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Conserved domains on  [gi|1802450525|dbj|BBK61373|]
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type VII secretion protein EssC [Amedibacterium intestinale]

Protein Classification

FHA and TrwB_TraG_TraD_VirD4 domain-containing protein( domain architecture ID 12875429)

FHA and TrwB_TraG_TraD_VirD4 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
T7_EssCb_Firm super family cl37349
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 269-1259 2.53e-149

type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]


The actual alignment was detected with superfamily member TIGR03928:

Pssm-ID: 274860 [Multi-domain]  Cd Length: 1296  Bit Score: 486.80  E-value: 2.53e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  269 AISQKSSLQqIIPSVTMAVSMMLTTmfwplISKYY-EKIRFKKQYNSLLNDYRRYLKVKNNEVYKYIQEKQCYERNKIED 347
Cdd:TIGR03928   55 SIFQPRGIF-IIASIAMSLVTIIFS-----TTTYFrEKKKYKKDVEKRNRSYRLYLDKKRKELQALSEKQRHVLHYHNPS 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  348 FITVKKYIETRSPCLWNRKKENDDFLYLHCGWKLKKIKAPISDKQEVFDLQKNEVKEE--YLKFVNSSYEiKYPFLVDLK 425
Cdd:TIGR03928  129 VEELKEMVENVNSRIWEKTPEHHDFLHVRLGTGNVPSSFEIKFPEEEFSQRKDELLDEaqELKEKYNTIE-NVPIVLDLS 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  426 KYTIGVYGEKALYYG--NMFILYIAALHSKKDVTIL-LVGEQEYLWKSKAKWI--SQVEENNIRHVYSDEKDIQKLLVYL 500
Cdd:TIGR03928  208 NGPIGYVGKRSLVLEelQNLVGQLAFFHSYHDVQFVtIFPEEEKKKWEWMRWLphFWLRDINVRGFVYNERTRDQLLNSL 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  501 -------KQKRSEN------RF---YIIVLLNisKKLtqqILNSV---YLMKNVKYIQC----CKE-KEMLSDSVDFIFS 556
Cdd:TIGR03928  288 yqilkerKLALDDAnskekkRFsphYVFLITD--RKL---ILDHVimeYLNEDPSELGIslifVQDvMESLPENVKTVID 362

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  557 TEDKN--VFYKENKKQENILFEVE--KKESTENLFRKLMLLQEFEEDKKDIYESFGVLSLYSCTCLNQLNILERWKESQS 632
Cdd:TIGR03928  363 IKNRNegEIVLEEGELVEKSFTPDhlDNEDLEEYSRTLAPLNHLQNLKNSIPESVTFLEMYGVKKVEELNIQERWAKNET 442

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  633 EDSLRVPIGIDEFNEYIWLDAHENAHGPHGLFAGTTGSGKSECILTYILSLSIQFSYEDVCFVIIDYKGGMMANALQGLP 712
Cdd:TIGR03928  443 YKSLAVPIGLRGKDDIVYLNLHEKAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMANLFKNLP 522

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  713 HVSCIMTNLCEDERRRMHLSLQSEVNRRQQIFANDSLGSMDiyKYQKLVHEQKRKEPIPHMFIVIDEFAQLKQQYPDFLD 792
Cdd:TIGR03928  523 HLLGTITNLDGAQSMRALASIKAELKKRQRLFGENNVNHIN--QYQKLYKQGKAKEPMPHLFLISDEFAELKSEQPEFMK 600

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  793 FLKQIARIGRSLGIHLLLATQKPFGVVDEEIWSNSHFHLCLKVQDRQDSMDMLKNDDAVYLKNPGEFYLQVGNNEVYVKG 872
Cdd:TIGR03928  601 ELVSTARIGRSLGVHLILATQKPSGVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEITVPGRAYLQVGNNEVYELF 680

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  873 KSAWTQQPYIDEKTKNDKEDkVLRI--------FNQQKELLKEVKPkTYREHTELQMIVFYLKKIAKGKCAKQLFFPNLK 944
Cdd:TIGR03928  681 QSAWSGAPYDPDKDKKEEED-IYMIndlgqyelLNEDLSGLKRKKE-IKEVPTELEAVIDEIQAYTEELNIEALPSPWLP 758

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  945 PDLERI------KSSLQNCWN---------MGMVDDISKQSQYPWILDISQFHHLLLIDSKE--KASFLNVFLQENENLY 1007
Cdd:TIGR03928  759 PLEEKIylddlhAVEFDKLWSkpkeplqatIGLLDDPELQSQEPLTLDLSKDGHLAIFGSPGygKSTFLQTLIMSLARQH 838

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525 1008 QDNPVYVYILAVHPGSKESLLQYPSVQEAISVEESEKIKHFLSYLKNRIRKRKK----------------NEEEKNDIVI 1071
Cdd:TIGR03928  839 SPEQLHFYLFDFGTNGLLPLKKLPHVADYFTLDEEEKIEKLIRRIKKEIDRRKKlfseygvasismynkaSGEKLPQIVI 918

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525 1072 VLQEFEYFKE--TFPELMEDILFLLREGEKTNIHFFVFGSDLQMIPYLLFPYFDLRIIGELREESSYITLLGNENLE--- 1146
Cdd:TIGR03928  919 IIDNYDAVKEepFYEDFEELLIQLAREGASLGIYLVMTAGRQNAVRMPLMNNIKTKIALYLIDKSEYRSIVGRTKFTiee 998

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525 1147 ---RPLHQKGSY--------VCDDGRQVKIVQLHKEIRV--SYKKHKKPWALPSISKVIPF----------PKTRKGYLF 1203
Cdd:TIGR03928  999 ipgRGLIKKDEPtlfqtalpVKGEDDLEVIENIKAEIQKmnEAWTGERPKPIPMVPEELSLeefreryevrKILEEGSIP 1078

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525 1204 IGIDKQSMEEYQVSF--------------EKEKFIVFLTNTTFLNGFVK-----GIKRQL-----QDHCAAYIENKKETK 1259
Cdd:TIGR03928 1079 IGLDEETVEPVYIDLtenphllivgesddGKTNVLKSLLKTLAKQEKEKiglidSIDRGLlayrdLKEVATYIEEKEDLK 1158
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 104-178 1.56e-20

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: 87.33  E-value: 1.56e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1802450525  104 DKKSFLLGRDDACDICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNKRVKEK-KLQDGDSIQIPGIQMLYV 178
Cdd:cd00060     17 TKGVVTIGRSPDCDIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNGTFVNGKRITPPvPLQDGDVIRLGDTTFRFE 92
 
