NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1841901216|ref|XP_034277454|]
View 

transcription factor 19 [Pantherophis guttatus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
7-144 4.97e-60

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: 190.32  E-value: 4.97e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841901216   7 PCFQLLRMGPASSGDlPNRDLYTFRPakPSCIYRLGRRAEVCDVILVSEQNPALISRVHAEIHAERDADsmaGEWRVGLV 86
Cdd:cd22685     1 PCFQLLRIGLSASRS-EPRDLYTFRP--DLCEYRIGRNPEVCDVFLCSSQHPNLISREHAEIHAERDGN---GNWKVLIE 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1841901216  87 DCSSYGTYINALRMSHGQRVDLNDGDLLTFGHSSPVPEgcVLPPPHGNSEFYFLFQKV 144
Cdd:cd22685    75 DRSTNGTYVNDVRLQDGQRRELSDGDTITFGHKNGRRV--KQWPYQKSSEFYFLFQKV 130
PHD_TCF19 cd15609
PHD finger found in Transcription factor 19 (TCF-19) and similar proteins; TCF-19, also termed ...
331-376 9.63e-24

PHD finger found in Transcription factor 19 (TCF-19) and similar proteins; TCF-19, also termed 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: 277082  Cd Length: 50  Bit Score: 92.53  E-value: 9.63e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1841901216 331 PCAAPRCRLPQDEMVEWVQCDGCDAWYHVACVGCSYSVVK--EADFRC 376
Cdd:cd15609     1 PCASPSCCLPQDETVSWVQCDDCDQWYHVACVGCDYNAVKdpDADFHC 48
 
Name Accession Description Interval E-value
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
7-144 4.97e-60

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: 190.32  E-value: 4.97e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841901216   7 PCFQLLRMGPASSGDlPNRDLYTFRPakPSCIYRLGRRAEVCDVILVSEQNPALISRVHAEIHAERDADsmaGEWRVGLV 86
Cdd:cd22685     1 PCFQLLRIGLSASRS-EPRDLYTFRP--DLCEYRIGRNPEVCDVFLCSSQHPNLISREHAEIHAERDGN---GNWKVLIE 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1841901216  87 DCSSYGTYINALRMSHGQRVDLNDGDLLTFGHSSPVPEgcVLPPPHGNSEFYFLFQKV 144
Cdd:cd22685    75 DRSTNGTYVNDVRLQDGQRRELSDGDTITFGHKNGRRV--KQWPYQKSSEFYFLFQKV 130
PHD_TCF19 cd15609
PHD finger found in Transcription factor 19 (TCF-19) and similar proteins; TCF-19, also termed ...
331-376 9.63e-24

PHD finger found in Transcription factor 19 (TCF-19) and similar proteins; TCF-19, also termed 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: 277082  Cd Length: 50  Bit Score: 92.53  E-value: 9.63e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1841901216 331 PCAAPRCRLPQDEMVEWVQCDGCDAWYHVACVGCSYSVVK--EADFRC 376
Cdd:cd15609     1 PCASPSCCLPQDETVSWVQCDDCDQWYHVACVGCDYNAVKdpDADFHC 48
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
39-116 1.91e-10

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 56.05  E-value: 1.91e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841901216  39 YRLGRRAEvCDVILVSEQnpalISRVHAEIHAErdadsmaGEWRVGLVDC-SSYGTYINALRMSHgQRVDLNDGDLLTF 116
Cdd:pfam00498   1 VTIGRSPD-CDIVLDDPS----VSRRHAEIRYD-------GGGRFYLEDLgSTNGTFVNGQRLGP-EPVRLKDGDVIRL 66
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
39-119 3.19e-10

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 56.50  E-value: 3.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841901216  39 YRLGRRAEvCDVILVSeqnpALISRVHAEIHAErdadsmAGEWRVglVDC-SSYGTYINalrmshGQRVD----LNDGDL 113
Cdd:COG1716    23 LTIGRAPD-NDIVLDD----PTVSRRHARIRRD------GGGWVL--EDLgSTNGTFVN------GQRVTepapLRDGDV 83

