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Conserved domains on  [gi|2217279114|ref|XP_047281858|]
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F-box DNA helicase 1 isoform X9 [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 ...
 137-184 1.41e-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: 1.41e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217279114 137 HICSLPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISDPLFIPWKKL 184
Cdd:cd22095     1 HIQQLPEELLRNIFAFLPAEDLYQNISLVCRHWRDIVSDPLFIPWKKL 48
UvrD super family cl33806
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
366-858 1.62e-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: 1.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 366 QLTHEQQLILNHKMEPLQVVkimAFAGTGKTSTLVKYA------EKWSQSRFLYVTF-NKS-------IAKQAERVFPSN 431
Cdd:COG0210     6 GLNPEQRAAVEHPEGPLLVL---AGAGSGKTRVLTHRIayliaeGGVDPEQILAVTFtNKAaremrerIEALLGRLARGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 432 VICkTFHSMAYGHIgRKYQSKKKLNlfklTPF----------MVNSVLAE----GKGGFIRaklvckTLENFFASA-DEE 496
Cdd:COG0210    83 WVG-TFHSLALRIL-RRHAELLGLP----PNFtildgddqlrLIKELLKElgldEKRFPPR------ELLSLISRAkNEG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 497 LTIDHVPIWCKNSQGQRVMV------EQSEKLNG-------VLEASRLWDNmrklgecteeahqmtHDGYLKLWQlskps 563
Cdd:COG0210   151 LTPEELAELLAADPEWRAAAelyeayQERLRANNaldfddlLLLAVRLLEE---------------NPEVLEKYQ----- 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 564 lASFDAIFVDEAQDCTPAIMNIV--LSQPCGKIF-VGDPHQQIYTFRGA--VN-ALFTV--PHTHVFYLTQSFRFGVEI- 634
Cdd:COG0210   211 -NRFRYILVDEYQDTNPAQYELLrlLAGDGRNLCvVGDDDQSIYGFRGAdpENiLRFEKdfPDAKVIKLEQNYRSTQNIl 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 635 -----------------------------AYVGATILD----VCKRVRKktlvggNHQSGIRgdaKGQVALLSRTNA--N 679
Cdd:COG0210   290 daanaviannpgrlgknlwtdngegekvrLYVAPDEEEearfVADEIRE------LHEEGVP---LSDIAVLYRTNAqsR 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 680 VFDEA-------VRVTEG-EFPSR---------IHLI-----------------GGIKSFGLDRI--------IDIW-IL 716
Cdd:COG0210   361 ALEEAlrragipYRVVGGlRFYERaeikdllayLRLLanpdddvallrilnvprRGIGAATLERLreaareegISLLeAL 440

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 717 LQPEEERR---KQNLVIKD--KFIRRWVHKEGF-------------SGFKRYVTAAEDKELEAKIA-------VVEKYNI 771
Cdd:COG0210   441 RDLGELAGlsgRAAKALRRfaELLEALRAAAERlpleellealldeSGYEEELREEAGEEAERRLEnleelvdAAARFEE 520

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 772 R-----IPELVQRIEkcHIEDLDFAEY-----ILGTVHKAKGLEFDTVHVL---DDFvkvpcarhnlpqLPHFRveSFS- 837
Cdd:COG0210   521 RnpgasLEAFLEELA--LLSDLDAADEdedavTLMTLHAAKGLEFPVVFLVgleEGL------------FPHQR--SLDd 584

