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Conserved domains on  [gi|915750964|gb|AKX69655|]
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ZEITLUPE, partial [Arabidopsis lyrata subsp. petraea]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F-box_AtADO-like cd22154
F-box domain found in Arabidopsis thaliana Adagio proteins (AtADO1/2/3) and similar proteins; ...
 114-160 2.00e-23

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: 92.55  E-value: 2.00e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 915750964 114 GLFQLSDEVVSMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRRVC 160
Cdd:cd22154    1 GIFQLSDEVLAQKILSRLTPRDVASVGSVCRRLYELTKNEDLWRMVC 47
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
211-476 2.17e-19

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 87.90  E-value: 2.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 211 RCNFSACAVGNRVVLFGGEGVNmQPMNDTFVLDLNSDypEWQhvKVSSPPPGRWGHTLSCVNGSNLVVFGGCGQQ----G 286
Cdd:COG3055   13 RSEAAAALLDGKVYVAGGLSGG-SASNSFEVYDPATN--TWS--ELAPLPGPPRHHAAAVAQDGKLYVFGGFTGAnpssT 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 287 LLNDVFVLNLDAKppTWREISGLapPLPRSWHSSCTLDGtKLIVSGGCADSGVlLSDTFLLDLSieKPVWREIPAAwtPP 366
Cdd:COG3055   88 PLNDVYVYDPATN--TWTKLAPM--PTPRGGATALLLDG-KIYVVGGWDDGGN-VAWVEVYDPA--TGTWTQLAPL--PT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 367 SRLGHTLSVYGGRKILMFGGLAKSGplrfrSSDVFTmdlseeepcwrcvTGSGMPGAGnpggvappprlDHVAVNLPGGR 446
Cdd:COG3055  158 PRDHLAAAVLPDGKILVIGGRNGSG-----FSNTWT-------------TLAPLPTAR-----------AGHAAAVLGGK 208

                        250       260       270
                 ....*....|....*....|....*....|
gi 915750964 447 ILIFGGSVAGLhsaSQLYLLDPTEDkpTWR 476
Cdd:COG3055  209 ILVFGGESGFS---DEVEAYDPATN--TWT 233
PRK13558 super family cl36264
bacterio-opsin activator; Provisional
 1-79 4.00e-11

bacterio-opsin activator; Provisional


The actual alignment was detected with superfamily member PRK13558:

Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 65.24  E-value: 4.00e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915750964   1 RFLQCRGPFAKRrhplvdsmvVSEIRKCIDEGIEFQGELLNFRKDGSPLMNRLRLTPIYGDDDTITHIIGIQffieTDI 79
Cdd:PRK13558 197 RFLQGEDTNEER---------VAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQ----TDV 262
 
Name Accession Description Interval E-value
F-box_AtADO-like cd22154
F-box domain found in Arabidopsis thaliana Adagio proteins (AtADO1/2/3) and similar proteins; ...
 114-160 2.00e-23

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: 92.55  E-value: 2.00e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 915750964 114 GLFQLSDEVVSMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRRVC 160
Cdd:cd22154    1 GIFQLSDEVLAQKILSRLTPRDVASVGSVCRRLYELTKNEDLWRMVC 47
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
211-476 2.17e-19

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 87.90  E-value: 2.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 211 RCNFSACAVGNRVVLFGGEGVNmQPMNDTFVLDLNSDypEWQhvKVSSPPPGRWGHTLSCVNGSNLVVFGGCGQQ----G 286
Cdd:COG3055   13 RSEAAAALLDGKVYVAGGLSGG-SASNSFEVYDPATN--TWS--ELAPLPGPPRHHAAAVAQDGKLYVFGGFTGAnpssT 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 287 LLNDVFVLNLDAKppTWREISGLapPLPRSWHSSCTLDGtKLIVSGGCADSGVlLSDTFLLDLSieKPVWREIPAAwtPP 366
Cdd:COG3055   88 PLNDVYVYDPATN--TWTKLAPM--PTPRGGATALLLDG-KIYVVGGWDDGGN-VAWVEVYDPA--TGTWTQLAPL--PT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 367 SRLGHTLSVYGGRKILMFGGLAKSGplrfrSSDVFTmdlseeepcwrcvTGSGMPGAGnpggvappprlDHVAVNLPGGR 446
Cdd:COG3055  158 PRDHLAAAVLPDGKILVIGGRNGSG-----FSNTWT-------------TLAPLPTAR-----------AGHAAAVLGGK 208

