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Conserved domains on  [gi|2420736736|gb|KAJ2259239|]
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hypothetical protein GGI13_000022 [Coemansia sp. RSA 455]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UPF0029 pfam01205
Uncharacterized protein family UPF0029;
198-304 6.01e-34

Uncharacterized protein family UPF0029;


:

Pssm-ID: 460111  Cd Length: 105  Bit Score: 120.22  E-value: 6.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736 198 KKSVFVAHVAQVHSGEDVQAVRDELMRDKKiaQATHNILAYRIRLDNGSICqdnDDDGETA--AGKRLGHLLQLVEAENV 275
Cdd:pfam01205   1 KKSKFIAHAAPVESEEEAKAFLEELKKEHK--KATHNCYAYRIGGEGGERS---SDDGEPGgtAGKPILEVLEGNGLTNV 75
                          90       100       110
                  ....*....|....*....|....*....|
gi 2420736736 276 VVVVTRWFGGTHLGPDRF-KLINNAARQAL 304
Cdd:pfam01205  76 LVVVTRYFGGIKLGPGGLvRAYSNAAREAL 105
RWD_IMPACT cd23821
RWD domain of protein IMPACT and related proteins; IMPACT, also imprinted and ancient gene ...
11-134 4.10e-20

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: 83.44  E-value: 4.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736  11 QDEIVALQAIFGEsaiEMCETAGPQRSFVLHAPLDMCEAR-ASIHIYLPETYPSGDPPIFEWIGAYdsnadsvvdkpgyv 89
Cdd:cd23821     1 AEEIEALEAIYGE---DFVVIDESARSFVIRIELDGPHLPpLVLRVHLPPDYPSHSPPIFELSAPW-------------- 63
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2420736736  90 iprrqlaLSKDMCGDIENELRRAWmEDMCYDVVIFTWITWLDTYL 134
Cdd:cd23821    64 -------LSGEERSELCAELDEIW-EENAGEPVLFQWVEWLREYL 100
 
Name Accession Description Interval E-value
UPF0029 pfam01205
Uncharacterized protein family UPF0029;
198-304 6.01e-34

Uncharacterized protein family UPF0029;


Pssm-ID: 460111  Cd Length: 105  Bit Score: 120.22  E-value: 6.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736 198 KKSVFVAHVAQVHSGEDVQAVRDELMRDKKiaQATHNILAYRIRLDNGSICqdnDDDGETA--AGKRLGHLLQLVEAENV 275
Cdd:pfam01205   1 KKSKFIAHAAPVESEEEAKAFLEELKKEHK--KATHNCYAYRIGGEGGERS---SDDGEPGgtAGKPILEVLEGNGLTNV 75
                          90       100       110
                  ....*....|....*....|....*....|
gi 2420736736 276 VVVVTRWFGGTHLGPDRF-KLINNAARQAL 304
Cdd:pfam01205  76 LVVVTRYFGGIKLGPGGLvRAYSNAAREAL 105
RWD_IMPACT cd23821
RWD domain of protein IMPACT and related proteins; IMPACT, also imprinted and ancient gene ...
11-134 4.10e-20

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: 83.44  E-value: 4.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736  11 QDEIVALQAIFGEsaiEMCETAGPQRSFVLHAPLDMCEAR-ASIHIYLPETYPSGDPPIFEWIGAYdsnadsvvdkpgyv 89
Cdd:cd23821     1 AEEIEALEAIYGE---DFVVIDESARSFVIRIELDGPHLPpLVLRVHLPPDYPSHSPPIFELSAPW-------------- 63
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2420736736  90 iprrqlaLSKDMCGDIENELRRAWmEDMCYDVVIFTWITWLDTYL 134
Cdd:cd23821    64 -------LSGEERSELCAELDEIW-EENAGEPVLFQWVEWLREYL 100
YIH1 COG1739
Putative translation regulator, IMPACT (imprinted ancient) protein family [General function ...
195-310 3.04e-12

