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Conserved domains on  [gi|665402799|ref|NP_001286723|]
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quaking related 58E-1, isoform C [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KH-I_KHDRBS cd22384
type I K homology (KH) RNA-binding domain found in the KH domain-containing, RNA-binding, ...
109-210 6.34e-56

type I K homology (KH) RNA-binding domain found in the KH domain-containing, RNA-binding, signal transduction-associated protein (KHDRBS) family; The KHDRBS family includes three members, KHDRBS1-3. KHDRBS1, also called GAP-associated tyrosine phosphoprotein p62, or Src-associated in mitosis 68 kDa protein, or Sam68, or p21 Ras GTPase-activating protein-associated p62, or p68, is an RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. It binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. It also binds poly(A). KHDRBS1 acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. It is recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. KHDRBS2, also called Sam68-like mammalian protein 1, or SLM-1, is an RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. It binds both poly(A) and poly(U) homopolymers. KHDRBS2 may function as an adapter protein for Src kinases during mitosis. KHDRBS3, also called RNA-binding protein T-Star, or Sam68-like mammalian protein 2, or SLM-2, or Sam68-like phosphotyrosine protein, is an RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. It binds optimally to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. It also binds poly(A). KHDRBS3 may play a role as a negative regulator of cell growth.


:

Pssm-ID: 411812 [Multi-domain]  Cd Length: 102  Bit Score: 177.86  E-value: 6.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402799 109 KPIRVAQKVLFPIKEYPKFNFVGKILGPKGNTLRQLQEETMCKMVVMGRNSMRDHGKEEELRSSGNPKYAHLSRDLHVEI 188
Cdd:cd22384    1 KPIKLSEKVLIPVKEFPKFNFVGKLLGPRGNTLKRLQEETGTKMSILGKGSMRDKAKEEELRKSGDPKYAHLNEDLHVLI 80
                         90       100
                 ....*....|....*....|..
gi 665402799 189 STVAPPAEAYHRISYALGEIRK 210
Cdd:cd22384   81 EAFAPPAEAYARLAHALAELRK 102
 
Name Accession Description Interval E-value
KH-I_KHDRBS cd22384
type I K homology (KH) RNA-binding domain found in the KH domain-containing, RNA-binding, ...
109-210 6.34e-56

type I K homology (KH) RNA-binding domain found in the KH domain-containing, RNA-binding, signal transduction-associated protein (KHDRBS) family; The KHDRBS family includes three members, KHDRBS1-3. KHDRBS1, also called GAP-associated tyrosine phosphoprotein p62, or Src-associated in mitosis 68 kDa protein, or Sam68, or p21 Ras GTPase-activating protein-associated p62, or p68, is an RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. It binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. It also binds poly(A). KHDRBS1 acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. It is recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. KHDRBS2, also called Sam68-like mammalian protein 1, or SLM-1, is an RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. It binds both poly(A) and poly(U) homopolymers. KHDRBS2 may function as an adapter protein for Src kinases during mitosis. KHDRBS3, also called RNA-binding protein T-Star, or Sam68-like mammalian protein 2, or SLM-2, or Sam68-like phosphotyrosine protein, is an RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. It binds optimally to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. It also binds poly(A). KHDRBS3 may play a role as a negative regulator of cell growth.


Pssm-ID: 411812 [Multi-domain]  Cd Length: 102  Bit Score: 177.86  E-value: 6.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402799 109 KPIRVAQKVLFPIKEYPKFNFVGKILGPKGNTLRQLQEETMCKMVVMGRNSMRDHGKEEELRSSGNPKYAHLSRDLHVEI 188
Cdd:cd22384    1 KPIKLSEKVLIPVKEFPKFNFVGKLLGPRGNTLKRLQEETGTKMSILGKGSMRDKAKEEELRKSGDPKYAHLNEDLHVLI 80
                         90       100
                 ....*....|....*....|..
gi 665402799 189 STVAPPAEAYHRISYALGEIRK 210
Cdd:cd22384   81 EAFAPPAEAYARLAHALAELRK 102
MSL5 COG5176
Splicing factor (branch point binding protein) [RNA processing and modification];
80-185 3.08e-11

