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Conserved domains on  [gi|30795119|ref|NP_835363|]
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F-box DNA helicase 1 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F-box_FBXO18 cd22095
F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called ...
 211-258 1.48e-25

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: 100.04  E-value: 1.48e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 30795119  211 HICSLPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISDPLFIPWKKL 258
Cdd:cd22095    1 HIQQLPEELLRNIFAFLPAEDLYQNISLVCRHWRDIVSDPLFIPWKKL 48
UvrD super family cl33806
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
440-932 1.84e-23

Superfamily I DNA or RNA helicase [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG0210:

Pssm-ID: 439980 [Multi-domain]  Cd Length: 721  Bit Score: 106.94  E-value: 1.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  440 QLTHEQQLILNHKMEPLQVVkimAFAGTGKTSTLVKYA------EKWSQSRFLYVTF-NKS-------IAKQAERVFPSN 505
Cdd:COG0210    6 GLNPEQRAAVEHPEGPLLVL---AGAGSGKTRVLTHRIayliaeGGVDPEQILAVTFtNKAaremrerIEALLGRLARGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  506 VICkTFHSMAYGHIgRKYQSKKKLNlfklTPF----------MVNSVLAE----GKGGFIRaklvckTLENFFASA-DEE 570
Cdd:COG0210   83 WVG-TFHSLALRIL-RRHAELLGLP----PNFtildgddqlrLIKELLKElgldEKRFPPR------ELLSLISRAkNEG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  571 LTIDHVPIWCKNSQGQRVMV------EQSEKLNG-------VLEASRLWDNmrklgecteeahqmtHDGYLKLWQlskps 637
Cdd:COG0210  151 LTPEELAELLAADPEWRAAAelyeayQERLRANNaldfddlLLLAVRLLEE---------------NPEVLEKYQ----- 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  638 lASFDAIFVDEAQDCTPAIMNIV--LSQPCGKIF-VGDPHQQIYTFRGA--VN-ALFTV--PHTHVFYLTQSFRFGVEI- 708
Cdd:COG0210  211 -NRFRYILVDEYQDTNPAQYELLrlLAGDGRNLCvVGDDDQSIYGFRGAdpENiLRFEKdfPDAKVIKLEQNYRSTQNIl 289

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  709 -----------------------------AYVGATILD----VCKRVRKktlvggNHQSGIRgdaKGQVALLSRTNA--N 753
Cdd:COG0210  290 daanaviannpgrlgknlwtdngegekvrLYVAPDEEEearfVADEIRE------LHEEGVP---LSDIAVLYRTNAqsR 360

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  754 VFDEA-------VRVTEG-EFPSR---------IHLI-----------------GGIKSFGLDRI--------IDIW-IL 790
Cdd:COG0210  361 ALEEAlrragipYRVVGGlRFYERaeikdllayLRLLanpdddvallrilnvprRGIGAATLERLreaareegISLLeAL 440

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  791 LQPEEERR---KQNLVIKD--KFIRRWVHKEGF-------------SGFKRYVTAAEDKELEAKIA-------VVEKYNI 845
Cdd:COG0210  441 RDLGELAGlsgRAAKALRRfaELLEALRAAAERlpleellealldeSGYEEELREEAGEEAERRLEnleelvdAAARFEE 520

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  846 R-----IPELVQRIEkcHIEDLDFAEY-----ILGTVHKAKGLEFDTVHVL---DDFvkvpcarhnlpqLPHFRveSFS- 911
Cdd:COG0210  521 RnpgasLEAFLEELA--LLSDLDAADEdedavTLMTLHAAKGLEFPVVFLVgleEGL------------FPHQR--SLDd 584

                        650       660
                 ....*....|....*....|....*
gi 30795119  912 ----EDEWNLLYVAVTRAKKRLIMT 932
Cdd:COG0210  585 eeelEEERRLFYVAITRARERLYLT 609
 
Name Accession Description Interval E-value
F-box_FBXO18 cd22095
F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called ...
 211-258 1.48e-25

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: 100.04  E-value: 1.48e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 30795119  211 HICSLPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISDPLFIPWKKL 258
Cdd:cd22095    1 HIQQLPEELLRNIFAFLPAEDLYQNISLVCRHWRDIVSDPLFIPWKKL 48
UvrD COG0210
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
440-932 1.84e-23

Superfamily I DNA or RNA helicase [Replication, recombination and repair];


Pssm-ID: 439980 [Multi-domain]  Cd Length: 721  Bit Score: 106.94  E-value: 1.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  440 QLTHEQQLILNHKMEPLQVVkimAFAGTGKTSTLVKYA------EKWSQSRFLYVTF-NKS-------IAKQAERVFPSN 505
Cdd:COG0210    6 GLNPEQRAAVEHPEGPLLVL---AGAGSGKTRVLTHRIayliaeGGVDPEQILAVTFtNKAaremrerIEALLGRLARGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  506 VICkTFHSMAYGHIgRKYQSKKKLNlfklTPF----------MVNSVLAE----GKGGFIRaklvckTLENFFASA-DEE 570
Cdd:COG0210   83 WVG-TFHSLALRIL-RRHAELLGLP----PNFtildgddqlrLIKELLKElgldEKRFPPR------ELLSLISRAkNEG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  571 LTIDHVPIWCKNSQGQRVMV------EQSEKLNG-------VLEASRLWDNmrklgecteeahqmtHDGYLKLWQlskps 637
Cdd:COG0210  151 LTPEELAELLAADPEWRAAAelyeayQERLRANNaldfddlLLLAVRLLEE---------------NPEVLEKYQ----- 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  638 lASFDAIFVDEAQDCTPAIMNIV--LSQPCGKIF-VGDPHQQIYTFRGA--VN-ALFTV--PHTHVFYLTQSFRFGVEI- 708
Cdd:COG0210  211 -NRFRYILVDEYQDTNPAQYELLrlLAGDGRNLCvVGDDDQSIYGFRGAdpENiLRFEKdfPDAKVIKLEQNYRSTQNIl 289