                         650       660
                  ....*....|....*....|....*
gi 2217279114 838 ----EDEWNLLYVAVTRAKKRLIMT 858
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 ...
 137-184 1.41e-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: 1.41e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217279114 137 HICSLPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISDPLFIPWKKL 184
Cdd:cd22095     1 HIQQLPEELLRNIFAFLPAEDLYQNISLVCRHWRDIVSDPLFIPWKKL 48
UvrD COG0210
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
366-858 1.62e-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: 1.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 366 QLTHEQQLILNHKMEPLQVVkimAFAGTGKTSTLVKYA------EKWSQSRFLYVTF-NKS-------IAKQAERVFPSN 431
Cdd:COG0210     6 GLNPEQRAAVEHPEGPLLVL---AGAGSGKTRVLTHRIayliaeGGVDPEQILAVTFtNKAaremrerIEALLGRLARGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 432 VICkTFHSMAYGHIgRKYQSKKKLNlfklTPF----------MVNSVLAE----GKGGFIRaklvckTLENFFASA-DEE 496
Cdd:COG0210    83 WVG-TFHSLALRIL-RRHAELLGLP----PNFtildgddqlrLIKELLKElgldEKRFPPR------ELLSLISRAkNEG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 497 LTIDHVPIWCKNSQGQRVMV------EQSEKLNG-------VLEASRLWDNmrklgecteeahqmtHDGYLKLWQlskps 563
Cdd:COG0210   151 LTPEELAELLAADPEWRAAAelyeayQERLRANNaldfddlLLLAVRLLEE---------------NPEVLEKYQ----- 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 564 lASFDAIFVDEAQDCTPAIMNIV--LSQPCGKIF-VGDPHQQIYTFRGA--VN-ALFTV--PHTHVFYLTQSFRFGVEI- 634
Cdd:COG0210   211 -NRFRYILVDEYQDTNPAQYELLrlLAGDGRNLCvVGDDDQSIYGFRGAdpENiLRFEKdfPDAKVIKLEQNYRSTQNIl 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 635 -----------------------------AYVGATILD----VCKRVRKktlvggNHQSGIRgdaKGQVALLSRTNA--N 679
Cdd:COG0210   290 daanaviannpgrlgknlwtdngegekvrLYVAPDEEEearfVADEIRE------LHEEGVP---LSDIAVLYRTNAqsR 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 680 VFDEA-------VRVTEG-EFPSR---------IHLI-----------------GGIKSFGLDRI--------IDIW-IL 716
Cdd:COG0210   361 ALEEAlrragipYRVVGGlRFYERaeikdllayLRLLanpdddvallrilnvprRGIGAATLERLreaareegISLLeAL 440

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 717 LQPEEERR---KQNLVIKD--KFIRRWVHKEGF-------------SGFKRYVTAAEDKELEAKIA-------VVEKYNI 771
Cdd:COG0210   441 RDLGELAGlsgRAAKALRRfaELLEALRAAAERlpleellealldeSGYEEELREEAGEEAERRLEnleelvdAAARFEE 520

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 772 R-----IPELVQRIEkcHIEDLDFAEY-----ILGTVHKAKGLEFDTVHVL---DDFvkvpcarhnlpqLPHFRveSFS- 837
Cdd:COG0210   521 RnpgasLEAFLEELA--LLSDLDAADEdedavTLMTLHAAKGLEFPVVFLVgleEGL------------FPHQR--SLDd 584

                         650       660
                  ....*....|....*....|....*
gi 2217279114 838 ----EDEWNLLYVAVTRAKKRLIMT 858
Cdd:COG0210   585 eeelEEERRLFYVAITRARERLYLT 609
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
 762-859 9.00e-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: 9.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 762 KIAVVEKYNIRIPELVQRIEKCHIEDLDFAEYILGTVHKAKGLEFDTVHVLDDFVKvpcarhnlpqlphfrvesfsEDEW 841
Cdd:cd18786    12 KGVVLTPYHRDRAYLNQYLQGLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTAN--------------------SLTP 71

                          90
                  ....*....|....*...
gi 2217279114 842 NLLYVAVTRAKKRLIMTK 859
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 ...
 797-862 3.82e-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: 68.97  E-value: 3.82e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217279114 797 TVHKAKGLEFDTVHVLDdfvkvpCARHNLPQLPHFRVESFSEDEWNLLYVAVTRAKKRLIMTKSLE 862
Cdd:pfam13361 318 TIHQAKGLEFDTVFLAG------LEEGIFPSYRSIKDEGNLEEERRLFYVAITRAKKRLYISYSKS 377
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 138-185 1.07e-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: 1.07e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217279114 138 ICSLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKLY 185
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLL-RLALVCRRWRELASDDSL--WRRLC 45
PRK13909 PRK13909
RecB-like helicase;
772-863 1.86e-07

RecB-like helicase;


Pssm-ID: 237554 [Multi-domain]  Cd Length: 910  Bit Score: 55.36  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 772 RIPELVQRIEKCHIEDLDFAEY---ILgTVHKAKGLEFDTVHVLDDFVKvPCARH----------NLPQLpHFRV---ES 835
Cdd:PRK13909  585 DIEEFLFKLEPCDKEIASEESKgvqIM-TVHKSKGLEFEHVIVCDRLGK-PNSDSsnllfeydgiELWQI-YYRIkgrEN 661

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2217279114 836 F---------------SEDEWNLLYVAVTRAKKRLIMTKSLEN 863
Cdd:PRK13909  662 FdkdyaralekekalkYEEEINVLYVAFTRAKNSLIVVKKDES 704
FBOX smart00256
A Receptor for Ubiquitination Targets;
141-184 3.70e-05

