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Conserved domains on  [gi|568911051|ref|XP_006497002|]
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centrosomal protein of 170 kDa isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CEP170_C pfam15308
CEP170 C-terminus; This family includes the C-terminus of centrosomal protein of 170 kDa ...
815-1496 0e+00

CEP170 C-terminus; This family includes the C-terminus of centrosomal protein of 170 kDa (CEP170).


:

Pssm-ID: 464633  Cd Length: 682  Bit Score: 844.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   815 GDKKESSKSLVRQGSFTIDKPSSNIPIELIPHINKQNSSvptalaltsasRLRERSDSLDTDSSMDTTLILKDTEAVMAF 894
Cdd:pfam15308   16 PDKEASSKSFVRQESFTKEKPSGNVPIEKLPHISSHPLL-----------RDLERSRSARMDHSQDTHLILKETETALAA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   895 LEAKLReDNNKTDEGPDTPSYNRDNSISPESDVDTASTISLVTGETERKSTQKRKSFTSLYKDRCSTSSPSKDVTKSGS- 973
Cdd:pfam15308   85 LEAKLL-SESKGDEGEGSPSGQPEDSLSGESDVDTASTVSLVSGKNEPSSTQKRKSISSLQKEKSSSSPSAQDKGSQPSa 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   974 REKI-EKKAKSRSADIGARADGRKFVQSsGRIRQP--SIDLTDDDQTSSVPHSAISDIMSSDQETYSCKSHGRTPLTSAD 1050
Cdd:pfam15308  164 RERLsEKRRKSRTPDDGGRAEAARRFQS-RRSRGPrgSLDLTDDEQTSSLPHLPISDIVSSDHETYSRPSSRRKPFTSPD 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1051 ehNIHSKLEGGKATKSKTSPVASgsTSKSTTLPRPRPTRTSLLRRARLGEASDSELADADKASVASEVSTTSSTSKpptG 1130
Cdd:pfam15308  243 --LLAQKEEQSKSSKSSQKVQQV--LTRSNSLSTPRPTRASLLRRARLGDASDNELADTDRASVASEVSATSKPPT---E 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1131 RRTISRIDLLAQPRRtRLGSLSARSDSEATISRSSASARTAE--AVIRSG--ARLVPSDKLSPRTRANSISRLSDSKVKS 1206
Cdd:pfam15308  316 AKKLSRLDILAMPRK-RAGSFTAPSDSEATTSRSGFSGRSVElyCSSRKGtvSEARAAARKTARTRANSISKQPFSRTRS 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1207 MSSTHgSPSVNSRWRRFPTDYASTSEDEFGSNRNSPKHTRLRTSPALKTTRMQSTGSAMPASSSfkHRIKEQEDY----- 1281
Cdd:pfam15308  395 SSAKY-SSSSNSRRRQQGSDYTSTSEEEYGSNHNSPKHKRSHTSTATQTPRAQGTGTARQKPPG--HRETEEEEYqpdpy 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1282 -IRDWTAHREEIARISQ----DLALIAREINDVAGEIDSVTSSGTAPSTTVSTAATTPGSAIDTREELVDRVFDESLNFR 1356
Cdd:pfam15308  472 pFQDWTAHSAEIARLSQdlakDLAILAREIHDVAGDGDSQSSSGTAPSTSLSSVPNTPASTISAREELVQHIPEASLNFQ 551
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1357 KIPPlvhsktpeGNNGRsVDSRPQPAEHPDHLTITRRRTWSRDEVMGDNLLLSSVFQFSRKIRQSIDKTAGKIRILFKDK 1436
Cdd:pfam15308  552 KVPP--------GSNGR-KDLDQNMNDSREDQLAKKRRPWNREEVILDNLMLNPVSQLSQAIRENTEQLAEKMKILFQNK 622
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1437 DRNWDDIENKLRAESEVPIVKTSSMEISSILQELKRVEKQLQVINAMIDPDGTLEALNNM 1496
Cdd:pfam15308  623 DRNWEEIEAKINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPDGTLDALTSN 682
FHA_Cep170A cd22724
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ...
1-106 2.06e-72

forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar proteins; Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). The FHA domain is a small phosphopeptide recognition module.


:

Pssm-ID: 438776 [Multi-domain]  Cd Length: 106  Bit Score: 236.41  E-value: 2.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051    1 MSLTSWFLVSSGGTRHRLPREMIFVGRDDCELMLQSRSVDKQHAVINYDASMDEHLVKDLGSLNGTFVNDVRIPEQTYIT 80
Cdd:cd22724     1 MSLTSWFLVSSGGTRHRLPREMIFVGRDDCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIPEQTYIT 80
                          90       100
                  ....*....|....*....|....*.
gi 568911051   81 LKLEDKLRFGYDTNLFTVVRGEMRVP 106
Cdd:cd22724    81 LKLDDKLRFGYDTNLFTVVRGEMRVP 106
COG3456 super family cl34616
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
8-235 1.35e-04

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


The actual alignment was detected with superfamily member COG3456:

Pssm-ID: 442679 [Multi-domain]  Cd Length: 402  Bit Score: 46.29  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051    8 LVSSGGTRHRLPREMIFVGRD-DCELMLQ--SRSVDKQHAVINYDAsmDEHLVKDLgSLNGTFVN--DVRIPEQTYITLK 82
Cdd:COG3456    13 LESGSAASATFGRGGGTIGRSaDCDWVLPdpDRSVSRRHAEIRFRD--GAFCLTDL-STNGTFLNgsDHPLGPGRPVRLR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   83 LEDKLRFGydtnlftvvrgemrvpeealkheKFTIQLQLSQKSSESELPKSASAK--GTDSKVEAAAEVQPRATEALKSE 160
Cdd:COG3456    90 DGDRLRIG-----------------------DYEIRVEISGEDEGADDPLAAAPEpaVSSPSNLSDTEAAPDAALAFSFS 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911051  161 EKPMDVSAM-PRGTPLYGQPSWWGDAEEDEQRAFKANGKPEGKSQEAGAsgcSTEAKHVEGQSAAASEEALF-PFCR 235
Cdd:COG3456   147 LDPLEALDEaATEAPATADDPPSLLPEDWLPSAAPVADEAAAQAIDQLP---SAAAPAPEPEPAADADHALLaALLR 220
 
Name Accession Description Interval E-value
CEP170_C pfam15308
CEP170 C-terminus; This family includes the C-terminus of centrosomal protein of 170 kDa ...
815-1496 0e+00

CEP170 C-terminus; This family includes the C-terminus of centrosomal protein of 170 kDa (CEP170).


Pssm-ID: 464633  Cd Length: 682  Bit Score: 844.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   815 GDKKESSKSLVRQGSFTIDKPSSNIPIELIPHINKQNSSvptalaltsasRLRERSDSLDTDSSMDTTLILKDTEAVMAF 894
Cdd:pfam15308   16 PDKEASSKSFVRQESFTKEKPSGNVPIEKLPHISSHPLL-----------RDLERSRSARMDHSQDTHLILKETETALAA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   895 LEAKLReDNNKTDEGPDTPSYNRDNSISPESDVDTASTISLVTGETERKSTQKRKSFTSLYKDRCSTSSPSKDVTKSGS- 973
Cdd:pfam15308   85 LEAKLL-SESKGDEGEGSPSGQPEDSLSGESDVDTASTVSLVSGKNEPSSTQKRKSISSLQKEKSSSSPSAQDKGSQPSa 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   974 REKI-EKKAKSRSADIGARADGRKFVQSsGRIRQP--SIDLTDDDQTSSVPHSAISDIMSSDQETYSCKSHGRTPLTSAD 1050
Cdd:pfam15308  164 RERLsEKRRKSRTPDDGGRAEAARRFQS-RRSRGPrgSLDLTDDEQTSSLPHLPISDIVSSDHETYSRPSSRRKPFTSPD 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1051 ehNIHSKLEGGKATKSKTSPVASgsTSKSTTLPRPRPTRTSLLRRARLGEASDSELADADKASVASEVSTTSSTSKpptG 1130
Cdd:pfam15308  243 --LLAQKEEQSKSSKSSQKVQQV--LTRSNSLSTPRPTRASLLRRARLGDASDNELADTDRASVASEVSATSKPPT---E 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1131 RRTISRIDLLAQPRRtRLGSLSARSDSEATISRSSASARTAE--AVIRSG--ARLVPSDKLSPRTRANSISRLSDSKVKS 1206
Cdd:pfam15308  316 AKKLSRLDILAMPRK-RAGSFTAPSDSEATTSRSGFSGRSVElyCSSRKGtvSEARAAARKTARTRANSISKQPFSRTRS 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1207 MSSTHgSPSVNSRWRRFPTDYASTSEDEFGSNRNSPKHTRLRTSPALKTTRMQSTGSAMPASSSfkHRIKEQEDY----- 1281
Cdd:pfam15308  395 SSAKY-SSSSNSRRRQQGSDYTSTSEEEYGSNHNSPKHKRSHTSTATQTPRAQGTGTARQKPPG--HRETEEEEYqpdpy 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1282 -IRDWTAHREEIARISQ----DLALIAREINDVAGEIDSVTSSGTAPSTTVSTAATTPGSAIDTREELVDRVFDESLNFR 1356
Cdd:pfam15308  472 pFQDWTAHSAEIARLSQdlakDLAILAREIHDVAGDGDSQSSSGTAPSTSLSSVPNTPASTISAREELVQHIPEASLNFQ 551
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1357 KIPPlvhsktpeGNNGRsVDSRPQPAEHPDHLTITRRRTWSRDEVMGDNLLLSSVFQFSRKIRQSIDKTAGKIRILFKDK 1436
Cdd:pfam15308  552 KVPP--------GSNGR-KDLDQNMNDSREDQLAKKRRPWNREEVILDNLMLNPVSQLSQAIRENTEQLAEKMKILFQNK 622
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1437 DRNWDDIENKLRAESEVPIVKTSSMEISSILQELKRVEKQLQVINAMIDPDGTLEALNNM 1496
Cdd:pfam15308  623 DRNWEEIEAKINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPDGTLDALTSN 682
FHA_Cep170A cd22724
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ...
1-106 2.06e-72

forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar proteins; Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438776 [Multi-domain]  Cd Length: 106  Bit Score: 236.41  E-value: 2.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051    1 MSLTSWFLVSSGGTRHRLPREMIFVGRDDCELMLQSRSVDKQHAVINYDASMDEHLVKDLGSLNGTFVNDVRIPEQTYIT 80
Cdd:cd22724     1 MSLTSWFLVSSGGTRHRLPREMIFVGRDDCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIPEQTYIT 80
                          90       100
                  ....*....|....*....|....*.
gi 568911051   81 LKLEDKLRFGYDTNLFTVVRGEMRVP 106
Cdd:cd22724    81 LKLDDKLRFGYDTNLFTVVRGEMRVP 106
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
10-90 5.06e-17

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 77.69  E-value: 5.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   10 SSGGTRHRLPREMIFVGRD-DCELMLQSRSVDKQHAVINYDAsmDEHLVKDLGSLNGTFVNDVRIPEQTyiTLKLEDKLR 88
Cdd:COG1716    10 PLAGRRFPLDGGPLTIGRApDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTEPA--PLRDGDVIR 85

                  ..
gi 568911051   89 FG 90
Cdd:COG1716    86 LG 87
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
23-89 3.18e-12

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 62.98  E-value: 3.18e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568911051    23 IFVGRD-DCELMLQSRSVDKQHAVINYDaSMDEHLVKDLGSLNGTFVNDVRIPEQTYItLKLEDKLRF 89
Cdd:pfam00498    1 VTIGRSpDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGPEPVR-LKDGDVIRL 66
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
23-73 5.81e-09

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 53.34  E-value: 5.81e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568911051     23 IFVGR--DDCELMLQSRSVDKQHAVINYDaSMDEHLVKDLGSLNGTFVNDVRI 73
Cdd:smart00240    1 VTIGRssEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
8-235 1.35e-04

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: 46.29  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051    8 LVSSGGTRHRLPREMIFVGRD-DCELMLQ--SRSVDKQHAVINYDAsmDEHLVKDLgSLNGTFVN--DVRIPEQTYITLK 82
Cdd:COG3456    13 LESGSAASATFGRGGGTIGRSaDCDWVLPdpDRSVSRRHAEIRFRD--GAFCLTDL-STNGTFLNgsDHPLGPGRPVRLR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   83 LEDKLRFGydtnlftvvrgemrvpeealkheKFTIQLQLSQKSSESELPKSASAK--GTDSKVEAAAEVQPRATEALKSE 160
Cdd:COG3456    90 DGDRLRIG-----------------------DYEIRVEISGEDEGADDPLAAAPEpaVSSPSNLSDTEAAPDAALAFSFS 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911051  161 EKPMDVSAM-PRGTPLYGQPSWWGDAEEDEQRAFKANGKPEGKSQEAGAsgcSTEAKHVEGQSAAASEEALF-PFCR 235
Cdd:COG3456   147 LDPLEALDEaATEAPATADDPPSLLPEDWLPSAAPVADEAAAQAIDQLP---SAAAPAPEPEPAADADHALLaALLR 220
 
Name Accession Description Interval E-value
CEP170_C pfam15308
CEP170 C-terminus; This family includes the C-terminus of centrosomal protein of 170 kDa ...
815-1496 0e+00

CEP170 C-terminus; This family includes the C-terminus of centrosomal protein of 170 kDa (CEP170).