Splicing factor (branch point binding protein) [RNA processing and modification];


Pssm-ID: 227503 [Multi-domain]  Cd Length: 269  Bit Score: 63.06  E-value: 3.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402799  80 KRLLDDEVEKILVSGRIPKPEIYANVYsEKPIRVAQKVLFPIKEYPKFNFVGKILGPKGNTLRQLQEETMCKMVVMGRNS 159
Cdd:COG5176  116 KKLEDERLWLKERAQKILPRFVLPNDY-IRPSKYQNKIYIPVQEYPESNFVGLLIGPRGSTLKQLERISRAKIAIRGSGS 194
                         90       100
                 ....*....|....*....|....*.
gi 665402799 160 MrdhgKEEELRSSGNPKYAHLSRDLH 185
Cdd:COG5176  195 V----KEGKISSDTPESLKNAEAVLH 216
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
128-176 3.95e-06

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 43.81  E-value: 3.95e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 665402799  128 NFVGKILGPKGNTLRQLQEETMCKMVVMGRNsmrDHGKEEELRSSGNPK 176
Cdd:pfam00013   9 SLVGLIIGKGGSNIKEIREETGAKIQIPPSE---SEGNERIVTITGTPE 54
KH smart00322
K homology RNA-binding domain;
128-163 4.93e-06

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 43.82  E-value: 4.93e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 665402799   128 NFVGKILGPKGNTLRQLQEETMCKMVVMGRNSMRDH 163
Cdd:smart00322  12 DKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERV 47
 
Name Accession Description Interval E-value
KH-I_KHDRBS cd22384
type I K homology (KH) RNA-binding domain found in the KH domain-containing, RNA-binding, ...
109-210 6.34e-56

type I K homology (KH) RNA-binding domain found in the KH domain-containing, RNA-binding, signal transduction-associated protein (KHDRBS) family; The KHDRBS family includes three members, KHDRBS1-3. KHDRBS1, also called GAP-associated tyrosine phosphoprotein p62, or Src-associated in mitosis 68 kDa protein, or Sam68, or p21 Ras GTPase-activating protein-associated p62, or p68, is an RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. It binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. It also binds poly(A). KHDRBS1 acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. It is recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. KHDRBS2, also called Sam68-like mammalian protein 1, or SLM-1, is an RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. It binds both poly(A) and poly(U) homopolymers. KHDRBS2 may function as an adapter protein for Src kinases during mitosis. KHDRBS3, also called RNA-binding protein T-Star, or Sam68-like mammalian protein 2, or SLM-2, or Sam68-like phosphotyrosine protein, is an RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. It binds optimally to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. It also binds poly(A). KHDRBS3 may play a role as a negative regulator of cell growth.


Pssm-ID: 411812 [Multi-domain]  Cd Length: 102  Bit Score: 177.86  E-value: 6.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402799 109 KPIRVAQKVLFPIKEYPKFNFVGKILGPKGNTLRQLQEETMCKMVVMGRNSMRDHGKEEELRSSGNPKYAHLSRDLHVEI 188
Cdd:cd22384    1 KPIKLSEKVLIPVKEFPKFNFVGKLLGPRGNTLKRLQEETGTKMSILGKGSMRDKAKEEELRKSGDPKYAHLNEDLHVLI 80
                         90       100
                 ....*....|....*....|..
gi 665402799 189 STVAPPAEAYHRISYALGEIRK 210
Cdd:cd22384   81 EAFAPPAEAYARLAHALAELRK 102
KH-I_KHDRBS2 cd22469
type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal ...
107-224 4.23e-46

type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal transduction-associated protein 2 (KHDRBS2) and similar proteins; KHDRBS2, also called Sam68-like mammalian protein 1, or SLM-1, is an RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. It binds both poly(A) and poly(U) homopolymers. KHDRBS2 may function as an adapter protein for Src kinases during mitosis.