                        250       260       270
                 ....*....|....*....|....*....|
gi 915750964 447 ILIFGGSVAGLhsaSQLYLLDPTEDkpTWR 476
Cdd:COG3055  209 ILVFGGESGFS---DEVEAYDPATN--TWT 233
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 1-79 4.00e-11

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 65.24  E-value: 4.00e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915750964   1 RFLQCRGPFAKRrhplvdsmvVSEIRKCIDEGIEFQGELLNFRKDGSPLMNRLRLTPIYGDDDTITHIIGIQffieTDI 79
Cdd:PRK13558 197 RFLQGEDTNEER---------VAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQ----TDV 262
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 123-160 2.48e-09

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 52.87  E-value: 2.48e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 915750964  123 VSMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRRVC 160
Cdd:pfam12937   8 ILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
PAS COG2202
PAS domain [Signal transduction mechanisms];
14-191 7.92e-09

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 56.57  E-value: 7.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964  14 HPLVDSMVVSEIRKCIDEGIEFQGELLNFRKDGSPLMNRLRLTPIYGDDDTITHIIGIQffieTDIdlgpvlgssTKEK- 92
Cdd:COG2202   61 PPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIA----RDI---------TERKr 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964  93 ------------------SIDGIYSALAAGE-RNVSRGMCGLFQLS-DEVVSMKILSRLTPRDVASVSSVCRRLyvLTKN 152
Cdd:COG2202  128 aeealreseerlrllvenAPDGIFVLDLDGRiLYVNPAAEELLGYSpEELLGKSLLDLLHPEDRERLLELLRRL--LEGG 205

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 915750964 153 EDLWRRVCQNAWGSETTRVLETVP-----GAKRLGWGRLARELT 191
Cdd:COG2202  206 RESYELELRLKDGDGRWVWVEASAvplrdGGEVIGVLGIVRDIT 249
Kelch_3 pfam13415
Galactose oxidase, central domain;
273-321 5.79e-07

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 46.13  E-value: 5.79e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 915750964  273 GSNLVVFGGCGQQG--LLNDVFVLNLDAKppTWREISGLapPLPRSWHSSC 321
Cdd:pfam13415   1 GDKLYIFGGLGFDGqtRLNDLYVYDLDTN--TWTQIGDL--PPPRSGHSAT 47
PLN02193 PLN02193
nitrile-specifier protein
 198-333 5.88e-07

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 51.88  E-value: 5.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 198 WRKLTVGGSVEPSRCNFSACAVGNRVVLFGGEGVNMQPMND-TFVLDLNSDypEWQhvkvSSPPPGRWGHtLSCVN---- 272
Cdd:PLN02193 153 WIKVEQKGEGPGLRCSHGIAQVGNKIYSFGGEFTPNQPIDKhLYVFDLETR--TWS----ISPATGDVPH-LSCLGvrmv 225

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915750964 273 --GSNLVVFGGCGQQGLLNDVFvlNLDAKPPTWREISGLAP-PLPRSWHsSCTLDGTKLIVSGG 333
Cdd:PLN02193 226 siGSTLYVFGGRDASRQYNGFY--SFDTTTNEWKLLTPVEEgPTPRSFH-SMAADEENVYVFGG 286
FBOX smart00256
A Receptor for Ubiquitination Targets;
118-158 7.75e-06

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 42.81  E-value: 7.75e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 915750964   118 LSDEVVsMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRR 158
Cdd:smart00256   1 LPDEIL-EEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFK 40
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 23-79 3.75e-05