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 41.65  E-value: 3.70e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2217279114  141 LPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKL 184
Cdd:smart00256   1 LPDEILEEILSKLDPKDLL-RLRKVSRKWRSLIDSHDF--WFKL 41
recB TIGR00609
exodeoxyribonuclease V, beta subunit; The RecBCD holoenzyme is a multifunctional nuclease with ...
 797-860 1.73e-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: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114  797 TVHKAKGLEFDTV--------HVLDDFVKVPCARH-----NLPQLPHF----RVESFSEDEwNLLYVAVTRAKKRLIMTK 859
Cdd:TIGR00609  657 TIHKSKGLEYPIVflpfitdaKKSNFASLHDQHSHeyqlyDFNQSEENqklaRVERLAEDL-RLLYVALTRAKKQLFIGI 735


                   .
gi 2217279114  860 S 860
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 ...
 137-184 1.41e-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: 1.41e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217279114 137 HICSLPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISDPLFIPWKKL 184
Cdd:cd22095     1 HIQQLPEELLRNIFAFLPAEDLYQNISLVCRHWRDIVSDPLFIPWKKL 48
UvrD COG0210
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
366-858 1.62e-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: 1.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 366 QLTHEQQLILNHKMEPLQVVkimAFAGTGKTSTLVKYA------EKWSQSRFLYVTF-NKS-------IAKQAERVFPSN 431
Cdd:COG0210     6 GLNPEQRAAVEHPEGPLLVL---AGAGSGKTRVLTHRIayliaeGGVDPEQILAVTFtNKAaremrerIEALLGRLARGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 432 VICkTFHSMAYGHIgRKYQSKKKLNlfklTPF----------MVNSVLAE----GKGGFIRaklvckTLENFFASA-DEE 496
Cdd:COG0210    83 WVG-TFHSLALRIL-RRHAELLGLP----PNFtildgddqlrLIKELLKElgldEKRFPPR------ELLSLISRAkNEG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 497 LTIDHVPIWCKNSQGQRVMV------EQSEKLNG-------VLEASRLWDNmrklgecteeahqmtHDGYLKLWQlskps 563
Cdd:COG0210   151 LTPEELAELLAADPEWRAAAelyeayQERLRANNaldfddlLLLAVRLLEE---------------NPEVLEKYQ----- 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 564 lASFDAIFVDEAQDCTPAIMNIV--LSQPCGKIF-VGDPHQQIYTFRGA--VN-ALFTV--PHTHVFYLTQSFRFGVEI- 634
Cdd:COG0210   211 -NRFRYILVDEYQDTNPAQYELLrlLAGDGRNLCvVGDDDQSIYGFRGAdpENiLRFEKdfPDAKVIKLEQNYRSTQNIl 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 635 -----------------------------AYVGATILD----VCKRVRKktlvggNHQSGIRgdaKGQVALLSRTNA--N 679
Cdd:COG0210   290 daanaviannpgrlgknlwtdngegekvrLYVAPDEEEearfVADEIRE------LHEEGVP---LSDIAVLYRTNAqsR 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 680 VFDEA-------VRVTEG-EFPSR---------IHLI-----------------GGIKSFGLDRI--------IDIW-IL 716
Cdd:COG0210   361 ALEEAlrragipYRVVGGlRFYERaeikdllayLRLLanpdddvallrilnvprRGIGAATLERLreaareegISLLeAL 440

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 717 LQPEEERR---KQNLVIKD--KFIRRWVHKEGF-------------SGFKRYVTAAEDKELEAKIA-------VVEKYNI 771
Cdd:COG0210   441 RDLGELAGlsgRAAKALRRfaELLEALRAAAERlpleellealldeSGYEEELREEAGEEAERRLEnleelvdAAARFEE 520

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 772 R-----IPELVQRIEkcHIEDLDFAEY-----ILGTVHKAKGLEFDTVHVL---DDFvkvpcarhnlpqLPHFRveSFS- 837
Cdd:COG0210   521 RnpgasLEAFLEELA--LLSDLDAADEdedavTLMTLHAAKGLEFPVVFLVgleEGL------------FPHQR--SLDd 584

                         650       660
                  ....*....|....*....|....*
gi 2217279114 838 ----EDEWNLLYVAVTRAKKRLIMT 858
Cdd:COG0210   585 eeelEEERRLFYVAITRARERLYLT 609
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
 762-859 9.00e-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: 9.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 762 KIAVVEKYNIRIPELVQRIEKCHIEDLDFAEYILGTVHKAKGLEFDTVHVLDDFVKvpcarhnlpqlphfrvesfsEDEW 841
Cdd:cd18786    12 KGVVLTPYHRDRAYLNQYLQGLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTAN--------------------SLTP 71