Pssm-ID: 411897 [Multi-domain]  Cd Length: 118  Bit Score: 153.35  E-value: 4.23e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402799 107 SEKPIRVAQKVLFPIKEYPKFNFVGKILGPKGNTLRQLQEETMCKMVVMGRNSMRDHGKEEELRSSGNPKYAHLSRDLHV 186
Cdd:cd22469    1 SNKNIKLSERVLIPVKQYPKFNFVGKLLGPRGNSLKRLQEETGAKMSILGKGSMRDKAKEEELRKSGEAKYAHLSDELHV 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 665402799 187 EISTVAPPAEAYHRISYALGEIRKFMIPDANDDIRLEQ 224
Cdd:cd22469   81 LIEVFAPPGEAYSRMSHALEEIKKFLVPDYNDEIRQEQ 118
KH-I_KHDRBS1 cd22468
type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal ...
109-214 5.04e-44

type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal transduction-associated protein 1 (KHDRBS1) and similar proteins; KHDRBS1, also called GAP-associated tyrosine phosphoprotein p62, or Src-associated in mitosis 68 kDa protein, or Sam68, or p21 Ras GTPase-activating protein-associated p62, or p68, is an RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. It binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. It also binds poly(A). KHDRBS1 acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. It is recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors.


Pssm-ID: 411896 [Multi-domain]  Cd Length: 106  Bit Score: 147.47  E-value: 5.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402799 109 KPIRVAQKVLFPIKEYPKFNFVGKILGPKGNTLRQLQEETMCKMVVMGRNSMRDHGKEEELRSSGNPKYAHLSRDLHVEI 188
Cdd:cd22468    1 KNMKLKERILIPVKQYPKFNFVGKILGPQGNTIKRLQEETGAKISVLGKGSMRDKAKEEELRKGGDPKYAHLNMDLHVFI 80
                         90       100
                 ....*....|....*....|....*.
gi 665402799 189 STVAPPAEAYHRISYALGEIRKFMIP 214
Cdd:cd22468   81 EVFGPPCEAYARMAHAMEEVKKFLVP 106
KH-I_KHDRBS3 cd22470
type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal ...
105-217 1.36e-41

type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal transduction-associated protein 3 (KHDRBS3) and similar proteins; KHDRBS3, also called RNA-binding protein T-Star, or Sam68-like mammalian protein 2, or SLM-2, or Sam68-like phosphotyrosine protein, is an RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. It binds optimally to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. It also binds poly(A). KHDRBS3 may play a role as a negative regulator of cell growth.


Pssm-ID: 411898 [Multi-domain]  Cd Length: 113  Bit Score: 141.34  E-value: 1.36e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402799 105 VYSEKPIRVAQKVLFPIKEYPKFNFVGKILGPKGNTLRQLQEETMCKMVVMGRNSMRDHGKEEELRSSGNPKYAHLSRDL 184
Cdd:cd22470    1 VVINKNMKLGQKVLIPVKQFPKFNFVGKLLGPRGNSLKRLQEETLTKMSILGKGSMRDKAKEEELRKSGEAKYFHLNDDL 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 665402799 185 HVEISTVAPPAEAYHRISYALGEIRKFMIPDAN 217
Cdd:cd22470   81 HVLIEVFAPPAEAYARMGHALEEIKKFLIPDYN 113
KH-I_Hqk_like cd22383
type I K homology (KH) RNA-binding domain found in protein quaking (Hqk) family; The Hqk ...
116-214 3.31e-31

type I K homology (KH) RNA-binding domain found in protein quaking (Hqk) family; The Hqk family includes Hqk and protein held out wings (how) found in Drosophila. Hqk, also called HqkI, is an RNA-binding protein that plays a central role in myelinization. It binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core sequence and regulates target mRNA stability. It acts by regulating pre-mRNA splicing, mRNA export and protein translation. Hqk is a regulator of oligodendrocyte differentiation and maturation in the brain that may play a role in myelin and oligodendrocyte dysfunction in schizophrenia. How, also called KH domain protein KH93F, or protein muscle-specific, or protein Struthio, or protein wings held out (who), or Quaking-related 93F (qkr93F), is an RNA-binding protein involved in the control of muscular and cardiac activity. It is required for integrin-mediated cell-adhesion in wing blade. It plays essential roles during embryogenesis, in late stages of somatic muscle development, for myotube migration and during metamorphosis for muscle reorganization.


