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Conserved domains on  [gi|6680447|ref|NP_032404|]
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protein IMPACT isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UPF0029 pfam01205
Uncharacterized protein family UPF0029;
181-288 1.88e-44

Uncharacterized protein family UPF0029;


:

Pssm-ID: 460111  Cd Length: 105  Bit Score: 147.18  E-value: 1.88e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680447    181 RRSTFQAHVAPVVCPEQVKLVLAKL-YENKKiasATHNIYAYRIFCEDKQtflqDCEDDGETA--AGGRLLHLMEILNVK 257
Cdd:pfam01205   1 KKSKFIAHAAPVESEEEAKAFLEELkKEHKK---ATHNCYAYRIGGEGGE----RSSDDGEPGgtAGKPILEVLEGNGLT 73
                          90       100       110
                  ....*....|....*....|....*....|..
gi 6680447    258 NVMVVVSRWYGGILLGPDRF-KHINNCARNIL 288
Cdd:pfam01205  74 NVLVVVTRYFGGIKLGPGGLvRAYSNAAREAL 105
RWD_IMPACT cd23821
RWD domain of protein IMPACT and related proteins; IMPACT, also imprinted and ancient gene ...
14-113 1.05e-42

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: 142.76  E-value: 1.05e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680447   14 EEIEAMAAIYGEEWCVIDENAKIFCIRVTDFmDDPKWTLCLQVMLPSEYPGTAPPSYQLNAPWLKGQERADLSNSLEEIY 93
Cdd:cd23821   2 EEIEALEAIYGEDFVVIDESARSFVIRIELD-GPHLPPLVLRVHLPPDYPSHSPPIFELSAPWLSGEERSELCAELDEIW 80
                        90       100
                ....*....|....*....|
gi 6680447   94 VHNMGESILYQWVEKIRDAL 113
Cdd:cd23821  81 EENAGEPVLFQWVEWLREYL 100
 
Name Accession Description Interval E-value
UPF0029 pfam01205
Uncharacterized protein family UPF0029;
181-288 1.88e-44

Uncharacterized protein family UPF0029;


Pssm-ID: 460111  Cd Length: 105  Bit Score: 147.18  E-value: 1.88e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680447    181 RRSTFQAHVAPVVCPEQVKLVLAKL-YENKKiasATHNIYAYRIFCEDKQtflqDCEDDGETA--AGGRLLHLMEILNVK 257
Cdd:pfam01205   1 KKSKFIAHAAPVESEEEAKAFLEELkKEHKK---ATHNCYAYRIGGEGGE----RSSDDGEPGgtAGKPILEVLEGNGLT 73
                          90       100       110
                  ....*....|....*....|....*....|..
gi 6680447    258 NVMVVVSRWYGGILLGPDRF-KHINNCARNIL 288
Cdd:pfam01205  74 NVLVVVTRYFGGIKLGPGGLvRAYSNAAREAL 105
RWD_IMPACT cd23821
RWD domain of protein IMPACT and related proteins; IMPACT, also imprinted and ancient gene ...
14-113 1.05e-42

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: 142.76  E-value: 1.05e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680447   14 EEIEAMAAIYGEEWCVIDENAKIFCIRVTDFmDDPKWTLCLQVMLPSEYPGTAPPSYQLNAPWLKGQERADLSNSLEEIY 93
Cdd:cd23821   2 EEIEALEAIYGEDFVVIDESARSFVIRIELD-GPHLPPLVLRVHLPPDYPSHSPPIFELSAPWLSGEERSELCAELDEIW 80
                        90       100
                ....*....|....*....|
gi 6680447   94 VHNMGESILYQWVEKIRDAL 113
Cdd:cd23821  81 EENAGEPVLFQWVEWLREYL 100
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
15-115 7.54e-28

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: 104.36  E-value: 7.54e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680447      15 EIEAMAAIYGEEWCVIDENAKIFCIRVT-----DFMDDPKWTLCLQVMLPSEYPGTAPPSYQLNAPWLKGQERADLSNSL 89
Cdd:smart00591   1 ELEALESIYPEDFEVIDEDARIPEITIKlspssDEGEDQYVSLTLQVKLPENYPDEAPPISLLNSEGLSDEQLAELLKKL 80
                           90       100
                   ....*....|....*....|....*.
gi 6680447      90 EEIYVHNMGESILYQWVEKIRDALIQ 115
Cdd:smart00591  81 EEIAEENLGEVMIFELVEKLQEFLSE 106
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
10-113 1.20e-19

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: 82.37  E-value: 1.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680447     10 QRQSEEIEAMAAIYGEEWCVIDENA-KIFCIRVT------DFMDDPKWTLCLQVMLPSEYPgTAPPSYQLNAPW-LKGQE 81
Cdd:pfam05773   1 EEQEEELEALESIYPDEFEVISDSPyESLEIEIKlsldsdESDSSHLPPLVLKFTLPEDYP-DEPPKISLSSPWnLSDEQ 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 6680447     82 RADLSNSLEEIYVHNMGESILYQWVEKIRDAL 113
Cdd:pfam05773  80 VLSLLEELEELAEENLGEVMIFELIEWLQENL 111
YIH1 COG1739
Putative translation regulator, IMPACT (imprinted ancient) protein family [General function ...
178-273 4.47e-18

