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Conserved domains on  [gi|17541280|ref|NP_501390|]
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K Homology domain-containing protein [Caenorhabditis elegans]

Protein Classification

KH domain-containing protein( domain architecture ID 464)

KH (K homology) domain-containing protein binds single-stranded RNA or DNA

CATH:  3.30.1370.10
Gene Ontology:  GO:0003676
PubMed:  18422648|11160884
SCOP:  4001190

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KH-I super family cl00098
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
120-221 1.95e-28

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.


The actual alignment was detected with superfamily member cd22383:

Pssm-ID: 469614 [Multi-domain]  Cd Length: 101  Bit Score: 103.98  E-value: 1.95e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541280 120 TLTESIRIPVETYPTYNFIGRIIGPRGTTAKQLEKDTGCRIMIRGNHSNKMyGNALHKTHGDGSQDAIDLPLRVIVETSG 199
Cdd:cd22383   1 KLSEKVYVPVDEYPDYNFVGRILGPRGMTAKQLEQDTGCKIMIRGKGSMRD-KKKEEANRGKPNWEHLNDDLHVLITVED 79
                        90       100
                ....*....|....*....|..
gi 17541280 200 PRREATARITAALETVQVLLVP 221
Cdd:cd22383  80 TENRAHIKLAKAVEEVKKLLIP 101
 
Name Accession Description Interval E-value
KH-I_Hqk_like cd22383
type I K homology (KH) RNA-binding domain found in protein quaking (Hqk) family; The Hqk ...
120-221 1.95e-28

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: 103.98  E-value: 1.95e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541280 120 TLTESIRIPVETYPTYNFIGRIIGPRGTTAKQLEKDTGCRIMIRGNHSNKMyGNALHKTHGDGSQDAIDLPLRVIVETSG 199
Cdd:cd22383   1 KLSEKVYVPVDEYPDYNFVGRILGPRGMTAKQLEQDTGCKIMIRGKGSMRD-KKKEEANRGKPNWEHLNDDLHVLITVED 79
                        90       100
                ....*....|....*....|..
gi 17541280 200 PRREATARITAALETVQVLLVP 221
Cdd:cd22383  80 TENRAHIKLAKAVEEVKKLLIP 101
MSL5 COG5176
Splicing factor (branch point binding protein) [RNA processing and modification];
122-245 2.48e-19

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


Pssm-ID: 227503 [Multi-domain]  Cd Length: 269  Bit Score: 84.64  E-value: 2.48e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541280 122 TESIRIPVETYPTYNFIGRIIGPRGTTAKQLEKDTGCRIMIRGNHSNKMYGNALHKTHGDGSQDAidlPLRVIVETS--- 198
Cdd:COG5176 149 QNKIYIPVQEYPESNFVGLLIGPRGSTLKQLERISRAKIAIRGSGSVKEGKISSDTPESLKNAEA---VLHCLIEADsed 225
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 17541280 199 GPRREATARITAALETVQVllvppPDGRDELKRRQLVELAIMNGTYR 245
Cdd:COG5176 226 KICRLIKSQLNAIREARRN-----PEGQNDLKRFQLRWLAHLNGTLR 267
KH smart00322
K homology RNA-binding domain;
122-168 1.94e-07

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 47.29  E-value: 1.94e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 17541280    122 TESIRIPVetyptyNFIGRIIGPRGTTAKQLEKDTGCRIMIRGNHSN 168
Cdd:smart00322   4 TIEVLIPA------DKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSE 44
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
122-169 4.34e-05

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: 40.34  E-value: 4.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 17541280   122 TESIRIPVEtyptynFIGRIIGPRGTTAKQLEKDTGCRIMIRGNHSNK 169
Cdd:pfam00013   1 TVEILVPSS------LVGLIIGKGGSNIKEIREETGAKIQIPPSESEG 42
 
Name Accession Description Interval E-value
KH-I_Hqk_like cd22383
type I K homology (KH) RNA-binding domain found in protein quaking (Hqk) family; The Hqk ...
120-221 1.95e-28