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 42.45  E-value: 3.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 915750964   23 SEIRKCIDEG-IEFQGELLNFRKDGSPLMNRLRLTPIYGDDDTITHIIGIQffieTDI 79
Cdd:pfam13426  38 ERLREALREGkAVREFEVVLYRKDGEPFPVLVSLAPIRDDGGELVGIIAIL----RDI 91
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 36-79 4.56e-03

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 34.85  E-value: 4.56e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 915750964    36 QGELLNFRKDGSPLMNRLRLTPIYGDDDTITHIIGIQffieTDI 79
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVV----RDI 40
 
Name Accession Description Interval E-value
F-box_AtADO-like cd22154
F-box domain found in Arabidopsis thaliana Adagio proteins (AtADO1/2/3) and similar proteins; ...
 114-160 2.00e-23

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: 92.55  E-value: 2.00e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 915750964 114 GLFQLSDEVVSMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRRVC 160
Cdd:cd22154    1 GIFQLSDEVLAQKILSRLTPRDVASVGSVCRRLYELTKNEDLWRMVC 47
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
211-476 2.17e-19

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 87.90  E-value: 2.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 211 RCNFSACAVGNRVVLFGGEGVNmQPMNDTFVLDLNSDypEWQhvKVSSPPPGRWGHTLSCVNGSNLVVFGGCGQQ----G 286
Cdd:COG3055   13 RSEAAAALLDGKVYVAGGLSGG-SASNSFEVYDPATN--TWS--ELAPLPGPPRHHAAAVAQDGKLYVFGGFTGAnpssT 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 287 LLNDVFVLNLDAKppTWREISGLapPLPRSWHSSCTLDGtKLIVSGGCADSGVlLSDTFLLDLSieKPVWREIPAAwtPP 366
Cdd:COG3055   88 PLNDVYVYDPATN--TWTKLAPM--PTPRGGATALLLDG-KIYVVGGWDDGGN-VAWVEVYDPA--TGTWTQLAPL--PT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 367 SRLGHTLSVYGGRKILMFGGLAKSGplrfrSSDVFTmdlseeepcwrcvTGSGMPGAGnpggvappprlDHVAVNLPGGR 446
Cdd:COG3055  158 PRDHLAAAVLPDGKILVIGGRNGSG-----FSNTWT-------------TLAPLPTAR-----------AGHAAAVLGGK 208

                        250       260       270
                 ....*....|....*....|....*....|
gi 915750964 447 ILIFGGSVAGLhsaSQLYLLDPTEDkpTWR 476
Cdd:COG3055  209 ILVFGGESGFS---DEVEAYDPATN--TWT 233
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
218-456 1.98e-16

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 79.43  E-value: 1.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 218 AVGNRVVLFGGEGVNM---QPMNDTFVLDLNSDypEWQhvKVSSPPPGRWGHTLSCVNGSNLVVfGGCGQQGLLNDVFVL 294
Cdd:COG3055   68 AQDGKLYVFGGFTGANpssTPLNDVYVYDPATN--TWT--KLAPMPTPRGGATALLLDGKIYVV-GGWDDGGNVAWVEVY 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 295 nlDAKPPTWREISGLapPLPRSWHSSCTLDGTKLIVSGGCADSGVLLSdtflldlsiekpvWREIPAAWTPpsRLGHTLS 374
Cdd:COG3055  143 --DPATGTWTQLAPL--PTPRDHLAAAVLPDGKILVIGGRNGSGFSNT-------------WTTLAPLPTA--RAGHAAA 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 375 VYGGrKILMFGGLAKSgplrfrSSDVFTMDLSEEEpcWRCVtgsgmpgagnpgGVAPPPRLDHVAVnLPGGRILIFGGSV 454
Cdd:COG3055  204 VLGG-KILVFGGESGF------SDEVEAYDPATNT--WTAL------------GELPTPRHGHAAV-LTDGKVYVIGGET 261


                 ..
gi 915750964 455 AG 456
Cdd:COG3055  262 KP 263
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
250-452 6.12e-16