                          90
                  ....*....|....*...
gi 2217279114 842 NLLYVAVTRAKKRLIMTK 859
Cdd:cd18786    72 RRLYVALTRARKRLVIYD 89
DEXQc_UvrD cd17932
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ...
 370-628 3.75e-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: 3.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 370 EQQLILNHKMEPLQVVkimAFAGTGKTSTLV-KYA-----EKWSQSRFLYVTFNKSIAKQ-AERVFP-------SNVICK 435
Cdd:cd17932     3 EQREAVTHPDGPLLVL---AGAGSGKTRVLThRIAylileGGVPPERILAVTFTNKAAKEmRERLRKllgeqlaSGVWIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 436 TFHSMAYgHIGRKYQSKKKLnlfkltpfmvnsvlaegkggfiraklvcktlenffasadeeltidhvpiwcknsqgqrvm 515
Cdd:cd17932    80 TFHSFAL-RILRRYGDFDDL------------------------------------------------------------ 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 516 veqseklngVLEASRLWDNMRKLgecteeahqmthdgyLKLWQlskpslASFDAIFVDEAQDCTPAIMNIV--LSQPCGK 593
Cdd:cd17932    99 ---------LLYALELLEENPDV---------------REKLQ------SRFRYILVDEYQDTNPLQYELLklLAGDGKN 148

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2217279114 594 IF-VGDPHQQIYTFRGAVNALFT-----VPHTHVFYLTQSF 628
Cdd:cd17932   149 LFvVGDDDQSIYGFRGADPENILdfekdFPDAKVIKLEENY 189
COG3972 COG3972
Superfamily I DNA and RNA helicases [Replication, recombination and repair];
365-870 1.23e-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: 1.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 365 IQLTHEQQLILnhKMEPLQVVKIMAFAGTGKTSTL----VKYAEKWSQSRFLYVTFNKSIAKQaervfpsnvicktfhsm 440
Cdd:COG3972   158 AVLDLQQERIA--RSIPDGPQRIRGVAGSGKTVLLaakaAYLALKHPGWRILVTCFNRSLADH----------------- 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 441 ayghigrkyqskkklnlfkltpfmvnsvlaegkggfIRAKLvcktlENFFASADEELTIDHVPIWCKNSQGQRVMVEQSE 520
Cdd:COG3972   219 ------------------------------------LRDLI-----PRFLRRFSNGEPEDNVKLIVFHAWGGKLLKQYGI 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 521 KLNGVLEASRLWDnmrklgECTEEAhqmthdgyLKLWQLSKPsLASFDAIFVDEAQDCTPAIMNIV---LSQPCGKIFV- 596
Cdd:COG3972   258 PPLTFSQPNEAFD------EACKAL--------LEAIQGEII-PPIYDAILIDEAQDFEPEFLRLLyqlLKPPKKRLIWa 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 597 GDPHQQIY--TFRGAVNALFTVPHTHVfyLTQSFRFGVEIAYVGATILDVCKRVRKktLVGGNHQSGIRgDAKGQVALLS 674
Cdd:COG3972   323 YDEAQNIYgrKIPSAGGIPAGIGRDTI--LKKNYRNTRPILTFAHAFGMGLLRPPG--LLQGDAEDYEV-ERPGDKVTLI 397

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 675 RTNANVFDEAVRVTEGEFPSRIHLIGGIKsfglDRIIDiwiLLQPEEERRKQNLVIkdkfirrwvhkegfsgfkrYVTAA 754
Cdd:COG3972   398 RPPEPAGRKGPLPEFKKYDDRAEELEAIA----EEIKK---NLRDEGLRPSDIAVI-------------------YLGNN 451

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 755 EDKELEAKIA-VVEKYNIRIpelvqrieKCHIEDLDFAEYI------LGTVHKAKGLEFDTVHVLddfvkvpcarhNLPQ 827
Cdd:COG3972   452 EAKELGDRLAaALERQGIDS--------YIAGARSDPNFFWkdggvtISTIHRAKGLEAPVVIIV-----------GLDQ 512