Pssm-ID: 411811 [Multi-domain]  Cd Length: 101  Bit Score: 113.61  E-value: 3.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402799 116 KVLFPIKEYPKFNFVGKILGPKGNTLRQLQEETMCKMVVMGRNSMRDHGKEEELRssGNPKYAHLSRDLHVEISTVAPPA 195
Cdd:cd22383    5 KVYVPVDEYPDYNFVGRILGPRGMTAKQLEQDTGCKIMIRGKGSMRDKKKEEANR--GKPNWEHLNDDLHVLITVEDTEN 82
                         90
                 ....*....|....*....
gi 665402799 196 EAYHRISYALGEIRKFMIP 214
Cdd:cd22383   83 RAHIKLAKAVEEVKKLLIP 101
KH-I_HOW cd22466
type I K homology (KH) RNA-binding domain found in Drosophila protein held out wings (how) and ...
110-214 2.03e-28

type I K homology (KH) RNA-binding domain found in Drosophila protein held out wings (how) and similar proteins; How, also called KH domain protein KH93F, or protein muscle-specific, or protein Struthio, or protein wings held out (who), or Quaking-related 93F (qkr93F), is an RNA-binding protein involved in the control of muscular and cardiac activity. It is required for integrin-mediated cell-adhesion in wing blade. It plays essential roles during embryogenesis, in late stages of somatic muscle development, for myotube migration and during metamorphosis for muscle reorganization.


Pssm-ID: 411894 [Multi-domain]  Cd Length: 105  Bit Score: 106.54  E-value: 2.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402799 110 PIRVAQKVLFPIKEYPKFNFVGKILGPKGNTLRQLQEETMCKMVVMGRNSMRDHGKEEELRssGNPKYAHLSRDLHVEIS 189
Cdd:cd22466    3 SVTLSEKVYVPVKEHPDYNFVGRILGPRGMTAKQLEQETGCKIMVRGKGSMRDKKKEDLNR--GKPNWEHLNDELHVLIT 80
                         90       100
                 ....*....|....*....|....*
gi 665402799 190 TVAPPAEAYHRISYALGEIRKFMIP 214
Cdd:cd22466   81 VEDTENRAKVKLQRAVEEVRKLLVP 105
KH-I_Hqk cd22465
type I K homology (KH) RNA-binding domain found in protein quaking (Hqk) and similar proteins; ...
112-216 3.98e-27

type I K homology (KH) RNA-binding domain found in protein quaking (Hqk) and similar proteins; Hqk, also called HqkI, is an RNA-binding protein that plays a central role in myelinization. It binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core sequence and regulates target mRNA stability. It acts by regulating pre-mRNA splicing, mRNA export and protein translation. Hqk is a regulator of oligodendrocyte differentiation and maturation in the brain that may play a role in myelin and oligodendrocyte dysfunction in schizophrenia.


Pssm-ID: 411893 [Multi-domain]  Cd Length: 103  Bit Score: 103.09  E-value: 3.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402799 112 RVAQKVLFPIKEYPKFNFVGKILGPKGNTLRQLQEETMCKMVVMGRNSMRDHGKEEELRssGNPKYAHLSRDLHVEISTV 191
Cdd:cd22465    1 QLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNR--GKPNWEHLNEDLHVLITVE 78
                         90       100
                 ....*....|....*....|....*
gi 665402799 192 APPAEAYHRISYALGEIRKFMIPDA 216
Cdd:cd22465   79 DAQNRAEIKLKRAVEEVKKLLVPAA 103
KH-I_SPIN1_like cd22467
type I K homology (KH) RNA-binding domain found in Oryza sativa SPL11-interacting protein 1 ...
120-214 7.74e-19

type I K homology (KH) RNA-binding domain found in Oryza sativa SPL11-interacting protein 1 (SPIN1) and similar proteins; SPIN1 is a K homology domain protein negatively regulated and ubiquitinated by the E3 ubiquitin ligase SPL11. It is involved in flowering time control in rice. SPIN1 binds DNA and RNA in vitro.