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 77.89  E-value: 6.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 250 EWQhvKVSSPPPGRWgHTLSCVNGSNLVVFGGCGQQGLLNDVFVLNLDAKppTWREISGLapPLPRSWHSSCTLDGTKLI 329
Cdd:COG3055    2 TWS--SLPDLPTPRS-EAAAALLDGKVYVAGGLSGGSASNSFEVYDPATN--TWSELAPL--PGPPRHHAAAVAQDGKLY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 330 VSGG---CADSGVLLSDTFLLDlsIEKPVWREIPAAwtPPSRLGHTLSVYGGrKILMFGGLAKSGPLRfrssDVFTMDLS 406
Cdd:COG3055   75 VFGGftgANPSSTPLNDVYVYD--PATNTWTKLAPM--PTPRGGATALLLDG-KIYVVGGWDDGGNVA----WVEVYDPA 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 915750964 407 EEEpcWRcvTGSGMPGagnpggvappPRLDHVAVNLPGGRILIFGG 452
Cdd:COG3055  146 TGT--WT--QLAPLPT----------PRDHLAAAVLPDGKILVIGG 177
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
302-476 2.52e-12

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 67.10  E-value: 2.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 302 TWREISGLapPLPRSwHSSCTLDGTKLIVSGGCADSGVLlSDTFLLDLSieKPVWREIPAAwtPPSRLGHTLSVYGGRKI 381
Cdd:COG3055    2 TWSSLPDL--PTPRS-EAAAALLDGKVYVAGGLSGGSAS-NSFEVYDPA--TNTWSELAPL--PGPPRHHAAAVAQDGKL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 382 LMFGGLAKSGPLRFRSSDVFTMDLSEEEpcWRcvtgsgmpgagnPGGVAPPPRLDHVAVnLPGGRILIFGGSVAGLHSAS 461
Cdd:COG3055   74 YVFGGFTGANPSSTPLNDVYVYDPATNT--WT------------KLAPMPTPRGGATAL-LLDGKIYVVGGWDDGGNVAW 138

                        170
                 ....*....|....*
gi 915750964 462 qLYLLDPTEDkpTWR 476
Cdd:COG3055  139 -VEVYDPATG--TWT 150
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 1-79 4.00e-11

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 65.24  E-value: 4.00e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915750964   1 RFLQCRGPFAKRrhplvdsmvVSEIRKCIDEGIEFQGELLNFRKDGSPLMNRLRLTPIYGDDDTITHIIGIQffieTDI 79
Cdd:PRK13558 197 RFLQGEDTNEER---------VAELREAIDEERPTSVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQ----TDV 262
PRK13559 PRK13559
hypothetical protein; Provisional
 1-79 1.44e-10

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 62.53  E-value: 1.44e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 915750964   1 RFLQcrgpfakrrHPLVDSMVVSEIRKCIDEGIEFQGELLNFRKDGSPLMNRLRLTPIYGDDDTITHIIGIQFFIeTDI 79
Cdd:PRK13559  92 RFLQ---------GAATDPIAVAKIRAAIAAEREIVVELLNYRKDGEPFWNALHLGPVYGEDGRLLYFFGSQWDV-TDI 160
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 123-160 2.48e-09

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 52.87  E-value: 2.48e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 915750964  123 VSMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRRVC 160
Cdd:pfam12937   8 ILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45
PAS COG2202
PAS domain [Signal transduction mechanisms];
14-191 7.92e-09

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 56.57  E-value: 7.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964  14 HPLVDSMVVSEIRKCIDEGIEFQGELLNFRKDGSPLMNRLRLTPIYGDDDTITHIIGIQffieTDIdlgpvlgssTKEK- 92
Cdd:COG2202   61 PPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIA----RDI---------TERKr 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964  93 ------------------SIDGIYSALAAGE-RNVSRGMCGLFQLS-DEVVSMKILSRLTPRDVASVSSVCRRLyvLTKN 152
Cdd:COG2202  128 aeealreseerlrllvenAPDGIFVLDLDGRiLYVNPAAEELLGYSpEELLGKSLLDLLHPEDRERLLELLRRL--LEGG 205