Name Accession Description Interval E-value
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 269-1259 2.53e-149

type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274860 [Multi-domain]  Cd Length: 1296  Bit Score: 486.80  E-value: 2.53e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  269 AISQKSSLQqIIPSVTMAVSMMLTTmfwplISKYY-EKIRFKKQYNSLLNDYRRYLKVKNNEVYKYIQEKQCYERNKIED 347
Cdd:TIGR03928   55 SIFQPRGIF-IIASIAMSLVTIIFS-----TTTYFrEKKKYKKDVEKRNRSYRLYLDKKRKELQALSEKQRHVLHYHNPS 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  348 FITVKKYIETRSPCLWNRKKENDDFLYLHCGWKLKKIKAPISDKQEVFDLQKNEVKEE--YLKFVNSSYEiKYPFLVDLK 425
Cdd:TIGR03928  129 VEELKEMVENVNSRIWEKTPEHHDFLHVRLGTGNVPSSFEIKFPEEEFSQRKDELLDEaqELKEKYNTIE-NVPIVLDLS 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  426 KYTIGVYGEKALYYG--NMFILYIAALHSKKDVTIL-LVGEQEYLWKSKAKWI--SQVEENNIRHVYSDEKDIQKLLVYL 500
Cdd:TIGR03928  208 NGPIGYVGKRSLVLEelQNLVGQLAFFHSYHDVQFVtIFPEEEKKKWEWMRWLphFWLRDINVRGFVYNERTRDQLLNSL 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  501 -------KQKRSEN------RF---YIIVLLNisKKLtqqILNSV---YLMKNVKYIQC----CKE-KEMLSDSVDFIFS 556
Cdd:TIGR03928  288 yqilkerKLALDDAnskekkRFsphYVFLITD--RKL---ILDHVimeYLNEDPSELGIslifVQDvMESLPENVKTVID 362

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  557 TEDKN--VFYKENKKQENILFEVE--KKESTENLFRKLMLLQEFEEDKKDIYESFGVLSLYSCTCLNQLNILERWKESQS 632
Cdd:TIGR03928  363 IKNRNegEIVLEEGELVEKSFTPDhlDNEDLEEYSRTLAPLNHLQNLKNSIPESVTFLEMYGVKKVEELNIQERWAKNET 442

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  633 EDSLRVPIGIDEFNEYIWLDAHENAHGPHGLFAGTTGSGKSECILTYILSLSIQFSYEDVCFVIIDYKGGMMANALQGLP 712
Cdd:TIGR03928  443 YKSLAVPIGLRGKDDIVYLNLHEKAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMANLFKNLP 522

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  713 HVSCIMTNLCEDERRRMHLSLQSEVNRRQQIFANDSLGSMDiyKYQKLVHEQKRKEPIPHMFIVIDEFAQLKQQYPDFLD 792
Cdd:TIGR03928  523 HLLGTITNLDGAQSMRALASIKAELKKRQRLFGENNVNHIN--QYQKLYKQGKAKEPMPHLFLISDEFAELKSEQPEFMK 600

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  793 FLKQIARIGRSLGIHLLLATQKPFGVVDEEIWSNSHFHLCLKVQDRQDSMDMLKNDDAVYLKNPGEFYLQVGNNEVYVKG 872
Cdd:TIGR03928  601 ELVSTARIGRSLGVHLILATQKPSGVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEITVPGRAYLQVGNNEVYELF 680

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  873 KSAWTQQPYIDEKTKNDKEDkVLRI--------FNQQKELLKEVKPkTYREHTELQMIVFYLKKIAKGKCAKQLFFPNLK 944
Cdd:TIGR03928  681 QSAWSGAPYDPDKDKKEEED-IYMIndlgqyelLNEDLSGLKRKKE-IKEVPTELEAVIDEIQAYTEELNIEALPSPWLP 758

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  945 PDLERI------KSSLQNCWN---------MGMVDDISKQSQYPWILDISQFHHLLLIDSKE--KASFLNVFLQENENLY 1007
Cdd:TIGR03928  759 PLEEKIylddlhAVEFDKLWSkpkeplqatIGLLDDPELQSQEPLTLDLSKDGHLAIFGSPGygKSTFLQTLIMSLARQH 838

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525 1008 QDNPVYVYILAVHPGSKESLLQYPSVQEAISVEESEKIKHFLSYLKNRIRKRKK----------------NEEEKNDIVI 1071
Cdd:TIGR03928  839 SPEQLHFYLFDFGTNGLLPLKKLPHVADYFTLDEEEKIEKLIRRIKKEIDRRKKlfseygvasismynkaSGEKLPQIVI 918

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525 1072 VLQEFEYFKE--TFPELMEDILFLLREGEKTNIHFFVFGSDLQMIPYLLFPYFDLRIIGELREESSYITLLGNENLE--- 1146
Cdd:TIGR03928  919 IIDNYDAVKEepFYEDFEELLIQLAREGASLGIYLVMTAGRQNAVRMPLMNNIKTKIALYLIDKSEYRSIVGRTKFTiee 998

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525 1147 ---RPLHQKGSY--------VCDDGRQVKIVQLHKEIRV--SYKKHKKPWALPSISKVIPF----------PKTRKGYLF 1203
Cdd:TIGR03928  999 ipgRGLIKKDEPtlfqtalpVKGEDDLEVIENIKAEIQKmnEAWTGERPKPIPMVPEELSLeefreryevrKILEEGSIP 1078

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525 1204 IGIDKQSMEEYQVSF--------------EKEKFIVFLTNTTFLNGFVK-----GIKRQL-----QDHCAAYIENKKETK 1259
Cdd:TIGR03928 1079 IGLDEETVEPVYIDLtenphllivgesddGKTNVLKSLLKTLAKQEKEKiglidSIDRGLlayrdLKEVATYIEEKEDLK 1158
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
 621-815 5.96e-24

FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.


Pssm-ID: 279863 [Multi-domain]  Cd Length: 219  Bit Score: 101.69  E-value: 5.96e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  621 LNILERWKESQSEDSLRVPIGIDEFNEYIWLDAHENAhgPHGLFAGTTGSGKSECILTYILSLSIQFSYEDVCFVIIDYK 700
Cdd:pfam01580    2 LEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMP--VHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  701 GGMMaNALQGLPHVscIMTNLCED-ER-RRMHLSLQSEVNRRQQIFANDSLGSM----------------DIYKYQKLVH 762
Cdd:pfam01580   80 MGEL-SAYEDIPHL--LSVPVATDpKRaLRALEWLVDEMERRYALFRALGVRSIagyngeiaedpldgfgDVFLVIYGVH 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1802450525  763 ----EQKRKEPIPHMFIVIDEFAQLKQQYPDF-----LDFLKQIARIGRSLGIHLLLATQKP 815
Cdd:pfam01580  157 vmctAGRWLEILPYLVVIVDERAELRLAAPKDsemrvEDAIVRLAQKGRAAGIHLLLATQRP 218
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 104-178 1.56e-20

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: 87.33  E-value: 1.56e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1802450525  104 DKKSFLLGRDDACDICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNKRVKEK-KLQDGDSIQIPGIQMLYV 178
Cdd:cd00060     17 TKGVVTIGRSPDCDIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNGTFVNGKRITPPvPLQDGDVIRLGDTTFRFE 92
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
104-178 1.97e-19

