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Conserved domains on  [gi|1519315558|ref|NP_056300|]
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RWD domain-containing protein 3 isoform a [Homo sapiens]

Protein Classification

RWD domain-containing protein( domain architecture ID 10651873)

RWD domain-containing protein such as RWD domain-containing protein 3 (RWDD3), also known as RSUME, a RWD-containing protein that enhances SUMO conjugation by interacting with the SUMO conjugase Ubc9, increases Ubc9 thioester formation and therefore favours sumoylation of specific targets

CATH:  3.10.110.10
Gene Ontology:  GO:0005515
PubMed:  26276859|25918163

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RWDD3_C cd24164
RWD domain-containing protein 3, C-terminal domain; RWDD3, also called RSUME, is a small ...
 139-247 6.53e-54

RWD domain-containing protein 3, C-terminal domain; RWDD3, also called RSUME, is a small protein containing an N-terminal RWD domain and a C-terminal domain of unknown function. RWDD3 acts by modulating post-translational modification (PTM) of proteins, and it also plays a role in tumorigenesis. The C-terminal domain is predicted (by AlphaFold) to adopt a fold similar to the C-terminal domain of Prp3, an essential U4/U6 di-snRNP-associated protein which plays a role in pre-mRNA splicing. The Prp3 C-terminal domain is a single-stranded RNA-binding domain.


:

Pssm-ID: 467815  Cd Length: 110  Bit Score: 170.11  E-value: 6.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558 139 LWITLLHLDHMRAKTKYVKIVEKWASDLRLTGRLMFMGKIILILLQGDRNNLKEYLILQKTSKVDVDSSGKKCKEKMISV 218
Cdd:cd24164     1 LETVLLRLDHMRAKAKYVKTLKKWTQELGLTGRLIFYGKLILILLQGTSENIKKYLVRLRTEKVDVDSRGRPCKERMMTV 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1519315558 219 LFETKVQT-EHKRFLAFEVKEYSALDELQK 247
Cdd:cd24164    81 LGERKVPTcEKSGFTEFEVLEPSSLEELLV 110
RWD_RWDD3 cd23819
RWD domain of RWD domain-containing protein 3 (RWDD3) and related proteins; RWDD3, also called ...
 7-112 7.51e-46

RWD domain of RWD domain-containing protein 3 (RWDD3) and related proteins; RWDD3, also called RWD domain-containing sumoylation enhancer (RSUME), acts as an enhancer of SUMO conjugation and has no effect on ubiquitination. It increases protein sumoylation (a dynamic ubiquitin-like post translational modification) of several proteins including HIF1alpha and I-kappa-B, through direct interaction with UBC9. Its RWD domain is required for the sumoylation enhancement activity.


:

Pssm-ID: 467655  Cd Length: 106  Bit Score: 149.40  E-value: 7.51e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558   7 EELSVLAAIFCRPHEWEVLSRSET-DGTVFRIHTKAEGFmDVDIPLELVFHLPVNYPSCLPGISINSEQLTRAQCVTVKE 85
Cdd:cd23819     1 DELSVLQAIFCGPGEFEVLSSSETsDGVSFKIQISVEGF-DEDIVLKLTFHLSPNYPSSLPDISVSSEQLTRAQCNDLQD 79

                          90       100
                  ....*....|....*....|....*..
gi 1519315558  86 NLLEQAESLLSEPMVHELVLWIQQNLR 112
Cdd:cd23819    80 SLLEYANSLLGEPMVLELVLWLQENLL 106
 
Name Accession Description Interval E-value
RWDD3_C cd24164
RWD domain-containing protein 3, C-terminal domain; RWDD3, also called RSUME, is a small ...
 139-247 6.53e-54

RWD domain-containing protein 3, C-terminal domain; RWDD3, also called RSUME, is a small protein containing an N-terminal RWD domain and a C-terminal domain of unknown function. RWDD3 acts by modulating post-translational modification (PTM) of proteins, and it also plays a role in tumorigenesis. The C-terminal domain is predicted (by AlphaFold) to adopt a fold similar to the C-terminal domain of Prp3, an essential U4/U6 di-snRNP-associated protein which plays a role in pre-mRNA splicing. The Prp3 C-terminal domain is a single-stranded RNA-binding domain.