Pssm-ID: 464633  Cd Length: 682  Bit Score: 844.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   815 GDKKESSKSLVRQGSFTIDKPSSNIPIELIPHINKQNSSvptalaltsasRLRERSDSLDTDSSMDTTLILKDTEAVMAF 894
Cdd:pfam15308   16 PDKEASSKSFVRQESFTKEKPSGNVPIEKLPHISSHPLL-----------RDLERSRSARMDHSQDTHLILKETETALAA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   895 LEAKLReDNNKTDEGPDTPSYNRDNSISPESDVDTASTISLVTGETERKSTQKRKSFTSLYKDRCSTSSPSKDVTKSGS- 973
Cdd:pfam15308   85 LEAKLL-SESKGDEGEGSPSGQPEDSLSGESDVDTASTVSLVSGKNEPSSTQKRKSISSLQKEKSSSSPSAQDKGSQPSa 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   974 REKI-EKKAKSRSADIGARADGRKFVQSsGRIRQP--SIDLTDDDQTSSVPHSAISDIMSSDQETYSCKSHGRTPLTSAD 1050
Cdd:pfam15308  164 RERLsEKRRKSRTPDDGGRAEAARRFQS-RRSRGPrgSLDLTDDEQTSSLPHLPISDIVSSDHETYSRPSSRRKPFTSPD 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1051 ehNIHSKLEGGKATKSKTSPVASgsTSKSTTLPRPRPTRTSLLRRARLGEASDSELADADKASVASEVSTTSSTSKpptG 1130
Cdd:pfam15308  243 --LLAQKEEQSKSSKSSQKVQQV--LTRSNSLSTPRPTRASLLRRARLGDASDNELADTDRASVASEVSATSKPPT---E 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1131 RRTISRIDLLAQPRRtRLGSLSARSDSEATISRSSASARTAE--AVIRSG--ARLVPSDKLSPRTRANSISRLSDSKVKS 1206
Cdd:pfam15308  316 AKKLSRLDILAMPRK-RAGSFTAPSDSEATTSRSGFSGRSVElyCSSRKGtvSEARAAARKTARTRANSISKQPFSRTRS 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1207 MSSTHgSPSVNSRWRRFPTDYASTSEDEFGSNRNSPKHTRLRTSPALKTTRMQSTGSAMPASSSfkHRIKEQEDY----- 1281
Cdd:pfam15308  395 SSAKY-SSSSNSRRRQQGSDYTSTSEEEYGSNHNSPKHKRSHTSTATQTPRAQGTGTARQKPPG--HRETEEEEYqpdpy 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1282 -IRDWTAHREEIARISQ----DLALIAREINDVAGEIDSVTSSGTAPSTTVSTAATTPGSAIDTREELVDRVFDESLNFR 1356
Cdd:pfam15308  472 pFQDWTAHSAEIARLSQdlakDLAILAREIHDVAGDGDSQSSSGTAPSTSLSSVPNTPASTISAREELVQHIPEASLNFQ 551
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1357 KIPPlvhsktpeGNNGRsVDSRPQPAEHPDHLTITRRRTWSRDEVMGDNLLLSSVFQFSRKIRQSIDKTAGKIRILFKDK 1436
Cdd:pfam15308  552 KVPP--------GSNGR-KDLDQNMNDSREDQLAKKRRPWNREEVILDNLMLNPVSQLSQAIRENTEQLAEKMKILFQNK 622
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051  1437 DRNWDDIENKLRAESEVPIVKTSSMEISSILQELKRVEKQLQVINAMIDPDGTLEALNNM 1496
Cdd:pfam15308  623 DRNWEEIEAKINAENEVPILKTSNKEISSILKELRRVQKQLEVINAIVDPDGTLDALTSN 682
FHA_Cep170A cd22724
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ...
1-106 2.06e-72

forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar proteins; Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438776 [Multi-domain]  Cd Length: 106  Bit Score: 236.41  E-value: 2.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051    1 MSLTSWFLVSSGGTRHRLPREMIFVGRDDCELMLQSRSVDKQHAVINYDASMDEHLVKDLGSLNGTFVNDVRIPEQTYIT 80
Cdd:cd22724     1 MSLTSWFLVSSGGTRHRLPREMIFVGRDDCELMLQSRSVDKQHAVINYDASTDEHKVKDLGSLNGTFVNDVRIPEQTYIT 80
                          90       100
                  ....*....|....*....|....*.
gi 568911051   81 LKLEDKLRFGYDTNLFTVVRGEMRVP 106
Cdd:cd22724    81 LKLDDKLRFGYDTNLFTVVRGEMRVP 106
FHA_Cep170B cd22725
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) ...
1-106 7.79e-61

forkhead associated (FHA) domain found in centrosomal protein of 170 kDa protein B (Cep170B) and similar proteins; Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438777 [Multi-domain]  Cd Length: 106  Bit Score: 203.23  E-value: 7.79e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051    1 MSLTSWFLVSSGGTRHRLPREMIFVGRDDCELMLQSRSVDKQHAVINYDASMDEHLVKDLGSLNGTFVNDVRIPEQTYIT 80
Cdd:cd22725     1 MSVTSWFLVSSSGTRHRLPREMIFVGREDCELMLQSRSVDKQHAVINYDQDTDEHWVKDLGSLNGTFVNDVRIPDQKYIT 80
                          90       100
                  ....*....|....*....|....*.
gi 568911051   81 LKLEDKLRFGYDTNLFTVVRGEMRVP 106
Cdd:cd22725    81 LKLNDVIRFGYDSNMYVLERSQHKVP 106
FHA_Cep170 cd22704
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ...
5-106 1.79e-60

forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438756 [Multi-domain]  Cd Length: 102  Bit Score: 202.16  E-value: 1.79e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051    5 SWFLVSSGGTRHRLPREMIFVGRDDCELMLQSRSVDKQHAVINYDASMDEHLVKDLGSLNGTFVNDVRIPEQTYITLKLE 84
Cdd:cd22704     1 SWCLVSSDGTRHRLPRSMLFVGREDCDLILQSRSVDKQHAVITYDQIDNEFKIKDLGSLNGTFVNDSRIPEQTYITLKLG 80
                          90       100
                  ....*....|....*....|..
gi 568911051   85 DKLRFGYDTNLFTVVRGEMRVP 106
Cdd:cd22704    81 DSIRFGYDTNVYRFEQLSLTTI 102
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
10-90 5.06e-17