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: 103.98  E-value: 1.95e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541280 120 TLTESIRIPVETYPTYNFIGRIIGPRGTTAKQLEKDTGCRIMIRGNHSNKMyGNALHKTHGDGSQDAIDLPLRVIVETSG 199
Cdd:cd22383   1 KLSEKVYVPVDEYPDYNFVGRILGPRGMTAKQLEQDTGCKIMIRGKGSMRD-KKKEEANRGKPNWEHLNDDLHVLITVED 79
                        90       100
                ....*....|....*....|..
gi 17541280 200 PRREATARITAALETVQVLLVP 221
Cdd:cd22383  80 TENRAHIKLAKAVEEVKKLLIP 101
KH-I_Hqk cd22465
type I K homology (KH) RNA-binding domain found in protein quaking (Hqk) and similar proteins; ...
120-223 5.21e-24

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: 92.69  E-value: 5.21e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541280 120 TLTESIRIPVETYPTYNFIGRIIGPRGTTAKQLEKDTGCRIMIRGNHSNKMYGNAlHKTHGDGSQDAIDLPLRVIVETSG 199
Cdd:cd22465   1 QLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKE-EQNRGKPNWEHLNEDLHVLITVED 79
                        90       100
                ....*....|....*....|....
gi 17541280 200 PRREATARITAALETVQVLLVPPP 223
Cdd:cd22465  80 AQNRAEIKLKRAVEEVKKLLVPAA 103
KH-I_HOW cd22466
type I K homology (KH) RNA-binding domain found in Drosophila protein held out wings (how) and ...
119-221 4.91e-23

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: 89.98  E-value: 4.91e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541280 119 VTLTESIRIPVETYPTYNFIGRIIGPRGTTAKQLEKDTGCRIMIRGNHSNKMYGNAlHKTHGDGSQDAIDLPLRVIVETS 198
Cdd:cd22466   4 VTLSEKVYVPVKEHPDYNFVGRILGPRGMTAKQLEQETGCKIMVRGKGSMRDKKKE-DLNRGKPNWEHLNDELHVLITVE 82
                        90       100
                ....*....|....*....|...
gi 17541280 199 GPRREATARITAALETVQVLLVP 221
Cdd:cd22466  83 DTENRAKVKLQRAVEEVRKLLVP 105
KH-I_KHDRBS1 cd22468
type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal ...
119-221 8.37e-20

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: 81.60  E-value: 8.37e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541280 119 VTLTESIRIPVETYPTYNFIGRIIGPRGTTAKQLEKDTGCRIMI--RGNHSNKMYGNALHKtHGDGSQDAIDLPLRVIVE 196
Cdd:cd22468   3 MKLKERILIPVKQYPKFNFVGKILGPQGNTIKRLQEETGAKISVlgKGSMRDKAKEEELRK-GGDPKYAHLNMDLHVFIE 81
                        90       100
                ....*....|....*....|....*
gi 17541280 197 TSGPRREATARITAALETVQVLLVP 221
Cdd:cd22468  82 VFGPPCEAYARMAHAMEEVKKFLVP 106
MSL5 COG5176
Splicing factor (branch point binding protein) [RNA processing and modification];
122-245 2.48e-19

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


Pssm-ID: 227503 [Multi-domain]  Cd Length: 269  Bit Score: 84.64  E-value: 2.48e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541280 122 TESIRIPVETYPTYNFIGRIIGPRGTTAKQLEKDTGCRIMIRGNHSNKMYGNALHKTHGDGSQDAidlPLRVIVETS--- 198
Cdd:COG5176 149 QNKIYIPVQEYPESNFVGLLIGPRGSTLKQLERISRAKIAIRGSGSVKEGKISSDTPESLKNAEA---VLHCLIEADsed 225
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 17541280 199 GPRREATARITAALETVQVllvppPDGRDELKRRQLVELAIMNGTYR 245
Cdd:COG5176 226 KICRLIKSQLNAIREARRN-----PEGQNDLKRFQLRWLAHLNGTLR 267
KH-I_BBP cd02395
type I K homology (KH) RNA-binding domain found in yeast branchpoint-bridging protein (BBP) ...
122-196 4.73e-19

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: 79.18  E-value: 4.73e-19
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17541280 122 TESIRIPVETYPTYNFIGRIIGPRGTTAKQLEKDTGCRIMIRGNHSNKmygnaLHKTHGDGS-QDAIDLPLRVIVE 196
Cdd:cd02395   3 QRKIYIPVDEYPDYNFIGLIIGPRGNTQKRMEKESGAKIAIRGKGSVK-----EGKGRSDPQpDPDEEEDLHVLIT 73
KH-I_SPIN1_like cd22467
type I K homology (KH) RNA-binding domain found in Oryza sativa SPL11-interacting protein 1 ...
122-221 2.05e-18