                  ....*.
gi 1841901216 114 LTFGHS 119
Cdd:COG1716    84 IRLGKT 89
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
337-379 1.87e-06

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 44.51  E-value: 1.87e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1841901216  337 CRLPQDEmVEWVQCDGCDAWYHVACVGCSY-SVVKEADFRCVAC 379
Cdd:smart00249   5 CGKPDDG-GELLQCDGCDRWYHQTCLGPPLlEEEPDGKWYCPKC 47
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
39-96 5.14e-05

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 40.24  E-value: 5.14e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1841901216   39 YRLGRRAEVCDVILvseqNPALISRVHAEIHaeRDADSmagewRVGLVDCSS-YGTYIN 96
Cdd:smart00240   1 VTIGRSSEDCDIQL----DGPSISRRHAVIV--YDGGG-----RFYLIDLGStNGTFVN 48
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
346-381 8.62e-05

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains. Several PHD fingers have been identified as binding modules of methylated histone H3.


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 39.78  E-value: 8.62e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1841901216 346 EWVQCDGCDAWYHVACVG--CSYSVVKEADFRCVACRS 381
Cdd:pfam00628  13 ELVQCDGCDDWFHLACLGppLDPAEIPSGEWLCPECKP 50
 
Name Accession Description Interval E-value
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
7-144 4.97e-60

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: 190.32  E-value: 4.97e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841901216   7 PCFQLLRMGPASSGDlPNRDLYTFRPakPSCIYRLGRRAEVCDVILVSEQNPALISRVHAEIHAERDADsmaGEWRVGLV 86
Cdd:cd22685     1 PCFQLLRIGLSASRS-EPRDLYTFRP--DLCEYRIGRNPEVCDVFLCSSQHPNLISREHAEIHAERDGN---GNWKVLIE 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1841901216  87 DCSSYGTYINALRMSHGQRVDLNDGDLLTFGHSSPVPEgcVLPPPHGNSEFYFLFQKV 144
Cdd:cd22685    75 DRSTNGTYVNDVRLQDGQRRELSDGDTITFGHKNGRRV--KQWPYQKSSEFYFLFQKV 130
PHD_TCF19 cd15609
PHD finger found in Transcription factor 19 (TCF-19) and similar proteins; TCF-19, also termed ...
331-376 9.63e-24

PHD finger found in Transcription factor 19 (TCF-19) and similar proteins; TCF-19, also termed 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: 277082  Cd Length: 50  Bit Score: 92.53  E-value: 9.63e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1841901216 331 PCAAPRCRLPQDEMVEWVQCDGCDAWYHVACVGCSYSVVK--EADFRC 376
Cdd:cd15609     1 PCASPSCCLPQDETVSWVQCDDCDQWYHVACVGCDYNAVKdpDADFHC 48
PHD3_KDM5A_like cd15610
PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A), 5B (KDM5B), and similar proteins; ...
331-379 2.81e-16

PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A), 5B (KDM5B), and similar proteins; The family includes KDM5A and KDM5B, both of which belong to the JARID subfamily within the JmjC proteins. KDM5A, also termed Histone demethylase JARID1A, or Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2), was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5A functions as the trimethylated histone H3 lysine 4 (H3K4me3) demethylase. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5B, also termed Cancer/testis antigen 31 (CT31), or Histone demethylase JARID1B, or Jumonji/ARID domain-containing protein 1B (JARID1B), or PLU-1, or retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A), has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well asTIEG1/KLF10 (transforming growth factor-beta inducible early gene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. The family also includes the Drosophila melanogaster protein little imaginal discs (Lid) that functions as a JmjC-dependent trimethyl histone H3K4 (H3K4me3) demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Members in this family contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the third PHD finger.