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 2217279114 828 LPHFrvESFsEDEWNLLYVAVTRAKKRLIMTKSLENILTLAGE 870
Cdd:COG3972   513 LAKG--ESL-ERLRNLLYVAMTRARGWLVVSGSGESMAELYDE 552
RecB COG1074
3#-5# helicase subunit RecB of the DNA repair enzyme RecBCD (exonuclease V) [Replication, ...
 567-858 6.70e-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: 6.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 567 FDAIFVDEAQDCTPAIMNIV-------LSQPCGKIFVGDPHQQIYTFRGA------------------------------ 609
Cdd:COG1074   285 YRHILVDEFQDTSPLQWEILrrlageaLADGRTLFLVGDPKQSIYRFRGAdpelflearralegrvdgerltlttnfrst 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 610 ------VNALFT---------VPHTHVFYLTQSFRFGVEIAYVGATILD-----------VCKRVRKKTLVGGNHQSGIR 663
Cdd:COG1074   365 pevvdaVNALFAqlmgagfgeIPYEPVEALRPGAYPAVELWPLEPDDVSeedarerearaVAARIRRLLAEGTTVEGGGR 444

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 664 GDAKGQVALLSRTN------ANVFDEA---VRVTEGE-------------------FPS-RIHLIGGIKS--FGLD---- 708
Cdd:COG1074   445 PVRPGDIAVLVRTRseaaaiARALKAAgipVAASDRLslfespevrdllallrallNPEdDLALAAVLRSplFGLSdedl 524

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 709 -------RIIDIWILLQPEEERRKQNLVIKDkfIRRWVHKEGFS----------GFKRYVTAAEDKE--------LEAKI 763
Cdd:COG1074   525 aalaadrKGESLWEALRAYERLARALERLRA--LRELARRLGLAellerlleetGLLERLLALPGGErrlanllhLDELL 602

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 764 AVVEKYNIR----IPELVQRIEKCHIEDLDFAEYILG---------TVHKAKGLEFDTVhvlddFVkvPCARHNLpqlph 830
Cdd:COG1074   603 QLALEYEQTggpgLAGFLRWLERLIEDGGDEEKRRLEsdadavrimTIHKSKGLEFPVV-----FL--PALRERA----- 670

                         410       420
                  ....*....|....*....|....*...
gi 2217279114 831 fRVESFSEdEWNLLYVAVTRAKKRLIMT 858
Cdd:COG1074   671 -RAEELAE-ELRLLYVALTRARDRLVLS 696
SF1_C_UvrD cd18807
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase ...
 795-858 1.88e-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: 65.72  E-value: 1.88e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217279114 795 LGTVHKAKGLEFDTVHVLDdfvkvpCARHNLPQLPHFRVESFSED----EWNLLYVAVTRAKKRLIMT 858
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 ...
 797-862 3.82e-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: 68.97  E-value: 3.82e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217279114 797 TVHKAKGLEFDTVHVLDdfvkvpCARHNLPQLPHFRVESFSEDEWNLLYVAVTRAKKRLIMTKSLE 862
Cdd:pfam13361 318 TIHQAKGLEFDTVFLAG------LEEGIFPSYRSIKDEGNLEEERRLFYVAITRAKKRLYISYSKS 377
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 138-185 1.07e-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: 1.07e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217279114 138 ICSLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKLY 185
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 ...
 797-858 7.17e-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: 7.17e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217279114 797 TVHKAKGLEFDTVHVLDDfvkvpcarhNLPQLPHFrvesfsEDEWNLLYVAVTRAKKRLIMT 858
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 ...
 367-611 1.61e-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: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 367 LTHEQQLILNHkmePLQVVKIMAFAGTGKTSTLV-KYA-----EKWSQSRFLYVTF-NKSIAKQAERV---FPSNVICK- 435
Cdd:pfam00580   1 LNPEQRKAVTH---LGGPLLVLAGAGSGKTRVLTeRIAylileGGIDPEEILAVTFtNKAAREMKERIlklLGKAELSEl 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 436 ---TFHSMA-------YGHIGRK-----YQSKKKLNLFKLTPFMVNSVLAEGKGGFIRAKLVCKTLENFFASADEELTID 500
Cdd:pfam00580  78 nisTFHSFClrilrkyANRIGLLpnfsiLDELDQLALLKELLEKDRLNLDPKLLRKLELKELISKAKNRLLSPEELQQGA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 501 HVPIWCKNSQGQRVMVEQSeKLNGVLEASRLwdnmrkLGECTEEAHQmtHDGYLKLWQlskpslASFDAIFVDEAQDCTP 580
Cdd:pfam00580 158 ADPRDKLAAEFYQEYQERL-KENNALDFDDL------LLLTLELLRS--DPELLEAYR------ERFKYILVDEFQDTNP 222