Pssm-ID: 411895  Cd Length: 101  Bit Score: 80.61  E-value: 7.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402799 120 PIKEYPKFNFVGKILGPKGNTLRQLQEETMCKMVVMGRNSMRDHGKEEELRssGNPKYAHLSRDLHVEISTVAPPAEAYH 199
Cdd:cd22467    9 PVDKYPNFNFVGRILGPRGNSLKRVEATTGCRVFIRGRGSIKDTAKEEKLR--DKPGYEHLNEPLHVLIEAELPANIIDA 86
                         90
                 ....*....|....*
gi 665402799 200 RISYALGEIRKFMIP 214
Cdd:cd22467   87 RLQHAQEIIEDLLKP 101
KH-I_BBP cd02395
type I K homology (KH) RNA-binding domain found in yeast branchpoint-bridging protein (BBP) ...
116-213 9.59e-15

type I K homology (KH) RNA-binding domain found in yeast branchpoint-bridging protein (BBP) and similar proteins; Yeast BBP, also called mud synthetic-lethal 5 protein, or splicing factor 1, or zinc finger protein BBP, is a mammalian splicing factor SF1 ortholog. It is involved in protein-protein interactions that bridge the 3' and 5' splice-site ends of the intron during the early steps of yeast pre-mRNA splicing. BBP interacts specifically with the pre-mRNA branchpoint sequence UACUAAC.


Pssm-ID: 411805 [Multi-domain]  Cd Length: 92  Bit Score: 68.78  E-value: 9.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402799 116 KVLFPIKEYPKFNFVGKILGPKGNTLRQLQEETMCKMVVMGRNSMrdhgKEEELRSSGNPKYAhLSRDLHVEIStvappA 195
Cdd:cd02395    5 KIYIPVDEYPDYNFIGLIIGPRGNTQKRMEKESGAKIAIRGKGSV----KEGKGRSDPQPDPD-EEEDLHVLIT-----A 74
                         90
                 ....*....|....*...
gi 665402799 196 EAYHRISYALGEIRKFMI 213
Cdd:cd02395   75 DTEEKVDKAAKLIEKLLI 92
KH-I_SF1 cd22382
type I K homology (KH) RNA-binding domain found in splicing factor 1 (SF1) and similar ...
112-165 6.14e-13

type I K homology (KH) RNA-binding domain found in splicing factor 1 (SF1) and similar proteins; SF1, also called branch point-binding protein, or BBP, or transcription factor ZFM1, or zinc finger gene in MEN1 locus, or zinc finger protein 162, is necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. It may act as transcription repressor.


Pssm-ID: 411810 [Multi-domain]  Cd Length: 93  Bit Score: 63.87  E-value: 6.14e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 665402799 112 RVAQKVLFPIKEYPKFNFVGKILGPKGNTLRQLQEETMCKMVVMGRNSMRDhGK 165
Cdd:cd22382    1 RVSDKVMIPQEEYPDINFVGLLIGPRGNTLKKIEKETGAKIMIRGKGSVKE-GK 53
MSL5 COG5176
Splicing factor (branch point binding protein) [RNA processing and modification];
80-185 3.08e-11

Splicing factor (branch point binding protein) [RNA processing and modification];


Pssm-ID: 227503 [Multi-domain]  Cd Length: 269  Bit Score: 63.06  E-value: 3.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665402799  80 KRLLDDEVEKILVSGRIPKPEIYANVYsEKPIRVAQKVLFPIKEYPKFNFVGKILGPKGNTLRQLQEETMCKMVVMGRNS 159
Cdd:COG5176  116 KKLEDERLWLKERAQKILPRFVLPNDY-IRPSKYQNKIYIPVQEYPESNFVGLLIGPRGSTLKQLERISRAKIAIRGSGS 194
                         90       100
                 ....*....|....*....|....*.
gi 665402799 160 MrdhgKEEELRSSGNPKYAHLSRDLH 185
Cdd:COG5176  195 V----KEGKISSDTPESLKNAEAVLH 216
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
128-176 3.95e-06

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 43.81  E-value: 3.95e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 665402799  128 NFVGKILGPKGNTLRQLQEETMCKMVVMGRNsmrDHGKEEELRSSGNPK 176
Cdd:pfam00013   9 SLVGLIIGKGGSNIKEIREETGAKIQIPPSE---SEGNERIVTITGTPE 54
KH smart00322
K homology RNA-binding domain;
128-163 4.93e-06