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  709 -----------------------------AYVGATILD----VCKRVRKktlvggNHQSGIRgdaKGQVALLSRTNA--N 753
Cdd:COG0210  290 daanaviannpgrlgknlwtdngegekvrLYVAPDEEEearfVADEIRE------LHEEGVP---LSDIAVLYRTNAqsR 360

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  754 VFDEA-------VRVTEG-EFPSR---------IHLI-----------------GGIKSFGLDRI--------IDIW-IL 790
Cdd:COG0210  361 ALEEAlrragipYRVVGGlRFYERaeikdllayLRLLanpdddvallrilnvprRGIGAATLERLreaareegISLLeAL 440

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  791 LQPEEERR---KQNLVIKD--KFIRRWVHKEGF-------------SGFKRYVTAAEDKELEAKIA-------VVEKYNI 845
Cdd:COG0210  441 RDLGELAGlsgRAAKALRRfaELLEALRAAAERlpleellealldeSGYEEELREEAGEEAERRLEnleelvdAAARFEE 520

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  846 R-----IPELVQRIEkcHIEDLDFAEY-----ILGTVHKAKGLEFDTVHVL---DDFvkvpcarhnlpqLPHFRveSFS- 911
Cdd:COG0210  521 RnpgasLEAFLEELA--LLSDLDAADEdedavTLMTLHAAKGLEFPVVFLVgleEGL------------FPHQR--SLDd 584

                        650       660
                 ....*....|....*....|....*
gi 30795119  912 ----EDEWNLLYVAVTRAKKRLIMT 932
Cdd:COG0210  585 eeelEEERRLFYVAITRARERLYLT 609
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
 836-933 9.71e-23

C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350173 [Multi-domain]  Cd Length: 89  Bit Score: 93.27  E-value: 9.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  836 KIAVVEKYNIRIPELVQRIEKCHIEDLDFAEYILGTVHKAKGLEFDTVHVLDDFVKvpcarhnlpqlphfrvesfsEDEW 915
Cdd:cd18786   12 KGVVLTPYHRDRAYLNQYLQGLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTAN--------------------SLTP 71

                         90
                 ....*....|....*...
gi 30795119  916 NLLYVAVTRAKKRLIMTK 933
Cdd:cd18786   72 RRLYVALTRARKRLVIYD 89
UvrD_C pfam13361
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ...
 871-936 3.25e-12

UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety of helicase enzymes. This domain has a AAA-like structural fold.


Pssm-ID: 433145 [Multi-domain]  Cd Length: 377  Bit Score: 69.36  E-value: 3.25e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30795119    871 TVHKAKGLEFDTVHVLDdfvkvpCARHNLPQLPHFRVESFSEDEWNLLYVAVTRAKKRLIMTKSLE 936
Cdd:pfam13361  318 TIHQAKGLEFDTVFLAG------LEEGIFPSYRSIKDEGNLEEERRLFYVAITRAKKRLYISYSKS 377
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 212-259 1.14e-11

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 60.19  E-value: 1.14e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 30795119    212 ICSLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKLY 259
Cdd:pfam12937    1 LSSLPDEILLQIFSYLDPKDLL-RLALVCRRWRELASDDSL--WRRLC 45
PRK13909 PRK13909
RecB-like helicase;
846-937 1.34e-07

RecB-like helicase;


Pssm-ID: 237554 [Multi-domain]  Cd Length: 910  Bit Score: 55.75  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119   846 RIPELVQRIEKCHIEDLDFAEY---ILgTVHKAKGLEFDTVHVLDDFVKvPCARH----------NLPQLpHFRV---ES 909
Cdd:PRK13909  585 DIEEFLFKLEPCDKEIASEESKgvqIM-TVHKSKGLEFEHVIVCDRLGK-PNSDSsnllfeydgiELWQI-YYRIkgrEN 661

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 30795119   910 F---------------SEDEWNLLYVAVTRAKKRLIMTKSLEN 937
Cdd:PRK13909  662 FdkdyaralekekalkYEEEINVLYVAFTRAKNSLIVVKKDES 704
FBOX smart00256
A Receptor for Ubiquitination Targets;
215-258 3.71e-05

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 41.65  E-value: 3.71e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 30795119     215 LPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKL 258
Cdd:smart00256    1 LPDEILEEILSKLDPKDLL-RLRKVSRKWRSLIDSHDF--WFKL 41
recB TIGR00609
exodeoxyribonuclease V, beta subunit; The RecBCD holoenzyme is a multifunctional nuclease with ...
 871-934 1.88e-04

exodeoxyribonuclease V, beta subunit; The RecBCD holoenzyme is a multifunctional nuclease with potent ATP-dependent exodeoxyribonuclease activity. Ejection of RecD, as occurs at chi recombinational hotspots, cripples exonuclease activity in favor of recombinagenic helicase activity. All proteins in this family for which functions are known are DNA-DNA helicases that are used as part of an exonuclease-helicase complex (made up of RecBCD homologs) that function to generate substrates for the initiation of recombination and recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273172 [Multi-domain]  Cd Length: 1087  Bit Score: 45.50  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119    871 TVHKAKGLEFDTV--------HVLDDFVKVPCARH-----NLPQLPHF----RVESFSEDEwNLLYVAVTRAKKRLIMTK 933
Cdd:TIGR00609  657 TIHKSKGLEYPIVflpfitdaKKSNFASLHDQHSHeyqlyDFNQSEENqklaRVERLAEDL-RLLYVALTRAKKQLFIGI 735


                   .
gi 30795119    934 S 934
Cdd:TIGR00609  736 A 736
 
Name Accession Description Interval E-value
F-box_FBXO18 cd22095
F-box domain found in F-box only protein 18 (FBXO18) and similar proteins; FBXO18, also called ...
 211-258 1.48e-25