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 77.69  E-value: 5.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   10 SSGGTRHRLPREMIFVGRD-DCELMLQSRSVDKQHAVINYDAsmDEHLVKDLGSLNGTFVNDVRIPEQTyiTLKLEDKLR 88
Cdd:COG1716    10 PLAGRRFPLDGGPLTIGRApDNDIVLDDPTVSRRHARIRRDG--GGWVLEDLGSTNGTFVNGQRVTEPA--PLRDGDVIR 85

                  ..
gi 568911051   89 FG 90
Cdd:COG1716    86 LG 87
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
10-90 6.64e-16

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: 74.23  E-value: 6.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   10 SSGGTRHRLPREMIFVGRD-DCELMLQSRSVDKQHAVINYDAsmDEHLVKDLGSLNGTFVNDVRIPEQTyiTLKLEDKLR 88
Cdd:cd00060     8 DGGGREFPLTKGVVTIGRSpDCDIVLDDPSVSRRHARIEVDG--GGVYLEDLGSTNGTFVNGKRITPPV--PLQDGDVIR 83

                  ..
gi 568911051   89 FG 90
Cdd:cd00060    84 LG 85
FHA_FHAD1 cd22700
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ...
25-92 3.04e-15

forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438752 [Multi-domain]  Cd Length: 96  Bit Score: 72.67  E-value: 3.04e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568911051   25 VGRDDCELMLQSRSVDKQHAVINYDASMDEHLVKDLGSLNGTFVNDVRIpEQTYITLKLEDKLRFGYD 92
Cdd:cd22700    20 IGREGCDLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQGTYVNDCRI-QNAAVRLAPGDVLRFGFG 86
FHA_Kanadaptin cd22677
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ...
25-96 2.29e-12

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: 64.88  E-value: 2.29e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911051   25 VGRD-DCELMLQSRSVDKQHAVINYDASMDEH----LVKDLGSLNGTFVNDVRIPEQTYITLKLEDKLRFGYDTNLF 96
Cdd:cd22677    26 FGRLpGCDVVLEHPSISRYHAVLQYRGDADDHdggfYLYDLGSTHGTFLNKQRIPPKQYYRLRVGHVLKFGGSTRLY 102
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
23-89 3.18e-12

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 62.98  E-value: 3.18e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568911051    23 IFVGRD-DCELMLQSRSVDKQHAVINYDaSMDEHLVKDLGSLNGTFVNDVRIPEQTYItLKLEDKLRF 89
Cdd:pfam00498    1 VTIGRSpDCDIVLDDPSVSRRHAEIRYD-GGGRFYLEDLGSTNGTFVNGQRLGPEPVR-LKDGDVIRL 66
FHA_SNIP1_DDL-like cd22676
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ...
25-94 1.66e-11

forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA domain-containing protein DDL, and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. This family also includes Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins. DDL, also called protein DAWDLE, is involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438728 [Multi-domain]  Cd Length: 111  Bit Score: 62.70  E-value: 1.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   25 VGRDD--CELMLQSRSVDKQHAVINYDASMDEHL----------VKDLGSLNGTFVNDVRIPEQTYITLKLEDKLRFGYD 92
Cdd:cd22676    25 IGRDRrvADIPLDHPSCSKQHAVIQFREVEKRNEgdvienirpyIIDLGSTNGTFLNGEKIEPRRYYELREKDVLKFGLS 104

                  ..
gi 568911051   93 TN 94
Cdd:cd22676   105 TR 106
FHA_MDC1 cd22665
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ...
13-90 7.95e-11

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: 60.32  E-value: 7.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   13 GTRHRLPREMIFVGRD-DCELMLQSRSVDKQHAVINYDAsmDEHLVKDLGSLNGTFVN-DVRIPEQTYITLKLEDKLRFG 90
Cdd:cd22665    13 EKDFPLYEGENVIGRDpSCSVVLPDKSVSKQHACIEVDG--GTHLIEDLGSTNGTRIGnKVRLKPNVRYELIDGDLLLFG 90
FHA_PS1-like cd22691
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ...
18-96 4.41e-09

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: 55.89  E-value: 4.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   18 LPREMIFVGR-DDCELMLQSRSVDKQHAVINYDASMDEHLVKDLGSLNGTFVNDVRIPEQTYITLKLEDKLRFGYDTNLF 96
Cdd:cd22691    26 EEEDILVVGRhPDCDIVLDHPSISRFHLEIRIIPSRRKITLTDLSSVHGTWVNGQRIEPGVPVELEEGDTVRLGASTRVY 105
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
23-73 5.81e-09

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 53.34  E-value: 5.81e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 568911051     23 IFVGR--DDCELMLQSRSVDKQHAVINYDaSMDEHLVKDLGSLNGTFVNDVRI 73
Cdd:smart00240    1 VTIGRssEDCDIQLDGPSISRRHAVIVYD-GGGRFYLIDLGSTNGTFVNGKRI 52
FHA_SNIP1 cd22718
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1) and ...
25-93 3.29e-08

forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1) and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex, which associates with both the 3'end of the CCND1 gene and its mRNA. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438770  Cd Length: 149  Bit Score: 54.32  E-value: 3.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   25 VGRDD--CELMLQSRSVDKQHAVINY--------DASMDEHL---VKDLGSLNGTFVNDVRIPEQTYITLKLEDKLRFGY 91
Cdd:cd22718    60 LGRDRkiADIPIDHPSCSKQHAVLQYrlveytrpDGTKGRRVrpyIIDLESANGTFLNNKKIEPQRYYELKEKDVLKFGF 139

