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Conserved domains on  [gi|193204147|ref|NP_001122591|]
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K Homology domain-containing protein [Caenorhabditis elegans]

Protein Classification

KH domain-containing protein( domain architecture ID 12202618)

K homology (KH) domain-containing protein may bind single-stranded RNA or DNA; similar to Caenorhabditis elegans messenger RNA-binding inhibitor of apoptosis 1 which binds to its own mRNA and target mRNAs to negatively regulate gene expression to modulate apoptosis and differentiation in the germline

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AKAP7_NLS pfam10469
AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic ...
177-392 3.23e-56

AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic AMP-dependent protein kinase A, PKA, anchor protein AKAP7. This protein anchors PKA for its role in regulating PKA-mediated gene transcription in both somatic cells and oocytes. AKAP7_NLS carries the nuclear localization signal (NLS) KKRKK, that indicates the cellular destiny of this anchor protein. Binding to the regulatory subunits RI and RII of PKA is mediated via the family AKAP7_RIRII_bdg. at the C-terminus. This family represents a region that contains two 2'5' RNA ligase like domains pfam02834. Presumably this domain carried out some as yet unknown enzymatic function.


:

Pssm-ID: 402204 [Multi-domain]  Cd Length: 207  Bit Score: 183.24  E-value: 3.23e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204147  177 NHFVALPCDQHEVQENFNIFKQMVMESDhfdsSCKNSQLFTKPTRLHLTLSVARIFDDMDLQKAVGAFEILEKEIRQIKD 256
Cdd:pfam10469   2 THFLSIPLNSPELRKRLEEFQESVLKQL----PGLDESLFIPPEKLHITLLVLVLLDDEEVARAKEALRECREEIKDILN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204147  257 SKPLIADIQGIDMMNDDPSQVFVLYAKVKGD----KVQEVANYVNRRLIELGVSSKNEHDNgsdaVKLHMTLMNSRYVTQ 332
Cdd:pfam10469  78 GNPLSLRFKGLETFNDDPSAVRVLYAKVEEDdhspKLQELADRIIRRFQEAGLLVKENNSR----VKLHMTLMNTRYRKK 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204147  333 SEKSGKSKeaalFDAKQVLEDLKDSYFGTFELKEICLCPMSSNSQtSDGkFYDKLAIIKL 392
Cdd:pfam10469 154 KYAKSKES----FDAREILDEFKDFDFGTQKVSELHLCSMGSSDE-SDG-FYHVEASVKL 207
KH smart00322
K homology RNA-binding domain;
99-164 5.62e-06

K homology RNA-binding domain;


:

Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 43.82  E-value: 5.62e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193204147    99 KKWISSINVAPCFIGKLIGTNRRTLNSLENETQCRVKTPRRNENI-ACEISSivSLECVQRCLDRLE 164
Cdd:smart00322   1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEErVVEITG--PPENVEKAAELIL 65
 
Name Accession Description Interval E-value
AKAP7_NLS pfam10469
AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic ...
177-392 3.23e-56

AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic AMP-dependent protein kinase A, PKA, anchor protein AKAP7. This protein anchors PKA for its role in regulating PKA-mediated gene transcription in both somatic cells and oocytes. AKAP7_NLS carries the nuclear localization signal (NLS) KKRKK, that indicates the cellular destiny of this anchor protein. Binding to the regulatory subunits RI and RII of PKA is mediated via the family AKAP7_RIRII_bdg. at the C-terminus. This family represents a region that contains two 2'5' RNA ligase like domains pfam02834. Presumably this domain carried out some as yet unknown enzymatic function.