Pssm-ID: 277083 [Multi-domain]  Cd Length: 50  Bit Score: 71.97  E-value: 2.81e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1841901216 331 PCAAPRCRLPQDEMVEWVQCDGCDAWYHVACVGCSYSVVKE-ADFRCVAC 379
Cdd:cd15610     1 SCSAKQCLKPTGDEVNWVQCDGCEEWFHLLCVGLSPEEVAEdEDYICPSC 50
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
28-117 1.15e-12

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: 63.89  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841901216  28 YTFRPAKPsciYRLGRRAevCDVILVSEQNpalISRVHAEI---HAERDADSMAGEWRVGLVDCSSYGTYINALRMSHGQ 104
Cdd:cd22667    14 YYLLPGGE---YTVGRKD--CDIIIVDDSS---ISRKHATLtvlHPEANLSDPDTRPELTLKDLSKYGTFVNGEKLKGGS 85
                          90
                  ....*....|...
gi 1841901216 105 RVDLNDGDLLTFG 117
Cdd:cd22667    86 EVTLKDGDVITFG 98
PHD3_KDM5B cd15687
PHD finger 3 found in lysine-specific demethylase 5B (KDM5B); KDM5B, also termed Cancer/testis ...
332-379 4.50e-11

PHD finger 3 found in lysine-specific demethylase 5B (KDM5B); KDM5B, also termed Cancer/testis antigen 31 (CT31), or Histone demethylase JARID1B, or Jumonji/ARID domain-containing protein 1B (JARID1B), or PLU-1, or retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A), is a member of the JARID subfamily within the JmjC proteins. It has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well as TIEG1/KLF10 (transforming growth factor-beta inducible early gene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. KDM5B contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the third PHD finger.


Pssm-ID: 277157  Cd Length: 50  Bit Score: 57.65  E-value: 4.50e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1841901216 332 CAAPRCRLPQDEMVEWVQCDG-CDAWYHVACVGCSYSVVKEADFRCVAC 379
Cdd:cd15687     2 CPAVSCLQPEGEEVDWVQCDGsCNRWFHQVCVGVSAEMAEKEDYICVSC 50
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
39-116 1.91e-10

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 56.05  E-value: 1.91e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841901216  39 YRLGRRAEvCDVILVSEQnpalISRVHAEIHAErdadsmaGEWRVGLVDC-SSYGTYINALRMSHgQRVDLNDGDLLTF 116
Cdd:pfam00498   1 VTIGRSPD-CDIVLDDPS----VSRRHAEIRYD-------GGGRFYLEDLgSTNGTFVNGQRLGP-EPVRLKDGDVIRL 66
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
39-119 3.19e-10

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 56.50  E-value: 3.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841901216  39 YRLGRRAEvCDVILVSeqnpALISRVHAEIHAErdadsmAGEWRVglVDC-SSYGTYINalrmshGQRVD----LNDGDL 113
Cdd:COG1716    23 LTIGRAPD-NDIVLDD----PTVSRRHARIRRD------GGGWVL--EDLgSTNGTFVN------GQRVTepapLRDGDV 83

                  ....*.
gi 1841901216 114 LTFGHS 119
Cdd:COG1716    84 IRLGKT 89
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
35-120 1.06e-09

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


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 54.97  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841901216  35 PSCIYRLGRRAEvCDVILvseqNPALISRVHAEIHAErdadsmAGEWRvgLVDCSS-YGTYINALRMSHgqRVDLNDGDL 113
Cdd:cd00060    17 TKGVVTIGRSPD-CDIVL----DDPSVSRRHARIEVD------GGGVY--LEDLGStNGTFVNGKRITP--PVPLQDGDV 81

                  ....*..
gi 1841901216 114 LTFGHSS 120
Cdd:cd00060    82 IRLGDTT 88
PHD3_KDM5A cd15686
PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A); KDM5A, also termed Histone ...
332-379 1.26e-09

PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A); KDM5A, also termed Histone demethylase JARID1A, or Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2), was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5A functions as a trimethylated histone H3 lysine 4 (H3K4me3) demethylase that belongs to the JARID subfamily within the JmjC proteins. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5A contains the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the third PHD finger.