Pssm-ID: 467815  Cd Length: 110  Bit Score: 170.11  E-value: 6.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558 139 LWITLLHLDHMRAKTKYVKIVEKWASDLRLTGRLMFMGKIILILLQGDRNNLKEYLILQKTSKVDVDSSGKKCKEKMISV 218
Cdd:cd24164     1 LETVLLRLDHMRAKAKYVKTLKKWTQELGLTGRLIFYGKLILILLQGTSENIKKYLVRLRTEKVDVDSRGRPCKERMMTV 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1519315558 219 LFETKVQT-EHKRFLAFEVKEYSALDELQK 247
Cdd:cd24164    81 LGERKVPTcEKSGFTEFEVLEPSSLEELLV 110
RWD_RWDD3 cd23819
RWD domain of RWD domain-containing protein 3 (RWDD3) and related proteins; RWDD3, also called ...
 7-112 7.51e-46

RWD domain of RWD domain-containing protein 3 (RWDD3) and related proteins; RWDD3, also called RWD domain-containing sumoylation enhancer (RSUME), acts as an enhancer of SUMO conjugation and has no effect on ubiquitination. It increases protein sumoylation (a dynamic ubiquitin-like post translational modification) of several proteins including HIF1alpha and I-kappa-B, through direct interaction with UBC9. Its RWD domain is required for the sumoylation enhancement activity.


Pssm-ID: 467655  Cd Length: 106  Bit Score: 149.40  E-value: 7.51e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558   7 EELSVLAAIFCRPHEWEVLSRSET-DGTVFRIHTKAEGFmDVDIPLELVFHLPVNYPSCLPGISINSEQLTRAQCVTVKE 85
Cdd:cd23819     1 DELSVLQAIFCGPGEFEVLSSSETsDGVSFKIQISVEGF-DEDIVLKLTFHLSPNYPSSLPDISVSSEQLTRAQCNDLQD 79

                          90       100
                  ....*....|....*....|....*..
gi 1519315558  86 NLLEQAESLLSEPMVHELVLWIQQNLR 112
Cdd:cd23819    80 SLLEYANSLLGEPMVLELVLWLQENLL 106
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
 8-114 1.97e-20

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: 83.56  E-value: 1.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558    8 ELSVLAAIFCRPHEWEVLSRSETDgTVFRIHTKAEGFMDVDIPLELVFHLPVNYPSCLPGISINSEQ-LTRAQCVTVKEN 86
Cdd:smart00591   1 ELEALESIYPEDFEVIDEDARIPE-ITIKLSPSSDEGEDQYVSLTLQVKLPENYPDEAPPISLLNSEgLSDEQLAELLKK 79

                           90       100
                   ....*....|....*....|....*...
gi 1519315558   87 LLEQAESLLSEPMVHELVLWIQQNLRHI 114
Cdd:smart00591  80 LEEIAEENLGEVMIFELVEKLQEFLSEF 107
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
 3-111 3.23e-18

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: 77.75  E-value: 3.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558   3 EPVQEELSVLAAIFcrPHEWEVLSRSETDGTVFRIHTK---AEGFMDVDIPLELVFHLPVNYPSCLPGISINSEQ-LTRA 78
Cdd:pfam05773   1 EEQEEELEALESIY--PDEFEVISDSPYESLEIEIKLSldsDESDSSHLPPLVLKFTLPEDYPDEPPKISLSSPWnLSDE 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1519315558  79 QCVTVKENLLEQAESLLSEPMVHELVLWIQQNL 111
Cdd:pfam05773  79 QVLSLLEELEELAEENLGEVMIFELIEWLQENL 111
 
Name Accession Description Interval E-value
RWDD3_C cd24164
RWD domain-containing protein 3, C-terminal domain; RWDD3, also called RSUME, is a small ...
 139-247 6.53e-54

RWD domain-containing protein 3, C-terminal domain; RWDD3, also called RSUME, is a small protein containing an N-terminal RWD domain and a C-terminal domain of unknown function. RWDD3 acts by modulating post-translational modification (PTM) of proteins, and it also plays a role in tumorigenesis. The C-terminal domain is predicted (by AlphaFold) to adopt a fold similar to the C-terminal domain of Prp3, an essential U4/U6 di-snRNP-associated protein which plays a role in pre-mRNA splicing. The Prp3 C-terminal domain is a single-stranded RNA-binding domain.