                  ..
gi 568911051   92 DT 93
Cdd:cd22718   140 SS 141
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
13-90 4.70e-08

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: 52.26  E-value: 4.70e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568911051    13 GTRHRLPREMIFVGRD-DCELMLQSRSVDKQHAVINYDAsmDEHLVKDLGSLNGTFVNDVRIPEQTyITLKLEDKLRFG 90
Cdd:pfam16697    9 GAEFPLEGGRYRIGSDpDCDIVLSDKEVSRVHLKLEVDD--EGWRLDDLGSGNGTLVNGQRVTELG-IALRPGDRIELG 84
FHA_PPP1R8 cd22674
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ...
26-98 5.63e-08

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: 52.27  E-value: 5.63e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568911051   26 GR--DDCELMLQSRSVDKQHAVINYDASMDEHLVKDLGSLNGTFVNDVRIPEQTYITLKLEDKLRFGYDTNLFTV 98
Cdd:cd22674    32 GRnsDVCDFVLDHPSCSRVHAALVYHKHLNRVFLIDLGSTHGTFVGGIRLEPHKPQQLPIDSTLRFGASTRRYIL 106
FHA_Rv1747-like_rpt1 cd22694
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
12-90 9.81e-08

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: 51.17  E-value: 9.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   12 GGTRHRLPREMIFVGRD-DCELMLQSRSVDKQHAVINYDAsmDEHLVKDLGSLNGTFVNDVRIPEqtyITLKLEDKLRFG 90
Cdd:cd22694     7 GGELRFDPGSSVRIGRDpDADVRLDDPRVSRRHALLEFDG--DGWVYTDLGSRNGTYLNGRRVQQ---VKLSDGTRVRLG 81
FHA_ArnA-like cd22680
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ...
20-95 1.15e-07

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: 51.19  E-value: 1.15e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568911051   20 REMIFVGRDD-CELMLQSRSVDKQHAVINYDAsmDEHLVKDLGSLNGTFVND-VRIPEQTyiTLKLEDKLRFGYDTNL 95
Cdd:cd22680    20 FSSVSIGRDPeNVIVIPDPFVSRNHARITVDS--NEIYIEDLGSTNGTFVNDfKRIKGPA--KLHPNDIIKLGRTTVL 93
FHA_DDL-like cd22719
forkhead associated (FHA) domain found in Arabidopsis thaliana FHA domain-containing protein ...
21-90 4.03e-07

forkhead associated (FHA) domain found in Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins; DDL, also called protein DAWDLE, is involved in microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438771 [Multi-domain]  Cd Length: 130  Bit Score: 50.57  E-value: 4.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   21 EMIFVGRDDCELMLQSRSV----------DKQHAVINY-------DASMDEHLVK----DLGSLNGTFVNDVRIPEQTYI 79
Cdd:cd22719    29 EPLHIHRQSCYLFGRERKVadiptdhpscSKQHAVIQYrltekegGDGMMGKAVRpyimDLGSTNGTFLNGERIEPQRYY 108
                          90
                  ....*....|.
gi 568911051   80 TLKLEDKLRFG 90
Cdd:cd22719   109 ELLEKDTIKFG 119
FHA_RNF8 cd22663
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ...
6-90 8.51e-07

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: 49.28  E-value: 8.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051    6 WFL--VSSGGTRHRLPREM---IFVGR---------DDCELMLqSRsvdkQHAVINYDASmDEHLVKDLGSLNGTFVNDV 71
Cdd:cd22663     1 WCLrrVGHGIDPLVLLLEDgkeVTVGRglgvtyqlvSTCPLMI-SR----NHCVLKKNDE-GQWTIKDNKSLNGVWVNGE 74
                          90
                  ....*....|....*....
gi 568911051   72 RIPEQTYITLKLEDKLRFG 90
Cdd:cd22663    75 RIEPLKPYPLNEGDLIQLG 93
FHA_AGGF1 cd22686
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ...
25-102 9.29e-07

forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438738 [Multi-domain]  Cd Length: 123  Bit Score: 49.20  E-value: 9.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   25 VGRD-DCELMLQ--SRSVDKQHAVINYDASMDEHLVKDLGSLNGTFVNDVRIPEQTYIT----LKLEDKLRFGYDTNLFT 97
Cdd:cd22686    30 IGREkDHGHTIRipELGVSKFHAEIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKEKSdpypLTHGDELKIGETTLLFH 109

                  ....*
gi 568911051   98 VVRGE 102
Cdd:cd22686   110 IHPGS 114
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
13-90 1.53e-06

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: 47.98  E-value: 1.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568911051   13 GTRHRLPREMIFVGRD-DCELMLQSRSVDKQHAVINYDASMDEHLVkDLGSLNGTFVNDVRIPEQtyITLKLEDKLRFG 90
Cdd:cd22673    13 GSRFPLTKKSCTFGRDlSCDIRIQLPGVSREHCRIEVDENGKAYLE-NLSTTNPTLVNGKAIEKS--AELKDGDVITIG 88
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
6-98 1.65e-06

