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Conserved domains on  [gi|19115314|ref|NP_594402|]
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protein Yih1 [Schizosaccharomyces pombe]

Protein Classification

IMPACT family protein( domain architecture ID 20256173)

IMPACT (imprinted ancient) family protein similar to Saccharomyces cerevisiae protein IMPACT homolog (YIH1), which is a translational regulator that ensures constant high levels of translation under amino acid starvation

CATH:  3.10.110.10
Gene Ontology:  GO:0034198|GO:0140311|GO:0006446|GO:0005515
PubMed:  11116084|26495453|26276859|25918163|24333428

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UPF0029 pfam01205
Uncharacterized protein family UPF0029;
153-259 8.64e-39

Uncharacterized protein family UPF0029;


:

Pssm-ID: 460111  Cd Length: 105  Bit Score: 131.39  E-value: 8.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314   153 RKSTFMAHATRVYSTEEVREALEDLYmdKKVAKANHNMVAYRIISPNGnviQDNDDDGESA--AGSRMSHLLTMMSAENV 230
Cdd:pfam01205   1 KKSKFIAHAAPVESEEEAKAFLEELK--KEHKKATHNCYAYRIGGEGG---ERSSDDGEPGgtAGKPILEVLEGNGLTNV 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 19115314   231 FVCVSRWFGGVHIGPDRF-KHINSSAREAV 259
Cdd:pfam01205  76 LVVVTRYFGGIKLGPGGLvRAYSNAAREAL 105
RWD_DRWD_ELF-like super family cl45901
RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF ...
 7-95 1.28e-25

RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF domains. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. The RWD domain (named after three major RWD-containing proteins: RING finger, WD-repeat-containing proteins and DEXD-like helicases) mediates protein-protein interactions in a variety of pathways in eukaryotes. The DRWD domain is responsible for substrate binding. It is involved in interactions with other kinetochore proteins. The ELF (N-terminal E2-like fold) domain is found in all Fanconi anemia group L protein (FANCL) homologs. It is required to promote efficient DNA damage-induced FANCD2 (Fanconi anemia group D2 protein) monoubiquitination in vertebrate cells.


The actual alignment was detected with superfamily member cd23822:

Pssm-ID: 480265  Cd Length: 97  Bit Score: 97.33  E-value: 1.28e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314   7 FQDELLALESIYPSCLLPISEQsfTYTLSIPD-SSVRLNIQFPLDYPNSAPTVLDAY--------GIDKTLAEDVLLSVA 77
Cdd:cd23822   1 LADEIEAINAIYPDCLVRLSPS--IYTLKIPDhEDVSIQLSFPSDYPDEPPHVLGVSssgargdgKYLKDLLEDILASVF 78

                        90
                ....*....|....*....
gi 19115314  78 T-GDVCIFSYMDLLKELVD 95
Cdd:cd23822  79 VpGEVCLFDFIEELREVLE 97
 
Name Accession Description Interval E-value
UPF0029 pfam01205
Uncharacterized protein family UPF0029;
153-259 8.64e-39

Uncharacterized protein family UPF0029;


Pssm-ID: 460111  Cd Length: 105  Bit Score: 131.39  E-value: 8.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314   153 RKSTFMAHATRVYSTEEVREALEDLYmdKKVAKANHNMVAYRIISPNGnviQDNDDDGESA--AGSRMSHLLTMMSAENV 230
Cdd:pfam01205   1 KKSKFIAHAAPVESEEEAKAFLEELK--KEHKKATHNCYAYRIGGEGG---ERSSDDGEPGgtAGKPILEVLEGNGLTNV 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 19115314   231 FVCVSRWFGGVHIGPDRF-KHINSSAREAV 259
Cdd:pfam01205  76 LVVVTRYFGGIKLGPGGLvRAYSNAAREAL 105
RWD_ScYIH1-like cd23822
RWD domain of Saccharomyces cerevisiae protein YIH1 and related proteins; YIH1, also called ...
 7-95 1.28e-25

RWD domain of Saccharomyces cerevisiae protein YIH1 and related proteins; YIH1, also called protein IMPACT homolog, is an actin-binding protein that acts as a translational regulator which ensures constant high levels of translation under amino acid starvation. It plays a role as a negative regulator of GCN2 kinase activity. It impairs GCN1-mediated GCN2 activation, and hence GCN2-mediated eIF-2-alpha phosphorylation in amino acid-starved cells and subsequent down-regulation of protein synthesis. In normal conditions, it resides in an actin complex and has no activity.


