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Conserved domains on  [gi|1898492883|gb|QNN81318|]
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mRuby2-FHA1-PKAsub-GFP1-10 [Cloning vector pcDNA3.1/AKAR]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FHA_RAD53-like_rpt1 cd22689
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
 254-367 2.54e-55

first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the first one. The FHA domain is a small phosphopeptide recognition module.


:

Pssm-ID: 438741 [Multi-domain]  Cd Length: 132  Bit Score: 184.02  E-value: 2.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883 254 RVICTTGQI---------------PIRDLSADISQVLKEKRSIKKVWTFGRNPACDYHLGNiSRLSNKHFQILLGE---- 314
Cdd:cd22689     1 RVATQTGQItqtqsqsqsltmtqePIRDLSGDISQVLKEKRSIKKVWTFGRHPACDYHLGN-SRLSNKHFQILLGEsdps 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1898492883 315 DGNLLLNDISTNGTWLNGQKVEKNSNQLLSQGDEITVGVGVESDILSLVIFIN 367
Cdd:cd22689    80 DGNVLLNDISSNGTWLNGQRLEKNSNQLLSQGDEITIGVGVTGDILSLVIFIN 132
GFP pfam01353
Green fluorescent protein;
13-221 2.54e-51

Green fluorescent protein;


:

Pssm-ID: 426217  Cd Length: 211  Bit Score: 176.22  E-value: 2.54e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883  13 MRMKVVMEGSVNGHQFKCTGEGEGNPYMGTQTMRITVIEGgPLPFAFDILATSFMYGSrtFIKYPKGiPDFFKQSFPEG- 91
Cdd:pfam01353   1 MTHDLHMEGSVNGHEFDIVGGGNGNPNDGSLETKVKSTKG-ALPFSPYLLAPHL*YYQ--YLPFPDG-TSPFQAAVENGg 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883  92 FTWERVTRYEDGGVVTVMQDTSLEDGCLVYHVQVRGVNFPSNGPVMQKKTKGWEPNTE-MMYPADGGLRGYTHMALKVDG 170
Cdd:pfam01353  77 YQVHRTFKFEDGGVLTIVFTYTYEGGHIKGEFTFQGSGFPPDGPVMTKSLTGWDPSVEkMIPRNDKTLVGDINWSLKLTD 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1898492883 171 GGHLSCSFVTTYRSKKTV-GNIKMPGIHAVDHRLERlEESDNEMFVVQREVA 221
Cdd:pfam01353 157 GKRYRAQVVTNYTFAKPVpAGLKLPPPHFVFRKIER-TGSKTEINLVEQQKA 207
GFP super family cl08319
Green fluorescent protein;
429-624 4.00e-16

Green fluorescent protein;


The actual alignment was detected with superfamily member pfam01353:

Pssm-ID: 426217  Cd Length: 211  Bit Score: 77.61  E-value: 4.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883 429 LDGDVNGHKFSVRGEGEGDATIGKLTLKFICTTGKLPVPWPTLVTTLTYGVqcFSRYPDHMkrhDFFKSAMPEG-YVQER 507
Cdd:pfam01353   7 MEGSVNGHEFDIVGGGNGNPNDGSLETKVKSTKGALPFSPYLLAPHL*YYQ--YLPFPDGT---SPFQAAVENGgYQVHR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883 508 TISFKDDGKYKTRAVVKFEGDTLVNRIELKGTDFKEDGNILGHKLEYnfNSHNVYITADKQKNGIKANFTVRHNVEDGS- 586
Cdd:pfam01353  82 TFKFEDGGVLTIVFTYTYEGGHIKGEFTFQGSGFPPDGPVMTKSLTG--WDPSVEKMIPRNDKTLVGDINWSLKLTDGKr 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1898492883 587 --VQLADHYQQNTPIGDGpVLLPDNHYLSTQTVLSKDPNE 624
Cdd:pfam01353 160 yrAQVVTNYTFAKPVPAG-LKLPPPHFVFRKIERTGSKTE 198
 