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: 100.04  E-value: 1.48e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 30795119  211 HICSLPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISDPLFIPWKKL 258
Cdd:cd22095    1 HIQQLPEELLRNIFAFLPAEDLYQNISLVCRHWRDIVSDPLFIPWKKL 48
UvrD COG0210
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
440-932 1.84e-23

Superfamily I DNA or RNA helicase [Replication, recombination and repair];


Pssm-ID: 439980 [Multi-domain]  Cd Length: 721  Bit Score: 106.94  E-value: 1.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  440 QLTHEQQLILNHKMEPLQVVkimAFAGTGKTSTLVKYA------EKWSQSRFLYVTF-NKS-------IAKQAERVFPSN 505
Cdd:COG0210    6 GLNPEQRAAVEHPEGPLLVL---AGAGSGKTRVLTHRIayliaeGGVDPEQILAVTFtNKAaremrerIEALLGRLARGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  506 VICkTFHSMAYGHIgRKYQSKKKLNlfklTPF----------MVNSVLAE----GKGGFIRaklvckTLENFFASA-DEE 570
Cdd:COG0210   83 WVG-TFHSLALRIL-RRHAELLGLP----PNFtildgddqlrLIKELLKElgldEKRFPPR------ELLSLISRAkNEG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  571 LTIDHVPIWCKNSQGQRVMV------EQSEKLNG-------VLEASRLWDNmrklgecteeahqmtHDGYLKLWQlskps 637
Cdd:COG0210  151 LTPEELAELLAADPEWRAAAelyeayQERLRANNaldfddlLLLAVRLLEE---------------NPEVLEKYQ----- 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  638 lASFDAIFVDEAQDCTPAIMNIV--LSQPCGKIF-VGDPHQQIYTFRGA--VN-ALFTV--PHTHVFYLTQSFRFGVEI- 708
Cdd:COG0210  211 -NRFRYILVDEYQDTNPAQYELLrlLAGDGRNLCvVGDDDQSIYGFRGAdpENiLRFEKdfPDAKVIKLEQNYRSTQNIl 289

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  709 -----------------------------AYVGATILD----VCKRVRKktlvggNHQSGIRgdaKGQVALLSRTNA--N 753
Cdd:COG0210  290 daanaviannpgrlgknlwtdngegekvrLYVAPDEEEearfVADEIRE------LHEEGVP---LSDIAVLYRTNAqsR 360

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  754 VFDEA-------VRVTEG-EFPSR---------IHLI-----------------GGIKSFGLDRI--------IDIW-IL 790
Cdd:COG0210  361 ALEEAlrragipYRVVGGlRFYERaeikdllayLRLLanpdddvallrilnvprRGIGAATLERLreaareegISLLeAL 440

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  791 LQPEEERR---KQNLVIKD--KFIRRWVHKEGF-------------SGFKRYVTAAEDKELEAKIA-------VVEKYNI 845
Cdd:COG0210  441 RDLGELAGlsgRAAKALRRfaELLEALRAAAERlpleellealldeSGYEEELREEAGEEAERRLEnleelvdAAARFEE 520

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  846 R-----IPELVQRIEkcHIEDLDFAEY-----ILGTVHKAKGLEFDTVHVL---DDFvkvpcarhnlpqLPHFRveSFS- 911
Cdd:COG0210  521 RnpgasLEAFLEELA--LLSDLDAADEdedavTLMTLHAAKGLEFPVVFLVgleEGL------------FPHQR--SLDd 584

                        650       660
                 ....*....|....*....|....*
gi 30795119  912 ----EDEWNLLYVAVTRAKKRLIMT 932
Cdd:COG0210  585 eeelEEERRLFYVAITRARERLYLT 609
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
 836-933 9.71e-23

C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350173 [Multi-domain]  Cd Length: 89  Bit Score: 93.27  E-value: 9.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  836 KIAVVEKYNIRIPELVQRIEKCHIEDLDFAEYILGTVHKAKGLEFDTVHVLDDFVKvpcarhnlpqlphfrvesfsEDEW 915
Cdd:cd18786   12 KGVVLTPYHRDRAYLNQYLQGLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTAN--------------------SLTP 71

                         90
                 ....*....|....*...
gi 30795119  916 NLLYVAVTRAKKRLIMTK 933
Cdd:cd18786   72 RRLYVALTRARKRLVIYD 89
DEXQc_UvrD cd17932
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ...
 444-702 4.08e-16

DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350690 [Multi-domain]  Cd Length: 189  Bit Score: 77.56  E-value: 4.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  444 EQQLILNHKMEPLQVVkimAFAGTGKTSTLV-KYA-----EKWSQSRFLYVTFNKSIAKQ-AERVFP-------SNVICK 509
Cdd:cd17932    3 EQREAVTHPDGPLLVL---AGAGSGKTRVLThRIAylileGGVPPERILAVTFTNKAAKEmRERLRKllgeqlaSGVWIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  510 TFHSMAYgHIGRKYQSKKKLnlfkltpfmvnsvlaegkggfiraklvcktlenffasadeeltidhvpiwcknsqgqrvm 589
Cdd:cd17932   80 TFHSFAL-RILRRYGDFDDL------------------------------------------------------------ 98

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  590 veqseklngVLEASRLWDNMRKLgecteeahqmthdgyLKLWQlskpslASFDAIFVDEAQDCTPAIMNIV--LSQPCGK 667
Cdd:cd17932   99 ---------LLYALELLEENPDV---------------REKLQ------SRFRYILVDEYQDTNPLQYELLklLAGDGKN 148

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 30795119  668 IF-VGDPHQQIYTFRGAVNALFT-----VPHTHVFYLTQSF 702
Cdd:cd17932  149 LFvVGDDDQSIYGFRGADPENILdfekdFPDAKVIKLEENY 189
COG3972 COG3972
Superfamily I DNA and RNA helicases [Replication, recombination and repair];
439-944 1.37e-14