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 915750964 153 EDLWRRVCQNAWGSETTRVLETVP-----GAKRLGWGRLARELT 191
Cdd:COG2202  206 RESYELELRLKDGDGRWVWVEASAvplrdGGEVIGVLGIVRDIT 249
F-box_FBXO3 cd22084
F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called ...
 115-164 1.77e-08

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: 50.34  E-value: 1.77e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 915750964 115 LFQLSDEVVsMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRRVCQNAW 164
Cdd:cd22084    1 LDDLPSDPL-LNILSFLDYRDLISCSQVCRRLNQLCSHDPLWKRLCKKYW 49
PRK13557 PRK13557
histidine kinase; Provisional
 1-72 1.49e-07

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 53.91  E-value: 1.49e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 915750964   1 RFLQcrgpfakrrHPLVDSMVVSEIRKCIDEGIEFQGELLNFRKDGSPLMNRLRLTPIYGDDDTITHIIGIQ 72
Cdd:PRK13557  79 RFLQ---------GPETDRATVAEVRDAIAERREIATEILNYRKDGSSFWNALFVSPVYNDAGDLVYFFGSQ 141
F-box_unchar cd22139
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 ...
 118-160 1.72e-07

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


Pssm-ID: 438911  Cd Length: 45  Bit Score: 47.62  E-value: 1.72e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 915750964 118 LSDEVVsMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRRVC 160
Cdd:cd22139    4 LPDELW-LHIFSFLSPKDLCQVALVCRRFNRLASDESLWKQIC 45
Kelch_3 pfam13415
Galactose oxidase, central domain;
273-321 5.79e-07

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 46.13  E-value: 5.79e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 915750964  273 GSNLVVFGGCGQQG--LLNDVFVLNLDAKppTWREISGLapPLPRSWHSSC 321
Cdd:pfam13415   1 GDKLYIFGGLGFDGqtRLNDLYVYDLDTN--TWTQIGDL--PPPRSGHSAT 47
PLN02193 PLN02193
nitrile-specifier protein
 198-333 5.88e-07

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 51.88  E-value: 5.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 198 WRKLTVGGSVEPSRCNFSACAVGNRVVLFGGEGVNMQPMND-TFVLDLNSDypEWQhvkvSSPPPGRWGHtLSCVN---- 272
Cdd:PLN02193 153 WIKVEQKGEGPGLRCSHGIAQVGNKIYSFGGEFTPNQPIDKhLYVFDLETR--TWS----ISPATGDVPH-LSCLGvrmv 225

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 915750964 273 --GSNLVVFGGCGQQGLLNDVFvlNLDAKPPTWREISGLAP-PLPRSWHsSCTLDGTKLIVSGG 333
Cdd:PLN02193 226 siGSTLYVFGGRDASRQYNGFY--SFDTTTNEWKLLTPVEEgPTPRSFH-SMAADEENVYVFGG 286
Kelch_4 pfam13418
Galactose oxidase, central domain;
211-261 6.55e-07

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 46.07  E-value: 6.55e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 915750964  211 RCNFSACAVGN-RVVLFGGEGVNMQPMNDTFVLDLNSDypEWQhvKVSSPPP 261
Cdd:pfam13418   2 RAYHTSTSIPDdTIYLFGGEGEDGTLLSDLWVFDLSTN--EWT--RLGSLPS 49
Kelch_3 pfam13415
Galactose oxidase, central domain;
220-269 3.56e-06

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 43.82  E-value: 3.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 915750964  220 GNRVVLFGGEGVNMQPM-NDTFVLDLNSDypEWqhVKVSSPPPGRWGHTLS 269
Cdd:pfam13415   1 GDKLYIFGGLGFDGQTRlNDLYVYDLDTN--TW--TQIGDLPPPRSGHSAT 47
F-box_AtGID2-like cd22151
F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, ...
 116-160 4.69e-06