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 84.24  E-value: 1.97e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1802450525  104 DKKSFLLGRDDACDICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNKRVKEK-KLQDGDSIQIPGIQMLYV 178
Cdd:COG1716     19 DGGPLTIGRAPDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTFVNGQRVTEPaPLRDGDVIRLGKTELRFR 94
FtsK COG1674
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
 631-815 2.42e-17

DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441280 [Multi-domain]  Cd Length: 611  Bit Score: 87.67  E-value: 2.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  631 QSEDSLRVPIGIDEFNEYIWLDAhenAHGPHGLFAGTTGSGKSECILTYILSLSIQFSYEDVCFVIIDYKggmMA--NAL 708
Cdd:COG1674    256 NSKSPLPIALGKDISGEPVVADL---AKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPK---MVelSVY 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  709 QGLPH-VSCIMTNLcederRRMHLSLQS---EVNRRQQIFANdsLGSMDIYKYQKLVHEQKRK-------EPIPHMFIVI 777
Cdd:COG1674    330 NGIPHlLTPVVTDP-----KKAANALKWavrEMERRYKLFAK--AGVRNIAGYNEKVREAKAKgeeeeglEPLPYIVVII 402

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1802450525  778 DEFAQLKQQYPDFLDFLkqIARI---GRSLGIHLLLATQKP 815
Cdd:COG1674    403 DELADLMMVAGKEVEEA--IARLaqkARAAGIHLILATQRP 441
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 108-170 3.75e-15

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 71.07  E-value: 3.75e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1802450525  108 FLLGRDDACDICINHPFVSKIHIRFEKQEQ-DLYLFDEESKNGVYVNNKRVKEKK--LQDGDSIQI 170
Cdd:pfam00498    1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGgRFYLEDLGSTNGTFVNGQRLGPEPvrLKDGDVIRL 66
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 623-858 5.23e-15

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 80.90  E-value: 5.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  623 ILERWKESQSEDSLRVPIGIDEFNEYIWLDAhenAHGPHGLFAGTTGSGKSECILTYILSLSIQFSYEDVCFVIIDYKgg 702
Cdd:PRK10263   977 VLDNAKFRDNPSPLTVVLGKDIAGEPVVADL---AKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPK-- 1051

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  703 MMA-NALQGLPHVSCIMTNLCEDERRRMHLSLqSEVNRRQQIFAndSLGSMDIYKYQKLVHEQKRK-------------- 767
Cdd:PRK10263  1052 MLElSVYEGIPHLLTEVVTDMKDAANALRWCV-NEMERRYKLMS--ALGVRNLAGYNEKIAEADRMmrpipdpywkpgds 1128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  768 --------EPIPHMFIVIDEFAQLKQQYPDFL-DFLKQIARIGRSLGIHLLLATQKP-FGVVDEEIWSNSHFHLCLKVQD 837
Cdd:PRK10263  1129 mdaqhpvlKKEPYIVVLVDEFADLMMTVGKKVeELIARLAQKARAAGIHLVLATQRPsVDVITGLIKANIPTRIAFTVSS 1208

                          250       260
                   ....*....|....*....|.
gi 1802450525  838 RQDSMDMLKNDDAVYLKNPGE 858
Cdd:PRK10263  1209 KIDSRTILDQAGAESLLGMGD 1229
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
 661-833 2.54e-07

TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.


Pssm-ID: 410871 [Multi-domain]  Cd Length: 144  Bit Score: 51.45  E-value: 2.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  661 HGLFAGTTGSGKSECI-LTYILSLSIQFSyedvcFVIIDYKGGMmanalqglphvsCIMTnlceDERRRMHLSLqsevnr 739
Cdd:cd01127      1 NTLVLGTTGSGKTTSIvIPLLDQAARGGS-----VIITDPKGEL------------FLVI----PDRDDSFAAL------ 53

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  740 RQQIFAndslgsmDIYKY-QKLVHEQKRKEPIPHMFIvIDEFAQLKqqypdFLDFLKQIARIGRSLGIHLLLATQ----- 813
Cdd:cd01127     54 RALFFN-------QLFRAlTELASLSPGRLPRRVWFI-LDEFANLG-----RIPNLPNLLATGRKRGISVVLILQslaql 120

                          170       180
                   ....*....|....*....|..
gi 1802450525  814 -KPFG-VVDEEIWSNSHFHLCL 833
Cdd:cd01127    121 eAVYGkDGAQTILGNCNTKLYL 142
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 108-157 4.01e-07

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 47.94  E-value: 4.01e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1802450525   108 FLLGRD-DACDICINHPFVSKIHIRFEKQEQ-DLYLFDEESKNGVYVNNKRV 157
Cdd:smart00240    1 VTIGRSsEDCDIQLDGPSISRRHAVIVYDGGgRFYLIDLGSTNGTFVNGKRI 52
 
Name Accession Description Interval E-value
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 269-1259 2.53e-149

type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274860 [Multi-domain]  Cd Length: 1296  Bit Score: 486.80  E-value: 2.53e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  269 AISQKSSLQqIIPSVTMAVSMMLTTmfwplISKYY-EKIRFKKQYNSLLNDYRRYLKVKNNEVYKYIQEKQCYERNKIED 347
Cdd:TIGR03928   55 SIFQPRGIF-IIASIAMSLVTIIFS-----TTTYFrEKKKYKKDVEKRNRSYRLYLDKKRKELQALSEKQRHVLHYHNPS 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  348 FITVKKYIETRSPCLWNRKKENDDFLYLHCGWKLKKIKAPISDKQEVFDLQKNEVKEE--YLKFVNSSYEiKYPFLVDLK 425
Cdd:TIGR03928  129 VEELKEMVENVNSRIWEKTPEHHDFLHVRLGTGNVPSSFEIKFPEEEFSQRKDELLDEaqELKEKYNTIE-NVPIVLDLS 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  426 KYTIGVYGEKALYYG--NMFILYIAALHSKKDVTIL-LVGEQEYLWKSKAKWI--SQVEENNIRHVYSDEKDIQKLLVYL 500
Cdd:TIGR03928  208 NGPIGYVGKRSLVLEelQNLVGQLAFFHSYHDVQFVtIFPEEEKKKWEWMRWLphFWLRDINVRGFVYNERTRDQLLNSL 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  501 -------KQKRSEN------RF---YIIVLLNisKKLtqqILNSV---YLMKNVKYIQC----CKE-KEMLSDSVDFIFS 556
Cdd:TIGR03928  288 yqilkerKLALDDAnskekkRFsphYVFLITD--RKL---ILDHVimeYLNEDPSELGIslifVQDvMESLPENVKTVID 362

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  557 TEDKN--VFYKENKKQENILFEVE--KKESTENLFRKLMLLQEFEEDKKDIYESFGVLSLYSCTCLNQLNILERWKESQS 632
Cdd:TIGR03928  363 IKNRNegEIVLEEGELVEKSFTPDhlDNEDLEEYSRTLAPLNHLQNLKNSIPESVTFLEMYGVKKVEELNIQERWAKNET 442

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  633 EDSLRVPIGIDEFNEYIWLDAHENAHGPHGLFAGTTGSGKSECILTYILSLSIQFSYEDVCFVIIDYKGGMMANALQGLP 712
Cdd:TIGR03928  443 YKSLAVPIGLRGKDDIVYLNLHEKAHGPHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKGGGMANLFKNLP 522