Superfamily I DNA and RNA helicases [Replication, recombination and repair];


Pssm-ID: 443172 [Multi-domain]  Cd Length: 565  Bit Score: 77.95  E-value: 1.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  439 IQLTHEQQLILnhKMEPLQVVKIMAFAGTGKTSTL----VKYAEKWSQSRFLYVTFNKSIAKQaervfpsnvicktfhsm 514
Cdd:COG3972  158 AVLDLQQERIA--RSIPDGPQRIRGVAGSGKTVLLaakaAYLALKHPGWRILVTCFNRSLADH----------------- 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  515 ayghigrkyqskkklnlfkltpfmvnsvlaegkggfIRAKLvcktlENFFASADEELTIDHVPIWCKNSQGQRVMVEQSE 594
Cdd:COG3972  219 ------------------------------------LRDLI-----PRFLRRFSNGEPEDNVKLIVFHAWGGKLLKQYGI 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  595 KLNGVLEASRLWDnmrklgECTEEAhqmthdgyLKLWQLSKPsLASFDAIFVDEAQDCTPAIMNIV---LSQPCGKIFV- 670
Cdd:COG3972  258 PPLTFSQPNEAFD------EACKAL--------LEAIQGEII-PPIYDAILIDEAQDFEPEFLRLLyqlLKPPKKRLIWa 322

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  671 GDPHQQIY--TFRGAVNALFTVPHTHVfyLTQSFRFGVEIAYVGATILDVCKRVRKktLVGGNHQSGIRgDAKGQVALLS 748
Cdd:COG3972  323 YDEAQNIYgrKIPSAGGIPAGIGRDTI--LKKNYRNTRPILTFAHAFGMGLLRPPG--LLQGDAEDYEV-ERPGDKVTLI 397

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  749 RTNANVFDEAVRVTEGEFPSRIHLIGGIKsfglDRIIDiwiLLQPEEERRKQNLVIkdkfirrwvhkegfsgfkrYVTAA 828
Cdd:COG3972  398 RPPEPAGRKGPLPEFKKYDDRAEELEAIA----EEIKK---NLRDEGLRPSDIAVI-------------------YLGNN 451

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  829 EDKELEAKIA-VVEKYNIRIpelvqrieKCHIEDLDFAEYI------LGTVHKAKGLEFDTVHVLddfvkvpcarhNLPQ 901
Cdd:COG3972  452 EAKELGDRLAaALERQGIDS--------YIAGARSDPNFFWkdggvtISTIHRAKGLEAPVVIIV-----------GLDQ 512

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 30795119  902 LPHFrvESFsEDEWNLLYVAVTRAKKRLIMTKSLENILTLAGE 944
Cdd:COG3972  513 LAKG--ESL-ERLRNLLYVAMTRARGWLVVSGSGESMAELYDE 552
RecB COG1074
3#-5# helicase subunit RecB of the DNA repair enzyme RecBCD (exonuclease V) [Replication, ...
 641-932 6.68e-14

3#-5# helicase subunit RecB of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440692 [Multi-domain]  Cd Length: 866  Bit Score: 76.15  E-value: 6.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  641 FDAIFVDEAQDCTPAIMNIV-------LSQPCGKIFVGDPHQQIYTFRGA------------------------------ 683
Cdd:COG1074  285 YRHILVDEFQDTSPLQWEILrrlageaLADGRTLFLVGDPKQSIYRFRGAdpelflearralegrvdgerltlttnfrst 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  684 ------VNALFT---------VPHTHVFYLTQSFRFGVEIAYVGATILD-----------VCKRVRKKTLVGGNHQSGIR 737
Cdd:COG1074  365 pevvdaVNALFAqlmgagfgeIPYEPVEALRPGAYPAVELWPLEPDDVSeedarerearaVAARIRRLLAEGTTVEGGGR 444

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  738 GDAKGQVALLSRTN------ANVFDEA---VRVTEGE-------------------FPS-RIHLIGGIKS--FGLD---- 782
Cdd:COG1074  445 PVRPGDIAVLVRTRseaaaiARALKAAgipVAASDRLslfespevrdllallrallNPEdDLALAAVLRSplFGLSdedl 524

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  783 -------RIIDIWILLQPEEERRKQNLVIKDkfIRRWVHKEGFS----------GFKRYVTAAEDKE--------LEAKI 837
Cdd:COG1074  525 aalaadrKGESLWEALRAYERLARALERLRA--LRELARRLGLAellerlleetGLLERLLALPGGErrlanllhLDELL 602

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  838 AVVEKYNIR----IPELVQRIEKCHIEDLDFAEYILG---------TVHKAKGLEFDTVhvlddFVkvPCARHNLpqlph 904
Cdd:COG1074  603 QLALEYEQTggpgLAGFLRWLERLIEDGGDEEKRRLEsdadavrimTIHKSKGLEFPVV-----FL--PALRERA----- 670

                        410       420
                 ....*....|....*....|....*...
gi 30795119  905 fRVESFSEdEWNLLYVAVTRAKKRLIMT 932
Cdd:COG1074  671 -RAEELAE-ELRLLYVALTRARDRLVLS 696
SF1_C_UvrD cd18807
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase ...
 869-932 1.61e-12

C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. This family also includes ATP-dependent helicase/nuclease AddA and helicase/nuclease RecBCD subunit RecB, among others. UvrD family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350194 [Multi-domain]  Cd Length: 150  Bit Score: 66.10  E-value: 1.61e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30795119  869 LGTVHKAKGLEFDTVHVLDdfvkvpCARHNLPQLPHFRVESFSED----EWNLLYVAVTRAKKRLIMT 932
Cdd:cd18807   88 LMTIHASKGLEFPVVFIVG------LGEGFIPSDASYHAAKEDEErleeERRLLYVALTRAKKELYLV 149
UvrD_C pfam13361
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ...
 871-936 3.25e-12

UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety of helicase enzymes. This domain has a AAA-like structural fold.


