARCAQVCRSW--KVITQSSSLW 41
NosD pfam05048
Periplasmic copper-binding protein (NosD); NosD is a periplasmic protein which is thought to ...
 726-845 1.23e-03

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


Pssm-ID: 428281 [Multi-domain]  Cd Length: 215  Bit Score: 41.25  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746 726 SNSINHNGASGLYVQSSEALHVITNVIHANGdRGITVAQSSQPTrVANNSISCNRQSGVKVEAQCKVELRGNGIYDNRGH 805
Cdd:pfam05048  55 TGNRISNLRYGIHLMNSNDNTISDNVFSGNT-AGIALMSSSNNT-LENNTISGNTNYGILLSDSSNNTISNNTISNNNGK 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217376746 806 GIITKGDSTIVIENDIIGNRGSGLQLLPRSDTkvikNRIH 845
Cdd:pfam05048 133 GIFLYNSDYNTITGNRITSNGIGIHFLAGSNG----NTIY 168
F-box_AtTIR1-like cd22159
F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), ...
 6-39 1.23e-03

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: 37.44  E-value: 1.23e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2217376746   6 LPLELWRMILAYLHLP-DLGRCSLVCRAWYELILS 39
Cdd:cd22159     4 LPDEILELIFSYLSDPwDRNSCSLVCKRWYRLERA 38
F-box_AtFBW1-like cd22157
F-box domain found in Arabidopsis thaliana F-box/WD-40 repeat-containing protein 1 (AtFBW1) ...
 5-39 1.33e-03

F-box domain found in Arabidopsis thaliana F-box/WD-40 repeat-containing protein 1 (AtFBW1) and similar proteins; AtFBW1, also called WD-40-associated F-box protein 1, is an F-box protein that contains four WD-40 repeats, which are separated from each other by a spacer region. Like other F-box proteins, AtFBW1 may be a component of SCF (Skp1 Cdc53 F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. This subfamily also contains many F-box only proteins that do not have any WD repeat. 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: 438928  Cd Length: 39  Bit Score: 37.06  E-value: 1.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2217376746   5 GLPLELWRMILAYLHLPDLGRCSLVCRAWYELILS 39
Cdd:cd22157     2 SLPDDLVEEILSRLPAKSLLRFRCVCKQWNSLISS 36
F-box_JHDM cd22122
F-box domain found in the JmjC domain-containing histone demethylation protein (JHDM) family; ...
 6-46 1.35e-03

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: 37.25  E-value: 1.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWYEliLSLDSTRWR 46
Cdd:cd22122     4 LPREVWLPVFQYLSPKDLCVCMRVCKTWNR--WCCDPSLWK 42
CASH smart00722
Domain present in carbohydrate binding proteins and sugar hydrolses;
455-584 1.57e-03

Domain present in carbohydrate binding proteins and sugar hydrolses;


Pssm-ID: 214788  Cd Length: 153  Bit Score: 40.18  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376746  455 EGNIFRNLTYAVRCIHNSKIIMLRN---DIYRCRASGI-----------FLRLEGGGLIAGNNIYHNAEAGVDIRKKSNP 520
Cdd:smart00722   3 NGTVLELLRGAVHYMYTSDIGGSGGaviDMGSGRGSNItinsndvrvdgVTIGGDGNAVTGIYVSASGDPVIQNDGTGKN 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217376746  521 LILCNQIHHGLR----SGIVVLGNGKGIIRNNQIFSNKEA---GIYILYHGNPVVSGNHIFKGRAAGIAVN 584
Cdd:smart00722  83 LIIDNVTFNGTEinsgAGIVVTAGSEGLFIGNRIIGNYVAtgdGNYLSDSSGGDLIGNRIYDNNRDGIAVV 153
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
 6-52 1.97e-03

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: 36.85  E-value: 1.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWYELILSldSTRWRQLCLGC 52
Cdd:cd22104     4 LPSVVLVHIFSYLPPRDRLRASSTCRRWREALFH--PSLWRSLRLHL 48
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
 5-38 1.98e-03

F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also called F-box and leucine-rich repeat protein 8, or F-box protein FBL8, 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: 438893  Cd Length: 35  Bit Score: 36.57  E-value: 1.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2217376746   5 GLPLELWRMILAYLHLPDLGRCSLVCRAWYELIL 38
Cdd:cd22121     2 ALPEEILVHIFRHLSLRDRYAAAQVCKHWREAAL 35
F-box_unchar cd22138
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 ...
 6-46 2.56e-03

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: 36.54  E-value: 2.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWYELILSldSTRWR 46
Cdd:cd22138     4 LPVECQLKIFSFLSEVDKCLAATVCRSWSELIRS--PRLWR 42
F-box_AtSKIP31-like cd22166
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 31 (AtSKIP31) and similar ...
 6-48 3.10e-03

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


Pssm-ID: 438937  Cd Length: 46  Bit Score: 36.28  E-value: 3.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRawYELILSLDSTRWRQL 48
Cdd:cd22166     4 LPPELFRHILKFLSPEDLTSCATVCR--FLRGAASDESLWRRL 44
F-box_FBXL7 cd22120
F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also ...
 6-48 6.01e-03

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


Pssm-ID: 438892  Cd Length: 44  Bit Score: 35.44  E-value: 6.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2217376746   6 LPLELWRMILAYLHLPDLGRCSLVCRAWYELIlsLDSTRWRQL 48
Cdd:cd22120     4 LPDDVILQIFSHLPTNQLCRCARVCRRWYNLA--WDPRLWTTI 44
F-box_FBXO13 cd22092
F-box domain found in F-box only protein 13 (FBXO13) and similar proteins; FBXO13, also called ...
 6-48 7.68e-03

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


Pssm-ID: 438864  Cd Length: 49  Bit Score: 35.47  E-value: 7.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217376746   6 LPLELWRMILAYLHLPDlgRC---SLVCRAWYEliLSLDSTRWRQL 48
Cdd:cd22092     5 LPDSILLKIFSYLSLQE--RClsaSLVCKYWRD--LCLDSQFWKQI 46
 
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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