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  713 HVSCIMTNLCEDERRRMHLSLQSEVNRRQQIFANDSLGSMDiyKYQKLVHEQKRKEPIPHMFIVIDEFAQLKQQYPDFLD 792
Cdd:TIGR03928  523 HLLGTITNLDGAQSMRALASIKAELKKRQRLFGENNVNHIN--QYQKLYKQGKAKEPMPHLFLISDEFAELKSEQPEFMK 600

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  793 FLKQIARIGRSLGIHLLLATQKPFGVVDEEIWSNSHFHLCLKVQDRQDSMDMLKNDDAVYLKNPGEFYLQVGNNEVYVKG 872
Cdd:TIGR03928  601 ELVSTARIGRSLGVHLILATQKPSGVVDDQIWSNSRFKLALKVQDASDSNEILKTPDAAEITVPGRAYLQVGNNEVYELF 680

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  873 KSAWTQQPYIDEKTKNDKEDkVLRI--------FNQQKELLKEVKPkTYREHTELQMIVFYLKKIAKGKCAKQLFFPNLK 944
Cdd:TIGR03928  681 QSAWSGAPYDPDKDKKEEED-IYMIndlgqyelLNEDLSGLKRKKE-IKEVPTELEAVIDEIQAYTEELNIEALPSPWLP 758

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  945 PDLERI------KSSLQNCWN---------MGMVDDISKQSQYPWILDISQFHHLLLIDSKE--KASFLNVFLQENENLY 1007
Cdd:TIGR03928  759 PLEEKIylddlhAVEFDKLWSkpkeplqatIGLLDDPELQSQEPLTLDLSKDGHLAIFGSPGygKSTFLQTLIMSLARQH 838

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525 1008 QDNPVYVYILAVHPGSKESLLQYPSVQEAISVEESEKIKHFLSYLKNRIRKRKK----------------NEEEKNDIVI 1071
Cdd:TIGR03928  839 SPEQLHFYLFDFGTNGLLPLKKLPHVADYFTLDEEEKIEKLIRRIKKEIDRRKKlfseygvasismynkaSGEKLPQIVI 918

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525 1072 VLQEFEYFKE--TFPELMEDILFLLREGEKTNIHFFVFGSDLQMIPYLLFPYFDLRIIGELREESSYITLLGNENLE--- 1146
Cdd:TIGR03928  919 IIDNYDAVKEepFYEDFEELLIQLAREGASLGIYLVMTAGRQNAVRMPLMNNIKTKIALYLIDKSEYRSIVGRTKFTiee 998

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525 1147 ---RPLHQKGSY--------VCDDGRQVKIVQLHKEIRV--SYKKHKKPWALPSISKVIPF----------PKTRKGYLF 1203
Cdd:TIGR03928  999 ipgRGLIKKDEPtlfqtalpVKGEDDLEVIENIKAEIQKmnEAWTGERPKPIPMVPEELSLeefreryevrKILEEGSIP 1078

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525 1204 IGIDKQSMEEYQVSF--------------EKEKFIVFLTNTTFLNGFVK-----GIKRQL-----QDHCAAYIENKKETK 1259
Cdd:TIGR03928 1079 IGLDEETVEPVYIDLtenphllivgesddGKTNVLKSLLKTLAKQEKEKiglidSIDRGLlayrdLKEVATYIEEKEDLK 1158
T7SS_EccC_a TIGR03924
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ...
 620-881 5.12e-58

type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274858 [Multi-domain]  Cd Length: 658  Bit Score: 213.30  E-value: 5.12e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  620 QLNILERWKESQSEDSLRVPIGIDEFNEYIWLDAHENAH---GPHGLFAGTTGSGKSECILTYILSLSIQFSYEDVCFVI 696
Cdd:TIGR03924  393 TLDVDRLWRPRPGRDRLRVPIGVGDDGEPVELDLKESAEggmGPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVL 472

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  697 IDYKGGMMANALQGLPHVSCIMTNLcEDER---RRMHLSLQSEVNRRQQIFanDSLGSM-DIYKYQKLVHEQKRKEPIPH 772
Cdd:TIGR03924  473 VDFKGGATFLGLEGLPHVSAVITNL-ADEAplvDRMQDALAGEMNRRQELL--RAAGNFaNVAEYEKARAAGADLPPLPA 549

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  773 MFIVIDEFAQLKQQYPDFLDFLKQIARIGRSLGIHLLLATQKpfgvVDE----EIWSNSHFHLCLKVQDRQDSMDMLKND 848
Cdd:TIGR03924  550 LFVVVDEFSELLSQHPDFADLFVAIGRLGRSLGVHLLLASQR----LDEgrlrGLESHLSYRIGLKTFSASESRAVLGVP 625

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1802450525  849 DAVYLKN-PGEFYLQVGnNEVYVKGKSAWTQQPY 881
Cdd:TIGR03924  626 DAYHLPStPGAGYLKVD-TAEPVRFRAAYVSGPY 658
FtsK_SpoIIIE pfam01580
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ...
 621-815 5.96e-24

FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.


Pssm-ID: 279863 [Multi-domain]  Cd Length: 219  Bit Score: 101.69  E-value: 5.96e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  621 LNILERWKESQSEDSLRVPIGIDEFNEYIWLDAHENAhgPHGLFAGTTGSGKSECILTYILSLSIQFSYEDVCFVIIDYK 700
Cdd:pfam01580    2 LEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMP--VHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  701 GGMMaNALQGLPHVscIMTNLCED-ER-RRMHLSLQSEVNRRQQIFANDSLGSM----------------DIYKYQKLVH 762
Cdd:pfam01580   80 MGEL-SAYEDIPHL--LSVPVATDpKRaLRALEWLVDEMERRYALFRALGVRSIagyngeiaedpldgfgDVFLVIYGVH 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1802450525  763 ----EQKRKEPIPHMFIVIDEFAQLKQQYPDF-----LDFLKQIARIGRSLGIHLLLATQKP 815
Cdd:pfam01580  157 vmctAGRWLEILPYLVVIVDERAELRLAAPKDsemrvEDAIVRLAQKGRAAGIHLLLATQRP 218
T7SS_EccC_b TIGR03925
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
 636-813 1.30e-20

type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274859 [Multi-domain]  Cd Length: 566  Bit Score: 97.76  E-value: 1.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  636 LRVPIGI-----DEFNEYIWLDAHenAHGPHGLFAGTTGSGKSECILTYILSLSIQFSYEDVCFVIIDYKGGMMAnALQG 710
Cdd:TIGR03925   53 LTVPVGIvdrpfEQRQDPLVVDLS--GAAGHVAIVGAPQSGKSTALRTLILALALTHTPEEVQFYCLDFGGGGLA-SLAD 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  711 LPHVSCIMTNLCEDERRRMHLSLQSEVNRRQQIFANDSLGSMDIYKYQKLVHEQkRKEPIPHMFIVIDEFAQLKQQYPDF 790
Cdd:TIGR03925  130 LPHVGGVAGRLDPERVRRTVAEVEGLLRRRERLFRTHGIDSMAQYRARRAAGRL-PEDPFGDVFLVIDGWGTLRQDFEDL 208