Pssm-ID: 277156  Cd Length: 52  Bit Score: 53.54  E-value: 1.26e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1841901216 332 CAAPRCRLPQDEMVEWVQCDG-CDAWYHVACVGCSYSVVKEADFRCVAC 379
Cdd:cd15686     3 CAAQNCQRPCKDKVDWVQCDGgCDEWFHQVCVGVSPEMAENEDYICINC 51
FHA_SNIP1_DDL-like cd22676
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ...
27-120 4.29e-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: 53.84  E-value: 4.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841901216  27 LYTFRPAKP---------SCiYRLGRRAEVCDVILvseQNPAlISRVHAEI----HAERDADSMAGEWRVGLVDCSSY-G 92
Cdd:cd22676     3 LYVFKGGEQletidihrqSA-YLIGRDRRVADIPL---DHPS-CSKQHAVIqfreVEKRNEGDVIENIRPYIIDLGSTnG 77
                          90       100
                  ....*....|....*....|....*...
gi 1841901216  93 TYINALRMSHGQRVDLNDGDLLTFGHSS 120
Cdd:cd22676    78 TFLNGEKIEPRRYYELREKDVLKFGLST 105
PHD_TCF19_like cd15517
PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...
335-379 9.49e-09

PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and KDM5B, and other similar proteins; TCF-19 was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It 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. KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interaction with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK, and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. This family also includes Caenorhabditis elegans Lysine-specific demethylase 7 homolog (ceKDM7A). ceKDM7A (also termed JmjC domain-containing protein 1.2, PHD finger protein 8 homolog, or PHF8 homolog) is a plant homeodomain (PHD)- and JmjC domain-containing protein that functions as a histone demethylase specific for H3K9me2 and H3K27me2. The binding of the PHD finger to H3K4me3 guides H3K9me2- and H3K27me2-specific demethylation by its catalytic JmjC domain in a trans-histone regulation mechanism. In addition, this family includes plant protein OBERON 1 and OBERON 2, Alfin1-like (AL) proteins, histone acetyltransferases (HATs) HAC, and AT-rich interactive domain-containing protein 4 (ARID4).


Pssm-ID: 276992 [Multi-domain]  Cd Length: 49  Bit Score: 51.01  E-value: 9.49e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1841901216 335 PRCRLP-QDEMVEWVQCDGCDAWYHVACVGCSYSVVK-EADFRCVAC 379
Cdd:cd15517     3 GICNLEtAAVDELWVQCDGCDKWFHQFCLGLSNERYAdEDKFKCPNC 49
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
39-120 1.19e-08

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: 52.23  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841901216  39 YRLGRrAEVCDVILvseQNPAlISRVHAEIHA---ERDADSMagewrVGLVDCSSYGTYINALRMSHGQRVDLNDGDLLT 115
Cdd:cd22670    24 ITIGR-SPSCDIVI---NDPF-VSRTHCRIYSvqfDESSAPL-----VYVEDLSSNGTYLNGKLIGRNNTVLLSDGDVIE 93

                  ....*
gi 1841901216 116 FGHSS 120
Cdd:cd22670    94 IAHSA 98
PHD2_3_BPTF cd15560
PHD finger 2 and 3 found in bromodomain and PHD finger-containing transcription factor (BPTF); ...
337-379 5.63e-07

PHD finger 2 and 3 found in bromodomain and PHD finger-containing transcription factor (BPTF); BPTF, also termed nucleosome-remodeling factor subunit BPTF, or fetal Alz-50 clone 1 protein (FAC1), or fetal Alzheimer antigen, functions as a transcriptional regulator that exhibits altered expression and subcellular localization during neuronal development and neurodegenerative diseases such as Alzheimer's disease. It interacts with the human orthologue of the Kelch-like Ech-associated protein (Keap1). Its function and subcellular localization can be regulated by Keap1. Moreover, BPTF is a novel DNA-binding protein that recognizes the DNA sequence CACAACAC and represses transcription through this site in a phosphorylation-dependent manner. Furthermore, BPTF interacts with the Myc-associated zinc finger protein (ZF87/MAZ) and alters its transcriptional activity, which has been implicated in gene regulation in neurodegeneration. Some family members contain two or three plant homeodomain (PHD) fingers, which may be involved in complex formation with histone H3 trimethylated at K4 (H3K4me3). This family corresponds to the second and third PHD fingers.