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: 77.92  E-value: 2.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541280 122 TESIRIPVETYPTYNFIGRIIGPRGTTAKQLEKDTGCRIMIRGNHSNKMYGNAlHKTHGDGSQDAIDLPLRVIVETSGPR 201
Cdd:cd22467   3 VLRLDVPVDKYPNFNFVGRILGPRGNSLKRVEATTGCRVFIRGRGSIKDTAKE-EKLRDKPGYEHLNEPLHVLIEAELPA 81
                        90       100
                ....*....|....*....|
gi 17541280 202 REATARITAALETVQVLLVP 221
Cdd:cd22467  82 NIIDARLQHAQEIIEDLLKP 101
KH-I_KHDRBS2 cd22469
type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal ...
119-233 2.31e-18

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: 78.24  E-value: 2.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541280 119 VTLTESIRIPVETYPTYNFIGRIIGPRGTTAKQLEKDTGCRIMI--RGNHSNKMYGNALHKThGDGSQDAIDLPLRVIVE 196
Cdd:cd22469   5 IKLSERVLIPVKQYPKFNFVGKLLGPRGNSLKRLQEETGAKMSIlgKGSMRDKAKEEELRKS-GEAKYAHLSDELHVLIE 83
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 17541280 197 TSGPRREATARITAALETVQVLLVppPDGRDELKRRQ 233
Cdd:cd22469  84 VFAPPGEAYSRMSHALEEIKKFLV--PDYNDEIRQEQ 118
KH-I_KHDRBS cd22384
type I K homology (KH) RNA-binding domain found in the KH domain-containing, RNA-binding, ...
119-216 1.12e-17

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: 75.78  E-value: 1.12e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541280 119 VTLTESIRIPVETYPTYNFIGRIIGPRGTTAKQLEKDTGCRIMI--RGNHSNKMYGNALHKThGDGSQDAIDLPLRVIVE 196
Cdd:cd22384   3 IKLSEKVLIPVKEFPKFNFVGKLLGPRGNTLKRLQEETGTKMSIlgKGSMRDKAKEEELRKS-GDPKYAHLNEDLHVLIE 81
                        90       100
                ....*....|....*....|
gi 17541280 197 TSGPRREATARITAALETVQ 216
Cdd:cd22384  82 AFAPPAEAYARLAHALAELR 101
KH-I_SF1 cd22382
type I K homology (KH) RNA-binding domain found in splicing factor 1 (SF1) and similar ...
121-169 7.11e-17

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: 73.50  E-value: 7.11e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 17541280 121 LTESIRIPVETYPTYNFIGRIIGPRGTTAKQLEKDTGCRIMIRGNHSNK 169
Cdd:cd22382   2 VSDKVMIPQEEYPDINFVGLLIGPRGNTLKKIEKETGAKIMIRGKGSVK 50
KH-I_KHDRBS3 cd22470
type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal ...
121-221 1.96e-13

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: 65.07  E-value: 1.96e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541280 121 LTESIRIPVETYPTYNFIGRIIGPRGTTAKQLEKDTGCRIMI--RGNHSNKMYGNALHKThGDGSQDAIDLPLRVIVETS 198
Cdd:cd22470   9 LGQKVLIPVKQFPKFNFVGKLLGPRGNSLKRLQEETLTKMSIlgKGSMRDKAKEEELRKS-GEAKYFHLNDDLHVLIEVF 87
                        90       100
                ....*....|....*....|...
gi 17541280 199 GPRREATARITAALETVQVLLVP 221
Cdd:cd22470  88 APPAEAYARMGHALEEIKKFLIP 110
KH smart00322
K homology RNA-binding domain;
122-168 1.94e-07

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 47.29  E-value: 1.94e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 17541280    122 TESIRIPVetyptyNFIGRIIGPRGTTAKQLEKDTGCRIMIRGNHSN 168
Cdd:smart00322   4 TIEVLIPA------DKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSE 44
KH-I_KHDC4_rpt2 cd22386
first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ...
121-167 3.47e-06