                          170       180
                   ....*....|....*....|...
gi 1802450525  791 LDFLKQIARIGRSLGIHLLLATQ 813
Cdd:TIGR03925  209 EDKVTDLAARGLAYGVHVVLTAS 231
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 104-178 1.56e-20

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: 87.33  E-value: 1.56e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1802450525  104 DKKSFLLGRDDACDICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNKRVKEK-KLQDGDSIQIPGIQMLYV 178
Cdd:cd00060     17 TKGVVTIGRSPDCDIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNGTFVNGKRITPPvPLQDGDVIRLGDTTFRFE 92
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
104-178 1.97e-19

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 84.24  E-value: 1.97e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1802450525  104 DKKSFLLGRDDACDICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNKRVKEK-KLQDGDSIQIPGIQMLYV 178
Cdd:COG1716     19 DGGPLTIGRAPDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTFVNGQRVTEPaPLRDGDVIRLGKTELRFR 94
FtsK COG1674
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ...
 631-815 2.42e-17

DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441280 [Multi-domain]  Cd Length: 611  Bit Score: 87.67  E-value: 2.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  631 QSEDSLRVPIGIDEFNEYIWLDAhenAHGPHGLFAGTTGSGKSECILTYILSLSIQFSYEDVCFVIIDYKggmMA--NAL 708
Cdd:COG1674    256 NSKSPLPIALGKDISGEPVVADL---AKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPK---MVelSVY 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  709 QGLPH-VSCIMTNLcederRRMHLSLQS---EVNRRQQIFANdsLGSMDIYKYQKLVHEQKRK-------EPIPHMFIVI 777
Cdd:COG1674    330 NGIPHlLTPVVTDP-----KKAANALKWavrEMERRYKLFAK--AGVRNIAGYNEKVREAKAKgeeeeglEPLPYIVVII 402

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1802450525  778 DEFAQLKQQYPDFLDFLkqIARI---GRSLGIHLLLATQKP 815
Cdd:COG1674    403 DELADLMMVAGKEVEEA--IARLaqkARAAGIHLILATQRP 441
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 108-170 3.75e-15

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 71.07  E-value: 3.75e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1802450525  108 FLLGRDDACDICINHPFVSKIHIRFEKQEQ-DLYLFDEESKNGVYVNNKRVKEKK--LQDGDSIQI 170
Cdd:pfam00498    1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGgRFYLEDLGSTNGTFVNGQRLGPEPvrLKDGDVIRL 66
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 623-858 5.23e-15

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 80.90  E-value: 5.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  623 ILERWKESQSEDSLRVPIGIDEFNEYIWLDAhenAHGPHGLFAGTTGSGKSECILTYILSLSIQFSYEDVCFVIIDYKgg 702
Cdd:PRK10263   977 VLDNAKFRDNPSPLTVVLGKDIAGEPVVADL---AKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPK-- 1051

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  703 MMA-NALQGLPHVSCIMTNLCEDERRRMHLSLqSEVNRRQQIFAndSLGSMDIYKYQKLVHEQKRK-------------- 767
Cdd:PRK10263  1052 MLElSVYEGIPHLLTEVVTDMKDAANALRWCV-NEMERRYKLMS--ALGVRNLAGYNEKIAEADRMmrpipdpywkpgds 1128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  768 --------EPIPHMFIVIDEFAQLKQQYPDFL-DFLKQIARIGRSLGIHLLLATQKP-FGVVDEEIWSNSHFHLCLKVQD 837
Cdd:PRK10263  1129 mdaqhpvlKKEPYIVVLVDEFADLMMTVGKKVeELIARLAQKARAAGIHLVLATQRPsVDVITGLIKANIPTRIAFTVSS 1208

                          250       260
                   ....*....|....*....|.
gi 1802450525  838 RQDSMDMLKNDDAVYLKNPGE 858
Cdd:PRK10263  1209 KIDSRTILDQAGAESLLGMGD 1229
FHA_Rv1747-like_rpt1 cd22694
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
 103-170 1.09e-13

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: 68.12  E-value: 1.09e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802450525  103 PDKKSFLLGRDDACDICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNKRVKEKKLQDGDSIQI 170
Cdd:cd22694     13 DPGSSVRIGRDPDADVRLDDPRVSRRHALLEFDGDGWVYTDLGSRNGTYLNGRRVQQVKLSDGTRVRL 80
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
 110-179 1.59e-11

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: 62.25  E-value: 1.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  110 LGRDDACDICINHPFVSKIHIRFEKqeqdlYLFDEE----------SKNGVYVNNKRVKEKK---LQDGDSIQIP-GIQM 175
Cdd:cd22670     26 IGRSPSCDIVINDPFVSRTHCRIYS-----VQFDESsaplvyvedlSSNGTYLNGKLIGRNNtvlLSDGDVIEIAhSATF 100


                   ....
gi 1802450525  176 LYVH 179
Cdd:cd22670    101 VYVH 104
FHA_ArnA-like cd22680
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ...
 87-170 1.67e-11

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: 61.97  E-value: 1.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525   87 LYMEELEKSTFISQKIP-DKKSFLLGRDDACDICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNN-KRVKEK-KLQ 163
Cdd:cd22680      1 LVLEILSSPNLTGKKFPfDFSSVSIGRDPENVIVIPDPFVSRNHARITVDSNEIYIEDLGSTNGTFVNDfKRIKGPaKLH 80


                   ....*..
gi 1802450525  164 DGDSIQI 170
Cdd:cd22680     81 PNDIIKL 87
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
 104-170 2.18e-11

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: 61.46  E-value: 2.18e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  104 DKKSFLLGRDDACDICINHPFVSKIH--IRFEKQEQdLYLFDEESKNGVYVNNKRVKEK-KLQDGDSIQI 170
Cdd:cd22673     19 TKKSCTFGRDLSCDIRIQLPGVSREHcrIEVDENGK-AYLENLSTTNPTLVNGKAIEKSaELKDGDVITI 87
FHA_EspA-like cd22698
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ...
 104-170 5.05e-11

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: 60.50  E-value: 5.05e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1802450525  104 DKKSFLLGRDDACDICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNKRVKEKKLQDGDSIQI 170
Cdd:cd22698     19 DQDEFTIGRSSNNDIRLNDHSVSRHHARIVRQGDKCNLTDLGSTNGTFLNGIRVGTHELKHGDRIQL 85
FHA_FhaB-like cd22693
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
 104-170 4.04e-10

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: 57.70  E-value: 4.04e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802450525  104 DKKSFLLGRDDACDICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNKRVKEKK-LQDGDSIQI 170
Cdd:cd22693     16 DKSGITIGRADDNDLVLSDDFVSSRHARIYLQGSSWYLEDLGSTNGTFVNGNRVTQPVvVQPGDTIRI 83
FHA_GarA_OdhI-like cd22684
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ...
 111-178 1.02e-09