Pssm-ID: 467658  Cd Length: 97  Bit Score: 97.33  E-value: 1.28e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314   7 FQDELLALESIYPSCLLPISEQsfTYTLSIPD-SSVRLNIQFPLDYPNSAPTVLDAY--------GIDKTLAEDVLLSVA 77
Cdd:cd23822   1 LADEIEAINAIYPDCLVRLSPS--IYTLKIPDhEDVSIQLSFPSDYPDEPPHVLGVSssgargdgKYLKDLLEDILASVF 78

                        90
                ....*....|....*....
gi 19115314  78 T-GDVCIFSYMDLLKELVD 95
Cdd:cd23822  79 VpGEVCLFDFIEELREVLE 97
YIH1 COG1739
Putative translation regulator, IMPACT (imprinted ancient) protein family [General function ...
 150-244 7.16e-14

Putative translation regulator, IMPACT (imprinted ancient) protein family [General function prediction only];


Pssm-ID: 441345 [Multi-domain]  Cd Length: 198  Bit Score: 68.59  E-value: 7.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314 150 ITDRKSTFMAHATRVYSTEEVREALEDLYmdKKVAKANHNMVAYRIISPNGnvIQDNDDDGESA--AGSRMshLLTMMSA 227
Cdd:COG1739  15 IEIKKSRFIAYAAPVESEEEAKAFIAEIR--KEHPDATHNCWAYRIGAPGE--IQRASDDGEPSgtAGKPI--LEVLQGR 88

                        90
                ....*....|....*....
gi 19115314 228 E--NVFVCVSRWFGGVHIG 244
Cdd:COG1739  89 GltNVLVVVTRYFGGIKLG 107
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
 5-92 1.11e-12

RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.


Pssm-ID: 399058  Cd Length: 111  Bit Score: 63.11  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314     5 EEFQDELLALESIYPSCLLPISEQSFT-YTLSIPDS------------SVRLNIQFPLDYPNSAP--TVLDAYGI---DK 66
Cdd:pfam05773   1 EEQEEELEALESIYPDEFEVISDSPYEsLEIEIKLSldsdesdsshlpPLVLKFTLPEDYPDEPPkiSLSSPWNLsdeQV 80

                          90       100
                  ....*....|....*....|....*....
gi 19115314    67 TLAEDVLLSVA---TGDVCIFSYMDLLKE 92
Cdd:pfam05773  81 LSLLEELEELAeenLGEVMIFELIEWLQE 109
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
 10-92 3.05e-10

domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily related to the UBCc domain;


Pssm-ID: 214735  Cd Length: 107  Bit Score: 56.21  E-value: 3.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314     10 ELLALESIYPSCLLPISEQS----FTYTLSIPD-------SSVRLNIQFPLDYPNSAPTV--LDAYGIDKTLAEDVLLSV 76
Cdd:smart00591   1 ELEALESIYPEDFEVIDEDAripeITIKLSPSSdegedqyVSLTLQVKLPENYPDEAPPIslLNSEGLSDEQLAELLKKL 80

                           90       100
                   ....*....|....*....|..
gi 19115314     77 AT------GDVCIFSYMDLLKE 92
Cdd:smart00591  81 EEiaeenlGEVMIFELVEKLQE 102
 
Name Accession Description Interval E-value
UPF0029 pfam01205
Uncharacterized protein family UPF0029;
153-259 8.64e-39

Uncharacterized protein family UPF0029;


Pssm-ID: 460111  Cd Length: 105  Bit Score: 131.39  E-value: 8.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314   153 RKSTFMAHATRVYSTEEVREALEDLYmdKKVAKANHNMVAYRIISPNGnviQDNDDDGESA--AGSRMSHLLTMMSAENV 230
Cdd:pfam01205   1 KKSKFIAHAAPVESEEEAKAFLEELK--KEHKKATHNCYAYRIGGEGG---ERSSDDGEPGgtAGKPILEVLEGNGLTNV 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 19115314   231 FVCVSRWFGGVHIGPDRF-KHINSSAREAV 259
Cdd:pfam01205  76 LVVVTRYFGGIKLGPGGLvRAYSNAAREAL 105
RWD_ScYIH1-like cd23822
RWD domain of Saccharomyces cerevisiae protein YIH1 and related proteins; YIH1, also called ...
 7-95 1.28e-25