Pssm-ID: 277035  Cd Length: 47  Bit Score: 45.80  E-value: 5.63e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1841901216 337 CRLPQDEMVEWVQCDGCDAWYHVACVGCSYSVVKEAD-FRCVAC 379
Cdd:cd15560     4 CRTPYDESQFYIGCDRCQDWFHGRCVGILQSEAEKIDeYVCPQC 47
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
40-188 1.50e-06

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


Pssm-ID: 442679 [Multi-domain]  Cd Length: 402  Bit Score: 49.76  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841901216  40 RLGRRAEvCDVILvseQNPAL-ISRVHAEIHAErdadsmAGEWRvgLVDCSSYGTYIN--ALRMSHGQRVDLNDGDLLTF 116
Cdd:COG3456    29 TIGRSAD-CDWVL---PDPDRsVSRRHAEIRFR------DGAFC--LTDLSTNGTFLNgsDHPLGPGRPVRLRDGDRLRI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841901216 117 GH------------SSPVPEGCVLPPPHGNSEFYFLFQKVRVRPQDFAAITEPKAPWASSSGFRPVLPSDNHRIHPLSRH 184
Cdd:COG3456    97 GDyeirveisgedeGADDPLAAAPEPAVSSPSNLSDTEAAPDAALAFSFSLDPLEALDEAATEAPATADDPPSLLPEDWL 176

                  ....
gi 1841901216 185 SPTS 188
Cdd:COG3456   177 PSAA 180
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
337-379 1.87e-06

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 44.51  E-value: 1.87e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1841901216  337 CRLPQDEmVEWVQCDGCDAWYHVACVGCSY-SVVKEADFRCVAC 379
Cdd:smart00249   5 CGKPDDG-GELLQCDGCDRWYHQTCLGPPLlEEEPDGKWYCPKC 47
FHA_RAD53-like_rpt2 cd22690
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
44-116 2.04e-06

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: 46.13  E-value: 2.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841901216  44 RAEVCDVILVSEQnpalISRVHAEIHAERDADSMAGEWrvgLVDCSSYGTYINALRMSHGQRVDLNDGDLLTF 116
Cdd:cd22690    25 RSKDCDEEITDPR----ISKHHCIITRKRSGKGLDDVY---VTDTSTNGTFINNNRLGKGSQSLLQDGDEIVL 90
PHD_TAF3 cd15522
PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed ...
335-379 3.23e-06

PHD finger found in transcription initiation factor TFIID subunit 3 (TAF3); TAF3 (also termed 140 kDa TATA box-binding protein-associated factor, TBP-associated factor 3, transcription initiation factor TFIID 140 kDa subunit (TAF140), or TAFII-140, is an integral component of TFIID) is a general initiation factor (GTF) that plays a key role in preinitiation complex (PIC) assembly through core promoter recognition. The interaction of H3K4me3 with TAF3 directs global TFIID recruitment to active genes, which regulates gene-selective functions of p53 in response to genotoxic stress. TAF3 is highly enriched in embryonic stem cells and is required for endoderm lineage differentiation and prevents premature specification of neuroectoderm and mesoderm. Moreover, TAF3, along with TRF3, forms a complex that is essential for myogenic differentiation. TAF3 contains a plant homeodomain (PHD) finger. This family also includes Drosophila melanogaster BIP2 (Bric-a-brac interacting protein 2) protein, which functions as an interacting partner of D. melanogaster p53 (Dmp53).


Pssm-ID: 276997 [Multi-domain]  Cd Length: 46  Bit Score: 43.81  E-value: 3.23e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1841901216 335 PRCRLPqDEMVEWVQCDGCDAWYHVACVGCSYSVVKEADFRCVAC 379
Cdd:cd15522     3 PICKKP-DDGSPMIGCDECDDWYHWECVGITDEPPEEDDWFCPKC 46
FHA_PPP1R8 cd22674
forkhead associated (FHA) domain found in protein phosphatase 1 regulatory inhibitor subunit 8 ...
39-120 3.24e-06

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: 45.33  E-value: 3.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841901216  39 YRLGRRAEVCDVILvseqNPALISRVHAEI--HAERDadsmagewRVGLVDC-SSYGTYINALRMSHGQRVDLNDGDLLT 115
Cdd:cd22674    29 YLFGRNSDVCDFVL----DHPSCSRVHAALvyHKHLN--------RVFLIDLgSTHGTFVGGIRLEPHKPQQLPIDSTLR 96