Pssm-ID: 433145 [Multi-domain]  Cd Length: 377  Bit Score: 69.36  E-value: 3.25e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30795119    871 TVHKAKGLEFDTVHVLDdfvkvpCARHNLPQLPHFRVESFSEDEWNLLYVAVTRAKKRLIMTKSLE 936
Cdd:pfam13361  318 TIHQAKGLEFDTVFLAG------LEEGIFPSYRSIKDEGNLEEERRLFYVAITRAKKRLYISYSKS 377
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 212-259 1.14e-11

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 60.19  E-value: 1.14e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 30795119    212 ICSLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKLY 259
Cdd:pfam12937    1 LSSLPDEILLQIFSYLDPKDLL-RLALVCRRWRELASDDSL--WRRLC 45
UvrD_C_2 pfam13538
UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety ...
 871-932 7.21e-10

UvrD-like helicase C-terminal domain; This domain is found at the C-terminus of a wide variety of helicase enzymes. This domain has a AAA-like structural fold.


Pssm-ID: 463913 [Multi-domain]  Cd Length: 52  Bit Score: 55.27  E-value: 7.21e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30795119    871 TVHKAKGLEFDTVHVLDDfvkvpcarhNLPQLPHFrvesfsEDEWNLLYVAVTRAKKRLIMT 932
Cdd:pfam13538    6 TVHKAQGSEFPAVFLVDP---------DLTAHYHS------MLRRRLLYTAVTRARKKLVLV 52
UvrD-helicase pfam00580
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural ...
 441-685 1.68e-09

UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural domains. The Rep family function as dimers. REP helicases catalyze ATP dependent unwinding of double stranded DNA to single stranded DNA. Swiss:P23478, Swiss:P08394 have large insertions near to the carboxy-terminus relative to other members of the family.


Pssm-ID: 395462 [Multi-domain]  Cd Length: 267  Bit Score: 59.95  E-value: 1.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119    441 LTHEQQLILNHkmePLQVVKIMAFAGTGKTSTLV-KYA-----EKWSQSRFLYVTF-NKSIAKQAERV---FPSNVICK- 509
Cdd:pfam00580    1 LNPEQRKAVTH---LGGPLLVLAGAGSGKTRVLTeRIAylileGGIDPEEILAVTFtNKAAREMKERIlklLGKAELSEl 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119    510 ---TFHSMA-------YGHIGRK-----YQSKKKLNLFKLTPFMVNSVLAEGKGGFIRAKLVCKTLENFFASADEELTID 574
Cdd:pfam00580   78 nisTFHSFClrilrkyANRIGLLpnfsiLDELDQLALLKELLEKDRLNLDPKLLRKLELKELISKAKNRLLSPEELQQGA 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119    575 HVPIWCKNSQGQRVMVEQSeKLNGVLEASRLwdnmrkLGECTEEAHQmtHDGYLKLWQlskpslASFDAIFVDEAQDCTP 654
Cdd:pfam00580  158 ADPRDKLAAEFYQEYQERL-KENNALDFDDL------LLLTLELLRS--DPELLEAYR------ERFKYILVDEFQDTNP 222

                          250       260       270
                   ....*....|....*....|....*....|....
gi 30795119    655 A---IMNIVLSQPCGKIFVGDPHQQIYTFRGAVN 685
Cdd:pfam00580  223 IqyrLLKLLAGGHENLFLVGDPDQSIYGFRGADI 256
HelD COG3973
DNA helicase IV [Replication, recombination and repair];
644-932 3.24e-09

DNA helicase IV [Replication, recombination and repair];


Pssm-ID: 443173 [Multi-domain]  Cd Length: 699  Bit Score: 61.03  E-value: 3.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  644 IFVDEAQDCTP----AIMNIVlsqPCGKI-FVGDPHQQIYTFRGA------VNALFTvPHTHVFYLTQSFRFGVEIAyvg 712
Cdd:COG3973  473 VVVDEAQDLSPmqwrVLKRRF---PSASFtIVGDLAQAIHPYRGAesweevLEPLGG-DRARLVELTKSYRSTAEIM--- 545

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  713 atilDVCKRVrkktlvggnhqsgIRGDAKGQVALLSrtnanVFDEAVRVTEGEFPSRIHLIGGIKsfgldRIIDIW---- 788
Cdd:COG3973  546 ----EFANRV-------------LRAAGPDLPPPES-----VRRHGEPPRVVRVPSEAELAAAVV-----EAVRELlaeg 598

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  789 -----ILLQPEEERRKqnlvikdkfIRRWVHKegfsGFKRYVTAAEDKELEAKIAVVekyniripelvqriekchiedld 863
Cdd:COG3973  599 egtiaVICKTAREAEA---------LYAALKA----GLPVTLIDDESEELEAGVVVL----------------------- 642

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30795119  864 faeyilgTVHKAKGLEFDTVHVLDdfvkvpcarhnlpqlPHFRVESfSEDEWNLLYVAVTRAKKRLIMT 932
Cdd:COG3973  643 -------PAYLAKGLEFDAVVVVD---------------PDEIVYE-SPRGRRLLYVALTRATHRLTVL 688
F-box_FBXO6-like cd22168
F-box domain found in F-box only proteins FBXO6, FBXO44 and similar proteins; This subfamily ...
 211-261 3.28e-08

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


Pssm-ID: 438939 [Multi-domain]  Cd Length: 82  Bit Score: 51.52  E-value: 3.28e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30795119  211 HICSLPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISDPLFipWKKLYHR 261
Cdd:cd22168    3 TISDLPEDVLLEILSLVPARDLILSCRLVCSRWRDLVDLPTL--WKRKCQR 51
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 214-248 4.43e-08

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: 49.75  E-value: 4.43e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 30795119  214 SLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIIS 248
Cdd:cd09917    2 DLPDEILLKILSYLDPRDLL-RLSLVCKRWRELAS 35
SF1_C_RecD cd18809
C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11. ...
 866-931 5.20e-08