RWD domain of Saccharomyces cerevisiae protein YIH1 and related proteins; YIH1, also called protein IMPACT homolog, is an actin-binding protein that acts as a translational regulator which ensures constant high levels of translation under amino acid starvation. It plays a role as a negative regulator of GCN2 kinase activity. It impairs GCN1-mediated GCN2 activation, and hence GCN2-mediated eIF-2-alpha phosphorylation in amino acid-starved cells and subsequent down-regulation of protein synthesis. In normal conditions, it resides in an actin complex and has no activity.


Pssm-ID: 467658  Cd Length: 97  Bit Score: 97.33  E-value: 1.28e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314   7 FQDELLALESIYPSCLLPISEQsfTYTLSIPD-SSVRLNIQFPLDYPNSAPTVLDAY--------GIDKTLAEDVLLSVA 77
Cdd:cd23822   1 LADEIEAINAIYPDCLVRLSPS--IYTLKIPDhEDVSIQLSFPSDYPDEPPHVLGVSssgargdgKYLKDLLEDILASVF 78

                        90
                ....*....|....*....
gi 19115314  78 T-GDVCIFSYMDLLKELVD 95
Cdd:cd23822  79 VpGEVCLFDFIEELREVLE 97
YIH1 COG1739
Putative translation regulator, IMPACT (imprinted ancient) protein family [General function ...
 150-244 7.16e-14

Putative translation regulator, IMPACT (imprinted ancient) protein family [General function prediction only];


Pssm-ID: 441345 [Multi-domain]  Cd Length: 198  Bit Score: 68.59  E-value: 7.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314 150 ITDRKSTFMAHATRVYSTEEVREALEDLYmdKKVAKANHNMVAYRIISPNGnvIQDNDDDGESA--AGSRMshLLTMMSA 227
Cdd:COG1739  15 IEIKKSRFIAYAAPVESEEEAKAFIAEIR--KEHPDATHNCWAYRIGAPGE--IQRASDDGEPSgtAGKPI--LEVLQGR 88

                        90
                ....*....|....*....
gi 19115314 228 E--NVFVCVSRWFGGVHIG 244
Cdd:COG1739  89 GltNVLVVVTRYFGGIKLG 107
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
 5-92 1.11e-12

RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. The function of this domain is unknown. GCN2 is the alpha-subunit of the only translation initiation factor (eIF2 alpha) kinase that appears in all eukaryotes. Its function requires an interaction with GCN1 via the domain at its N-terminus, which is termed the RWD domain after three major RWD-containing proteins: RING finger-containing proteins, WD-repeat-containing proteins, and yeast DEAD (DEXD)-like helicases. The structure forms an alpha + beta sandwich fold consisting of two layers: a four-stranded antiparallel beta-sheet, and three side-by-side alpha-helices.


Pssm-ID: 399058  Cd Length: 111  Bit Score: 63.11  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314     5 EEFQDELLALESIYPSCLLPISEQSFT-YTLSIPDS------------SVRLNIQFPLDYPNSAP--TVLDAYGI---DK 66
Cdd:pfam05773   1 EEQEEELEALESIYPDEFEVISDSPYEsLEIEIKLSldsdesdsshlpPLVLKFTLPEDYPDEPPkiSLSSPWNLsdeQV 80

                          90       100
                  ....*....|....*....|....*....
gi 19115314    67 TLAEDVLLSVA---TGDVCIFSYMDLLKE 92
Cdd:pfam05773  81 LSLLEELEELAeenLGEVMIFELIEWLQE 109
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
 10-92 3.05e-10

domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily related to the UBCc domain;