                  ....*
gi 1841901216 116 FGHSS 120
Cdd:cd22674    97 FGAST 101
FHA_Kanadaptin cd22677
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ...
44-120 3.98e-06

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: 45.24  E-value: 3.98e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1841901216  44 RAEVCDVILvseQNPAlISRVHAEIHAERDADSMAGEWRvgLVDC-SSYGTYINALRMSHGQRVDLNDGDLLTFGHSS 120
Cdd:cd22677    28 RLPGCDVVL---EHPS-ISRYHAVLQYRGDADDHDGGFY--LYDLgSTHGTFLNKQRIPPKQYYRLRVGHVLKFGGST 99
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
337-379 6.76e-06

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) finger typically characterized as Cys4HisCys3, and a non-canonical extended PHD finger, characterized as Cys2HisCys5HisCys2His. Variations include the RAG2 PHD finger characterized by Cys3His2Cys2His and the PHD finger 5 found in nuclear receptor-binding SET domain-containing proteins characterized by Cys4HisCys2His. The PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. Single or multiple copies of PHD fingers have been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors. The PHD finger domain SF is structurally similar to the RING and FYVE_like superfamilies.


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 42.69  E-value: 6.76e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1841901216 337 CRLPQDEMVEWVQCDGCDAWYHVACVGCSY-SVVKEADFRCVAC 379
Cdd:cd15489     5 CGKGGDLGGELLQCDGCGKWFHADCLGPPLsSFVPNGKWICPVC 48
FHA_CHFR cd22672
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ...
44-118 8.32e-06

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: 44.21  E-value: 8.32e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841901216  44 RAEVCDVILVSEQnpaLISRVHAEIhaERDADSmagewRVGLVDCSSYGTYINALRMSHGQRVDLNDGDLLTFGH 118
Cdd:cd22672    27 RAKDCDLSFPGNK---LVSGDHCKI--IRDEKG-----QVWLEDTSTNGTLVNKVKVVKGQKVELKHGDVIYLVY 91
FHA_DUN1-like cd22683
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ...
41-117 3.80e-05

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: 42.09  E-value: 3.80e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1841901216  41 LGRRAEvCDVILVSeqnpALISRVHAEIHAERDadsmagewRVGLVDCSSY-GTYINALRMShGQRVDLNDGDLLTFG 117
Cdd:cd22683    25 IGRSRS-CDLVLSD----PSISRFHAELRLEQN--------GINVIDNNSAnGTFINGKRIK-GKTYILKNGDIIVFG 88
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
39-96 5.14e-05

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 40.24  E-value: 5.14e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1841901216   39 YRLGRRAEVCDVILvseqNPALISRVHAEIHaeRDADSmagewRVGLVDCSS-YGTYIN 96
Cdd:smart00240   1 VTIGRSSEDCDIQL----DGPSISRRHAVIV--YDGGG-----RFYLIDLGStNGTFVN 48
FHA_MDC1 cd22665
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ...
44-117 7.88e-05

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


Pssm-ID: 438717 [Multi-domain]  Cd Length: 97  Bit Score: 41.06  E-value: 7.88e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1841901216  44 RAEVCDVILvseQNPAlISRVHAEIhaERDAdsmaGEWRVGlvDCSSY-GTYINA-LRMSHGQRVDLNDGDLLTFG 117
Cdd:cd22665    27 RDPSCSVVL---PDKS-VSKQHACI--EVDG----GTHLIE--DLGSTnGTRIGNkVRLKPNVRYELIDGDLLLFG 90
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
346-381 8.62e-05

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains. Several PHD fingers have been identified as binding modules of methylated histone H3.