C-terminal helicase domain of RecD family helicases; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD family helicases are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350196 [Multi-domain]  Cd Length: 80  Bit Score: 51.02  E-value: 5.20e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30795119  866 EYILG---TVHKAKGLEFDTVHVLddfvkvpcarhnlpqLPhfrvESFSEDEWNLLYVAVTRAKKRLIM 931
Cdd:cd18809   29 ERLQAyamTIHKSQGSEFDRVIVV---------------LP----TSHPMLSRGLLYTALTRARKLLTL 78
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 668-931 6.36e-08

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 56.52  E-value: 6.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  668 IFVGDPHQ----QiytfRGAV-NALFTVPHTHVFYLTQSFRFGveiayvgatildvckrvrkktlvggnHQSGIrgdakg 742
Cdd:COG0507  250 ILVGDPDQlpsvG----AGAVlRDLIESGTVPVVELTEVYRQA--------------------------DDSRI------ 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  743 qVALLSRTNANVFDEAVrvtEGEFPSRIHLIGGIKSFGLDRIIDIWILLqPEEERRKQ------------NLVIKDKFIR 810
Cdd:COG0507  294 -IELAHAIREGDAPEAL---NARYADVVFVEAEDAEEAAEAIVELYADR-PAGGEDIQvlaptnagvdalNQAIREALNP 368

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119  811 RWVHKEGFSGFKRYVTAAEDK--------ELEAK---IAVVEKYNIRIPELVQRIEKCHIEDLDFAEYI---LG---TVH 873
Cdd:COG0507  369 AGELERELAEDGELELYVGDRvmftrndyDLGVFngdIGTVLSIDEDEGRLTVRFDGREIVTYDPSELDqleLAyaiTVH 448

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30795119  874 KAKGLEFDTVHVLddfvkvpcarhnlpqLPHFRVESFSedeWNLLYVAVTRAKKRLIM 931
Cdd:COG0507  449 KSQGSTFDRVILV---------------LPSEHSPLLS---RELLYTALTRARELLTL 488
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 212-252 1.31e-07

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


Pssm-ID: 425796  Cd Length: 43  Bit Score: 48.69  E-value: 1.31e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 30795119    212 ICSLPSEVLRHVFAFLPVEDLyWNLSLVCHLWREIISDPLF 252
Cdd:pfam00646    1 LLDLPDDLLLEILSRLDPKDL-LRLSLVSKRWRSLVDSLKL 40
PRK13909 PRK13909
RecB-like helicase;
846-937 1.34e-07

RecB-like helicase;


Pssm-ID: 237554 [Multi-domain]  Cd Length: 910  Bit Score: 55.75  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119   846 RIPELVQRIEKCHIEDLDFAEY---ILgTVHKAKGLEFDTVHVLDDFVKvPCARH----------NLPQLpHFRV---ES 909
Cdd:PRK13909  585 DIEEFLFKLEPCDKEIASEESKgvqIM-TVHKSKGLEFEHVIVCDRLGK-PNSDSsnllfeydgiELWQI-YYRIkgrEN 661

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 30795119   910 F---------------SEDEWNLLYVAVTRAKKRLIMTKSLEN 937
Cdd:PRK13909  662 FdkdyaralekekalkYEEEINVLYVAFTRAKNSLIVVKKDES 704
F-box_FBXO33 cd22104
F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called ...
 214-258 1.31e-06

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: 46.09  E-value: 1.31e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 30795119  214 SLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKL 258
Cdd:cd22104    3 NLPSVVLVHIFSYLPPRDRL-RASSTCRRWREALFHPSL--WRSL 44
F-box_FBXL4 cd22117
F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also ...
 215-261 7.15e-06

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


Pssm-ID: 438889  Cd Length: 47  Bit Score: 43.76  E-value: 7.15e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 30795119  215 LPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKLYHR 261
Cdd:cd22117    4 LPYELIQLILSYLDLPSLC-RLSQTCKLFRKHCYDPLL--WKELNLQ 47
FBOX smart00256
A Receptor for Ubiquitination Targets;
215-258 3.71e-05

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 41.65  E-value: 3.71e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 30795119     215 LPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKL 258
Cdd:smart00256    1 LPDEILEEILSKLDPKDLL-RLRKVSRKWRSLIDSHDF--WFKL 41
F-box_FBXO10 cd22090
F-box domain found in F-box only protein 10 (FBXO10) and similar proteins; FBXO10, also called ...
 211-259 4.29e-05

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: 41.95  E-value: 4.29e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 30795119  211 HICSLPSEVLRHVFAFLPVEDLyWNLSLVCHLWREIISDPLFIPWKKLY 259
Cdd:cd22090    1 EVTGLPLELWRLILAYLPVRDL-CRCCQVCRAWYELILSLDSTRWKQLY 48
recB TIGR00609
exodeoxyribonuclease V, beta subunit; The RecBCD holoenzyme is a multifunctional nuclease with ...
 871-934 1.88e-04

exodeoxyribonuclease V, beta subunit; The RecBCD holoenzyme is a multifunctional nuclease with potent ATP-dependent exodeoxyribonuclease activity. Ejection of RecD, as occurs at chi recombinational hotspots, cripples exonuclease activity in favor of recombinagenic helicase activity. All proteins in this family for which functions are known are DNA-DNA helicases that are used as part of an exonuclease-helicase complex (made up of RecBCD homologs) that function to generate substrates for the initiation of recombination and recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273172 [Multi-domain]  Cd Length: 1087  Bit Score: 45.50  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30795119    871 TVHKAKGLEFDTV--------HVLDDFVKVPCARH-----NLPQLPHF----RVESFSEDEwNLLYVAVTRAKKRLIMTK 933
Cdd:TIGR00609  657 TIHKSKGLEYPIVflpfitdaKKSNFASLHDQHSHeyqlyDFNQSEENqklaRVERLAEDL-RLLYVALTRAKKQLFIGI 735