Pssm-ID: 467815  Cd Length: 110  Bit Score: 170.11  E-value: 6.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558 139 LWITLLHLDHMRAKTKYVKIVEKWASDLRLTGRLMFMGKIILILLQGDRNNLKEYLILQKTSKVDVDSSGKKCKEKMISV 218
Cdd:cd24164     1 LETVLLRLDHMRAKAKYVKTLKKWTQELGLTGRLIFYGKLILILLQGTSENIKKYLVRLRTEKVDVDSRGRPCKERMMTV 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1519315558 219 LFETKVQT-EHKRFLAFEVKEYSALDELQK 247
Cdd:cd24164    81 LGERKVPTcEKSGFTEFEVLEPSSLEELLV 110
RWD_RWDD3 cd23819
RWD domain of RWD domain-containing protein 3 (RWDD3) and related proteins; RWDD3, also called ...
 7-112 7.51e-46

RWD domain of RWD domain-containing protein 3 (RWDD3) and related proteins; RWDD3, also called RWD domain-containing sumoylation enhancer (RSUME), acts as an enhancer of SUMO conjugation and has no effect on ubiquitination. It increases protein sumoylation (a dynamic ubiquitin-like post translational modification) of several proteins including HIF1alpha and I-kappa-B, through direct interaction with UBC9. Its RWD domain is required for the sumoylation enhancement activity.


Pssm-ID: 467655  Cd Length: 106  Bit Score: 149.40  E-value: 7.51e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558   7 EELSVLAAIFCRPHEWEVLSRSET-DGTVFRIHTKAEGFmDVDIPLELVFHLPVNYPSCLPGISINSEQLTRAQCVTVKE 85
Cdd:cd23819     1 DELSVLQAIFCGPGEFEVLSSSETsDGVSFKIQISVEGF-DEDIVLKLTFHLSPNYPSSLPDISVSSEQLTRAQCNDLQD 79

                          90       100
                  ....*....|....*....|....*..
gi 1519315558  86 NLLEQAESLLSEPMVHELVLWIQQNLR 112
Cdd:cd23819    80 SLLEYANSLLGEPMVLELVLWLQENLL 106
Prp3_C-like cd24140
C-terminal domain of Prp3 and related proteins; This group contains the C-terminal domains of ...
 139-246 5.96e-41

C-terminal domain of Prp3 and related proteins; This group contains the C-terminal domains of Prp3 and RWD domain-containing proteins 2/3. Predicted structures (by AlphaFold) of the C-terminal domains of RWDD2 and RWDD3 reveal similarity to the C-terminal domain of Prp3, an essential U4/U6 di-snRNP-associated protein which plays a role in pre-mRNA splicing. The Prp3 C-terminal domain is a single-stranded RNA-binding domain.


Pssm-ID: 467812  Cd Length: 117  Bit Score: 137.01  E-value: 5.96e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558 139 LWITLLHLDHMRAKTKYVKIVEKWASdLRLTGRLMFMGKIILILLQGDRNNLKEYLILQKTSKVDVDSSGK--------K 210
Cdd:cd24140     1 YHCKVFHFKHLQNKKKRFKIKENSKE-LSLKGLCMRIRDPGIIIVVGNEKSCKEYENLVKKRKWNEDFELHtntgdikeK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1519315558 211 CKEKMISVLFETKVQT--EHKRFLAFEVKEYSALDELQ 246
Cdd:cd24140    80 CHNNSISKTWEGYLQDckFKGWFLKVCNDQYSLLRTLG 117
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
 8-114 1.97e-20

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: 83.56  E-value: 1.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558    8 ELSVLAAIFCRPHEWEVLSRSETDgTVFRIHTKAEGFMDVDIPLELVFHLPVNYPSCLPGISINSEQ-LTRAQCVTVKEN 86
Cdd:smart00591   1 ELEALESIYPEDFEVIDEDARIPE-ITIKLSPSSDEGEDQYVSLTLQVKLPENYPDEAPPISLLNSEgLSDEQLAELLKK 79

                           90       100
                   ....*....|....*....|....*...
gi 1519315558   87 LLEQAESLLSEPMVHELVLWIQQNLRHI 114
Cdd:smart00591  80 LEEIAEENLGEVMIFELVEKLQEFLSEF 107
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
 3-111 3.23e-18

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: 77.75  E-value: 3.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558   3 EPVQEELSVLAAIFcrPHEWEVLSRSETDGTVFRIHTK---AEGFMDVDIPLELVFHLPVNYPSCLPGISINSEQ-LTRA 78
Cdd:pfam05773   1 EEQEEELEALESIY--PDEFEVISDSPYESLEIEIKLSldsDESDSSHLPPLVLKFTLPEDYPDEPPKISLSSPWnLSDE 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1519315558  79 QCVTVKENLLEQAESLLSEPMVHELVLWIQQNL 111
Cdd:pfam05773  79 QVLSLLEELEELAEENLGEVMIFELIEWLQENL 111
RWD_GCN2 cd23823
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called ...
 6-114 7.42e-13