Name Accession Description Interval E-value
FHA_RAD53-like_rpt1 cd22689
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
 254-367 2.54e-55

first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the first one. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438741 [Multi-domain]  Cd Length: 132  Bit Score: 184.02  E-value: 2.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883 254 RVICTTGQI---------------PIRDLSADISQVLKEKRSIKKVWTFGRNPACDYHLGNiSRLSNKHFQILLGE---- 314
Cdd:cd22689     1 RVATQTGQItqtqsqsqsltmtqePIRDLSGDISQVLKEKRSIKKVWTFGRHPACDYHLGN-SRLSNKHFQILLGEsdps 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1898492883 315 DGNLLLNDISTNGTWLNGQKVEKNSNQLLSQGDEITVGVGVESDILSLVIFIN 367
Cdd:cd22689    80 DGNVLLNDISSNGTWLNGQRLEKNSNQLLSQGDEITIGVGVTGDILSLVIFIN 132
GFP pfam01353
Green fluorescent protein;
13-221 2.54e-51

Green fluorescent protein;


Pssm-ID: 426217  Cd Length: 211  Bit Score: 176.22  E-value: 2.54e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883  13 MRMKVVMEGSVNGHQFKCTGEGEGNPYMGTQTMRITVIEGgPLPFAFDILATSFMYGSrtFIKYPKGiPDFFKQSFPEG- 91
Cdd:pfam01353   1 MTHDLHMEGSVNGHEFDIVGGGNGNPNDGSLETKVKSTKG-ALPFSPYLLAPHL*YYQ--YLPFPDG-TSPFQAAVENGg 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883  92 FTWERVTRYEDGGVVTVMQDTSLEDGCLVYHVQVRGVNFPSNGPVMQKKTKGWEPNTE-MMYPADGGLRGYTHMALKVDG 170
Cdd:pfam01353  77 YQVHRTFKFEDGGVLTIVFTYTYEGGHIKGEFTFQGSGFPPDGPVMTKSLTGWDPSVEkMIPRNDKTLVGDINWSLKLTD 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1898492883 171 GGHLSCSFVTTYRSKKTV-GNIKMPGIHAVDHRLERlEESDNEMFVVQREVA 221
Cdd:pfam01353 157 GKRYRAQVVTNYTFAKPVpAGLKLPPPHFVFRKIER-TGSKTEINLVEQQKA 207
GFP pfam01353
Green fluorescent protein;
429-624 4.00e-16

Green fluorescent protein;


Pssm-ID: 426217  Cd Length: 211  Bit Score: 77.61  E-value: 4.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883 429 LDGDVNGHKFSVRGEGEGDATIGKLTLKFICTTGKLPVPWPTLVTTLTYGVqcFSRYPDHMkrhDFFKSAMPEG-YVQER 507
Cdd:pfam01353   7 MEGSVNGHEFDIVGGGNGNPNDGSLETKVKSTKGALPFSPYLLAPHL*YYQ--YLPFPDGT---SPFQAAVENGgYQVHR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883 508 TISFKDDGKYKTRAVVKFEGDTLVNRIELKGTDFKEDGNILGHKLEYnfNSHNVYITADKQKNGIKANFTVRHNVEDGS- 586
Cdd:pfam01353  82 TFKFEDGGVLTIVFTYTYEGGHIKGEFTFQGSGFPPDGPVMTKSLTG--WDPSVEKMIPRNDKTLVGDINWSLKLTDGKr 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1898492883 587 --VQLADHYQQNTPIGDGpVLLPDNHYLSTQTVLSKDPNE 624
Cdd:pfam01353 160 yrAQVVTNYTFAKPVPAG-LKLPPPHFVFRKIERTGSKTE 198
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 285-351 3.60e-13

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 64.52  E-value: 3.60e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1898492883 285 WTFGRNPACDYHLGNiSRLSNKHFQILLGEDGNLLLNDI-STNGTWLNGQKVEKNSnQLLSQGDEITV 351
Cdd:pfam00498   1 VTIGRSPDCDIVLDD-PSVSRRHAEIRYDGGGRFYLEDLgSTNGTFVNGQRLGPEP-VRLKDGDVIRL 66
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
282-352 6.89e-11