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


Pssm-ID: 441345 [Multi-domain]  Cd Length: 198  Bit Score: 80.53  E-value: 4.47e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680447  178 ITDRRSTFQAHVAPVVCPEQVKLVLAKLyeNKKIASATHNIYAYRIFCEDKQtflQDCEDDGE---TAagGR-LLHLMEI 253
Cdd:COG1739  15 IEIKKSRFIAYAAPVESEEEAKAFIAEI--RKEHPDATHNCWAYRIGAPGEI---QRASDDGEpsgTA--GKpILEVLQG 87
                        90       100
                ....*....|....*....|
gi 6680447  254 LNVKNVMVVVSRWYGGILLG 273
Cdd:COG1739  88 RGLTNVLVVVTRYFGGIKLG 107
 
Name Accession Description Interval E-value
UPF0029 pfam01205
Uncharacterized protein family UPF0029;
181-288 1.88e-44

Uncharacterized protein family UPF0029;


Pssm-ID: 460111  Cd Length: 105  Bit Score: 147.18  E-value: 1.88e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680447    181 RRSTFQAHVAPVVCPEQVKLVLAKL-YENKKiasATHNIYAYRIFCEDKQtflqDCEDDGETA--AGGRLLHLMEILNVK 257
Cdd:pfam01205   1 KKSKFIAHAAPVESEEEAKAFLEELkKEHKK---ATHNCYAYRIGGEGGE----RSSDDGEPGgtAGKPILEVLEGNGLT 73
                          90       100       110
                  ....*....|....*....|....*....|..
gi 6680447    258 NVMVVVSRWYGGILLGPDRF-KHINNCARNIL 288
Cdd:pfam01205  74 NVLVVVTRYFGGIKLGPGGLvRAYSNAAREAL 105
RWD_IMPACT cd23821
RWD domain of protein IMPACT and related proteins; IMPACT, also imprinted and ancient gene ...
14-113 1.05e-42

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: 142.76  E-value: 1.05e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680447   14 EEIEAMAAIYGEEWCVIDENAKIFCIRVTDFmDDPKWTLCLQVMLPSEYPGTAPPSYQLNAPWLKGQERADLSNSLEEIY 93
Cdd:cd23821   2 EEIEALEAIYGEDFVVIDESARSFVIRIELD-GPHLPPLVLRVHLPPDYPSHSPPIFELSAPWLSGEERSELCAELDEIW 80
                        90       100
                ....*....|....*....|
gi 6680447   94 VHNMGESILYQWVEKIRDAL 113
Cdd:cd23821  81 EENAGEPVLFQWVEWLREYL 100
RWD smart00591
domain in RING finger and WD repeat containing proteins and DEXDc-like helicases subfamily ...
15-115 7.54e-28

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: 104.36  E-value: 7.54e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680447      15 EIEAMAAIYGEEWCVIDENAKIFCIRVT-----DFMDDPKWTLCLQVMLPSEYPGTAPPSYQLNAPWLKGQERADLSNSL 89
Cdd:smart00591   1 ELEALESIYPEDFEVIDEDARIPEITIKlspssDEGEDQYVSLTLQVKLPENYPDEAPPISLLNSEGLSDEQLAELLKKL 80
                           90       100
                   ....*....|....*....|....*.
gi 6680447      90 EEIYVHNMGESILYQWVEKIRDALIQ 115
Cdd:smart00591  81 EEIAEENLGEVMIFELVEKLQEFLSE 106
RWD pfam05773
RWD domain; This domain was identified in WD40 repeat proteins and Ring finger domain proteins. ...
10-113 1.20e-19

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: 82.37  E-value: 1.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680447     10 QRQSEEIEAMAAIYGEEWCVIDENA-KIFCIRVT------DFMDDPKWTLCLQVMLPSEYPgTAPPSYQLNAPW-LKGQE 81
Cdd:pfam05773   1 EEQEEELEALESIYPDEFEVISDSPyESLEIEIKlsldsdESDSSHLPPLVLKFTLPEDYP-DEPPKISLSSPWnLSDEQ 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 6680447     82 RADLSNSLEEIYVHNMGESILYQWVEKIRDAL 113
Cdd:pfam05773  80 VLSLLEELEELAEENLGEVMIFELIEWLQENL 111
YIH1 COG1739
Putative translation regulator, IMPACT (imprinted ancient) protein family [General function ...
178-273 4.47e-18