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: 63.39  E-value: 7.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558   6 QEELSVLAAIFcrPHEWEVLSRSETDG--TVFRIHTKAEGFMD--VDIPLELVFHLPVNYPSCLPGISI-NSEQLTRAQC 80
Cdd:cd23823     5 EEELEALQSIY--GDDFEDLSSKKAVWspPEFRIRLRPQEGESeeNHVSVDLHVKFPPTYPDVPPEIELeNVKGLSDEQL 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1519315558  81 VTVKENLLEQAESLLSEPMVHELVLWIQQNLRHI 114
Cdd:cd23823    83 EELLKELEELAKELLGEEMIFELAEAVQEFLEEH 116
RWD_DRWD_ELF-like cd11605
RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF ...
 11-107 1.08e-10

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: 57.19  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558  11 VLAAIFcrPHEWEVLSrsETDGTVFRIHTKAEgFMDVDIPLELVFHLPVNY-PSCLPGISINSEQLTRAQCVTV-KENLL 88
Cdd:cd11605     1 ALESIY--GDELEVLS--DDSPLRFSIRLSPE-EEEDDPPLELEFTLPPGYpPEEPPLITLRSPKLSSAERLSLlKLELE 75

                          90
                  ....*....|....*....
gi 1519315558  89 EQAESLLSEPMVHELVLWI 107
Cdd:cd11605    76 EAAEENLGEPMLFDLVEAL 94
RWD_RNF25 cd23818
RWD domain of RING finger protein 25 (RNF25) and related proteins; RNF25 (EC 2.3.2.27), also ...
 5-104 3.28e-10

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: 56.01  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558   5 VQEELSVLAAIFcrPHEWEVLSRSEtDGTVFRIHTK---AEGFMDVDIPLELVFHLPVNYPSCLPGISI-NSEQLTRAQC 80
Cdd:cd23818     1 LEEELEALEAIY--PDELKVVSEDG-APTELSITLHpatADDESEQYVRLTLVITLPPGYPEEPPKISLrNPRGLSDARL 77

                          90       100
                  ....*....|....*....|....
gi 1519315558  81 VTVKENLLEQAESLLSEPMVHELV 104
Cdd:cd23818    78 ARLLSLLKELAEERAGEPMLFELI 101
RWD_RWDD2 cd23829
RWD domain of RWD domain-containing protein 2A (RWDD2A), 2B (RWDD2B) and related proteins; ...
 7-111 5.10e-10

RWD domain of RWD domain-containing protein 2A (RWDD2A), 2B (RWDD2B) and related proteins; This subfamily includes RWDD2A, previously known as RWD domain-containing 2 (RWDD2) and RWDD2B, previously known in humans as chromosome 21 open reading frame (C21orf6). C21orf6 appears to be involved in monosomy 21 phenotype. The RWD domain may mediate protein-protein interactions.


Pssm-ID: 467663  Cd Length: 129  Bit Score: 56.04  E-value: 5.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558   7 EELSVLAAIFCRP-----HEWEVLS------RSETDGTV-----FRIHTKAEGfmdVDIPLELVFHLPVNYPSCLPGISI 70
Cdd:cd23829     7 SEIEMLQSMFPNEgelklDDPSAVAdlkrflEGDTDSPLpsrleFTINLKIEE---PKVKVELSVTLPHEYPSVPPEIFV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1519315558  71 NSEQLTRAQCVTVKENLLEQAESLLS-EPMVHELVLWIQQNL 111
Cdd:cd23829    84 RSDSLSRSQQRQLNEDLSEYISSLERgELCILQIVQWLQDNA 125
RWD_YLR419W-like cd23827
RWD domain of Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and related ...
 6-115 8.24e-09

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: 52.25  E-value: 8.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558   6 QEELSVLAAIFcrPHEWEVLSRSEtdgtvFRIhtKAEGFMDVDIPLELVFHLPVNYPSCLPGISINSEQL----TRAQCV 81
Cdd:cd23827     2 DEEIEALEAIY--GEKFEVISDDS-----CEI--TLNSPTKTKPSLKLKFYKSSSYPNSLPGIFISSSDKlpayIKLAII 72

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1519315558  82 tvkENLLEQA-ESLLSEPMVHELVLWIQQNLRHIL 115
Cdd:cd23827    73 ---RQLLQYArDNLLGDPMIFSIVEWLEENIEEII 104
RWD_IMPACT cd23821
RWD domain of protein IMPACT and related proteins; IMPACT, also imprinted and ancient gene ...
 6-111 7.04e-08