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 59.20  E-value: 6.89e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1898492883 282 KKVWTFGRNPACDYHLGN--ISRlsnKHFQILLgEDGNLLLNDI-STNGTWLNGQKVEknSNQLLSQGDEITVG 352
Cdd:COG1716    20 GGPLTIGRAPDNDIVLDDptVSR---RHARIRR-DGGGWVLEDLgSTNGTFVNGQRVT--EPAPLRDGDVIRLG 87
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 285-335 4.33e-07

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 46.79  E-value: 4.33e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1898492883  285 WTFGRNPA-CDYHLGNiSRLSNKHFQILLGEDGNLLLNDI-STNGTWLNGQKV 335
Cdd:smart00240   1 VTIGRSSEdCDIQLDG-PSISRRHAVIVYDGGGRFYLIDLgSTNGTFVNGKRI 52
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
 286-352 1.72e-06

type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274537 [Multi-domain]  Cd Length: 396  Bit Score: 50.83  E-value: 1.72e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1898492883 286 TFGRNPACDYHL----GNISRLsnkHFQILlGEDGNLLLNDISTNGTWLN--GQKVEKNSNQLLSQGDEITVG 352
Cdd:TIGR03354  27 TIGRSEDCDWVLpdpeRHVSGR---HARIR-YRDGAYLLTDLSTNGVFLNgsGSPLGRGNPVRLEQGDRLRLG 95
 
Name Accession Description Interval E-value
FHA_RAD53-like_rpt1 cd22689
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
 254-367 2.54e-55

first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the first one. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438741 [Multi-domain]  Cd Length: 132  Bit Score: 184.02  E-value: 2.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883 254 RVICTTGQI---------------PIRDLSADISQVLKEKRSIKKVWTFGRNPACDYHLGNiSRLSNKHFQILLGE---- 314
Cdd:cd22689     1 RVATQTGQItqtqsqsqsltmtqePIRDLSGDISQVLKEKRSIKKVWTFGRHPACDYHLGN-SRLSNKHFQILLGEsdps 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1898492883 315 DGNLLLNDISTNGTWLNGQKVEKNSNQLLSQGDEITVGVGVESDILSLVIFIN 367
Cdd:cd22689    80 DGNVLLNDISSNGTWLNGQRLEKNSNQLLSQGDEITIGVGVTGDILSLVIFIN 132
GFP pfam01353
Green fluorescent protein;
13-221 2.54e-51

Green fluorescent protein;


Pssm-ID: 426217  Cd Length: 211  Bit Score: 176.22  E-value: 2.54e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883  13 MRMKVVMEGSVNGHQFKCTGEGEGNPYMGTQTMRITVIEGgPLPFAFDILATSFMYGSrtFIKYPKGiPDFFKQSFPEG- 91
Cdd:pfam01353   1 MTHDLHMEGSVNGHEFDIVGGGNGNPNDGSLETKVKSTKG-ALPFSPYLLAPHL*YYQ--YLPFPDG-TSPFQAAVENGg 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883  92 FTWERVTRYEDGGVVTVMQDTSLEDGCLVYHVQVRGVNFPSNGPVMQKKTKGWEPNTE-MMYPADGGLRGYTHMALKVDG 170
Cdd:pfam01353  77 YQVHRTFKFEDGGVLTIVFTYTYEGGHIKGEFTFQGSGFPPDGPVMTKSLTGWDPSVEkMIPRNDKTLVGDINWSLKLTD 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1898492883 171 GGHLSCSFVTTYRSKKTV-GNIKMPGIHAVDHRLERlEESDNEMFVVQREVA 221
Cdd:pfam01353 157 GKRYRAQVVTNYTFAKPVpAGLKLPPPHFVFRKIER-TGSKTEINLVEQQKA 207
GFP pfam01353
Green fluorescent protein;
429-624 4.00e-16

Green fluorescent protein;