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: 56.62  E-value: 1.02e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802450525  111 GRDDACDICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNKRVKEKKLQDGDSIQIPGIQMLYV 178
Cdd:cd22684     26 GRHPESDIFLDDVTVSRRHAEFRRAEGGFVVRDVGSLNGTYVNRERIDSAVLRNGDEVQIGKFRLVFF 93
FHA_MDC1 cd22665
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ...
 109-170 8.93e-09

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: 54.16  E-value: 8.93e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1802450525  109 LLGRDDACDICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNK-RVKEK---KLQDGDSIQI 170
Cdd:cd22665     24 VIGRDPSCSVVLPDKSVSKQHACIEVDGGTHLIEDLGSTNGTRIGNKvRLKPNvryELIDGDLLLF 89
FHA_SNIP1_DDL-like cd22676
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ...
 102-170 8.95e-09

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: 54.61  E-value: 8.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  102 IPDKKSFLLGRD-DACDICINHPFVSKIH--IRFEKQEQDL----------YLFDEESKNGVYVNNKRVKEKK---LQDG 165
Cdd:cd22676     17 IHRQSAYLIGRDrRVADIPLDHPSCSKQHavIQFREVEKRNegdvienirpYIIDLGSTNGTFLNGEKIEPRRyyeLREK 96


                   ....*
gi 1802450525  166 DSIQI 170
Cdd:cd22676     97 DVLKF 101
FHA_DUN1-like cd22683
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ...
 102-178 1.73e-08

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: 53.26  E-value: 1.73e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802450525  102 IPDKKSFLLGRDDACDICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNKRVKEK--KLQDGDSIQIPGIQMLYV 178
Cdd:cd22683     17 ITNRNVTTIGRSRSCDLVLSDPSISRFHAELRLEQNGINVIDNNSANGTFINGKRIKGKtyILKNGDIIVFGKCSFLIK 95
FHA_Kanadaptin cd22677
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ...
 88-178 2.28e-08

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: 53.33  E-value: 2.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525   88 YMEELEKSTFISQKIP-DKKSF-LLGRDDACDICINHPFVSKIH------IRFEKQEQDLYLFDEESKNGVYVNNKRVKE 159
Cdd:cd22677      2 YSLEVLKNGVIVETLDlNGKSFyVFGRLPGCDVVLEHPSISRYHavlqyrGDADDHDGGFYLYDLGSTHGTFLNKQRIPP 81

                           90       100
                   ....*....|....*....|..
gi 1802450525  160 K---KLQDGDSIQIPGIQMLYV 178
Cdd:cd22677     82 KqyyRLRVGHVLKFGGSTRLYI 103
HerA COG0433
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ...
 735-861 4.59e-08

Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];


Pssm-ID: 440202 [Multi-domain]  Cd Length: 388  Bit Score: 56.92  E-value: 4.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  735 SEVNRR-QQIFANDSLgsMDIYKYQKLVHEQKRKEPiPHmFIVIDEfAQL--KQQYPDFLDFLKQIARIGRSLGIHLLLA 811
Cdd:COG0433    225 SGLPEElQSTFVLWLL--RELFEARPEVGDADDRKL-PL-VLVIDE-AHLlaPAAPSALLEILERIAREGRKFGVGLILA 299

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1802450525  812 TQKPfGVVDEEIWSNSHFHLCLKVQDRQD------SMDMLKNDDAVYLKN--PGEFYL 861
Cdd:COG0433    300 TQRP-SDIDEDVLSQLGTQIILRLFNPRDqkavkaAAETLSEDLLERLPSlgTGEALV 356
FHA_PPP1R8 cd22674
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ...
 102-169 1.02e-07

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: 51.50  E-value: 1.02e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1802450525  102 IPDKKSFLLGRD-DACDICINHPFVSKIH--IRFEKQEQDLYLFDEESKNGVYVNNKRVKEKK---LQDGDSIQ 169
Cdd:cd22674     23 IDEKKYYLFGRNsDVCDFVLDHPSCSRVHaaLVYHKHLNRVFLIDLGSTHGTFVGGIRLEPHKpqqLPIDSTLR 96
FHA_PS1-like cd22691
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ...
 99-177 1.56e-07

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: 51.27  E-value: 1.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525   99 SQKIPDKKSFLLGRDDACDICINHPFVSKIH--IRFEKQEQDLYLFDEESKNGVYVNNKRV---KEKKLQDGDSIQIPGI 173
Cdd:cd22691     22 FSKSEEEDILVVGRHPDCDIVLDHPSISRFHleIRIIPSRRKITLTDLSSVHGTWVNGQRIepgVPVELEEGDTVRLGAS 101


                   ....
gi 1802450525  174 QMLY 177
Cdd:cd22691    102 TRVY 105
TrwB_TraG_TraD_VirD4 cd01127
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ...
 661-833 2.54e-07

TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.


Pssm-ID: 410871 [Multi-domain]  Cd Length: 144  Bit Score: 51.45  E-value: 2.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  661 HGLFAGTTGSGKSECI-LTYILSLSIQFSyedvcFVIIDYKGGMmanalqglphvsCIMTnlceDERRRMHLSLqsevnr 739
Cdd:cd01127      1 NTLVLGTTGSGKTTSIvIPLLDQAARGGS-----VIITDPKGEL------------FLVI----PDRDDSFAAL------ 53

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  740 RQQIFAndslgsmDIYKY-QKLVHEQKRKEPIPHMFIvIDEFAQLKqqypdFLDFLKQIARIGRSLGIHLLLATQ----- 813
Cdd:cd01127     54 RALFFN-------QLFRAlTELASLSPGRLPRRVWFI-LDEFANLG-----RIPNLPNLLATGRKRGISVVLILQslaql 120

                          170       180
                   ....*....|....*....|..
gi 1802450525  814 -KPFG-VVDEEIWSNSHFHLCL 833
Cdd:cd01127    121 eAVYGkDGAQTILGNCNTKLYL 142
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 108-157 4.01e-07

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 47.94  E-value: 4.01e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1802450525   108 FLLGRD-DACDICINHPFVSKIHIRFEKQEQ-DLYLFDEESKNGVYVNNKRV 157
Cdd:smart00240    1 VTIGRSsEDCDIQLDGPSISRRHAVIVYDGGgRFYLIDLGSTNGTFVNGKRI 52
FHA_Slr1951-like cd22697
forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar ...
 92-178 5.69e-07

forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Synechocystis sp. protein Slr1951 and protein Sll1895. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438749 [Multi-domain]  Cd Length: 102  Bit Score: 49.00  E-value: 5.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525   92 LEKSTFISQKIPDKKSFLLGRDDACDICINHPFVSKIHIRFEKQ-----EQDLYLFDE-----ESKNGVYVNNKRVKEKK 161
Cdd:cd22697      4 ELDGNVRREIRLDEPIYTIGRHPGNDIQIPSQQISRRHATLRRKinpnlDISFWIIDGdlegaESLNGLWVNGERILQHE 83