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: 48.09  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051    6 WFLVSS---GGTRHRLP--REMIfVGRDDCELMLQ-SRSVDKQHAVINYDASMDEHL---------VKDLgSLNGTFVND 70
Cdd:cd22667     1 WWLLSEqdgAGTSYYLLpgGEYT-VGRKDCDIIIVdDSSISRKHATLTVLHPEANLSdpdtrpeltLKDL-SKYGTFVNG 78
                          90       100
                  ....*....|....*....|....*...
gi 568911051   71 VRIPEQTYITLKLEDKLRFGYDTNLFTV 98
Cdd:cd22667    79 EKLKGGSEVTLKDGDVITFGVLGSKFRV 106
FHA_FhaB-like cd22693
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
13-90 3.03e-06

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: 46.91  E-value: 3.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568911051   13 GTRHRLPREMIFVGR-DDCELMLQSRSVDKQHAVINYDASmdEHLVKDLGSLNGTFVNDVRIPEQtyITLKLEDKLRFG 90
Cdd:cd22693    10 GQTFPIDKSGITIGRaDDNDLVLSDDFVSSRHARIYLQGS--SWYLEDLGSTNGTFVNGNRVTQP--VVVQPGDTIRIG 84
FHA_Ct664-like cd22696
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar ...
24-80 3.37e-06

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: 47.10  E-value: 3.37e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568911051   24 FVGRDD--CELMLQSRSVDKQHAVINYDasmDEH--LVKDLGSLNGTFVNDVRIPEQTYIT 80
Cdd:cd22696    24 FIGKDPtvCDIVLQDPSISRQHARLSID---QDNrvFIEDLSSKNGVLVNGKPIEGKEEIS 81
FHA_Par42-like cd22675
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar ...
16-101 1.45e-05

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: 45.62  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   16 HRLPreMIFVGRDD-CELMLQSRSVDKQHAVINYDASMDEHLVKDLGSLNGTFVNDVRIPEQTYITLKLEDKLRFGYDTN 94
Cdd:cd22675    26 DRFP--FYLFGRSPvCDYVLEHPSISSVHAVLVFHGEQKCFVLMDLGSTNGVKLNGKRIEKGRPLPLPVGSVIQFGFSAR 103

                  ....*..
gi 568911051   95 LFTVVRG 101
Cdd:cd22675   104 KYKVRKG 110
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
9-89 1.82e-05

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: 45.30  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051    9 VSSGGTRHRLP---REMIFVGRDD-CELMLQSRSVDKQHAVI---NYDASMDeHLV--KDLgSLNGTFVNDVRIPEQTYI 79
Cdd:cd22670     7 SSPGSTDIVLPiykNQVITIGRSPsCDIVINDPFVSRTHCRIysvQFDESSA-PLVyvEDL-SSNGTYLNGKLIGRNNTV 84
                          90
                  ....*....|
gi 568911051   80 TLKLEDKLRF 89
Cdd:cd22670    85 LLSDGDVIEI 94
FHA_DgcB-like cd22682
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ...
23-90 2.94e-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: 44.44  E-value: 2.94e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568911051   23 IFVGRD-DCELMLQSRSVDKQHAVInyDASMDEHLVKDLGSLNGTFVNDVRIPEQTYITLKLEDKLRFG 90
Cdd:cd22682    22 IVIGRSvESQVQIDDDSVSRYHAKL--AVNPSAVSIIDLGSTNGTIVNGKKIPKLASCDLQNGDQIKIG 88
FHA_PML1-like cd22681
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ...
23-89 4.52e-05

forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 (PML1) and similar proteins; PML1 is an FHA domain-containing protein required for efficient splicing and pre-mRNA nuclear retention. It is a component of the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3, and PML1. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438733 [Multi-domain]  Cd Length: 129  Bit Score: 44.74  E-value: 4.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568911051   23 IFVGRDD--------CELMLQSRSVDKQHAVI---NYDASMDEHLVkDLGSLNGTFVNDVRIPEQTYITLKLEDKLRF 89
Cdd:cd22681    42 YLIGREKgesteivvADIGIPEETCSKQHCVIqfrNVKGILKPYIM-DLDSSNGTCLNDNVIPSSRYVELRSGDVITF 118
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
8-235 1.35e-04