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: 43.46  E-value: 4.69e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 915750964 116 FQLSDEVVSmKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRRVC 160
Cdd:cd22151    1 RKLPDDLLQ-EIFKRLDPKSLARAACVCRRWRAAARSESLWENAC 44
FBOX smart00256
A Receptor for Ubiquitination Targets;
118-158 7.75e-06

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 42.81  E-value: 7.75e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 915750964   118 LSDEVVsMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRR 158
Cdd:smart00256   1 LPDEIL-EEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFK 40
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 117-151 8.72e-06

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: 42.43  E-value: 8.72e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 915750964 117 QLSDEVVsMKILSRLTPRDVASVSSVCRRLYVLTK 151
Cdd:cd09917    2 DLPDEIL-LKILSYLDPRDLLRLSLVCKRWRELAS 35
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 115-158 1.29e-05

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: 42.14  E-value: 1.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 915750964  115 LFQLSDEVVsMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRR 158
Cdd:pfam00646   1 LLDLPDDLL-LEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWKK 43
PLN02153 PLN02153
epithiospecifier protein
 198-454 1.77e-05

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 46.90  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 198 WRKLTVGGSVEPS-RCNFSACAVGNRVVLFGGEGV-NMQPMNDTFVLDLNSDypEWQHVKVSSPPPgrwghTLSCVN--- 272
Cdd:PLN02153   9 WIKVEQKGGKGPGpRCSHGIAVVGDKLYSFGGELKpNEHIDKDLYVFDFNTH--TWSIAPANGDVP-----RISCLGvrm 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 273 ---GSNLVVFGGCGQQGLLNDVFvlNLDAKPPTWREISGL---APPLPRSWHSSCTlDGTKLIVSGGCADSGVLLSDTFL 346
Cdd:PLN02153  82 vavGTKLYIFGGRDEKREFSDFY--SYDTVKNEWTFLTKLdeeGGPEARTFHSMAS-DENHVYVFGGVSKGGLMKTPERF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 915750964 347 LDL---SIEKPVWREIP-AAWTPPSRLGHTLSVYGGrKILMFGGLAKS----GPLRFRSSDVFTMDLSEEEpcWRCVTGS 418
Cdd:PLN02153 159 RTIeayNIADGKWVQLPdPGENFEKRGGAGFAVVQG-KIWVVYGFATSilpgGKSDYESNAVQFFDPASGK--WTEVETT 235

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 915750964 419 gmpgagnpgGVAPPPR--LDHVAVnlpGGRILIFGGSV 454
Cdd:PLN02153 236 ---------GAKPSARsvFAHAVV---GKYIIIFGGEV 261
F-box_FBXO7 cd22087
F-box domain found in F-box only protein 7 (FBXO7) and similar proteins; FBXO7, also called ...
 118-160 3.24e-05

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


Pssm-ID: 438859  Cd Length: 45  Bit Score: 41.13  E-value: 3.24e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 915750964 118 LSDEVvSMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRRVC 160
Cdd:cd22087    4 LPPEI-KLRILSLLDVRSLLSLSQVCRDLNSATNDQLLWRFLL 45
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 23-79 3.75e-05

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 42.45  E-value: 3.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 915750964   23 SEIRKCIDEG-IEFQGELLNFRKDGSPLMNRLRLTPIYGDDDTITHIIGIQffieTDI 79
Cdd:pfam13426  38 ERLREALREGkAVREFEVVLYRKDGEPFPVLVSLAPIRDDGGELVGIIAIL----RDI 91
Kelch_4 pfam13418
Galactose oxidase, central domain;
262-314 3.78e-05

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 41.06  E-value: 3.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 915750964  262 GRWGHTLSCVNGSNLVVFGGCGQQG-LLNDVFVLNLDAKppTWREIsglaPPLP 314
Cdd:pfam13418   1 PRAYHTSTSIPDDTIYLFGGEGEDGtLLSDLWVFDLSTN--EWTRL----GSLP 48
F-box_FBXW4 cd20090
F-box domain found in F-box/WD repeat-containing protein 4 (FBXW4) and similar proteins; FBXW4, ...
 115-158 5.08e-05