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


Pssm-ID: 441345 [Multi-domain]  Cd Length: 198  Bit Score: 64.35  E-value: 3.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736 195 LEMKKSVFVAHVAQVHSGEDVQAVRDELmRdKKIAQATHNILAYRIRLDNGsiCQDNDDDGE---TAA--------GKRL 263
Cdd:COG1739    15 IEIKKSRFIAYAAPVESEEEAKAFIAEI-R-KEHPDATHNCWAYRIGAPGE--IQRASDDGEpsgTAGkpilevlqGRGL 90
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2420736736 264 GHLLQLVeaenvvvvvTRWFGGTHLGpdrfkLIN---NAARQALEAGGFI 310
Cdd:COG1739    91 TNVLVVV---------TRYFGGIKLGag--gLVRaygGAAAEALEAAGIV 129
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
8-134 3.17e-09

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: 53.87  E-value: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736   8 QRQQDEIVALQAIFGESAIEMCETA--GPQRSFVLHAPLDMCEARA----SIHIYLPETYPSgDPPIFewigaydsnadS 81
Cdd:pfam05773   1 EEQEEELEALESIYPDEFEVISDSPyeSLEIEIKLSLDSDESDSSHlpplVLKFTLPEDYPD-EPPKI-----------S 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2420736736  82 VVDKPGyvIPRRQLAlskdmcgDIENELRRAWmEDMCYDVVIFTWITWLDTYL 134
Cdd:pfam05773  69 LSSPWN--LSDEQVL-------SLLEELEELA-EENLGEVMIFELIEWLQENL 111
IMPACT_YIGZ TIGR00257
uncharacterized protein, YigZ family; This uncharacterized protein family includes YigZ, which ...
196-289 6.96e-08

uncharacterized protein, YigZ family; This uncharacterized protein family includes YigZ, which has been crystallized, from E. coli. YigZ is homologous to the protein product of the mouse IMPACT gene. Crystallography shows a two-domain stucture, and the C-terminal domain is suggested to bind nucleic acids. The function is unknown. Note that the ortholog from E. coli was shown fused to the pepQ gene in GenBank entry X54687. This caused occasional misidentification of this protein as pepQ; this family is found in a number of species that lack pepQ. [Unknown function, General]


Pssm-ID: 129359 [Multi-domain]  Cd Length: 204  Bit Score: 52.11  E-value: 6.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736 196 EMKKSVFVAHVAQVHSGEDVQAVRDELmrDKKIAQATHNILAYRIRLDNGSICQDNDDDGETA--AGKRLGHLLQLVEAE 273
Cdd:TIGR00257  16 EIKKSRFITYLAHTEGVDDAKKFIEKI--KKEHPNATHHCVAFVIGAPDDIQQLGFSDDGEPAgtAGKPMLSVLMGSGLG 93
                          90
                  ....*....|....*.
gi 2420736736 274 NVVVVVTRWFGGTHLG 289
Cdd:TIGR00257  94 DITAVVVRYFGGILLG 109
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
13-137 5.99e-07

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: 47.35  E-value: 5.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736   13 EIVALQAIFGESAIEMCETA-GPQRSFVLHAPLDMCE---ARASIHIYLPETYPSGDPPIFEwigaydSNADsvvdkpgy 88
Cdd:smart00591   1 ELEALESIYPEDFEVIDEDArIPEITIKLSPSSDEGEdqyVSLTLQVKLPENYPDEAPPISL------LNSE-------- 66
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2420736736   89 viprrqlALSKDMCGDIENELRRAWMEDMCyDVVIFTWITWLDTYLTEL 137
Cdd:smart00591  67 -------GLSDEQLAELLKKLEEIAEENLG-EVMIFELVEKLQEFLSEF 107
 
Name Accession Description Interval E-value
UPF0029 pfam01205
Uncharacterized protein family UPF0029;
198-304 6.01e-34

Uncharacterized protein family UPF0029;


Pssm-ID: 460111  Cd Length: 105  Bit Score: 120.22  E-value: 6.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736 198 KKSVFVAHVAQVHSGEDVQAVRDELMRDKKiaQATHNILAYRIRLDNGSICqdnDDDGETA--AGKRLGHLLQLVEAENV 275
Cdd:pfam01205   1 KKSKFIAHAAPVESEEEAKAFLEELKKEHK--KATHNCYAYRIGGEGGERS---SDDGEPGgtAGKPILEVLEGNGLTNV 75
                          90       100       110
                  ....*....|....*....|....*....|
gi 2420736736 276 VVVVTRWFGGTHLGPDRF-KLINNAARQAL 304
Cdd:pfam01205  76 LVVVTRYFGGIKLGPGGLvRAYSNAAREAL 105
RWD_IMPACT cd23821
RWD domain of protein IMPACT and related proteins; IMPACT, also imprinted and ancient gene ...
11-134 4.10e-20