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: 44.47  E-value: 3.47e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 17541280 121 LTESIRIPVETY-PTYNFIGRIIGPRGTTAKQLEKDTGCRIMIRGNHS 167
Cdd:cd22386   3 YQEKVFVGLEHApPGFNVRGKLIGPGGSNVKHIQQETGAKVQLRGKGS 50
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
123-168 1.29e-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: 41.90  E-value: 1.29e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 17541280 123 ESIRIPVEtyptynFIGRIIGPRGTTAKQLEKDTGCRIMIRGNHSN 168
Cdd:cd00105   1 EEIEVPSE------LVGLIIGKGGSTIKEIEEETGARIQIPKEGEG 40
KH-I_PNPase cd02393
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ...
123-162 3.13e-05

type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase (PNPase) and similar proteins; PNPase, also called polynucleotide phosphorylase, is a polyribonucleotide nucleotidyl transferase that degrades mRNA in prokaryotes and plant chloroplasts. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. It is also involved, along with RNase II, in tRNA processing. The C-terminal region of PNPase contains domains homologous to those in other RNA binding proteins: a KH domain and an S1 domain. The model corresponds to the KH domain.


Pssm-ID: 411803 [Multi-domain]  Cd Length: 70  Bit Score: 40.92  E-value: 3.13e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 17541280 123 ESIRIPVEtyptynFIGRIIGPRGTTAKQLEKDTGCRIMI 162
Cdd:cd02393   6 TTIKIPPD------KIGDVIGPGGKTIRAIIEETGAKIDI 39
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
122-169 4.34e-05

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: 40.34  E-value: 4.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 17541280   122 TESIRIPVEtyptynFIGRIIGPRGTTAKQLEKDTGCRIMIRGNHSNK 169
Cdd:pfam00013   1 TVEILVPSS------LVGLIIGKGGSNIKEIREETGAKIQIPPSESEG 42
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
119-162 8.75e-05

second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411875 [Multi-domain]  Cd Length: 80  Bit Score: 40.09  E-value: 8.75e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 17541280 119 VTLTesIRIPVETyptynfIGRIIGPRGTTAKQLEKDTGCRIMI 162
Cdd:cd22447   4 QNLT--VPIPAST------RARIIGKKGANLKQIREKTGVRIDI 39
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
121-162 1.71e-04

first 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 first one.


Pssm-ID: 411824 [Multi-domain]  Cd Length: 68  Bit Score: 38.77  E-value: 1.71e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 17541280 121 LTESIRIPVetyptyNFIGRIIGPRGTTAKQLEKDTGCRIMI 162
Cdd:cd22396   1 VTEEYKVPD------KMVGLIIGRGGEQINRLQAESGAKIQI 36
KH-I_AKAP1 cd22395
type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 ...
134-194 2.13e-04

type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa, or AKAP 149, or dual specificity A-kinase-anchoring protein 1, or D-AKAP-1, or protein kinase A-anchoring protein 1 (PRKA1), or spermatid A-kinase anchor protein 84, or S-AKAP84, is a novel developmentally regulated A kinase anchor protein of male germ cells. It binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane.


Pssm-ID: 411823 [Multi-domain]  Cd Length: 68  Bit Score: 38.66  E-value: 2.13e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17541280 134 TYNFI------GRIIGPRGTTAKQLEKDTGCRIMIRGNHSNKMYgnalhKT-HGDGSQDAIDLPLRVI 194
Cdd:cd22395   1 VYEFEvpselvGRLIGKQGRNVKQLKQKSGAKIYIKPHPYTQNF-----QIcSIEGTQQQIDKALKLI 63
KH-I_RIK_like_rpt2 cd22472
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein RIK and ...
129-217 1.19e-03

second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein RIK and similar proteins; RIK, also called rough sheath 2-interacting KH domain protein, or RS2-interacting KH domain protein, is a RNA binding protein that acts together with RS2/AS1 in the recruitment of HIRA. RIK contains two type I K homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411900  Cd Length: 96  Bit Score: 37.42  E-value: 1.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541280 129 VETYPTYNFIGRIIGPRGTTAKQLEKDTGCRIMIRGnhsnkmygnalhktHGDGSQDAIDLPLRVIVETSGPRREATARI 208
Cdd:cd22472  11 IEAPPSFNLAGRIRGPNNSYLQHIASATGATVALRG--------------RGSGGAPEGPEPLHLFLSASDPKALEEARG 76
                        90
                ....*....|.
gi 17541280 209 TAA--LETVQV 217
Cdd:cd22472  77 LAEnlIDTVRA 87
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
122-208 1.28e-03

sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the sixth one.