                   .
gi 30795119    934 S 934
Cdd:TIGR00609  736 A 736
F-box_FBXO45 cd22111
F-box domain found in F-box only protein 45 (FBXO45) and similar proteins; FBXO45, also called ...
 215-243 1.91e-04

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: 39.57  E-value: 1.91e-04
                         10        20
                 ....*....|....*....|....*....
gi 30795119  215 LPSEVLRHVFAFLPVEDLYwNLSLVCHLW 243
Cdd:cd22111    4 LPSRVLEVIFSYLDLPDLR-NCSLVCKSW 31
recB TIGR00609
exodeoxyribonuclease V, beta subunit; The RecBCD holoenzyme is a multifunctional nuclease with ...
 641-683 3.37e-04

exodeoxyribonuclease V, beta subunit; The RecBCD holoenzyme is a multifunctional nuclease with potent ATP-dependent exodeoxyribonuclease activity. Ejection of RecD, as occurs at chi recombinational hotspots, cripples exonuclease activity in favor of recombinagenic helicase activity. All proteins in this family for which functions are known are DNA-DNA helicases that are used as part of an exonuclease-helicase complex (made up of RecBCD homologs) that function to generate substrates for the initiation of recombination and recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273172 [Multi-domain]  Cd Length: 1087  Bit Score: 44.73  E-value: 3.37e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 30795119    641 FDAIFVDEAQDCTP---AIMN-IVLSQPCGK-IFVGDPHQQIYTFRGA 683
Cdd:TIGR00609  297 YPIALIDEFQDTDPqqyRIFSkLFIAQKETSlFLIGDPKQAIYSFRGA 344
F-box_FBXO42 cd22110
F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called ...
 212-249 3.57e-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: 38.86  E-value: 3.57e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 30795119  212 ICSLPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISD 249
Cdd:cd22110    1 INDLPEEILEYILSYLSPYGDLKSAALVCKRWHRIIKG 38
F-box_4 pfam15966
F-box;
211-248 3.79e-04

F-box;


Pssm-ID: 464958  Cd Length: 116  Bit Score: 41.12  E-value: 3.79e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 30795119    211 HICSLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIIS 248
Cdd:pfam15966    4 SLSSLPFEVLQHIASFLDSFSLS-QLSLVSRLMREVCA 40
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
 637-684 3.86e-04

DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. Their helicase core is surrounded by C and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains or domains engaged in protein-protein interactions. SF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 438706 [Multi-domain]  Cd Length: 121  Bit Score: 41.32  E-value: 3.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30795119  637 SLASFDAIFVDEAQDCTPAIMNIV--LSQPCGK-IFVGDPHQQIYTFRGAV 684
Cdd:cd17914   43 AAAQLDNILVDEAAQILEPETSRLidLALDQGRvILVGDHDQLGPVWRGAV 93
F-box_FBXO4 cd22085
F-box domain found in F-box only protein 4 (FBXO4) and similar proteins; FBXO4, also called ...
 212-261 5.37e-04

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


Pssm-ID: 438857  Cd Length: 50  Bit Score: 38.93  E-value: 5.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 30795119  212 ICSLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKLYHR 261
Cdd:cd22085    3 LNHLPIDLQLYILSFLSPHDLC-QLGLTSHYWHTLVRDPLL--WRYFLLR 49
F-box_FBXO3 cd22084
F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called ...
 212-262 6.42e-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: 38.39  E-value: 6.42e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30795119  212 ICSLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKLYHRY 262
Cdd:cd22084    1 LDDLPSDPLLNILSFLDYRDLI-SCSQVCRRLNQLCSHDPL--WKRLCKKY 48
F-box_FBXL8 cd22121
F-box domain found in F-box/LRR-repeat protein 8 (FBXL8) and similar proteins; FBXL8, also ...
 214-248 9.91e-04

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: 37.72  E-value: 9.91e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 30795119  214 SLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIIS 248
Cdd:cd22121    2 ALPEEILVHIFRHLSLRDRY-AAAQVCKHWREAAL 35
F-box_FBXL12 cd22123
F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also ...
 212-249 1.07e-03

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


Pssm-ID: 438895  Cd Length: 42  Bit Score: 37.71  E-value: 1.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 30795119  212 ICSLPSEVLRHVFAFLPVEDLYWNlSLVCHLWREIISD 249
Cdd:cd22123    1 LDQLPENVLLEILSYLPVRDLLRI-SRVCKRWRRLVYD 37
F-box_FBXW5 cd22132
F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, ...
 215-260 1.38e-03

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: 37.59  E-value: 1.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 30795119  215 LPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKLYH 260
Cdd:cd22132    4 LPDSLLLHIFSYLSPKDLL-AAGQVCKQWYRVSRDEFL--WKELFY 46
F-box_FBXO13 cd22092
F-box domain found in F-box only protein 13 (FBXO13) and similar proteins; FBXO13, also called ...
 211-258 2.13e-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: 37.01  E-value: 2.13e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 30795119  211 HICSLPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISDPLFipWKKL 258
Cdd:cd22092    1 NINQLPDSILLKIFSYLSLQERCLSASLVCKYWRDLCLDSQF--WKQI 46
F-box_AtSKIP31-like cd22166
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 31 (AtSKIP31) and similar ...
 214-259 2.26e-03