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: 83.44  E-value: 4.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736  11 QDEIVALQAIFGEsaiEMCETAGPQRSFVLHAPLDMCEAR-ASIHIYLPETYPSGDPPIFEWIGAYdsnadsvvdkpgyv 89
Cdd:cd23821     1 AEEIEALEAIYGE---DFVVIDESARSFVIRIELDGPHLPpLVLRVHLPPDYPSHSPPIFELSAPW-------------- 63
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2420736736  90 iprrqlaLSKDMCGDIENELRRAWmEDMCYDVVIFTWITWLDTYL 134
Cdd:cd23821    64 -------LSGEERSELCAELDEIW-EENAGEPVLFQWVEWLREYL 100
YIH1 COG1739
Putative translation regulator, IMPACT (imprinted ancient) protein family [General function ...
195-310 3.04e-12

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


Pssm-ID: 441345 [Multi-domain]  Cd Length: 198  Bit Score: 64.35  E-value: 3.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736 195 LEMKKSVFVAHVAQVHSGEDVQAVRDELmRdKKIAQATHNILAYRIRLDNGsiCQDNDDDGE---TAA--------GKRL 263
Cdd:COG1739    15 IEIKKSRFIAYAAPVESEEEAKAFIAEI-R-KEHPDATHNCWAYRIGAPGE--IQRASDDGEpsgTAGkpilevlqGRGL 90
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2420736736 264 GHLLQLVeaenvvvvvTRWFGGTHLGpdrfkLIN---NAARQALEAGGFI 310
Cdd:COG1739    91 TNVLVVV---------TRYFGGIKLGag--gLVRaygGAAAEALEAAGIV 129
RWD_RNF14 cd23820
RWD domain of RING finger protein 14 (RNF14) and related proteins; RNF14, also called androgen ...
10-130 3.51e-10

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: 56.99  E-value: 3.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736  10 QQDEIVALQAIFGESA--------------------------IEMCETAGPQRSFVLHA--PLdmcearaSIHIYLPETY 61
Cdd:cd23820     1 QEDELEALEAIYPDDLvvdsdsssgrgsleipvelepplsvvLSSDGSDEGERTLKVSHlpPI-------TLRFSLPPGY 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2420736736  62 PSGDPPIFE----WigaydsnadsvvdkpgyviprrqlaLSKDMCGDIENELRRAWmEDMCYDVVIFTWITWL 130
Cdd:cd23820    74 PSTSPPEFTlecsW-------------------------LSPEQLSALCERLDELW-EENGGDVVLFSWIDFL 120
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
8-134 3.17e-09

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: 53.87  E-value: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736   8 QRQQDEIVALQAIFGESAIEMCETA--GPQRSFVLHAPLDMCEARA----SIHIYLPETYPSgDPPIFewigaydsnadS 81
Cdd:pfam05773   1 EEQEEELEALESIYPDEFEVISDSPyeSLEIEIKLSLDSDESDSSHlpplVLKFTLPEDYPD-EPPKI-----------S 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2420736736  82 VVDKPGyvIPRRQLAlskdmcgDIENELRRAWmEDMCYDVVIFTWITWLDTYL 134
Cdd:pfam05773  69 LSSPWN--LSDEQVL-------SLLEELEELA-EENLGEVMIFELIEWLQENL 111
RWD_DRWD_ELF-like cd11605
RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF ...
16-130 3.95e-08