Pssm-ID: 214735  Cd Length: 107  Bit Score: 56.21  E-value: 3.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314     10 ELLALESIYPSCLLPISEQS----FTYTLSIPD-------SSVRLNIQFPLDYPNSAPTV--LDAYGIDKTLAEDVLLSV 76
Cdd:smart00591   1 ELEALESIYPEDFEVIDEDAripeITIKLSPSSdegedqyVSLTLQVKLPENYPDEAPPIslLNSEGLSDEQLAELLKKL 80

                           90       100
                   ....*....|....*....|..
gi 19115314     77 AT------GDVCIFSYMDLLKE 92
Cdd:smart00591  81 EEiaeenlGEVMIFELVEKLQE 102
RWD_IMPACT cd23821
RWD domain of protein IMPACT and related proteins; IMPACT, also imprinted and ancient gene ...
 8-92 1.84e-09

RWD domain of protein IMPACT and related proteins; IMPACT, also imprinted and ancient gene protein homolog, acts as a translational regulator that ensures constant high levels of translation upon a variety of stress conditions, such as amino acid starvation, UV-C irradiation, proteasome inhibitor treatment, and glucose deprivation. It plays a role as a negative regulator of EIF2AK4/GCN2 kinase activity. It impairs GCN1-mediated EIF2AK4/GCN2 activation, and hence EIF2AK4/GCN2-mediated eIF-2-alpha phosphorylation and subsequent down-regulation of protein synthesis. IMPACT may be required to regulate translation in specific neuronal cells under amino acid starvation conditions by preventing GCN2 activation and therefore ATF4 synthesis. Through its inhibitory action on EIF2AK4/GCN2, IMPACT plays a role in differentiation of neuronal cells by stimulating neurite outgrowth.


Pssm-ID: 467657  Cd Length: 101  Bit Score: 53.78  E-value: 1.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314   8 QDELLALESIYPSCLLPISEQSFTYTLSIPDSS-----VRLNIQFPLDYPNSAP---TVLDAYGIDKTLAE--DVLLSVA 77
Cdd:cd23821   1 AEEIEALEAIYGEDFVVIDESARSFVIRIELDGphlppLVLRVHLPPDYPSHSPpifELSAPWLSGEERSElcAELDEIW 80

                        90
                ....*....|....*...
gi 19115314  78 T---GDVCIFSYMDLLKE 92
Cdd:cd23821  81 EenaGEPVLFQWVEWLRE 98
RWD_RNF14 cd23820
RWD domain of RING finger protein 14 (RNF14) and related proteins; RNF14, also called androgen ...
 8-92 4.28e-07

RWD domain of RING finger protein 14 (RNF14) and related proteins; RNF14, also called androgen receptor (AR)-associated protein 54 (ARA54), HFB30, or Triad2 protein, is an RBR-type E3 ubiquitin-protein ligase (EC 2.3.2.31) that is highly expressed in the testis and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3). Its differential localization may play an important role in testicular development and spermatogenesis in humans. RNF14 functions as a transcriptional regulator of mitochondrial and immune function in muscles. It is a ligand-dependent AR co-activator that enhances AR-dependent transcriptional activation. It also may participate in enhancing cell cycle progression and cell proliferation via induction of cyclin D1. Moreover, RNF14 is crucial for colon cancer cell survival. It acts as a new enhancer of Wnt-dependent transcriptional outputs that act at the level of the T-cell factor/lymphoid enhancer factor (TCF/LEF)-beta-catenin complex.


Pssm-ID: 467656 [Multi-domain]  Cd Length: 125  Bit Score: 47.74  E-value: 4.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314   8 QDELLALESIYPSCLLPISEQSFTY-TLSIPDS---------------------------SVRLNIQFPLDYPNSAPTV- 58
Cdd:cd23820   2 EDELEALEAIYPDDLVVDSDSSSGRgSLEIPVElepplsvvlssdgsdegertlkvshlpPITLRFSLPPGYPSTSPPEf 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 19115314  59 -LDAYGIDKTLAEDV---LLSVAT---GDVCIFSYMDLLKE 92
Cdd:cd23820  82 tLECSWLSPEQLSALcerLDELWEengGDVVLFSWIDFLQD 122
RWD_GCN2 cd23823
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called ...
 4-92 8.67e-07

RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called eukaryotic translation initiation factor 2-alpha kinase 4 (EIF2AK4), acts as a metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to low amino acid availability. It also plays a role in modulating the adaptive immune response to yellow fever virus infection and promotes dendritic cells to initiate autophagy and antigene presentation to both CD4(+) and CD8(+) T-cells under amino acid starvation.