                           90
                   ....*....|....*...
gi 1802450525  162 LQDGDSIQI-PGIQMLYV 178
Cdd:cd22697     84 LVNGDEIALgPKIVLRYQ 101
FHA_RNF8 cd22663
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ...
 103-170 7.61e-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: 48.89  E-value: 7.61e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1802450525  103 PDKKSFLLGR--DDACDI-CINHPFVSKIHIRFEKQEQDLYLF-DEESKNGVYVNNKRVKEKK---LQDGDSIQI 170
Cdd:cd22663     18 EDGKEVTVGRglGVTYQLvSTCPLMISRNHCVLKKNDEGQWTIkDNKSLNGVWVNGERIEPLKpypLNEGDLIQL 92
FHA_Rv1747-like_rpt2 cd22737
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
 110-170 2.31e-06

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: 47.10  E-value: 2.31e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1802450525  110 LGRDDACDICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNKRVKEKKLQDGDSIQI 170
Cdd:cd22737     25 IGRASDNDIVIPEGSVSRHHATLVPTPGGTQIRDLRSTNGTFVNGLRVDAALLHDGDVVTI 85
FHA_RAD53-like_rpt1 cd22689
first forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
 105-170 4.25e-06

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


Pssm-ID: 438741 [Multi-domain]  Cd Length: 132  Bit Score: 47.66  E-value: 4.25e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1802450525  105 KKSFLLGRDDACDICINHPFVSKIHIRF---EKQEQDLYLFDEE-SKNGVYVNNKRVKEKK---LQDGDSIQI 170
Cdd:cd22689     44 KKVWTFGRHPACDYHLGNSRLSNKHFQIllgESDPSDGNVLLNDiSSNGTWLNGQRLEKNSnqlLSQGDEITI 116
FHA_AGGF1 cd22686
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ...
 110-179 4.82e-06

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: 47.28  E-value: 4.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  110 LGRDDAC--DICINHPFVSKIH--IRFEKQEQDLYLFDEESKNGVYVNNKRVKEKK-------LQDGDSIQIPGIQML-Y 177
Cdd:cd22686     30 IGREKDHghTIRIPELGVSKFHaeIYYDDDEQSYTIVDLGSQNGTYLNGVRISQPKeksdpypLTHGDELKIGETTLLfH 109


                   ..
gi 1802450525  178 VH 179
Cdd:cd22686    110 IH 111
FHA_Par42-like cd22675
forkhead associated (FHA) domain found in Trypanosoma brucei Parvulin 42 (TbPar42) and similar ...
 108-161 9.05e-06

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: 46.01  E-value: 9.05e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1802450525  108 FLLGRDDACDICINHPFVSKIH--IRFEKQEQDLYLFDEESKNGVYVNNKRVKEKK 161
Cdd:cd22675     31 YLFGRSPVCDYVLEHPSISSVHavLVFHGEQKCFVLMDLGSTNGVKLNGKRIEKGR 86
FHA_SNIP1 cd22718
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1) and ...
 107-161 1.31e-05

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: 46.62  E-value: 1.31e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802450525  107 SFLLGRD-DACDICINHPFVSKIH-------IRFEKQEQDL------YLFDEESKNGVYVNNKRVKEKK 161
Cdd:cd22718     57 AYLLGRDrKIADIPIDHPSCSKQHavlqyrlVEYTRPDGTKgrrvrpYIIDLESANGTFLNNKKIEPQR 125
FHA_CHFR cd22672
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ...
 99-170 1.47e-05

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: 45.36  E-value: 1.47e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1802450525   99 SQKIP-DKKSFLLGRDDACDICI-NHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNKRV-KEKK--LQDGDSIQI 170
Cdd:cd22672     13 SPPILlRKDEFTIGRAKDCDLSFpGNKLVSGDHCKIIRDEKGQVWLEDTSTNGTLVNKVKVvKGQKveLKHGDVIYL 89
FHA_Cep170 cd22704
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ...
 108-168 3.09e-05

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: 44.23  E-value: 3.09e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1802450525  108 FLLGRDDaCDICINHPFVSKIH--IRFEKQEQDLYLFDEESKNGVYVNNKRVKEK---KLQDGDSI 168
Cdd:cd22704     19 LFVGRED-CDLILQSRSVDKQHavITYDQIDNEFKIKDLGSLNGTFVNDSRIPEQtyiTLKLGDSI 83
FHA_OdhI-like cd22721
forkhead associated (FHA) domain found in Corynebacterium glutamicum oxoglutarate ...
 104-178 5.66e-05

forkhead associated (FHA) domain found in Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI) and similar proteins; OdhI is an essential component of the PknG signaling pathway. It regulates glutamate production under biotin non-limiting conditions. 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: 438773 [Multi-domain]  Cd Length: 102  Bit Score: 43.54  E-value: 5.66e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1802450525  104 DKKSFLLGRDDACDICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNKRVKEKKLQDGDSIQIPGIQMLYV 178
Cdd:cd22721     27 DQPTTTAGRHPESDIFLDDVTVSRRHAEFRINEGEFEVVDVGSLNGTYVNREPRNAQVMQTGDEIQIGKFRLVFL 101
FHA_DgcB-like cd22682
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ...
 83-170 5.79e-05

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


Pssm-ID: 438734 [Multi-domain]  Cd Length: 96  Bit Score: 43.29  E-value: 5.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525   83 SLVLLYMEELEKSTF-ISQKipdkkSFLLGRDDACDICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNKRV---K 158
Cdd:cd22682      1 ALLMIIGPPGVGKQFpITES-----TIVIGRSVESQVQIDDDSVSRYHAKLAVNPSAVSIIDLGSTNGTIVNGKKIpklA 75

                           90
                   ....*....|..
gi 1802450525  159 EKKLQDGDSIQI 170
Cdd:cd22682     76 SCDLQNGDQIKI 87
VirB4 COG3451
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ...
 774-866 6.50e-05

Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442674 [Multi-domain]  Cd Length: 546  Bit Score: 47.25  E-value: 6.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  774 FIVIDEFAQLkQQYPDFLDFLKQIARIGRSLGIHLLLATQKPFGVVDEE----IWSNSHFHLCLK--VQDRQDSMDMLKN 847
Cdd:COG3451    409 LIVIDEAWLL-LDNPAFAEFLEEWLKTLRKYNGAVIFATQSVEDFLSSPiaeaIIENSATKILLPqpKADIEDYAELLGL 487

                           90       100
                   ....*....|....*....|....*
gi 1802450525  848 DDAV--YLKNP----GEFYLQVGNN 866
Cdd:COG3451    488 SEREleLIRSAgrgkRDFLIKQGNG 512
T7_EssCb_Firm TIGR03928
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ...
 618-837 7.53e-05

type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274860 [Multi-domain]  Cd Length: 1296  Bit Score: 47.29  E-value: 7.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  618 LNQLNILERWKESQSEDSLRVPIGIDEfnEYIWLDAHENAHGPHGLFAGTTGSGKSECILTYILSLSIQFSYEdvcFVII 697
Cdd:TIGR03928 1057 LSLEEFRERYEVRKILEEGSIPIGLDE--ETVEPVYIDLTENPHLLIVGESDDGKTNVLKSLLKTLAKQEKEK---IGLI 1131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  698 DYKGGMMAnALQGLPHVSCIMTNlcEDERRRMHLSLQSEVNRRQQIFANDSLGSMDIYKYQKlvheqkrkepiphMFIVI 777
Cdd:TIGR03928 1132 DSIDRGLL-AYRDLKEVATYIEE--KEDLKEILAELKEEIELREAAYKEALQNETGEPAFKP-------------ILLII 1195