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: 50.26  E-value: 3.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736  16 ALQAIFGESAIEMCETAGPQRSFVLHAPLDMCEARASIHIYLPETYPSGDPPIFEwigaydsnadsVVDKPGyvIPRRQL 95
Cdd:cd11605     1 ALESIYGDELEVLSDDSPLRFSIRLSPEEEEDDPPLELEFTLPPGYPPEEPPLIT-----------LRSPKL--SSAERL 67
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2420736736  96 ALSKDMCGDIENELRrawmedmcYDVVIFTWITWL 130
Cdd:cd11605    68 SLLKLELEEAAEENL--------GEPMLFDLVEAL 94
IMPACT_YIGZ TIGR00257
uncharacterized protein, YigZ family; This uncharacterized protein family includes YigZ, which ...
196-289 6.96e-08

uncharacterized protein, YigZ family; This uncharacterized protein family includes YigZ, which has been crystallized, from E. coli. YigZ is homologous to the protein product of the mouse IMPACT gene. Crystallography shows a two-domain stucture, and the C-terminal domain is suggested to bind nucleic acids. The function is unknown. Note that the ortholog from E. coli was shown fused to the pepQ gene in GenBank entry X54687. This caused occasional misidentification of this protein as pepQ; this family is found in a number of species that lack pepQ. [Unknown function, General]


Pssm-ID: 129359 [Multi-domain]  Cd Length: 204  Bit Score: 52.11  E-value: 6.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736 196 EMKKSVFVAHVAQVHSGEDVQAVRDELmrDKKIAQATHNILAYRIRLDNGSICQDNDDDGETA--AGKRLGHLLQLVEAE 273
Cdd:TIGR00257  16 EIKKSRFITYLAHTEGVDDAKKFIEKI--KKEHPNATHHCVAFVIGAPDDIQQLGFSDDGEPAgtAGKPMLSVLMGSGLG 93
                          90
                  ....*....|....*.
gi 2420736736 274 NVVVVVTRWFGGTHLG 289
Cdd:TIGR00257  94 DITAVVVRYFGGILLG 109
RWD_GCN2 cd23823
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called ...
8-137 5.37e-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: 47.60  E-value: 5.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736   8 QRQQDEIVALQAIFGE--SAIEMCETAGPQRSFVLH-----APLDMCEARASIHIYLPETYPSGdPPIFEwigaydsnad 80
Cdd:cd23823     2 EEQEEELEALQSIYGDdfEDLSSKKAVWSPPEFRIRlrpqeGESEENHVSVDLHVKFPPTYPDV-PPEIE---------- 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2420736736  81 svvdkpgyVIPRRQlaLSKDMCGDIENELrRAWMEDMCYDVVIFTWITWLDTYLTEL 137
Cdd:cd23823    71 --------LENVKG--LSDEQLEELLKEL-EELAKELLGEEMIFELAEAVQEFLEEH 116
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
13-137 5.99e-07

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: 47.35  E-value: 5.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736   13 EIVALQAIFGESAIEMCETA-GPQRSFVLHAPLDMCE---ARASIHIYLPETYPSGDPPIFEwigaydSNADsvvdkpgy 88
Cdd:smart00591   1 ELEALESIYPEDFEVIDEDArIPEITIKLSPSSDEGEdqyVSLTLQVKLPENYPDEAPPISL------LNSE-------- 66
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2420736736   89 viprrqlALSKDMCGDIENELRRAWMEDMCyDVVIFTWITWLDTYLTEL 137
Cdd:smart00591  67 -------GLSDEQLAELLKKLEEIAEENLG-EVMIFELVEKLQEFLSEF 107
RWD_ScYIH1-like cd23822
RWD domain of Saccharomyces cerevisiae protein YIH1 and related proteins; YIH1, also called ...
11-134 4.35e-03

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: 36.08  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2420736736  11 QDEIVALQAIFGESAIEmcetAGPQRsFVLHAPLDmceARASIHIYLPETYPSGDPPIFEwigaydsnadsvVDKPGYVI 90
Cdd:cd23822     2 ADEIEAINAIYPDCLVR----LSPSI-YTLKIPDH---EDVSIQLSFPSDYPDEPPHVLG------------VSSSGARG 61
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2420736736  91 PRRQLalsKDMCGDIeneLRRAWMEDmcyDVVIFTWITWLDTYL 134
Cdd:cd23822    62 DGKYL---KDLLEDI---LASVFVPG---EVCLFDFIEELREVL 96
 
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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