Pssm-ID: 467659  Cd Length: 117  Bit Score: 46.83  E-value: 8.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314   4 NEEFQDELLALESIYPSCLLPISE-----QSFTYTLSI-PDS--------SVRLNIQFPLDYPNSAP--TVLDAYGIDKT 67
Cdd:cd23823   1 EEEQEEELEALQSIYGDDFEDLSSkkavwSPPEFRIRLrPQEgeseenhvSVDLHVKFPPTYPDVPPeiELENVKGLSDE 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 19115314  68 LAEDVLLSVAT------GDVCIFSYMDLLKE 92
Cdd:cd23823  81 QLEELLKELEElakellGEEMIFELAEAVQE 111
RWD_YLR419W-like cd23827
RWD domain of Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and related ...
 7-92 6.95e-06

RWD domain of Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and related proteins; YLR419W (EC 3.6.4.13) may act as an ATP-binding RNA helicase. The RWD domain may mediate protein-protein interactions.


Pssm-ID: 467662  Cd Length: 104  Bit Score: 43.77  E-value: 6.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314   7 FQDELLALESIYPSCLLPISEQSFTYTLSIPDS---SVRLNIQFPLDYPNSAPTV-------LDAY---GIDKTLAEDVL 73
Cdd:cd23827   1 WDEEIEALEAIYGEKFEVISDDSCEITLNSPTKtkpSLKLKFYKSSSYPNSLPGIfisssdkLPAYiklAIIRQLLQYAR 80

                        90
                ....*....|....*....
gi 19115314  74 LSvATGDVCIFSYMDLLKE 92
Cdd:cd23827  81 DN-LLGDPMIFSIVEWLEE 98
RWD_RWDD1 cd23816
RWD domain of RWD domain-containing protein 1 (RWDD1) and related proteins; RWDD1, also called ...
 4-95 1.35e-04

RWD domain of RWD domain-containing protein 1 (RWDD1) and related proteins; RWDD1, also called DRG family-regulatory protein 2 (DFRP2), or PTD013, interacts with DRG2 and protects DRG2 from proteolytic degradation. It is an androgen receptor-interacting protein that functions as a coactivator of androgen-dependent transcription.


Pssm-ID: 467652  Cd Length: 118  Bit Score: 40.74  E-value: 1.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314   4 NEEFQDELLALESIYPSCLLPISEQ---SFTYTLSIPDS-------SVRLNIQFPLDYPNSAP--TVLDAYGIDKTLAED 71
Cdd:cd23816   2 KEEQRNELEALESIYPDEFTVLSEEppiSFTITVTSEEEenedetvSVTLKFTYTEKYPDEAPliEIISHENLEDEDIED 81

                        90       100       110
                ....*....|....*....|....*....|....
gi 19115314  72 V---LLSVAT---GDVCIFSYM----DLLKELVD 95
Cdd:cd23816  82 LlelLEQQAEenlGMVMVFTIVsavqEKLNEIVD 115
RWD_DRWD_ELF-like cd11605
RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF ...
 13-85 3.34e-04

RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF domains. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. The RWD domain (named after three major RWD-containing proteins: RING finger, WD-repeat-containing proteins and DEXD-like helicases) mediates protein-protein interactions in a variety of pathways in eukaryotes. The DRWD domain is responsible for substrate binding. It is involved in interactions with other kinetochore proteins. The ELF (N-terminal E2-like fold) domain is found in all Fanconi anemia group L protein (FANCL) homologs. It is required to promote efficient DNA damage-induced FANCD2 (Fanconi anemia group D2 protein) monoubiquitination in vertebrate cells.