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


Pssm-ID: 438937  Cd Length: 46  Bit Score: 37.05  E-value: 2.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 30795119  214 SLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKLY 259
Cdd:cd22166    3 KLPPELFRHILKFLSPEDLT-SCATVCRFLRGAASDESL--WRRLY 45
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
 871-929 3.07e-03

exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha subunit, RecD. RecD is part of a RecBCD complex. A related family in the Gram-positive bacteria separates in a phylogenetic tree, has an additional N-terminal extension of about 200 residues, and is not supported as a member of a RecBCD complex by neighboring genes. The related family is consequently described by a different model. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273631 [Multi-domain]  Cd Length: 582  Bit Score: 41.28  E-value: 3.07e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 30795119    871 TVHKAKGLEFDTVHVlddfvkvpcarhnlpQLPHFRVESFSEDewnLLYVAVTRAKKRL 929
Cdd:TIGR01447  521 TVHKSQGSEFDHVIL---------------ILPNGNSPVLTRE---LLYTGITRAKDQL 561
F-box_FBXW9 cd22135
F-box domain found in F-box/WD repeat-containing protein 9 (FBXW9) and similar proteins; FBXW9, ...
 214-249 3.74e-03

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


Pssm-ID: 438907  Cd Length: 45  Bit Score: 36.10  E-value: 3.74e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 30795119  214 SLPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISD 249
Cdd:cd22135    3 SLPPELLLHICSYLDARFVLHVLPLVCKTFRDILSD 38
recB PRK10876
exonuclease V subunit beta; Provisional
 646-683 5.75e-03

exonuclease V subunit beta; Provisional


Pssm-ID: 236784 [Multi-domain]  Cd Length: 1181  Bit Score: 40.72  E-value: 5.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 30795119   646 VDEAQDCTPA----IMNIVLSQP-CGKIFVGDPHQQIYTFRGA 683
Cdd:PRK10876  383 IDEFQDTDPQqyriFRRIYRHQPeTALLLIGDPKQAIYAFRGA 425
F-box_FBXO30-like cd22101
F-box domain found in F-box only protein 30 (FBXO30), F-box only protein 40 (FBXO40) and ...
 212-248 6.13e-03

F-box domain found in F-box only protein 30 (FBXO30), F-box only protein 40 (FBXO40) and similar proteins; FBXO30, also called FBX30, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It is required for muscle atrophy following denervation. FBXO30 regulates mammopoiesis by targeting the bipolar mitotic kinesin Eg5. FBXO40, also called FBX40, or muscle disease-related protein, is a probable substrate-recognition component of an SCF-type E3 ubiquitin ligase complex that may function in myogenesis. 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: 438873  Cd Length: 45  Bit Score: 35.81  E-value: 6.13e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 30795119  212 ICSLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIIS 248
Cdd:cd22101    1 LSSLPFEILQHIARFLDSFSLC-NLSLVSRLMREVCC 36
F-box_FBXL6 cd22119
F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also ...
 214-252 6.28e-03

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


Pssm-ID: 438891  Cd Length: 47  Bit Score: 35.69  E-value: 6.28e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 30795119  214 SLPSEVLRHVFAFL-----PVEDLYwNLSLVCHLWREIISDPLF 252
Cdd:cd22119    3 RLPPEILVKIFQFAvategAVPLLC-RLSRVCRLWREVALDPSL 45
F-box_FBXO15 cd22093
F-box domain found in F-box only protein 15 (FBXO15) and similar proteins; FBXO15, also called ...
 212-259 7.40e-03

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


Pssm-ID: 438865  Cd Length: 46  Bit Score: 35.30  E-value: 7.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 30795119  212 ICSLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKLY 259
Cdd:cd22093    1 IERLPSEILLKILSYLDASSLL-CISCVNKLFYQLANDNAL--WRKLY 45
F-box_AtSKIP19-like cd22164
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 19 (AtSKIP19) and similar ...
 215-259 7.63e-03

F-box domain found in Arabidopsis thaliana SKP1-interacting partner 19 (AtSKIP19) and similar proteins; AtSKIP19, also called F-box protein SKIP19, or F-box/LRR-repeat protein 20 (FBL20), is a component of SCF (SPK1/ASK-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It interacts with CUL1 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: 438935 [Multi-domain]  Cd Length: 47  Bit Score: 35.27  E-value: 7.63e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 30795119  215 LPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISDPLFipWKKLY 259
Cdd:cd22164    5 LPDDLTASILSRLGAIDILTNAQKVCKLWRRICKDPSM--WRVID 47
F-box_FBXO31 cd22102
F-box domain found in F-box only protein 31 (FBXO31) and similar proteins; FBXO31, also called ...
 212-247 8.63e-03

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


Pssm-ID: 438874  Cd Length: 48  Bit Score: 35.48  E-value: 8.63e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 30795119  212 ICSLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREII 247
Cdd:cd22102    1 ILDLPPELLVEIFSSLPGTDLP-SLAQVCKKFREIL 35
F-box_AtFBW1-like cd22157
F-box domain found in Arabidopsis thaliana F-box/WD-40 repeat-containing protein 1 (AtFBW1) ...
 214-252 9.15e-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: 35.13  E-value: 9.15e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 30795119  214 SLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLF 252
Cdd:cd22157    2 SLPDDLVEEILSRLPAKSLL-RFRCVCKQWNSLISSPSF 39
F-box_FBA cd22083
F-box domain found in the F-box associated (FBA) family of F-box proteins; The F-box ...
 214-248 9.28e-03

F-box domain found in the F-box associated (FBA) family of F-box proteins; The F-box associated (FBA) family is composed of FBXO2, FBXO6, FBXO17, FBXO27, and FBXO44, which contain a conserved G domain that mediates substrate binding. Members of this family play diverse roles in glycoprotein quality control. They bind high mannose and sulfated glycoproteins, with one FBA protein, FBXO44, failing to bind any glycans on the tested arrays. FBA proteins are components of canonical SCF (Skp1, Cullin1, and Rbx1) complexes, yet FBXO2 bound very little Cullin1, suggesting that FBXO2 may exist primarily as a heterodimer with Skp1. 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: 438855  Cd Length: 37  Bit Score: 35.06  E-value: 9.28e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 30795119  214 SLPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIIS 248
Cdd:cd22083    3 EIPEELLLEILTHVPATSLITNCRLVCTLWRDIID 37
 
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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