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: 49.54  E-value: 7.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558   6 QEELSVLAAIFcrPHEWEVLSRSETdgtVFRIHTKAEGfmDVDIPLELVFHLPVNYPS-CLPGISINSEQLTRAQCVTVK 84
Cdd:cd23821     1 AEEIEALEAIY--GEDFVVIDESAR---SFVIRIELDG--PHLPPLVLRVHLPPDYPShSPPIFELSAPWLSGEERSELC 73

                          90       100
                  ....*....|....*....|....*..
gi 1519315558  85 ENLLEQAESLLSEPMVHELVLWIQQNL 111
Cdd:cd23821    74 AELDEIWEENAGEPVLFQWVEWLREYL 100
RWD_RWDD1 cd23816
RWD domain of RWD domain-containing protein 1 (RWDD1) and related proteins; RWDD1, also called ...
 6-117 9.07e-06

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: 43.82  E-value: 9.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558   6 QEELSVLAAIFcrPHEWEVLSRSetDGTVFRIHTKAEGFMDVDIPLE--LVFHLPVNYPSCLPGISINS-EQLTRAQCVT 82
Cdd:cd23816     6 RNELEALESIY--PDEFTVLSEE--PPISFTITVTSEEEENEDETVSvtLKFTYTEKYPDEAPLIEIIShENLEDEDIED 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1519315558  83 VKENLLEQAESLLSEPMVHELVLWIQQNLRHILSQ 117
Cdd:cd23816    82 LLELLEQQAEENLGMVMVFTIVSAVQEKLNEIVDQ 116
RWD_RNF14 cd23820
RWD domain of RING finger protein 14 (RNF14) and related proteins; RNF14, also called androgen ...
 6-106 1.40e-04

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: 40.81  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558   6 QEELSVLAAIFcrpHEWEVLSRSETDGTV---------------FRIHTKAEGFMDVDI----PLELVFHLPVNYPSCL- 65
Cdd:cd23820     2 EDELEALEAIY---PDDLVVDSDSSSGRGsleipvelepplsvvLSSDGSDEGERTLKVshlpPITLRFSLPPGYPSTSp 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1519315558  66 PGISINSEQLTRAQCVTVKENLLEqaeslLSEPMVHELVLW 106
Cdd:cd23820    79 PEFTLECSWLSPEQLSALCERLDE-----LWEENGGDVVLF 114
RWDD2_C cd24163
C-terminal domain of RWD domain-containing protein 2; RWDD2A, as well as RWDD2B, are small ...
 139-261 1.72e-04

C-terminal domain of RWD domain-containing protein 2; RWDD2A, as well as RWDD2B, are small proteins that contain an N-terminal RWD domain and a C-terminal domain of unknown function. The C-terminal domain is predicted (by AlphaFold) to adopt a fold similar to the C-terminal domain of Prp3, an essential U4/U6 di-snRNP-associated protein which plays a role in pre-mRNA splicing. The Prp3 C-terminal domain is a single-stranded RNA-binding domain.


Pssm-ID: 467814  Cd Length: 122  Bit Score: 40.32  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558 139 LWItLLHldHMRAKTKYVKIVEkWASDLRLTGRLMFmGKIILILLQGDRNNLKEYL-ILQKTSKvdvdssgKKCK---EK 214
Cdd:cd24163     4 RWI-YSH--HIYSKKKRKDIVE-WAKELGLTGFSKP-GKPGVICVEGDEEDVDEYVrRIRRLRW-------KKIQvrgEE 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1519315558 215 MISVLFETKVQTEHKRFLAFEVKEY--SALDELQKEFETAGLKKLFSEF 261
Cdd:cd24163    72 VIEVPRFFGEEEDEERALPGGFRELheDLMGELAAFLEEAGLEELFLTL 120
RWD-RWDD4 cd23817
RWD domain of RWD domain-containing protein 4 (RWDD4) and related proteins; RWDD4, also called ...
 6-111 4.26e-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: 35.95  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315558   6 QEELSVLAAIFcrphEWEVLSRSETDGTV-FRI----HTKAegFMdvdipLELVFhlPVNYPSCLPGISINS---EQLTR 77
Cdd:cd23817     1 EEELEVLLSIY----EGDENFKQISDTTFqYKYgedgDPKS--FL-----LEISW--PENYPEEPPIINLDAfynKHISS 67

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1519315558  78 AQCVTVKENLLEQAESLLSEPMVHELVLWIQQNL 111
Cdd:cd23817    68 SVKEKIVSKLNEEAEQNLGSAMTYTLFEWAKENA 101
 
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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