Pssm-ID: 426217  Cd Length: 211  Bit Score: 77.61  E-value: 4.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883 429 LDGDVNGHKFSVRGEGEGDATIGKLTLKFICTTGKLPVPWPTLVTTLTYGVqcFSRYPDHMkrhDFFKSAMPEG-YVQER 507
Cdd:pfam01353   7 MEGSVNGHEFDIVGGGNGNPNDGSLETKVKSTKGALPFSPYLLAPHL*YYQ--YLPFPDGT---SPFQAAVENGgYQVHR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883 508 TISFKDDGKYKTRAVVKFEGDTLVNRIELKGTDFKEDGNILGHKLEYnfNSHNVYITADKQKNGIKANFTVRHNVEDGS- 586
Cdd:pfam01353  82 TFKFEDGGVLTIVFTYTYEGGHIKGEFTFQGSGFPPDGPVMTKSLTG--WDPSVEKMIPRNDKTLVGDINWSLKLTDGKr 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1898492883 587 --VQLADHYQQNTPIGDGpVLLPDNHYLSTQTVLSKDPNE 624
Cdd:pfam01353 160 yrAQVVTNYTFAKPVPAG-LKLPPPHFVFRKIERTGSKTE 198
FHA_CHFR cd22672
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ...
 281-351 3.03e-13

forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also called RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22 and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated-(FHA) domain and a RING-HC finger. The CHFR FHA domain has been crystallized as a segment-swapped dimer. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438724 [Multi-domain]  Cd Length: 108  Bit Score: 66.16  E-value: 3.03e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1898492883 281 IKKVWTFGRNPACDYHLGNISRLSNKHFQILLGEDGNLLLNDISTNGTWLNGQKVEKNSNQLLSQGDEITV 351
Cdd:cd22672    19 RKDEFTIGRAKDCDLSFPGNKLVSGDHCKIIRDEKGQVWLEDTSTNGTLVNKVKVVKGQKVELKHGDVIYL 89
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 285-351 3.60e-13

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 64.52  E-value: 3.60e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1898492883 285 WTFGRNPACDYHLGNiSRLSNKHFQILLGEDGNLLLNDI-STNGTWLNGQKVEKNSnQLLSQGDEITV 351
Cdd:pfam00498   1 VTIGRSPDCDIVLDD-PSVSRRHAEIRYDGGGRFYLEDLgSTNGTFVNGQRLGPEP-VRLKDGDVIRL 66
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 282-352 2.03e-12

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 63.45  E-value: 2.03e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1898492883 282 KKVWTFGRNPACDYHLGNiSRLSNKHFQILLgEDGNLLLNDI-STNGTWLNGQKVEKnsNQLLSQGDEITVG 352
Cdd:cd00060    18 KGVVTIGRSPDCDIVLDD-PSVSRRHARIEV-DGGGVYLEDLgSTNGTFVNGKRITP--PVPLQDGDVIRLG 85
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
 283-351 2.39e-12

forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438722 [Multi-domain]  Cd Length: 105  Bit Score: 63.40  E-value: 2.39e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1898492883 283 KVWTFGRNPACDYHLgNISRLSNKHFQI---LLGEDGNLL--LNDISTNGTWLNGQKVEKNSNQLLSQGDEITV 351
Cdd:cd22670    22 QVITIGRSPSCDIVI-NDPFVSRTHCRIysvQFDESSAPLvyVEDLSSNGTYLNGKLIGRNNTVLLSDGDVIEI 94
FHA_CHK2 cd22666
forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; ...
 281-349 1.30e-11

forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; Chk2, also called Hucds1, Cds1 homolog, or serine/threonine-protein kinase Chk2, plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438718 [Multi-domain]  Cd Length: 112  Bit Score: 61.49  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883 281 IKKVWTFGRNPACDYHLGN--------ISRLSNKHFQI----LLGEDGNLLLNDISTNGTWLNGQKVEKNSNQLLSQGDE 348
Cdd:cd22666    17 VKDEYTFGRDKSCDYCFDSpalkktsyYRTYSKKHFRIfrekGSKNTYPVFLEDHSSNGTFVNGEKIGKGKKRPLNNNDE 96


                  .
gi 1898492883 349 I 349
Cdd:cd22666    97 I 97
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
282-352 6.89e-11

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 59.20  E-value: 6.89e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1898492883 282 KKVWTFGRNPACDYHLGN--ISRlsnKHFQILLgEDGNLLLNDI-STNGTWLNGQKVEknSNQLLSQGDEITVG 352
Cdd:COG1716    20 GGPLTIGRAPDNDIVLDDptVSR---RHARIRR-DGGGWVLEDLgSTNGTFVNGQRVT--EPAPLRDGDVIRLG 87
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
 286-352 2.92e-10

Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442679 [Multi-domain]  Cd Length: 402  Bit Score: 62.47  E-value: 2.92e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1898492883 286 TFGRNPACDYHL----GNISRLsnkHFQILLgEDGNLLLNDISTNGTWLNGQKVE--KNSNQLLSQGDEITVG 352
Cdd:COG3456    29 TIGRSADCDWVLpdpdRSVSRR---HAEIRF-RDGAFCLTDLSTNGTFLNGSDHPlgPGRPVRLRDGDRLRIG 97
FHA_RAD53-like_rpt2 cd22690
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
 286-351 3.03e-10

second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the second one. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438742 [Multi-domain]  Cd Length: 105  Bit Score: 57.69  E-value: 3.03e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883 286 TFGRNPACDYHLgNISRLSNKHFQILLGEDGNLL----LNDISTNGTWLNGQKVEKNSNQLLSQGDEITV 351
Cdd:cd22690    22 FIGRSKDCDEEI-TDPRISKHHCIITRKRSGKGLddvyVTDTSTNGTFINNNRLGKGSQSLLQDGDEIVL 90
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
 282-352 5.65e-09

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 53.76  E-value: 5.65e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1898492883 282 KKVWTFGRNPACD--YHLGNISRlsnKHFQILLGEDGNLLLNDIS-TNGTWLNGQKVEKNSNqlLSQGDEITVG 352
Cdd:cd22673    20 KKSCTFGRDLSCDirIQLPGVSR---EHCRIEVDENGKAYLENLStTNPTLVNGKAIEKSAE--LKDGDVITIG 88
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
 282-352 2.09e-07

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 49.18  E-value: 2.09e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1898492883 282 KKVWTFGRNPACDYHLGNISrLSNKHFQILLGEDGNLLLNDISTNGTWLNGQKVEKNSNqLLSQGDEITVG 352
Cdd:pfam16697  16 GGRYRIGSDPDCDIVLSDKE-VSRVHLKLEVDDEGWRLDDLGSGNGTLVNGQRVTELGI-ALRPGDRIELG 84
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 285-335 4.33e-07

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 46.79  E-value: 4.33e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1898492883  285 WTFGRNPA-CDYHLGNiSRLSNKHFQILLGEDGNLLLNDI-STNGTWLNGQKV 335
Cdd:smart00240   1 VTIGRSSEdCDIQLDG-PSISRRHAVIVYDGGGRFYLIDLgSTNGTFVNGKRI 52
FHA_GarA_OdhI-like cd22684
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ...
 284-352 1.38e-06

forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium glutamicum OdhI and similar proteins; This family includes Mycobacterium tuberculosis glycogen accumulation regulator GarA and Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI). GarA is involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB. GarA binds to Kgd, Gdh, GltB, PknB, and the N-terminal region of PknG via its FHA domain. OdhI is an essential component of the PknG signaling pathway. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438736 [Multi-domain]  Cd Length: 94  Bit Score: 46.99  E-value: 1.38e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1898492883 284 VWTFGRNPACDYHLGNISrLSNKHFQILLGEDGNLLLNDISTNGTWLNGQKVEKnsnQLLSQGDEITVG 352
Cdd:cd22684    22 VTTAGRHPESDIFLDDVT-VSRRHAEFRRAEGGFVVRDVGSLNGTYVNRERIDS---AVLRNGDEVQIG 86
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
 286-352 1.72e-06

type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274537 [Multi-domain]  Cd Length: 396  Bit Score: 50.83  E-value: 1.72e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1898492883 286 TFGRNPACDYHL----GNISRLsnkHFQILlGEDGNLLLNDISTNGTWLN--GQKVEKNSNQLLSQGDEITVG 352
Cdd:TIGR03354  27 TIGRSEDCDWVLpdpeRHVSGR---HARIR-YRDGAYLLTDLSTNGVFLNgsGSPLGRGNPVRLEQGDRLRLG 95
FHA_PPP1R8 cd22674
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ...
 280-352 1.15e-05

forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 (PPP1R8) and similar proteins; PPP1R8, also called nuclear inhibitor of protein phosphatase 1 (NIPP-1), is an inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. It may also be involved in pre-mRNA splicing and binds DNA and might act as a transcriptional repressor. PPP1R8 seems to be required for cell proliferation. PPP1R8 contains an FHA domain that mediates interactions with threonine-phosphorylated maternal embryonic leucine zipper kinase (MELK). The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438726 [Multi-domain]  Cd Length: 108  Bit Score: 44.56  E-value: 1.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1898492883 280 SIKKVWTFGRNP-ACDYHLGNISrLSNKHFQILLGEDGN-LLLNDI-STNGTWLNGQKVEKNSNQLLSQGDEITVG 352
Cdd:cd22674    24 DEKKYYLFGRNSdVCDFVLDHPS-CSRVHAALVYHKHLNrVFLIDLgSTHGTFVGGIRLEPHKPQQLPIDSTLRFG 98
FHA_DgcB-like cd22682
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ...
 288-352 2.82e-05

forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.


Pssm-ID: 438734 [Multi-domain]  Cd Length: 96  Bit Score: 43.29  E-value: 2.82e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1898492883 288 GRNPACDYHLGNISrLSNKHFQILLGEDGNLLLNDISTNGTWLNGQKVEKNSNQLLSQGDEITVG 352
Cdd:cd22682    25 GRSVESQVQIDDDS-VSRYHAKLAVNPSAVSIIDLGSTNGTIVNGKKIPKLASCDLQNGDQIKIG 88
FHA_PS1-like cd22691
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ...
 286-352 3.26e-05

forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) and similar proteins; PS1 is an FHA domain-containing protein required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. It is not involved in female meiosis. Mutations in PS1 lead to the production of diploid pollen grains. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438743 [Multi-domain]  Cd Length: 113  Bit Score: 43.56  E-value: 3.26e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1898492883 286 TFGRNPACDYHLG--NISRLsnkHFQI-LLGEDGNLLLNDI-STNGTWLNGQKVEKNSNQLLSQGDEITVG 352
Cdd:cd22691    32 VVGRHPDCDIVLDhpSISRF---HLEIrIIPSRRKITLTDLsSVHGTWVNGQRIEPGVPVELEEGDTVRLG 99
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
 254-352 8.48e-05

forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar proteins; TCF-19, also called transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3.


Pssm-ID: 438737 [Multi-domain]  Cd Length: 130  Bit Score: 42.79  E-value: 8.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883 254 RVICTTGQIPIRDLSAdISQVLKEKRsikkvwtFGRNPA-CD------YHLGNISRlsnKHFQI----LLGEDGNLLLND 322
Cdd:cd22685     7 RIGLSASRSEPRDLYT-FRPDLCEYR-------IGRNPEvCDvflcssQHPNLISR---EHAEIhaerDGNGNWKVLIED 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 1898492883 323 ISTNGTWLNGQKVEKNSNQLLSQGDEITVG 352
Cdd:cd22685    76 RSTNGTYVNDVRLQDGQRRELSDGDTITFG 105
FHA_Kanadaptin cd22677
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ...
 273-352 1.48e-04

forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438729 [Multi-domain]  Cd Length: 106  Bit Score: 41.39  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883 273 QVLKEKRSIKKV-------WTFGRNPACDYHLGNISrLSNKH--FQ---ILLGEDGNLLLNDI-STNGTWLNGQKVEKNS 339
Cdd:cd22677     5 EVLKNGVIVETLdlngksfYVFGRLPGCDVVLEHPS-ISRYHavLQyrgDADDHDGGFYLYDLgSTHGTFLNKQRIPPKQ 83

                          90
                  ....*....|...
gi 1898492883 340 NQLLSQGDEITVG 352
Cdd:cd22677    84 YYRLRVGHVLKFG 96
FHA_Ct664-like cd22696
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar ...
 283-352 1.92e-04

forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Chlamydia trachomatis Ct664 protein. Ct664 situates within the type III secretion system cluster that also encodes an STPK (CT673 in C. trachomatis), suggesting a role of CT664 in the chlamydial type III secretion system by mediating phosphorylation-dependent protein-protein interactions. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438748 [Multi-domain]  Cd Length: 97  Bit Score: 40.94  E-value: 1.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1898492883 283 KVWTFGRNPA-CDYHLGNISrLSNKHFQILLGEDGNLLLNDI-STNGTWLNGQKVEknSNQLLSQGDEITVG 352
Cdd:cd22696    21 KTYFIGKDPTvCDIVLQDPS-ISRQHARLSIDQDNRVFIEDLsSKNGVLVNGKPIE--GKEEISGSDVISLG 89
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
 282-354 1.94e-04

forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438719 [Multi-domain]  Cd Length: 108  Bit Score: 41.16  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898492883 282 KKVWTFGRNpACDYHLGNISRLSNKHFQILLGEDGN----------LLLNDISTNGTWLNGQKVEKNSNQLLSQGDEITV 351
Cdd:cd22667    19 GGEYTVGRK-DCDIIIVDDSSISRKHATLTVLHPEAnlsdpdtrpeLTLKDLSKYGTFVNGEKLKGGSEVTLKDGDVITF 97


                  ...
gi 1898492883 352 GVG 354
Cdd:cd22667    98 GVL 100
FHA_RNF8 cd22663
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ...
 286-353 2.00e-04

forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438715 [Multi-domain]  Cd Length: 110  Bit Score: 41.19  E-value: 2.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1898492883 286 TFGRNPACDYHL-----GNISRlsnKHFQILLGEDGNLLLNDI-STNGTWLNGQKVEKNSNQLLSQGDEITVGV 353
Cdd:cd22663    24 TVGRGLGVTYQLvstcpLMISR---NHCVLKKNDEGQWTIKDNkSLNGVWVNGERIEPLKPYPLNEGDLIQLGV 94
FHA_EspA-like cd22698
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ...
 286-352 2.04e-04

forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438750 [Multi-domain]  Cd Length: 93  Bit Score: 40.47  E-value: 2.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1898492883 286 TFGRNPACDYHLGNISrLSNKHFQILLGEDGNLLLNDISTNGTWLNGQKVEKNSnqlLSQGDEITVG 352
Cdd:cd22698    24 TIGRSSNNDIRLNDHS-VSRHHARIVRQGDKCNLTDLGSTNGTFLNGIRVGTHE---LKHGDRIQLG 86
FHA_FhaA-like cd22668
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
 286-354 6.56e-04

forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438720 [Multi-domain]  Cd Length: 91  Bit Score: 38.99  E-value: 6.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1898492883 286 TFGRNPACDYHLGNISrLSNKHFQILLGEDGNLLLNDISTNGTWLNGQKVEknSNQLLSQGDEITVGVG 354
Cdd:cd22668    21 IIGRGSDADFRLPDTG-VSRRHAEIRWDGQVAHLTDLGSTNGTTVNNAPVT--PEWRLADGDVITLGHS 86
FHA_Par42-like cd22675
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar ...
 285-337 9.43e-04

forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar proteins; TbPar42 is a nuclear protein that plays a key role in parasite cell proliferation. It exhibits an N-terminal forkhead associated (FHA)-domain and a peptidyl-prolyl-cis/trans-isomerase (PPIase) domain, both connected by a linker. Its PPIase domain adopts a parvulin fold and reflects structural elements of Pin1-type proteins but is catalytically inactive. Its FHA domain may be involved in the binding of phosphorylated target proteins. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438727 [Multi-domain]  Cd Length: 113  Bit Score: 39.46  E-value: 9.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1898492883 285 WTFGRNPACDYHLGNISrLSNKHFQILL-GEDGNLLLNDI-STNGTWLNGQKVEK 337
Cdd:cd22675    31 YLFGRSPVCDYVLEHPS-ISSVHAVLVFhGEQKCFVLMDLgSTNGVKLNGKRIEK 84
FHA_Rv1747-like_rpt1 cd22694
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
 288-352 1.84e-03

first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438746 [Multi-domain]  Cd Length: 93  Bit Score: 38.08  E-value: 1.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1898492883 288 GRNPACDYHLGNiSRLSNKHFQILLGEDGNLLLNDISTNGTWLNGQKVeknSNQLLSQGDEITVG 352
Cdd:cd22694    21 GRDPDADVRLDD-PRVSRRHALLEFDGDGWVYTDLGSRNGTYLNGRRV---QQVKLSDGTRVRLG 81
 
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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