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


Pssm-ID: 441345 [Multi-domain]  Cd Length: 198  Bit Score: 80.53  E-value: 4.47e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680447  178 ITDRRSTFQAHVAPVVCPEQVKLVLAKLyeNKKIASATHNIYAYRIFCEDKQtflQDCEDDGE---TAagGR-LLHLMEI 253
Cdd:COG1739  15 IEIKKSRFIAYAAPVESEEEAKAFIAEI--RKEHPDATHNCWAYRIGAPGEI---QRASDDGEpsgTA--GKpILEVLQG 87
                        90       100
                ....*....|....*....|
gi 6680447  254 LNVKNVMVVVSRWYGGILLG 273
Cdd:COG1739  88 RGLTNVLVVVTRYFGGIKLG 107
RWD_RNF14 cd23820
RWD domain of RING finger protein 14 (RNF14) and related proteins; RNF14, also called androgen ...
12-114 9.09e-14

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: 67.00  E-value: 9.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680447   12 QSEEIEAMAAIYGEEwCVIDENAKIFCIRVT---------------DFMDDPKWTLCLQ--------VMLPSEYPGTAPP 68
Cdd:cd23820   1 QEDELEALEAIYPDD-LVVDSDSSSGRGSLEipvelepplsvvlssDGSDEGERTLKVShlppitlrFSLPPGYPSTSPP 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 6680447   69 SYQLNAPWLKGQERADLSNSLEEIYVHNMGESILYQWVEKIRDALI 114
Cdd:cd23820  80 EFTLECSWLSPEQLSALCERLDELWEENGGDVVLFSWIDFLQDEAL 125
RWD_DRWD_ELF-like cd11605
RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF ...
18-109 7.89e-13

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: 63.36  E-value: 7.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680447   18 AMAAIYGEEWCVIDENAKI-FCIRVTDFMDDPKWTLCLQVMLPSEYPGTAPPSYQLNAPWLKGQER-ADLSNSLEEIYVH 95
Cdd:cd11605   1 ALESIYGDELEVLSDDSPLrFSIRLSPEEEEDDPPLELEFTLPPGYPPEEPPLITLRSPKLSSAERlSLLKLELEEAAEE 80
                        90
                ....*....|....
gi 6680447   96 NMGESILYQWVEKI 109
Cdd:cd11605  81 NLGEPMLFDLVEAL 94
RWD_GCN2 cd23823
RWD domain of eIF-2-alpha kinase GCN2 and related proteins; GCN2 (EC 2.7.11.1), also called ...
9-113 4.79e-08

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: 50.68  E-value: 4.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680447    9 SQRQSEEIEAMAAIYGEEWCVIDENAKI-----FCIRVTDFMDDPKW---TLCLQVMLPSEYPgTAPPSYQLNAPwlKG- 79
Cdd:cd23823   1 EEEQEEELEALQSIYGDDFEDLSSKKAVwsppeFRIRLRPQEGESEEnhvSVDLHVKFPPTYP-DVPPEIELENV--KGl 77
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 6680447   80 --QERADLSNSLEEIYVHNMGESILYQWVEKIRDAL 113
Cdd:cd23823  78 sdEQLEELLKELEELAKELLGEEMIFELAEAVQEFL 113
RWD_RNF25 cd23818
RWD domain of RING finger protein 25 (RNF25) and related proteins; RNF25 (EC 2.3.2.27), also ...
13-114 6.69e-06

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: 44.45  E-value: 6.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680447   13 SEEIEAMAAIYGEEWCVIDENA--KIFCIRV---TDFMDDPKWTLC-LQVMLPSEYPGTaPPSYQL-NAPWLKGQERADL 85
Cdd:cd23818   2 EEELEALEAIYPDELKVVSEDGapTELSITLhpaTADDESEQYVRLtLVITLPPGYPEE-PPKISLrNPRGLSDARLARL 80
                        90       100
                ....*....|....*....|....*....
gi 6680447   86 SNSLEEIYVHNMGESILYQWVEKIRDALI 114
Cdd:cd23818  81 LSLLKELAEERAGEPMLFELIELAKEFLT 109
RWD_RWDD3 cd23819
RWD domain of RWD domain-containing protein 3 (RWDD3) and related proteins; RWDD3, also called ...
14-111 1.13e-05

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: 43.47  E-value: 1.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680447   14 EEIEAMAAIYGE--EWCVIDENAKIFCIRVTDFM----DDPKWTLCLQVMLPSEYPGTaPPSYQLNAPWLKGQERADLSN 87
Cdd:cd23819   1 DELSVLQAIFCGpgEFEVLSSSETSDGVSFKIQIsvegFDEDIVLKLTFHLSPNYPSS-LPDISVSSEQLTRAQCNDLQD 79
                        90       100
                ....*....|....*....|....
gi 6680447   88 SLEEIYVHNMGESILYQWVEKIRD 111
Cdd:cd23819  80 SLLEYANSLLGEPMVLELVLWLQE 103
RWD_YLR419W-like cd23827
RWD domain of Saccharomyces cerevisiae putative ATP-dependent RNA helicase YLR419W and related ...
13-67 2.53e-03

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: 36.84  E-value: 2.53e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6680447   13 SEEIEAMAAIYGEEWCVIDENAkiFCIRVTDFMDDPKwTLCLQVMLPSEYPGTAP 67
Cdd:cd23827   2 DEEIEALEAIYGEKFEVISDDS--CEITLNSPTKTKP-SLKLKFYKSSSYPNSLP 53
 
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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