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: 46.29  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051    8 LVSSGGTRHRLPREMIFVGRD-DCELMLQ--SRSVDKQHAVINYDAsmDEHLVKDLgSLNGTFVN--DVRIPEQTYITLK 82
Cdd:COG3456    13 LESGSAASATFGRGGGTIGRSaDCDWVLPdpDRSVSRRHAEIRFRD--GAFCLTDL-STNGTFLNgsDHPLGPGRPVRLR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   83 LEDKLRFGydtnlftvvrgemrvpeealkheKFTIQLQLSQKSSESELPKSASAK--GTDSKVEAAAEVQPRATEALKSE 160
Cdd:COG3456    90 DGDRLRIG-----------------------DYEIRVEISGEDEGADDPLAAAPEpaVSSPSNLSDTEAAPDAALAFSFS 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911051  161 EKPMDVSAM-PRGTPLYGQPSWWGDAEEDEQRAFKANGKPEGKSQEAGAsgcSTEAKHVEGQSAAASEEALF-PFCR 235
Cdd:COG3456   147 LDPLEALDEaATEAPATADDPPSLLPEDWLPSAAPVADEAAAQAIDQLP---SAAAPAPEPEPAADADHALLaALLR 220
FHA_GarA_OdhI-like cd22684
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ...
13-90 2.45e-04

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: 41.60  E-value: 2.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568911051   13 GTRHRLPREMIFVGRD-DCELMLQSRSVDKQHAviNYDASMDEHLVKDLGSLNGTFVNDVRIPEqtyITLKLEDKLRFG 90
Cdd:cd22684    13 GARFLLDQDVTTAGRHpESDIFLDDVTVSRRHA--EFRRAEGGFVVRDVGSLNGTYVNRERIDS---AVLRNGDEVQIG 86
FHA_EspA-like cd22698
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ...
17-100 3.36e-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: 41.24  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   17 RLPREMIFVGRD-DCELMLQSRSVDKQHAVINYDAsmDEHLVKDLGSLNGTFVNDVRIpeqTYITLKLEDKLRFGydtnl 95
Cdd:cd22698    17 ELDQDEFTIGRSsNNDIRLNDHSVSRHHARIVRQG--DKCNLTDLGSTNGTFLNGIRV---GTHELKHGDRIQLG----- 86

                  ....*
gi 568911051   96 FTVVR 100
Cdd:cd22698    87 ETIFR 91
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
25-92 4.49e-04

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: 42.02  E-value: 4.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911051   25 VGR--DDCELMLQSRS----VDKQHAVI---NYDASMDEHLVKDLgSLNGTFVNDVRIPEQTYITLKLEDKLRFGYD 92
Cdd:cd22685    32 IGRnpEVCDVFLCSSQhpnlISREHAEIhaeRDGNGNWKVLIEDR-STNGTYVNDVRLQDGQRRELSDGDTITFGHK 107
FHA_DUN1-like cd22683
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ...
20-90 5.85e-04

forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438735 [Multi-domain]  Cd Length: 96  Bit Score: 40.55  E-value: 5.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568911051   20 REMIFVGRD-DCELMLQSRSVDKQHAVINYDASMdeHLVKDLGSLNGTFVNDVRIPEQTYItLKLEDKLRFG 90
Cdd:cd22683    20 RNVTTIGRSrSCDLVLSDPSISRFHAELRLEQNG--INVIDNNSANGTFINGKRIKGKTYI-LKNGDIIVFG 88
FHA_FhaA-like cd22668
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
18-73 6.94e-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: 40.14  E-value: 6.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568911051   18 LPREMIFVGR-DDCELMLQSRSVDKQHAVINYDaSMDEHLVkDLGSLNGTFVNDVRI 73
Cdd:cd22668    15 LREGSNIIGRgSDADFRLPDTGVSRRHAEIRWD-GQVAHLT-DLGSTNGTTVNNAPV 69
FHA_RAD53-like_rpt2 cd22690
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
18-99 9.63e-04

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: 40.35  E-value: 9.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911051   18 LPREMIFVGR-DDCELMLQSRSVDKQHAVI---NYDASMDEHLVKDLgSLNGTFVNDVRIPEQTYITLKLEDKLRFGYDT 93
Cdd:cd22690    16 LTQNTTFIGRsKDCDEEITDPRISKHHCIItrkRSGKGLDDVYVTDT-STNGTFINNNRLGKGSQSLLQDGDEIVLIWDK 94

                  ....*.
gi 568911051   94 NLFTVV 99
Cdd:cd22690    95 NNKEKI 100
FHA_PP2C70-like cd22678
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ...
31-95 2.48e-03

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: 38.88  E-value: 2.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568911051   31 ELMLQSRSVDKQHAVINYDASMDEHLVKDLGSLNGTFVNDVRI-PEQTYITLKLEDKLRFGYDTNL 95
Cdd:cd22678    34 DIALKDDEVSGKHARIEWNSTGSKWELVDLGSLNGTLVNGESIsPNGRPVVLSSGDVITLGSETKI 99
FHA_Rv1747-like_rpt2 cd22737
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
12-73 6.24e-03

second 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 second FHA domain, which has a circularly permuted FHA domain fold with a conserved pThr-binding interface.


Pssm-ID: 439356 [Multi-domain]  Cd Length: 93  Bit Score: 37.47  E-value: 6.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568911051   12 GGTRHR--LPREMIFVGR-DDCELMLQSRSVDKQHAVINYDASMDEhlVKDLGSLNGTFVNDVRI 73
Cdd:cd22737    10 DGDTLTfeLPPQAVRIGRaSDNDIVIPEGSVSRHHATLVPTPGGTQ--IRDLRSTNGTFVNGLRV 72
 
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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