Pssm-ID: 467641  Cd Length: 94  Bit Score: 39.09  E-value: 3.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314  13 ALESIYPSCLLPISEQS---FTYTLS----IPDSSVRLNIQFPLDY-PNSAPTVL-----DAYGIDKTLAEDVLLSVAT- 78
Cdd:cd11605   1 ALESIYGDELEVLSDDSplrFSIRLSpeeeEDDPPLELEFTLPPGYpPEEPPLITlrspkLSSAERLSLLKLELEEAAEe 80


                ....*....
gi 19115314  79 --GDVCIFS 85
Cdd:cd11605  81 nlGEPMLFD 89
RWD_RNF25 cd23818
RWD domain of RING finger protein 25 (RNF25) and related proteins; RNF25 (EC 2.3.2.27), also ...
 7-58 6.44e-04

RWD domain of RING finger protein 25 (RNF25) and related proteins; RNF25 (EC 2.3.2.27), also known as AO7, is a putative E3 ubiquitin-protein ligase that was initially identified as an interacting protein of the E2 ubiquitin-conjugating enzyme, Ubc5B. It is ubiquitously expressed in various tissues and is predominantly localized in the nucleus. RNF25 activates nuclear factor (NF)-kappaB-dependent gene expression upon stimulation with interleukin-1 beta (IL-1beta), or tumor necrosis factor (TNF), or overexpression of NF-kappaB-inducing kinase. It interacts with the p65 transactivation domain (TAD) and modulates its transcriptional activity.


Pssm-ID: 467654  Cd Length: 109  Bit Score: 38.29  E-value: 6.44e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115314   7 FQDELLALESIYPSCLLPISEQSFTYTLSI---PDS---------SVRLNIQFPLDYPNSAPTV 58
Cdd:cd23818   1 LEEELEALEAIYPDELKVVSEDGAPTELSItlhPATaddeseqyvRLTLVITLPPGYPEEPPKI 64
DRWD-N_FANCL cd23831
N-terminal double-RWD domain of Fanconi anemia group L protein (FANCL) and related proteins; ...
 14-58 2.41e-03

N-terminal double-RWD domain of Fanconi anemia group L protein (FANCL) and related proteins; FANCL, also called E3 ubiquitin-protein ligase FANCL, Fanconi anemia-associated polypeptide of 43 kDa (FAAP43), or RING-type E3 ubiquitin transferase FANCL, is an E3 ubiquitin-protein ligase component of the Fanconi anemia (FA) core complex which functions in the repair of interstrand crosslinks (ICLs), a toxic form of DNA damage. FANCL, works in conjunction with the E2 conjugating enzyme UBE2T (FANCT) to add a single ubiquitin to specific lysine residues on FANCD2 and FANCI. The mono-ubiquitinated FANCI-FANCD2 complex is thought to recruit downstream DNA-repair proteins for ICL processing. FANCL is composed of an N-terminal E2-like fold (ELF) domain, a novel double-RWD (DRWD) domain, and a C-terminal RING domain predicted to facilitate E2 binding. The DRWD domain is responsible for substrate binding. The model corresponds to the N-terminal DRWD domain (DRWD-N).


Pssm-ID: 467665  Cd Length: 75  Bit Score: 36.03  E-value: 2.41e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 19115314  14 LESIYPSCLLPISEqSFTY-TLSIPDSSVR---LNIQFPLDYPNSAPTV 58
Cdd:cd23831   3 LEAIGWDRVSSIDD-DLSSiTLKIVDSAGRehlLTVKLPSDYPAEPPTC 50
RWD-RWDD4 cd23817
RWD domain of RWD domain-containing protein 4 (RWDD4) and related proteins; RWDD4, also called ...
 8-62 2.73e-03

RWD domain of RWD domain-containing protein 4 (RWDD4) and related proteins; RWDD4, also called protein FAM28A, is a target of the tumor suppressor MicroRNA (MiR)-506 in bladder cancer cells. Downregulation of RWDD4 suppresses bladder cancer cell proliferation, migration and invasion. RWDD4 has also been identified as a modifier of metastasis in human prostate cancer.


Pssm-ID: 467653  Cd Length: 104  Bit Score: 36.72  E-value: 2.73e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115314   8 QDELLALESIYP--SCLLPISEQSFTYTLSIPDS--SVRLNIQFPLDYPNSAPTV-LDAY 62
Cdd:cd23817   1 EEELEVLLSIYEgdENFKQISDTTFQYKYGEDGDpkSFLLEISWPENYPEEPPIInLDAF 60
 
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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