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2217279114 581 A---IMNIVLSQPCGKIFVGDPHQQIYTFRGAVN 611
Cdd:pfam00580 223 IqyrLLKLLAGGHENLFLVGDPDQSIYGFRGADI 256
HelD COG3973
DNA helicase IV [Replication, recombination and repair];
570-858 2.94e-09

DNA helicase IV [Replication, recombination and repair];


Pssm-ID: 443173 [Multi-domain]  Cd Length: 699  Bit Score: 61.03  E-value: 2.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 570 IFVDEAQDCTP----AIMNIVlsqPCGKI-FVGDPHQQIYTFRGA------VNALFTvPHTHVFYLTQSFRFGVEIAyvg 638
Cdd:COG3973   473 VVVDEAQDLSPmqwrVLKRRF---PSASFtIVGDLAQAIHPYRGAesweevLEPLGG-DRARLVELTKSYRSTAEIM--- 545

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 639 atilDVCKRVrkktlvggnhqsgIRGDAKGQVALLSrtnanVFDEAVRVTEGEFPSRIHLIGGIKsfgldRIIDIW---- 714
Cdd:COG3973   546 ----EFANRV-------------LRAAGPDLPPPES-----VRRHGEPPRVVRVPSEAELAAAVV-----EAVRELlaeg 598

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 715 -----ILLQPEEERRKqnlvikdkfIRRWVHKegfsGFKRYVTAAEDKELEAKIAVVekyniripelvqriekchiedld 789
Cdd:COG3973   599 egtiaVICKTAREAEA---------LYAALKA----GLPVTLIDDESEELEAGVVVL----------------------- 642

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217279114 790 faeyilgTVHKAKGLEFDTVHVLDdfvkvpcarhnlpqlPHFRVESfSEDEWNLLYVAVTRAKKRLIMT 858
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 ...
 137-187 2.84e-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: 51.90  E-value: 2.84e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217279114 137 HICSLPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISDPLFipWKKLYHR 187
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 ...
 140-174 4.46e-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: 4.46e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2217279114 140 SLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIIS 174
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. ...
 792-857 4.82e-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: 4.82e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217279114 792 EYILG---TVHKAKGLEFDTVHVLddfvkvpcarhnlpqLPhfrvESFSEDEWNLLYVAVTRAKKRLIM 857
Cdd:cd18809    29 ERLQAyamTIHKSQGSEFDRVIVV---------------LP----TSHPMLSRGLLYTALTRARKLLTL 78
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 594-857 5.79e-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: 5.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 594 IFVGDPHQ----QiytfRGAV-NALFTVPHTHVFYLTQSFRFGveiayvgatildvckrvrkktlvggnHQSGIrgdakg 668
Cdd:COG0507   250 ILVGDPDQlpsvG----AGAVlRDLIESGTVPVVELTEVYRQA--------------------------DDSRI------ 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 669 qVALLSRTNANVFDEAVrvtEGEFPSRIHLIGGIKSFGLDRIIDIWILLqPEEERRKQ------------NLVIKDKFIR 736
Cdd:COG0507   294 -IELAHAIREGDAPEAL---NARYADVVFVEAEDAEEAAEAIVELYADR-PAGGEDIQvlaptnagvdalNQAIREALNP 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 737 RWVHKEGFSGFKRYVTAAEDK--------ELEAK---IAVVEKYNIRIPELVQRIEKCHIEDLDFAEYI---LG---TVH 799
Cdd:COG0507   369 AGELERELAEDGELELYVGDRvmftrndyDLGVFngdIGTVLSIDEDEGRLTVRFDGREIVTYDPSELDqleLAyaiTVH 448

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217279114 800 KAKGLEFDTVHVLddfvkvpcarhnlpqLPHFRVESFSedeWNLLYVAVTRAKKRLIM 857
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 ...
 138-178 1.38e-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: 1.38e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217279114 138 ICSLPSEVLRHVFAFLPVEDLyWNLSLVCHLWREIISDPLF 178
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDL-LRLSLVSKRWRSLVDSLKL 40
PRK13909 PRK13909
RecB-like helicase;
772-863 1.86e-07

RecB-like helicase;


Pssm-ID: 237554 [Multi-domain]  Cd Length: 910  Bit Score: 55.36  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114 772 RIPELVQRIEKCHIEDLDFAEY---ILgTVHKAKGLEFDTVHVLDDFVKvPCARH----------NLPQLpHFRV---ES 835
Cdd:PRK13909  585 DIEEFLFKLEPCDKEIASEESKgvqIM-TVHKSKGLEFEHVIVCDRLGK-PNSDSsnllfeydgiELWQI-YYRIkgrEN 661

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2217279114 836 F---------------SEDEWNLLYVAVTRAKKRLIMTKSLEN 863
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 ...
 140-184 1.10e-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: 1.10e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2217279114 140 SLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKL 184
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 ...
 141-187 7.12e-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: 7.12e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217279114 141 LPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKLYHR 187
Cdd:cd22117     4 LPYELIQLILSYLDLPSLC-RLSQTCKLFRKHCYDPLL--WKELNLQ 47
FBOX smart00256
A Receptor for Ubiquitination Targets;
141-184 3.70e-05

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 41.65  E-value: 3.70e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2217279114  141 LPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKL 184
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 ...
 137-185 3.87e-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: 3.87e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2217279114 137 HICSLPSEVLRHVFAFLPVEDLyWNLSLVCHLWREIISDPLFIPWKKLY 185
Cdd:cd22090     1 EVTGLPLELWRLILAYLPVRDL-CRCCQVCRAWYELILSLDSTRWKQLY 48
recB TIGR00609
exodeoxyribonuclease V, beta subunit; The RecBCD holoenzyme is a multifunctional nuclease with ...
 797-860 1.73e-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: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279114  797 TVHKAKGLEFDTV--------HVLDDFVKVPCARH-----NLPQLPHF----RVESFSEDEwNLLYVAVTRAKKRLIMTK 859
Cdd:TIGR00609  657 TIHKSKGLEYPIVflpfitdaKKSNFASLHDQHSHeyqlyDFNQSEENqklaRVERLAEDL-RLLYVALTRAKKQLFIGI 735


                   .
gi 2217279114  860 S 860
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 ...
 141-169 1.90e-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: 1.90e-04
                          10        20
                  ....*....|....*....|....*....
gi 2217279114 141 LPSEVLRHVFAFLPVEDLYwNLSLVCHLW 169
Cdd:cd22111     4 LPSRVLEVIFSYLDLPDLR-NCSLVCKSW 31
recB TIGR00609
exodeoxyribonuclease V, beta subunit; The RecBCD holoenzyme is a multifunctional nuclease with ...
 567-609 3.08e-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: 3.08e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2217279114  567 FDAIFVDEAQDCTP---AIMN-IVLSQPCGK-IFVGDPHQQIYTFRGA 609
Cdd:TIGR00609  297 YPIALIDEFQDTDPqqyRIFSkLFIAQKETSlFLIGDPKQAIYSFRGA 344
F-box_4 pfam15966
F-box;
137-174 3.44e-04

F-box;


Pssm-ID: 464958  Cd Length: 116  Bit Score: 41.12  E-value: 3.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2217279114 137 HICSLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIIS 174
Cdd:pfam15966   4 SLSSLPFEVLQHIASFLDSFSLS-QLSLVSRLMREVCA 40
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
 563-610 3.57e-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: 3.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217279114 563 SLASFDAIFVDEAQDCTPAIMNIV--LSQPCGK-IFVGDPHQQIYTFRGAV 610
Cdd:cd17914    43 AAAQLDNILVDEAAQILEPETSRLidLALDQGRvILVGDHDQLGPVWRGAV 93
F-box_FBXO42 cd22110
F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called ...
 138-175 3.77e-04

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


Pssm-ID: 438882  Cd Length: 38  Bit Score: 38.86  E-value: 3.77e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2217279114 138 ICSLPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISD 175
Cdd:cd22110     1 INDLPEEILEYILSYLSPYGDLKSAALVCKRWHRIIKG 38
F-box_FBXO4 cd22085
F-box domain found in F-box only protein 4 (FBXO4) and similar proteins; FBXO4, also called ...
 138-187 4.47e-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: 4.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217279114 138 ICSLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKLYHR 187
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 ...
 138-188 5.35e-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: 38.78  E-value: 5.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217279114 138 ICSLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKLYHRY 188
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 ...
 140-174 9.21e-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: 9.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2217279114 140 SLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIIS 174
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 ...
 138-175 9.33e-04

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


Pssm-ID: 438895  Cd Length: 42  Bit Score: 37.71  E-value: 9.33e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2217279114 138 ICSLPSEVLRHVFAFLPVEDLYWNlSLVCHLWREIISD 175
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, ...
 141-186 1.27e-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: 1.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217279114 141 LPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKLYH 186
Cdd:cd22132     4 LPDSLLLHIFSYLSPKDLL-AAGQVCKQWYRVSRDEFL--WKELFY 46
F-box_AtSKIP31-like cd22166
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 31 (AtSKIP31) and similar ...
 140-185 1.86e-03