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1802450525  778 DEFAQLKQQYPDFL-DFLKQIARIGRSLGIHLLLATQ-----KPFGVVDEEIWSNSHFHLCLKVQD 837
Cdd:TIGR03928 1196 DDLEDFIQRTDLEIqDILALIMKNGKKLGIHFIVAGThselsKSYDGVPKEIKQLRTGILGMRKSD 1261
FHA_PML1-like cd22681
forkhead associated (FHA) domain found in Saccharomyces cerevisiae pre-mRNA leakage protein 1 ...
 104-169 9.22e-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: 43.58  E-value: 9.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  104 DKKSFLLGRDDA-------CDICINHPFVSKIH--IRFEKQEQDL--YLFDEESKNGVYVNNKRVKEKK---LQDGDSIQ 169
Cdd:cd22681     38 SPSCYLIGREKGesteivvADIGIPEETCSKQHcvIQFRNVKGILkpYIMDLDSSNGTCLNDNVIPSSRyveLRSGDVIT 117
T7SS_EccC_b TIGR03925
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ...
 631-704 1.16e-04

type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274859 [Multi-domain]  Cd Length: 566  Bit Score: 46.52  E-value: 1.16e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1802450525  631 QSEDSLRVPIGIDEFN-EYIWLDAHENahgPHGLFAGTTGSGKSECILTYILSLSIQFSYEDVCFVIIDYKGGMM 704
Cdd:TIGR03925  337 GGAPRLRVPLGLGESDlAPVYVDFAES---PHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYRRTLL 408
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
 102-168 1.49e-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: 43.17  E-value: 1.49e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802450525  102 IPDKKSFLLGRD-DACDICIN---HP-FVSKIH--IRFEKQEQDL--YLFDEESKNGVYVNNKRVKEKK---LQDGDSI 168
Cdd:cd22685     24 RPDLCEYRIGRNpEVCDVFLCssqHPnLISREHaeIHAERDGNGNwkVLIEDRSTNGTYVNDVRLQDGQrreLSDGDTI 102
FHA_GarA-like cd22720
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation ...
 99-178 1.67e-04

forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation regulator GarA and similar proteins; GarA is an FHA domain-containing protein involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent ON/OFF molecular switch that modulates the activities of KGD, GDH and GltB. Its FHA domain has dual specificity. It binds to both phosphorylated upstream partners, such as the kinases PknB and PknG, and nonphosphorylated downstream partners, such as the 2-oxoglutarate decarboxylase KGD. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438772 [Multi-domain]  Cd Length: 100  Bit Score: 42.30  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525   99 SQKIPDKKSFLLGRDDACDICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNKRVKEKKLQDGDSIQIPGIQMLYV 178
Cdd:cd22720     17 SRFLLDQAITSAGRHPDSDIFLDDVTVSRRHAEFRLENNEFNVVDVGSLNGTYVNREPVDSAVLANGDEVQIGKFRLVFL 96
VirD4 COG3505
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ...
 763-840 1.69e-04

Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442728 [Multi-domain]  Cd Length: 402  Bit Score: 45.75  E-value: 1.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  763 EQKRKEPIPHMFIvIDEFAQLKQqypdfLDFLKQIARIGRSLGIHLLLATQ------KPFGV-VDEEIWSNSHFHLCLKV 835
Cdd:COG3505    240 ERSGRLPRPVLLL-LDEFANLGR-----LPSLETLLATGRGYGIRLVLILQslaqleAIYGEeGAETILGNCGTKIFLGV 313


                   ....*
gi 1802450525  836 QDRQD 840
Cdd:COG3505    314 NDPET 318
FHA_RAD53-like_rpt2 cd22690
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
 107-168 2.36e-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: 41.89  E-value: 2.36e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  107 SFLLGRDDACDICINHPFVSKIH--IRFEKQEQDL---YLFDEeSKNGVYVNNKRVKEKK---LQDGDSI 168
Cdd:cd22690     20 TTFIGRSKDCDEEITDPRISKHHciITRKRSGKGLddvYVTDT-STNGTFINNNRLGKGSqslLQDGDEI 88
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
 105-169 3.75e-04

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


Pssm-ID: 438719 [Multi-domain]  Cd Length: 108  Bit Score: 41.16  E-value: 3.75e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802450525  105 KKSFLLGRDDACDICINHPFVSKIHIRFE-----------KQEQDLYLFDeESKNGVYVNNKRVK---EKKLQDGDSIQ 169
Cdd:cd22667     19 GGEYTVGRKDCDIIIVDDSSISRKHATLTvlhpeanlsdpDTRPELTLKD-LSKYGTFVNGEKLKggsEVTLKDGDVIT 96
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
 108-170 5.16e-04

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: 40.32  E-value: 5.16e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1802450525  108 FLLGRDDACDICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNKRVKEKK--LQDGDSIQI 170
Cdd:pfam16697   19 YRIGSDPDCDIVLSDKEVSRVHLKLEVDDEGWRLDDLGSGNGTLVNGQRVTELGiaLRPGDRIEL 83
FHA_CHK2 cd22666
forkhead associated (FHA) domain found in checkpoint kinase 2 (Chk2) and similar proteins; ...
 105-170 2.05e-03

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


Pssm-ID: 438718 [Multi-domain]  Cd Length: 112  Bit Score: 39.15  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  105 KKSFLLGRDDACDICINHP---------FVSKIH--IRFEKQEQDLYL-FDEE-SKNGVYVNNKRV-KEKK--LQDGDSI 168
Cdd:cd22666     18 KDEYTFGRDKSCDYCFDSPalkktsyyrTYSKKHfrIFREKGSKNTYPvFLEDhSSNGTFVNGEKIgKGKKrpLNNNDEI 97


                   ..
gi 1802450525  169 QI 170
Cdd:cd22666     98 AL 99
FHA_ZEP-like cd22702
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ...
 103-170 4.37e-03

forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438754 [Multi-domain]  Cd Length: 123  Bit Score: 38.56  E-value: 4.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802450525  103 PDKKSFLLGRDDACD-----ICINHPFVSKIHIRFEKQEQDLYLFDEESKNGVYVNNKRVKEK--------KLQDGDSIQ 169
Cdd:cd22702     29 DEKQPCIIGSDPHQAisgisVVIPSPQVSELHARITCKNGAFFLTDLGSEHGTWINDNEGRRYrappnfpvRLHPSDVIE 108


                   .
gi 1802450525  170 I 170
Cdd:cd22702    109 F 109
 
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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