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Conserved domains on  [gi|2053522371|gb|QWT24552|]
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FHA domain-containing protein [Subtercola sp. PAMC28395]

Protein Classification

FHA domain-containing protein( domain architecture ID 11447961)

FHA (forkhead-associated) domain-containing protein participates in signal transduction pathways via protein-protein interactions involving recognition of pThr and pTyr phosphopeptides

CATH:  2.60.200.20
Gene Ontology:  GO:0005515
PubMed:  10518219|11069759|7482699
SCOP:  4002605

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
360-470 1.89e-11

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


:

Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 60.36  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053522371 360 AGRLLVSTGA----EVELDRD-VVIGRKPSAgrvsagsmphlvTVPSPDQDISRNHLAIRREGIHVFAVDLDTTNGTRLY 434
Cdd:COG1716     1 MARLVVLEGPlagrRFPLDGGpLTIGRAPDN------------DIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTFVN 68

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2053522371 435 RpgrapERLhpQEPTMLANGDLLDLGDgVSVVFEAP 470
Cdd:COG1716    69 G-----QRV--TEPAPLRDGDVIRLGK-TELRFRLS 96
 
Name Accession Description Interval E-value
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
360-470 1.89e-11

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 60.36  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053522371 360 AGRLLVSTGA----EVELDRD-VVIGRKPSAgrvsagsmphlvTVPSPDQDISRNHLAIRREGIHVFAVDLDTTNGTRLY 434
Cdd:COG1716     1 MARLVVLEGPlagrRFPLDGGpLTIGRAPDN------------DIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTFVN 68

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2053522371 435 RpgrapERLhpQEPTMLANGDLLDLGDgVSVVFEAP 470
Cdd:COG1716    69 G-----QRV--TEPAPLRDGDVIRLGK-TELRFRLS 96
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 366-468 2.31e-09

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: 54.20  E-value: 2.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053522371 366 STGAEVELDRD-VVIGRKPSAgrvsagsmphlvTVPSPDQDISRNHLAIRREGIHVFAVDLDTTNGTRLYRpgrapERLH 444
Cdd:cd00060     9 GGGREFPLTKGvVTIGRSPDC------------DIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNGTFVNG-----KRIT 71

                          90       100
                  ....*....|....*....|....
gi 2053522371 445 PqePTMLANGDLLDLGDgVSVVFE 468
Cdd:cd00060    72 P--PVPLQDGDVIRLGD-TTFRFE 92
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 377-459 4.18e-06

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 44.10  E-value: 4.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053522371 377 VVIGRKPSAgrvsagsmphlvTVPSPDQDISRNHLAIRR-EGIHVFAVDLDTTNGTRLyrpgraPERLHPQEPTMLANGD 455
Cdd:pfam00498   1 VTIGRSPDC------------DIVLDDPSVSRRHAEIRYdGGGRFYLEDLGSTNGTFV------NGQRLGPEPVRLKDGD 62


                  ....
gi 2053522371 456 LLDL 459
Cdd:pfam00498  63 VIRL 66
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 402-433 8.87e-03

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 34.46  E-value: 8.87e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2053522371  402 PDQDISRNHLAIRREGIH-VFAVDLDTTNGTRL 433
Cdd:smart00240  15 DGPSISRRHAVIVYDGGGrFYLIDLGSTNGTFV 47
 
Name Accession Description Interval E-value
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
360-470 1.89e-11

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 60.36  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053522371 360 AGRLLVSTGA----EVELDRD-VVIGRKPSAgrvsagsmphlvTVPSPDQDISRNHLAIRREGIHVFAVDLDTTNGTRLY 434
Cdd:COG1716     1 MARLVVLEGPlagrRFPLDGGpLTIGRAPDN------------DIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTFVN 68

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2053522371 435 RpgrapERLhpQEPTMLANGDLLDLGDgVSVVFEAP 470
Cdd:COG1716    69 G-----QRV--TEPAPLRDGDVIRLGK-TELRFRLS 96
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 366-468 2.31e-09

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: 54.20  E-value: 2.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053522371 366 STGAEVELDRD-VVIGRKPSAgrvsagsmphlvTVPSPDQDISRNHLAIRREGIHVFAVDLDTTNGTRLYRpgrapERLH 444
Cdd:cd00060     9 GGGREFPLTKGvVTIGRSPDC------------DIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNGTFVNG-----KRIT 71

                          90       100
                  ....*....|....*....|....
gi 2053522371 445 PqePTMLANGDLLDLGDgVSVVFE 468
Cdd:cd00060    72 P--PVPLQDGDVIRLGD-TTFRFE 92
FHA_ArnA-like cd22680
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ...
 367-453 9.64e-09

forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438732 [Multi-domain]  Cd Length: 96  Bit Score: 52.73  E-value: 9.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053522371 367 TGAEVELDRD-VVIGRKPSagrvsagsmphlVTVPSPDQDISRNHLAIRREGIHVFAVDLDTTNGTRLY--RPGRAPERL 443
Cdd:cd22680    12 TGKKFPFDFSsVSIGRDPE------------NVIVIPDPFVSRNHARITVDSNEIYIEDLGSTNGTFVNdfKRIKGPAKL 79

                          90
                  ....*....|
gi 2053522371 444 HPQEPTMLAN 453
Cdd:cd22680    80 HPNDIIKLGR 89
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
 358-461 9.22e-08

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: 54.00  E-value: 9.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053522371 358 VSAGRLLVSTGAEVELDRD-VVIGRKPSAgrvsagsmpHLVtVPSPDQDISRNHLAIRREGIHVFAVDLdTTNGTRLyrp 436
Cdd:COG3456     8 INSPDLESGSAASATFGRGgGTIGRSADC---------DWV-LPDPDRSVSRRHAEIRFRDGAFCLTDL-STNGTFL--- 73

                          90       100
                  ....*....|....*....|....*
gi 2053522371 437 GRAPERLHPQEPTMLANGDLLDLGD 461
Cdd:COG3456    74 NGSDHPLGPGRPVRLRDGDRLRIGD 98
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 377-459 4.18e-06

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 44.10  E-value: 4.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053522371 377 VVIGRKPSAgrvsagsmphlvTVPSPDQDISRNHLAIRR-EGIHVFAVDLDTTNGTRLyrpgraPERLHPQEPTMLANGD 455
Cdd:pfam00498   1 VTIGRSPDC------------DIVLDDPSVSRRHAEIRYdGGGRFYLEDLGSTNGTFV------NGQRLGPEPVRLKDGD 62


                  ....
gi 2053522371 456 LLDL 459
Cdd:pfam00498  63 VIRL 66
FHA_MDC1 cd22665
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ...
 378-461 1.06e-04

forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438717 [Multi-domain]  Cd Length: 97  Bit Score: 41.06  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053522371 378 VIGRKPSagrvsagsmphlVTVPSPDQDISRNHLAIRREGIHVFAVDLDTTNGTRLyrpgRAPERLHPQEPTMLANGDLL 457
Cdd:cd22665    24 VIGRDPS------------CSVVLPDKSVSKQHACIEVDGGTHLIEDLGSTNGTRI----GNKVRLKPNVRYELIDGDLL 87


                  ....
gi 2053522371 458 DLGD 461
Cdd:cd22665    88 LFGD 91
FHA_PS1-like cd22691
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ...
 363-460 2.41e-03

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: 37.78  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2053522371 363 LLVSTGAEVELDRDVVIGRKPSAGRVsagsmphlVTVPSpdqdISRNHLAIRR--EGIHVFAVDLDTTNGTRLyrpgrAP 440
Cdd:cd22691    17 FLHGKFSKSEEEDILVVGRHPDCDIV--------LDHPS----ISRFHLEIRIipSRRKITLTDLSSVHGTWV-----NG 79

                          90       100
                  ....*....|....*....|
gi 2053522371 441 ERLHPQEPTMLANGDLLDLG 460
Cdd:cd22691    80 QRIEPGVPVELEEGDTVRLG 99
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 402-433 8.87e-03

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 34.46  E-value: 8.87e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2053522371  402 PDQDISRNHLAIRREGIH-VFAVDLDTTNGTRL 433
Cdd:smart00240  15 DGPSISRRHAVIVYDGGGrFYLIDLGSTNGTFV 47
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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