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


Pssm-ID: 438937  Cd Length: 46  Bit Score: 37.05  E-value: 1.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217279114 140 SLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKLY 185
Cdd:cd22166     3 KLPPELFRHILKFLSPEDLT-SCATVCRFLRGAASDESL--WRRLY 45
F-box_FBXO13 cd22092
F-box domain found in F-box only protein 13 (FBXO13) and similar proteins; FBXO13, also called ...
 137-184 2.06e-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: 2.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217279114 137 HICSLPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISDPLFipWKKL 184
Cdd:cd22092     1 NINQLPDSILLKIFSYLSLQERCLSASLVCKYWRDLCLDSQF--WKQI 46
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
 797-855 2.81e-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: 2.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217279114 797 TVHKAKGLEFDTVHVlddfvkvpcarhnlpQLPHFRVESFSEDewnLLYVAVTRAKKRL 855
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, ...
 140-175 3.72e-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: 3.72e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2217279114 140 SLPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISD 175
Cdd:cd22135     3 SLPPELLLHICSYLDARFVLHVLPLVCKTFRDILSD 38
recB PRK10876
exonuclease V subunit beta; Provisional
 572-609 5.27e-03

exonuclease V subunit beta; Provisional


Pssm-ID: 236784 [Multi-domain]  Cd Length: 1181  Bit Score: 40.72  E-value: 5.27e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2217279114  572 VDEAQDCTPA----IMNIVLSQP-CGKIFVGDPHQQIYTFRGA 609
Cdd:PRK10876   383 IDEFQDTDPQqyriFRRIYRHQPeTALLLIGDPKQAIYAFRGA 425
F-box_FBXL6 cd22119
F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also ...
 140-182 5.50e-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: 5.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217279114 140 SLPSEVLRHVFAFL-----PVEDLYwNLSLVCHLWREIISDPLFipWK 182
Cdd:cd22119     3 RLPPEILVKIFQFAvategAVPLLC-RLSRVCRLWREVALDPSL--WT 47
F-box_FBXO30-like cd22101
F-box domain found in F-box only protein 30 (FBXO30), F-box only protein 40 (FBXO40) and ...
 138-174 6.04e-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: 35.43  E-value: 6.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2217279114 138 ICSLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIIS 174
Cdd:cd22101     1 LSSLPFEILQHIARFLDSFSLC-NLSLVSRLMREVCC 36
F-box_AtSKIP19-like cd22164
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 19 (AtSKIP19) and similar ...
 141-185 7.29e-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: 7.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2217279114 141 LPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISDPLFipWKKLY 185
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 ...
 138-173 8.09e-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: 8.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2217279114 138 ICSLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREII 173
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) ...
 140-178 8.59e-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: 34.74  E-value: 8.59e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2217279114 140 SLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLF 178
Cdd:cd22157     2 SLPDDLVEEILSRLPAKSLL-RFRCVCKQWNSLISSPSF 39
F-box_FBXO17-like cd22169
F-box domain found in F-box only protein 17 (FBXO17), F-box only protein 27 (FBXO27) and ...
 141-183 8.71e-03

F-box domain found in F-box only protein 17 (FBXO17), F-box only protein 27 (FBXO27) and similar proteins; This subfamily includes FBXO17 and FBXO27. FBXO17 is also called FBX17, F-box only protein 26 (FBX26/FBXO26), or FBG4, while FBXO27 is also called FBX27, or F-box/G-domain protein 5. FBXO17 and FBXO27 are the substrate-recognition components of SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. They can recognize and bind denatured glycoproteins, which are modified with complex-type oligosaccharides. FBXO17 also recognizes sulfated glycans but does not bind high-mannose glycoproteins. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438940  Cd Length: 48  Bit Score: 35.09  E-value: 8.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2217279114 141 LPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISDPLfiPWKK 183
Cdd:cd22169     4 LPEELLLLVLSHVPARTLVTRCRLVCRDWRDLVDGPT--LWKL 44
F-box_FBXO15 cd22093
F-box domain found in F-box only protein 15 (FBXO15) and similar proteins; FBXO15, also called ...
 138-185 8.79e-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: 8.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217279114 138 ICSLPSEVLRHVFAFLPVEDLYwNLSLVCHLWREIISDPLFipWKKLY 185
Cdd:cd22093     1 IERLPSEILLKILSYLDASSLL-CISCVNKLFYQLANDNAL--WRKLY 45
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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