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 39.78  E-value: 8.62e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1841901216 346 EWVQCDGCDAWYHVACVG--CSYSVVKEADFRCVACRS 381
Cdd:pfam00628  13 ELVQCDGCDDWFHLACLGppLDPAEIPSGEWLCPECKP 50
PHD_PHF3_like cd15552
PHD finger found in PHD finger protein 3 (PHF3), and death-inducer obliterator variants Dido1, ...
337-379 4.25e-04

PHD finger found in PHD finger protein 3 (PHF3), and death-inducer obliterator variants Dido1, Dido2, and Dido3; PHF3 is a human homolog of yeast protein bypass of Ess1 (Bye1), a nuclear protein with a domain resembling the central domain in the transcription elongation factor TFIIS. It is ubiquitously expressed in normal tissues including brain, but its expression is significantly reduced or lost in glioblastomas. PHF3 contains an N-terminal plant homeodomain (PHD) finger, a central RNA polymerase II (Pol II)-binding TFIIS-like domain (TLD) domain, and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain. This family also includes Dido gene encoding three alternative splicing variants (Dido1, 2, and 3), which have been implicated in a number of cellular processes such as apoptosis and chromosomal segregation, particularly in the hematopoietic system. Dido1 is important for maintaining embryonic stem (ES) cells and directly regulates the expression of pluripotency factors. It is the shortest isoform that contains only a highly conserved PHD finger responsible for the binding of histone H3 with a higher affinity for trimethylated lysine4 (H3K4me3). Gene Dido1 is a Bone morphogenetic protein (BMP) target gene and promotes BMP-induced melanoma progression. It also triggers apoptosis after nuclear translocation and caspase upregulation. Dido3 is the largest isoform and is ubiquitously expressed in all human tissues. It is dispensable for ES cell self-renewal and pluripotency, but is involved in the maintenance of stem cell genomic stability and tumorigenesis. Dido3 contains a PHD finger, a transcription elongation factor S-II subunit M (TFSIIM) domain, a SPOC module, and a long C-terminal region (CT) of unknown homology.


Pssm-ID: 277027  Cd Length: 50  Bit Score: 37.76  E-value: 4.25e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1841901216 337 CRLPQDE--MVEwvqCDGCDAWYHVACVGCSYSVVKEA-----DFRCVAC 379
Cdd:cd15552     4 CRKPHNNrfMIC---CDRCEEWFHGDCVGITEAQGKEMeenieEYVCPKC 50
FHA_PS1-like cd22691
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ...
44-120 1.22e-03

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


Pssm-ID: 438743 [Multi-domain]  Cd Length: 113  Bit Score: 38.17  E-value: 1.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1841901216  44 RAEVCDVILvseqNPALISRVHAEIHaerdadSMAGEWRVGLVDCSS-YGTYINALRMSHGQRVDLNDGDLLTFGHSS 120
Cdd:cd22691    35 RHPDCDIVL----DHPSISRFHLEIR------IIPSRRKITLTDLSSvHGTWVNGQRIEPGVPVELEEGDTVRLGAST 102
PHD_Ecm5p_Lid2p_like cd15518
PHD finger found in Saccharomyces cerevisiae extracellular matrix protein 5 (Ecm5p), ...
337-379 1.77e-03

PHD finger found in Saccharomyces cerevisiae extracellular matrix protein 5 (Ecm5p), Schizosaccharomyces pombe Lid2 complex component Lid2p, and similar proteins; The family includes Saccharomyces cerevisiae Ecm5p, Schizosaccharomyces pombe Lid2 complex component Lid2p, and similar proteins. Ecm5p is a JmjC domain-containing protein that directly removes histone lysine methylation via a hydroxylation reaction. It associates with the yeast Snt2p and Rpd3 deacetylase, which may play a role in regulating transcription in response to oxidative stress. Ecm5p promotes oxidative stress tolerance, while Snt2p ultimately decreases tolerance. Ecm5p contains an N-terminal ARID domain, a JmjC domain, and a C-terminal plant homeodomain (PHD) finger. Lid2p is a trimethyl H3K4 (H3K4me3) demethylase responsible for H3K4 hypomethylation in heterochromatin. It interacts with the histone lysine-9 methyltransferase, Clr4, through the Dos1/Clr8-Rik1 complex, and mediates H3K9 methylation and small RNA production. It also acts cooperatively with the histone modification enzymes Set1 and Lsd1 and plays an essential role in cross-talk between H3K4 and H3K9 methylation in euchromatin. Lid2p contains a JmjC domain, three PHD fingers and a JmjN domain. This model includes the second PHD finger of Lid2p.