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 43.82  E-value: 4.93e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 665402799   128 NFVGKILGPKGNTLRQLQEETMCKMVVMGRNSMRDH 163
Cdd:smart00322  12 DKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERV 47
KH-I_FUBP3_rpt2 cd22483
second type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
115-188 1.11e-05

second type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 3 (FUBP3) and similar proteins; FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP3 contains four K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411911 [Multi-domain]  Cd Length: 83  Bit Score: 43.36  E-value: 1.11e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665402799 115 QKVLFPIKEypkfnfVGKILGPKGNTLRQLQEETMCKMVVMGRNSMRDhGKEEELRSSGNPKYAHLSRDLHVEI 188
Cdd:cd22483    7 QEILIPASK------VGLVIGKGGETIKQLQERTGVKMIMIQDGPLPT-GADKPLRITGDPFKVQQAREMVLEI 73
KH-I_FUBP_rpt2 cd22397
second type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
130-175 3.19e-05

second type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411825 [Multi-domain]  Cd Length: 69  Bit Score: 41.46  E-value: 3.19e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 665402799 130 VGKILGPKGNTLRQLQEETMCKMvVMGRNSMRDHGKEEELRSSGNP 175
Cdd:cd22397   11 VGLIIGKGGETIKQLQERAGVKM-VMIQDGPQPTGQDKPLRITGDP 55
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
128-176 8.45e-05

K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability.


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 39.97  E-value: 8.45e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 665402799 128 NFVGKILGPKGNTLRQLQEETMCKMVVMGRNsmrDHGKEEELRSSGNPK 176
Cdd:cd00105    8 ELVGLIIGKGGSTIKEIEEETGARIQIPKEG---EGSGERVVTITGTPE 53
KH-I_FUBP1_rpt2 cd22481
second type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
131-188 3.70e-04

second type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 1 (FUBP1) and similar proteins; FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP1 contains four K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411909 [Multi-domain]  Cd Length: 71  Bit Score: 38.45  E-value: 3.70e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 665402799 131 GKILGPKGNTLRQLQEETMCKMvVMGRNSMRDHGKEEELRSSGNPKYAHLSRDLHVEI 188
Cdd:cd22481   14 GLVIGKGGETIKQLQERAGVKM-VMIQDGPQNTGADKPLRITGDPYKVQQAKEMVLEL 70
KH-I_KHDC4_rpt2 cd22386
first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ...
116-159 4.23e-04

first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein 4 (KHDC4) and similar proteins; KHDC4, also called Brings lots of money 7 (Blom7), or pre-mRNA splicing factor protein KHDC4, is an RNA-binding protein involved in pre-mRNA splicing. It interacts with the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome. KHDC4 binds preferentially RNA with A/C rich sequences and poly-C stretches. KHDC4 contains two type I K homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411814 [Multi-domain]  Cd Length: 102  Bit Score: 39.08  E-value: 4.23e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 665402799 116 KVLFPIKEYPK-FNFVGKILGPKGNTLRQLQEETMCKMVVMGRNS 159
Cdd:cd22386    6 KVFVGLEHAPPgFNVRGKLIGPGGSNVKHIQQETGAKVQLRGKGS 50
KH-I_PEPPER_rpt1_like cd22459
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
130-154 9.56e-03

first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER, flowering locus K homology domain protein (FLK), RNA-binding KH domain-containing protein RCF3 and KH domain-containing protein HEN4. PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 and HEN4 contain five KH RNA-binding domains. The model corresponds to the KH1 domain of PEPPER and FLK, as well as KH1 and KH3 domains of RCF3 and HEN4.


Pssm-ID: 411887 [Multi-domain]  Cd Length: 69  Bit Score: 34.51  E-value: 9.56e-03
                         10        20
                 ....*....|....*....|....*
gi 665402799 130 VGKILGPKGNTLRQLQEETMCKMVV 154
Cdd:cd22459   13 AGSVIGKGGEIIKQLRQETGARIKV 37
 
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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