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: 40.66  E-value: 5.08e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 915750964 115 LFQLSDEVVsMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRR 158
Cdd:cd20090    2 LLDLPDDLL-FLIFSYLDPASLGRLSQVCRRLYRLISRDAVWRR 44
F-box_FBXO11 cd22091
F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called ...
 117-158 7.00e-05

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: 40.10  E-value: 7.00e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 915750964 117 QLSDEVVsMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRR 158
Cdd:cd22091    3 ELPDEVL-LKIFSYLLEQDLCRAAQVCKRFNTLANDPELWKR 43
F-box_FBXO9 cd22089
F-box domain found in F-box only protein 9 (FBXO9) and similar proteins; FBXO9, also called ...
 118-160 7.00e-05

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: 40.29  E-value: 7.00e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 915750964 118 LSDEVVsMKIL----SRLTPRDVASVSSVCRRLYVLTKNEDLWRRVC 160
Cdd:cd22089    6 LPSEIL-LYILrwvvSDLDLRSLEQLSLVCRKFYLLARDPSIWRLAC 51
F-box_ScMFB1-like cd22146
F-box domain found in Saccharomyces cerevisiae mitochondrial F-box protein MFB1 (ScMFB1) and ...
 115-157 2.39e-04

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


Pssm-ID: 438917  Cd Length: 42  Bit Score: 38.39  E-value: 2.39e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 915750964 115 LFQLSDEVVsMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWR 157
Cdd:cd22146    1 LLGLPLEIL-FEILIYLDIPDILNLSKTCRFLYVLLNDEILWR 42
F-box_DdgacFF-like cd22148
F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) ...
 115-158 2.93e-04

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: 38.42  E-value: 2.93e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 915750964 115 LFQLSDEVVSMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRR 158
Cdd:cd22148    1 FISLLPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELWKA 44
Kelch_4 pfam13418
Galactose oxidase, central domain;
314-367 3.77e-04

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 38.36  E-value: 3.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 915750964  314 PRSWHSSCTLDGTKLIVSGGCADSGVLLSDTFLLDLSieKPVWREIPaawTPPS 367
Cdd:pfam13418   1 PRAYHTSTSIPDDTIYLFGGEGEDGTLLSDLWVFDLS--TNEWTRLG---SLPS 49
F-box_FBXW5 cd22132
F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, ...
 126-158 7.89e-04

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: 37.21  E-value: 7.89e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 915750964 126 KILSRLTPRDVASVSSVCRRLYVLTKNEDLWRR 158
Cdd:cd22132   11 HIFSYLSPKDLLAAGQVCKQWYRVSRDEFLWKE 43
F-box_AtSKIP3-like cd22162
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 3 (AtSKIP3) and similar ...
 117-158 8.13e-04

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


Pssm-ID: 438933  Cd Length: 46  Bit Score: 37.18  E-value: 8.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 915750964 117 QLSDEVVSmKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRR 158
Cdd:cd22162    3 DLPEDCIA-LILSFTSPRDVCRLSAVSKTFRSAAESDVVWER 43
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 368-417 1.02e-03

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 36.93  E-value: 1.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 915750964  368 RLGHTLSVYGGRKILMFGGLAKSGPLRFRSSdvftMDLSEEEPCWRCVTG 417
Cdd:pfam07646   1 PRYPHASSVPGGKLYVVGGSDGLGDLSSSDV----LVYDPETNVWTEVPR 46
F-box_DmSKP2-like cd22149
F-box domain found in Drosophila melanogaster S-phase kinase-associated protein 2 (DmSKP2) and ...
 118-158 1.96e-03