Pssm-ID: 276993  Cd Length: 45  Bit Score: 35.79  E-value: 1.77e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1841901216 337 CRLPQDEMVewVQCDGCDAWYHVACVGCSYSVVKEAD-FRCVAC 379
Cdd:cd15518     4 CRQGEGGTM--IECEICKEWYHVKCIKNGRWKLDDDDkFVCPIC 45
PHD_HAC_like cd15614
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ...
342-361 5.11e-03

PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar proteins; This family includes A. thaliana HACs (HAC1/2/4/5/12), which are histone acetyltransferases of the p300/CREB-binding protein (CBP) co-activator family. CBP-type HAT proteins are also found in animals, but absent in fungi. The domain architecture of CBP-type HAT proteins differs between plants and animals. Members in this family contain an N-terminal partially conserved KIX domain, a Zf-TAZ domain, a Cysteine rich CBP-type HAT domain that harbors a plant homeodomain (PHD) finger, a Zf-ZZ domain, and a Zf-TAZ domain. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins.


Pssm-ID: 277086  Cd Length: 73  Bit Score: 35.41  E-value: 5.11e-03
                          10        20
                  ....*....|....*....|..
gi 1841901216 342 DEMVE--WVQCDGCDAWYHVAC 361
Cdd:cd15614    32 DEEFEeaWVQCDKCERWQHQIC 53
PHD_PHF2 cd15641
PHD finger found in lysine-specific demethylase PHF2; PHF2, also termed GRC5, or PHD finger ...
337-379 5.20e-03

PHD finger found in lysine-specific demethylase PHF2; PHF2, also termed GRC5, or PHD finger protein 2, is a histone lysine demethylase ubiquitously expressed in various tissues. It contains a plant homeodomain (PHD) finger and a JmjC domain and plays an important role in adipogenesis. The PHD finger domain can recognize trimethylated histone H3 lysine 4 (H3K4me3). PHF2 also has dimethylated histone H3 lysine 9(H3K9me2) demethylase activity and acts as a coactivator of several metabolism-related transcription factors. Moreover, it can demethylate ARID5B and further forms a complex with demethylated ARD5B to bind the promoter regions of target genes. The overexpression of PHF2 is involved in the progression of esophageal squamous cell carcinoma (ESCC).


Pssm-ID: 277111  Cd Length: 50  Bit Score: 34.99  E-value: 5.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1841901216 337 CRLPQDEMVEWVQCDGCDAWYHVACVGCSYSVVKEAD-FRCVAC 379
Cdd:cd15641     4 CRLPYDVTRFMIECDACKDWFHGSCVGVEEEEAPDIDiYHCPNC 47
PHD_PHF8 cd15642
PHD finger found in histone lysine demethylase PHF8; PHF8, also termed PHD finger protein 8, ...
337-380 5.70e-03

PHD finger found in histone lysine demethylase PHF8; PHF8, also termed PHD finger protein 8, or KDM7B, is a monomethylated histone H4 lysine 20 (H4K20me1) demethylase that transcriptionally regulates many cell cycle genes. It also preferentially acts on H3K9me2 and H3K9me1. PHF8 is modulated by CDC20-containing anaphase-promoting complex (APC (cdc20)) and plays an important role in the G2/M transition. It acts as a critical molecular sensor for mediating retinoic acid (RA) treatment response in RAR alpha-fusion-induced leukemia. Moreover, PHF8 is essential for cytoskeleton dynamics and is associated with X-linked mental retardation. PHF8 contains an N-terminal plant homeodomain (PHD) finger followed by a JmjC domain. The PHD finger mediates binding to nucleosomes at active gene promoters and the JmjC domain catalyzes the demethylation of mono- or dimethyl-lysines.


Pssm-ID: 277112  Cd Length: 52  Bit Score: 34.61  E-value: 5.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1841901216 337 CRLPQDEMVEWVQCDGCDAWYHVACVGCSYSVVKEAD-FRCVACR 380
Cdd:cd15642     5 CRLPYDVTRFMIECDVCQDWFHGSCVGVEEEKAAEIDlYHCPNCQ 49
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH