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Conserved domains on  [gi|504408279|ref|WP_014595381|]
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type VI secretion system-associated FHA domain protein TagH [Stutzerimonas stutzeri]

Protein Classification

type VI secretion system-associated FHA domain protein( domain architecture ID 11496642)

type VI secretion system-associated FHA domain protein is part of the type VI secretion loci

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
 3-387 1.29e-127

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: 373.24  E-value: 1.29e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279    3 LVFDMVGAQQFVPGLLTTKTFKQAGGVIGRAEGCDWVIPDRKRVLSGRHAVISYRDGAFFLTDTSSNGIQLKDSGASLVK 82
Cdd:TIGR03354   1 LVLTVLNAHQLTPGIAAQKTFGTNGGTIGRSEDCDWVLPDPERHVSGRHARIRYRDGAYLLTDLSTNGVFLNGSGSPLGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279   83 GQPQRIEHGSVYCLGDFEIRARL-----IQDPARFEGDIGRPQPAGTIIPDDAFLD-LDPLVAMDQQERIYAEVDDLDLT 156
Cdd:TIGR03354  81 GNPVRLEQGDRLRLGDYEIRVSLgdplvSRQASESRADTSLPTAGGPPTPDPAPLAqLDPLKALDQEPLSAADLDDLSAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279  157 LVAPQRQAQQRDYARIDTESLPLPELVMPPTAAEPKREPEPE-RLPPGFWERFGEALGIDLGGMDEDQRQALALNAARLL 235
Cdd:TIGR03354 161 LFPPLDARLPAFAAPIDAEPTMVPPFVPLPAPEPAPAPASQApSSDAVALTPFLRGLGLPLELLDSQAAEDVLEELGRLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279  236 KQSVAGLQQSLRTRSELKNELRLALTTVQSAGNNPLKHSADASEALNALLRGGKPGQLSAEQAVGRAFRDLQAHQVALLA 315
Cdd:TIGR03354 241 RAMVEGLLQLLRARAELKNELRLNQTTIRPAENNPLKFSADYDEALAVLLAPRSPGHLSAEAAIEEAFRDLRAHQVALLA 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504408279  316 ASRAAVHAMFEQLAPEQLALRFEREGRkPLLATAGSR----WRAYRRLHHSLGQDAD-WSERLFARDFAKTYEEQVR 387
Cdd:TIGR03354 321 AVRAALRRMLDAFSPEALEARFEQYRR-SGLLLFGGRdawaWDMYLRYYRELRSDREqGFERLFGEDFAQAYEEALR 396
 
Name Accession Description Interval E-value
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
 3-387 1.29e-127

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: 373.24  E-value: 1.29e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279    3 LVFDMVGAQQFVPGLLTTKTFKQAGGVIGRAEGCDWVIPDRKRVLSGRHAVISYRDGAFFLTDTSSNGIQLKDSGASLVK 82
Cdd:TIGR03354   1 LVLTVLNAHQLTPGIAAQKTFGTNGGTIGRSEDCDWVLPDPERHVSGRHARIRYRDGAYLLTDLSTNGVFLNGSGSPLGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279   83 GQPQRIEHGSVYCLGDFEIRARL-----IQDPARFEGDIGRPQPAGTIIPDDAFLD-LDPLVAMDQQERIYAEVDDLDLT 156
Cdd:TIGR03354  81 GNPVRLEQGDRLRLGDYEIRVSLgdplvSRQASESRADTSLPTAGGPPTPDPAPLAqLDPLKALDQEPLSAADLDDLSAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279  157 LVAPQRQAQQRDYARIDTESLPLPELVMPPTAAEPKREPEPE-RLPPGFWERFGEALGIDLGGMDEDQRQALALNAARLL 235
Cdd:TIGR03354 161 LFPPLDARLPAFAAPIDAEPTMVPPFVPLPAPEPAPAPASQApSSDAVALTPFLRGLGLPLELLDSQAAEDVLEELGRLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279  236 KQSVAGLQQSLRTRSELKNELRLALTTVQSAGNNPLKHSADASEALNALLRGGKPGQLSAEQAVGRAFRDLQAHQVALLA 315
Cdd:TIGR03354 241 RAMVEGLLQLLRARAELKNELRLNQTTIRPAENNPLKFSADYDEALAVLLAPRSPGHLSAEAAIEEAFRDLRAHQVALLA 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504408279  316 ASRAAVHAMFEQLAPEQLALRFEREGRkPLLATAGSR----WRAYRRLHHSLGQDAD-WSERLFARDFAKTYEEQVR 387
Cdd:TIGR03354 321 AVRAALRRMLDAFSPEALEARFEQYRR-SGLLLFGGRdawaWDMYLRYYRELRSDREqGFERLFGEDFAQAYEEALR 396
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
 1-387 8.54e-99

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: 299.75  E-value: 8.54e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279   1 MELVFDMVGAQQFVPGLLTTKTFKQAGGVIGRAEGCDWVIPDRKRVLSGRHAVISYRDGAFFLTDTSSNGIQLKDSGASL 80
Cdd:COG3456    1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRSADCDWVLPDPDRSVSRRHAEIRFRDGAFCLTDLSTNGTFLNGSDHPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279  81 VKGQPQRIEHGSVYCLGDFEIRARLIQ-DPARFEGDIGRPQPA---------GTIIPDDAFLD---LDPLVAMDQQERIY 147
Cdd:COG3456   81 GPGRPVRLRDGDRLRIGDYEIRVEISGeDEGADDPLAAAPEPAvsspsnlsdTEAAPDAALAFsfsLDPLEALDEAATEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279 148 AEVDDLDLTLVaPQRQAQQRDYARIDTESLPLPELvmpPTAAEPKREPEPER-LPPGFWERFGEALGIDLGGMDEDQRQA 226
Cdd:COG3456  161 PATADDPPSLL-PEDWLPSAAPVADEAAAQAIDQL---PSAAAPAPEPEPAAdADHALLAALLRGLGLDLELLDSQDAED 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279 227 LALNAARLLKQSVAGLQQSLRTRSELKNELRLALTTVQSAGNNPLKHSADASEALNALLRGGKPGQLSAEQAVGRAFRDL 306
Cdd:COG3456  237 FLEELGRLLRAAVEGLLDLLRARAEFKNEFRLDQTMLRPIENNPLKFSPDYEEALALLLAPKSPGFLSAPAAVAESLRDL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279 307 QAHQVALLAASRAAVHAMFEQLAPEQLALRFEREGRkplLATAGSRWRAYRRLHHSLGQDADWS-ERLFARDFAKTYEEQ 385
Cdd:COG3456  317 RLHQLALLAAIQAALRALLDAFSPEALERRFERRLF---GSRKAKAWDMYEAYYQELSSERQQGfEKLFGEVFAQAYDRA 393


                 ..
gi 504408279 386 VR 387
Cdd:COG3456  394 LR 395
T6SS_FHA_C pfam20232
C-terminal domain of Type VI secretion system FHA protein; This presumed domain is found at ...
 210-385 4.41e-50

C-terminal domain of Type VI secretion system FHA protein; This presumed domain is found at the C-terminus of a group of proteins thought to be expressed in a Type VI secretion system locus. These proteins contain an N-terminal FHA domain. The function of this domain is unknown.


Pssm-ID: 466383  Cd Length: 180  Bit Score: 166.66  E-value: 4.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279  210 EALGIDLGGMDEDQRQALALNAARLLKQSVAGLQQSLRTRSELKNELRLALTTVQSAGNNPLKHSADASEALNALLRGGK 289
Cdd:pfam20232   1 EGAGLDPSALPGEETEELARELGQLLRAAVQGLMDLLRARAAVKNEFRAERTMIQPRENNPLKFSPDAEDALRQLLGKKR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279  290 PGQLSAEQAVGRAFRDLQAHQVALLAASRAAVHAMFEQLAPEQLALRFEREGRKPLLATAGSR---WRAYRRLHHSLGQD 366
Cdd:pfam20232  81 PGFLSPPEAVQEAFDDLQAHQLAMMAGIRAALEALLERFSPEALEARFRERGGLGGLLPGARKarlWDLYVEYYEELASD 160

                         170       180
                  ....*....|....*....|
gi 504408279  367 A-DWSERLFARDFAKTYEEQ 385
Cdd:pfam20232 161 AeDGFQDLFGEAFAEAYEDQ 180
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 29-102 5.97e-14

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: 66.92  E-value: 5.97e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504408279  29 VIGRAEGCDWVIPDRKrvLSGRHAVISYRDGAFFLTDTSS-NGIqlkdsgasLVKGQP----QRIEHGSVYCLGDFEIR 102
Cdd:cd00060   22 TIGRSPDCDIVLDDPS--VSRRHARIEVDGGGVYLEDLGStNGT--------FVNGKRitppVPLQDGDVIRLGDTTFR 90
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 29-73 5.76e-05

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 40.24  E-value: 5.76e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 504408279    29 VIGRAE-GCDWVIPDRKrvLSGRHAVISYR-DGAFFLTDTSS-NGIQL 73
Cdd:smart00240   2 TIGRSSeDCDIQLDGPS--ISRRHAVIVYDgGGRFYLIDLGStNGTFV 47
 
Name Accession Description Interval E-value
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
 3-387 1.29e-127

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: 373.24  E-value: 1.29e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279    3 LVFDMVGAQQFVPGLLTTKTFKQAGGVIGRAEGCDWVIPDRKRVLSGRHAVISYRDGAFFLTDTSSNGIQLKDSGASLVK 82
Cdd:TIGR03354   1 LVLTVLNAHQLTPGIAAQKTFGTNGGTIGRSEDCDWVLPDPERHVSGRHARIRYRDGAYLLTDLSTNGVFLNGSGSPLGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279   83 GQPQRIEHGSVYCLGDFEIRARL-----IQDPARFEGDIGRPQPAGTIIPDDAFLD-LDPLVAMDQQERIYAEVDDLDLT 156
Cdd:TIGR03354  81 GNPVRLEQGDRLRLGDYEIRVSLgdplvSRQASESRADTSLPTAGGPPTPDPAPLAqLDPLKALDQEPLSAADLDDLSAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279  157 LVAPQRQAQQRDYARIDTESLPLPELVMPPTAAEPKREPEPE-RLPPGFWERFGEALGIDLGGMDEDQRQALALNAARLL 235
Cdd:TIGR03354 161 LFPPLDARLPAFAAPIDAEPTMVPPFVPLPAPEPAPAPASQApSSDAVALTPFLRGLGLPLELLDSQAAEDVLEELGRLL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279  236 KQSVAGLQQSLRTRSELKNELRLALTTVQSAGNNPLKHSADASEALNALLRGGKPGQLSAEQAVGRAFRDLQAHQVALLA 315
Cdd:TIGR03354 241 RAMVEGLLQLLRARAELKNELRLNQTTIRPAENNPLKFSADYDEALAVLLAPRSPGHLSAEAAIEEAFRDLRAHQVALLA 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504408279  316 ASRAAVHAMFEQLAPEQLALRFEREGRkPLLATAGSR----WRAYRRLHHSLGQDAD-WSERLFARDFAKTYEEQVR 387
Cdd:TIGR03354 321 AVRAALRRMLDAFSPEALEARFEQYRR-SGLLLFGGRdawaWDMYLRYYRELRSDREqGFERLFGEDFAQAYEEALR 396
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
 1-387 8.54e-99

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: 299.75  E-value: 8.54e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279   1 MELVFDMVGAQQFVPGLLTTKTFKQAGGVIGRAEGCDWVIPDRKRVLSGRHAVISYRDGAFFLTDTSSNGIQLKDSGASL 80
Cdd:COG3456    1 MPLTLRIINSPDLESGSAASATFGRGGGTIGRSADCDWVLPDPDRSVSRRHAEIRFRDGAFCLTDLSTNGTFLNGSDHPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279  81 VKGQPQRIEHGSVYCLGDFEIRARLIQ-DPARFEGDIGRPQPA---------GTIIPDDAFLD---LDPLVAMDQQERIY 147
Cdd:COG3456   81 GPGRPVRLRDGDRLRIGDYEIRVEISGeDEGADDPLAAAPEPAvsspsnlsdTEAAPDAALAFsfsLDPLEALDEAATEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279 148 AEVDDLDLTLVaPQRQAQQRDYARIDTESLPLPELvmpPTAAEPKREPEPER-LPPGFWERFGEALGIDLGGMDEDQRQA 226
Cdd:COG3456  161 PATADDPPSLL-PEDWLPSAAPVADEAAAQAIDQL---PSAAAPAPEPEPAAdADHALLAALLRGLGLDLELLDSQDAED 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279 227 LALNAARLLKQSVAGLQQSLRTRSELKNELRLALTTVQSAGNNPLKHSADASEALNALLRGGKPGQLSAEQAVGRAFRDL 306
Cdd:COG3456  237 FLEELGRLLRAAVEGLLDLLRARAEFKNEFRLDQTMLRPIENNPLKFSPDYEEALALLLAPKSPGFLSAPAAVAESLRDL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279 307 QAHQVALLAASRAAVHAMFEQLAPEQLALRFEREGRkplLATAGSRWRAYRRLHHSLGQDADWS-ERLFARDFAKTYEEQ 385
Cdd:COG3456  317 RLHQLALLAAIQAALRALLDAFSPEALERRFERRLF---GSRKAKAWDMYEAYYQELSSERQQGfEKLFGEVFAQAYDRA 393


                 ..
gi 504408279 386 VR 387
Cdd:COG3456  394 LR 395
T6SS_FHA_C pfam20232
C-terminal domain of Type VI secretion system FHA protein; This presumed domain is found at ...
 210-385 4.41e-50

C-terminal domain of Type VI secretion system FHA protein; This presumed domain is found at the C-terminus of a group of proteins thought to be expressed in a Type VI secretion system locus. These proteins contain an N-terminal FHA domain. The function of this domain is unknown.


Pssm-ID: 466383  Cd Length: 180  Bit Score: 166.66  E-value: 4.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279  210 EALGIDLGGMDEDQRQALALNAARLLKQSVAGLQQSLRTRSELKNELRLALTTVQSAGNNPLKHSADASEALNALLRGGK 289
Cdd:pfam20232   1 EGAGLDPSALPGEETEELARELGQLLRAAVQGLMDLLRARAAVKNEFRAERTMIQPRENNPLKFSPDAEDALRQLLGKKR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279  290 PGQLSAEQAVGRAFRDLQAHQVALLAASRAAVHAMFEQLAPEQLALRFEREGRKPLLATAGSR---WRAYRRLHHSLGQD 366
Cdd:pfam20232  81 PGFLSPPEAVQEAFDDLQAHQLAMMAGIRAALEALLERFSPEALEARFRERGGLGGLLPGARKarlWDLYVEYYEELASD 160

                         170       180
                  ....*....|....*....|
gi 504408279  367 A-DWSERLFARDFAKTYEEQ 385
Cdd:pfam20232 161 AeDGFQDLFGEAFAEAYEDQ 180
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 29-102 5.97e-14

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: 66.92  E-value: 5.97e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504408279  29 VIGRAEGCDWVIPDRKrvLSGRHAVISYRDGAFFLTDTSS-NGIqlkdsgasLVKGQP----QRIEHGSVYCLGDFEIR 102
Cdd:cd00060   22 TIGRSPDCDIVLDDPS--VSRRHARIEVDGGGVYLEDLGStNGT--------FVNGKRitppVPLQDGDVIRLGDTTFR 90
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
16-102 2.35e-12

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 62.67  E-value: 2.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279  16 GLLTTKTFKQAGG--VIGRAEGCDWVIPDRKrvLSGRHAVISYRDGAFFLTDT-SSNGIqlkdsgasLVKGQ----PQRI 88
Cdd:COG1716    9 GPLAGRRFPLDGGplTIGRAPDNDIVLDDPT--VSRRHARIRRDGGGWVLEDLgSTNGT--------FVNGQrvtePAPL 78

                         90
                 ....*....|....
gi 504408279  89 EHGSVYCLGDFEIR 102
Cdd:COG1716   79 RDGDVIRLGKTELR 92
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 29-93 2.67e-10

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 55.66  E-value: 2.67e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504408279   29 VIGRAEGCDWVIPDrkRVLSGRHAVISYRDG-AFFLTDT-SSNGIQLKDsgaSLVKGQPQRIEHGSV 93
Cdd:pfam00498   2 TIGRSPDCDIVLDD--PSVSRRHAEIRYDGGgRFYLEDLgSTNGTFVNG---QRLGPEPVRLKDGDV 63
FHA_CHFR cd22672
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ...
 29-93 7.79e-10

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: 55.76  E-value: 7.79e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504408279  29 VIGRAEGCDWVIPDRKRVlSGRHAVISY-RDGAFFLTDTSSNGIQLkdSGASLVKGQPQRIEHGSV 93
Cdd:cd22672   24 TIGRAKDCDLSFPGNKLV-SGDHCKIIRdEKGQVWLEDTSTNGTLV--NKVKVVKGQKVELKHGDV 86
FHA_MDC1 cd22665
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ...
 29-100 3.96e-08

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: 50.69  E-value: 3.96e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504408279  29 VIGRAEGCDWVIPDRKrvLSGRHAVISYRDGAFFLTD-TSSNGIQLKdSGASLVKGQPQRIEHGSVYCLGDFE 100
Cdd:cd22665   24 VIGRDPSCSVVLPDKS--VSKQHACIEVDGGTHLIEDlGSTNGTRIG-NKVRLKPNVRYELIDGDLLLFGDVK 93
FHA_FhaA-like cd22668
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
 20-104 4.90e-06

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: 44.38  E-value: 4.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504408279  20 TKTFKQAGGVIGRAEGCDWVIPDRkrVLSGRHAVISYRDGAFFLTD-TSSNGIQLKDSGASLvkgqPQRIEHGSVYCLGD 98
Cdd:cd22668   12 VYQLREGSNIIGRGSDADFRLPDT--GVSRRHAEIRWDGQVAHLTDlGSTNGTTVNNAPVTP----EWRLADGDVITLGH 85


                 ....*.
gi 504408279  99 FEIRAR 104
Cdd:cd22668   86 SEIIVR 91
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 29-73 5.76e-05

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 40.24  E-value: 5.76e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 504408279    29 VIGRAE-GCDWVIPDRKrvLSGRHAVISYR-DGAFFLTDTSS-NGIQL 73
Cdd:smart00240   2 TIGRSSeDCDIQLDGPS--ISRRHAVIVYDgGGRFYLIDLGStNGTFV 47
FHA_RAD53-like_rpt2 cd22690
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
 29-91 8.22e-05

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: 41.51  E-value: 8.22e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504408279  29 VIGRAEGCDWVIPDRKrvLSGRHAVIsYRD------GAFFLTDTSSNGIQLkdSGASLVKGQPQRIEHG 91
Cdd:cd22690   22 FIGRSKDCDEEITDPR--ISKHHCII-TRKrsgkglDDVYVTDTSTNGTFI--NNNRLGKGSQSLLQDG 85
FHA_PP2C70-like cd22678
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ...
 30-99 1.44e-04

forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438730 [Multi-domain]  Cd Length: 102  Bit Score: 40.81  E-value: 1.44e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504408279  30 IGRAEGCDWVIPDRKrvLSGRHAVISY--RDGAFFLTDT-SSNGIQLkDSGASLVKGQPQRIEHGSVYCLGDF 99
Cdd:cd22678   27 IGRIQRGDIALKDDE--VSGKHARIEWnsTGSKWELVDLgSLNGTLV-NGESISPNGRPVVLSSGDVITLGSE 96
FHA_SLMAP cd22679
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ...
 45-70 3.10e-04

forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438731 [Multi-domain]  Cd Length: 126  Bit Score: 40.33  E-value: 3.10e-04
                         10        20
                 ....*....|....*....|....*..
gi 504408279  45 RVLSGRHAVISYRDGAFFLTDT-SSNG 70
Cdd:cd22679   47 KVLSRNHALLWYDDGKFYLQDTkSSNG 73
FHA_EspA-like cd22698
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ...
 30-76 4.80e-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: 38.93  E-value: 4.80e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504408279  30 IGRAEGCDWVIPDRKrvLSGRHAVISYRDGAFFLTDTSS------NGIQLKDS 76
Cdd:cd22698   25 IGRSSNNDIRLNDHS--VSRHHARIVRQGDKCNLTDLGStngtflNGIRVGTH 75
FHA_Rv1747-like_rpt1 cd22694
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
 29-75 9.60e-04

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: 9.60e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 504408279  29 VIGRAEGCDWVIPDRkrVLSGRHAVISYRDGAFFLTDTSS-NGIQLKD 75
Cdd:cd22694   19 RIGRDPDADVRLDDP--RVSRRHALLEFDGDGWVYTDLGSrNGTYLNG 64
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
 29-93 2.02e-03

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: 37.59  E-value: 2.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504408279  29 VIGRAEGCDWVIPDrkRVLSGRHAVI------SYRDGAFFLTDTSSNGIQLKDsgaSLVKGQPQRI-EHGSV 93
Cdd:cd22670   25 TIGRSPSCDIVIND--PFVSRTHCRIysvqfdESSAPLVYVEDLSSNGTYLNG---KLIGRNNTVLlSDGDV 91
FHA_FhaB-like cd22693
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
 13-76 8.60e-03

forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438745 [Multi-domain]  Cd Length: 91  Bit Score: 35.36  E-value: 8.60e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504408279  13 FVPGLLTTKTFK--QAGGVIGRAEGCDWVIPDRkrVLSGRHAVISYRDGAFFLTDT-SSNGIQLKDS 76
Cdd:cd22693    3 IIEGTLQGQTFPidKSGITIGRADDNDLVLSDD--FVSSRHARIYLQGSSWYLEDLgSTNGTFVNGN 67
 
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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