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: 36.20  E-value: 1.96e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 915750964 118 LSDEVVsMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRR 158
Cdd:cd22149    4 LSDEII-LSIFKWLPKKTLARCARVCRRWKRLCFDESLWRR 43
F-box_EMI cd22086
F-box domain found in the early mitotic inhibitor (EMI) family of F-box proteins; The EMI ...
 115-162 1.97e-03

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


Pssm-ID: 438858  Cd Length: 48  Bit Score: 35.94  E-value: 1.97e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 915750964 115 LFQLSDEVVSMKILSRLTPRDVASVSSVCRRlyvltknedlWRRVCQN 162
Cdd:cd22086    3 LHKRNCPHILSKILSYLSPEDLCRVSCVSKT----------WRQICLS 40
F-box_AtSKIP31-like cd22166
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 31 (AtSKIP31) and similar ...
 123-158 2.49e-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: 35.90  E-value: 2.49e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 915750964 123 VSMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRR 158
Cdd:cd22166    8 LFRHILKFLSPEDLTSCATVCRFLRGAASDESLWRR 43
F-box_FBXO24 cd22098
F-box domain found in F-box only protein 24 (FBXO24) and similar proteins; FBXO24, also called ...
 118-160 2.80e-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: 35.76  E-value: 2.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 915750964 118 LSDEVVsMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRRVC 160
Cdd:cd22098    5 LPPEIL-DRIISFLPVKDIVSLGQTCRYFHEVCNSEAVWRRLC 46
F-box_FBXO41 cd22109
F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called ...
 127-160 3.78e-03

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: 35.38  E-value: 3.78e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 915750964 127 ILSRLTPRDVASVSSVCRRLYVLTKNEDLWRRVC 160
Cdd:cd22109   14 VFSYLDTKSLLRCAEVCREWRDVSRHPALWQRVC 47
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 36-79 4.56e-03

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 34.85  E-value: 4.56e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 915750964    36 QGELLNFRKDGSPLMNRLRLTPIYGDDDTITHIIGIQffieTDI 79
Cdd:smart00086   1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVV----RDI 40
F-box_FBXO21 cd22096
F-box domain found in F-box only protein 21 (FBXO21) and similar proteins; FBXO21, also called ...
 115-159 5.14e-03

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: 34.97  E-value: 5.14e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 915750964 115 LFQLSDEVVSMKILSR-LTPRDVASVSSVCRRLYVLTKNEDLWRRV 159
Cdd:cd22096    1 LLELPDELLEYILCSDnLDHHDIIRLSCTCRRLREVCQSGKVWREK 46
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 314-361 6.11e-03

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 34.62  E-value: 6.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 915750964  314 PRSWHSSCTLDGtKLIVSGGCADSGVLLSDTFlLDLSIEKPVWREIPA 361
Cdd:pfam07646   1 PRYPHASSVPGG-KLYVVGGSDGLGDLSSSDV-LVYDPETNVWTEVPR 46
F-box_AtSKIP22-like cd22165
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 22 (AtSKIP22) and similar ...
 115-160 8.71e-03

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: 34.17  E-value: 8.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 915750964 115 LFQLSDEVvSMKILSRLTPRDVASVSSVCRRLYVLTKNEDLWRRVC 160
Cdd:cd22165    2 LMRLPTEL-KLKILELLPGVDLARMACVCSELRFLASNDDLWKQKF 46
Kelch_4 pfam13418
Galactose oxidase, central domain;
433-476 9.29e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 34.12  E-value: 9.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 915750964  433 PRLDHVAVNLPGGRILIFGGSVAGLHSASQLYLLDPTEDkpTWR 476
Cdd:pfam13418   1 PRAYHTSTSIPDDTIYLFGGEGEDGTLLSDLWVFDLSTN--EWT 42
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 263-309 9.90e-03

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 34.23  E-value: 9.90e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 915750964  263 RWGHTLSCVNGSNLVVFGGCGQQGLLNDVFVLNLDAKPPTWREISGL 309
Cdd:pfam07646   1 PRYPHASSVPGGKLYVVGGSDGLGDLSSSDVLVYDPETNVWTEVPRL 47
 
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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