Pssm-ID: 411879 [Multi-domain]  Cd Length: 69  Bit Score: 36.66  E-value: 1.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17541280 122 TESIRIPVETYptynfiGRIIGPRGTTAKQLEKDTGCRIMIRGnhsnkmygnalhkthgdgsQDAIDLPLRVivetSGPR 201
Cdd:cd22451   2 SIDIDIPKEYH------RAIIGKGGAVLRELEAETGCRIQVPK-------------------KDDPSGKIRI----TGAR 52
                        90
                ....*....|
gi 17541280 202 ---REATARI 208
Cdd:cd22451  53 dgvEAATAKI 62
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
136-173 1.47e-03

type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box protein 53 (DDX53) and similar proteins; DDX43 (also called cancer/testis antigen 13, or DEAD box protein HAGE, or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 (also called cancer-associated gene protein, or cancer/testis antigen 26, or DEAD box protein CAGE) shows high expression level in various tumors and is involved in anti-cancer drug resistance. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation.


Pssm-ID: 411858 [Multi-domain]  Cd Length: 66  Bit Score: 36.11  E-value: 1.47e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 17541280 136 NFIGRIIGPRGTTAKQLEKDTGCRIMI-RGNHSN--KMYGN 173
Cdd:cd22430   9 SLVGAVIGRGGSKIRELEESTGSKIKIiKGGQEAevKIFGS 49
KH-I_KRR1_rpt2 cd22394
second type I K homology (KH) RNA-binding domain found in KRR1 small subunit processome ...
140-165 3.04e-03

second type I K homology (KH) RNA-binding domain found in KRR1 small subunit processome component and similar proteins; KRR1, also called HIV-1 Rev-binding protein 2, or KRR-R motif-containing protein 1, or Rev-interacting protein 1, or Rip-1, or ribosomal RNA assembly protein KRR1, is a nucleolar protein required for 40S ribosome biogenesis. It is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. KRR1 contains two K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411822  Cd Length: 93  Bit Score: 36.01  E-value: 3.04e-03
                        10        20
                ....*....|....*....|....*.
gi 17541280 140 RIIGPRGTTAKQLEKDTGCRIMIRGN 165
Cdd:cd22394  24 RLIGPNGSTLKAIELLTKCYILVQGN 49
KH-I_IGF2BP1_rpt2 cd22493
second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ...
127-162 4.31e-03

second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 mRNA-binding protein 1 (IGF2BP1) and similar proteins; IGF2BP1, also called IGF2 mRNA-binding protein 1 (IMP-1), or coding region determinant-binding protein (CRD-BP), or IGF-II mRNA-binding protein 1, or VICKZ family member 1 (VICKZ1), or zipcode-binding protein 1 (ZBP-1), is an RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. It regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. IGF2BP1 can form homodimers and heterodimers with IGF2BP1 and IGF2BP3. It contains four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the second one.


Pssm-ID: 411921  Cd Length: 97  Bit Score: 35.80  E-value: 4.31e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 17541280 127 IPVETYPTYNFIGRIIGPRGTTAKQLEKDTGCRIMI 162
Cdd:cd22493   5 VPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITI 40
KH-I_PEPPER_rpt1_like cd22459
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
138-162 6.60e-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: 6.60e-03
                        10        20
                ....*....|....*....|....*
gi 17541280 138 IGRIIGPRGTTAKQLEKDTGCRIMI 162
Cdd:cd22459  13 AGSVIGKGGEIIKQLRQETGARIKV 37
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
122-162 8.80e-03

third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the third one.


Pssm-ID: 411835 [Multi-domain]  Cd Length: 62  Bit Score: 33.72  E-value: 8.80e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 17541280 122 TESIRIPVETYPtynFIgriIGPRGTTAKQLEKDTGCRIMI 162
Cdd:cd22407   1 TERLDIPKVYHP---FI---AGPNNENVKELQEETGVRINI 35
 
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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