Pssm-ID: 402204 [Multi-domain]  Cd Length: 207  Bit Score: 183.24  E-value: 3.23e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204147  177 NHFVALPCDQHEVQENFNIFKQMVMESDhfdsSCKNSQLFTKPTRLHLTLSVARIFDDMDLQKAVGAFEILEKEIRQIKD 256
Cdd:pfam10469   2 THFLSIPLNSPELRKRLEEFQESVLKQL----PGLDESLFIPPEKLHITLLVLVLLDDEEVARAKEALRECREEIKDILN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204147  257 SKPLIADIQGIDMMNDDPSQVFVLYAKVKGD----KVQEVANYVNRRLIELGVSSKNEHDNgsdaVKLHMTLMNSRYVTQ 332
Cdd:pfam10469  78 GNPLSLRFKGLETFNDDPSAVRVLYAKVEEDdhspKLQELADRIIRRFQEAGLLVKENNSR----VKLHMTLMNTRYRKK 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204147  333 SEKSGKSKeaalFDAKQVLEDLKDSYFGTFELKEICLCPMSSNSQtSDGkFYDKLAIIKL 392
Cdd:pfam10469 154 KYAKSKES----FDAREILDEFKDFDFGTQKVSELHLCSMGSSDE-SDG-FYHVEASVKL 207
PLN00108 PLN00108
unknown protein; Provisional
178-366 2.05e-10

unknown protein; Provisional


Pssm-ID: 177724  Cd Length: 257  Bit Score: 60.85  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204147 178 HFVALPCDQH-EVQENFNIFKQMVMESDHFDSSCKNSQL---------FTKPTRLHLTLSVARIFDDMDLQKAVGAFEIL 247
Cdd:PLN00108  38 HFVSLPLAIYpDLKKNIEAFQNSVLGNNDKDPLKFQSTLaemgieksiFVSPKTFHLTVVMLKLENNESVVKAQNILKSI 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204147 248 EKEIRQIKDSKPLIADIQGIDMMNDDPSQVFVLYAKVkgDKVQEVANYVNRRLIELGvSSKNEHDNGSDA---VKLHMTL 324
Cdd:PLN00108 118 CSNVRQALKDRPVFIRLRGLDCMNGSLDKTRVLYAPV--EEVGHEGRLLNACHVIID-AFENAGFAGKDAksrLKLHATL 194
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 193204147 325 MNSRYvtqseKSGKSKEAALFDAKQVLEDLKDSYFGTFELKE 366
Cdd:PLN00108 195 MNASY-----RKDKSKKMDTFDAREIHKEFENKDWGTYLIRE 231
KH smart00322
K homology RNA-binding domain;
99-164 5.62e-06

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 43.82  E-value: 5.62e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193204147    99 KKWISSINVAPCFIGKLIGTNRRTLNSLENETQCRVKTPRRNENI-ACEISSivSLECVQRCLDRLE 164
Cdd:smart00322   1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEErVVEITG--PPENVEKAAELIL 65
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
104-164 3.43e-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: 41.13  E-value: 3.43e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193204147 104 SINVAPCFIGKLIGTNRRTLNSLENETQCRVKTPRRNENIA---CEISSivSLECVQRCLDRLE 164
Cdd:cd00105    2 EIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGervVTITG--TPEAVEKAKELIE 63
ThpR COG1514
RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and ...
179-393 2.43e-04

RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441123 [Multi-domain]  Cd Length: 181  Bit Score: 41.55  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204147 179 FVALPCDQhEVQENFNIFKQmvmesdHFDSSCKNSqlFTKPTRLHLTLSVARIFDDMDLQKAVgafEILEKEIRQIKdsk 258
Cdd:COG1514    4 FIALPPPE-ELREALAALRA------RLKAAPGGR--WVRPENLHLTLAFLGEVDEERLEALA---EALARAAAGAP--- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204147 259 PLIADIQGIDmmnddpsqVF------VLYAKVKG-DKVQEVANYVNRRLIELGVSSKNEhdngsdAVKLHMTLMNsryvt 331
Cdd:COG1514   69 PFELRLDGLG--------AFprprprVLWLGVEPsPELLALHRRLRAALARAGLPPERR------PFVPHVTLAR----- 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193204147 332 qseksGKSKEAALFDAkqvLEDLKDSYFGTFELKEICLcpMSSnSQTSDGKFYDKLAIIKLA 393
Cdd:COG1514  130 -----GKRPAPPLAPA---LAELRDFEFPEFTVDEFVL--YES-ELTPDGPRYEVLAEFPLG 180
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
111-164 4.83e-04

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: 38.03  E-value: 4.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 193204147  111 FIGKLIGTNRRTLNSLENETQCRVKTPRRNENIACEISSIV-SLECVQRCLDRLE 164
Cdd:pfam00013  10 LVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTITgTPEAVEAAKALIE 64
 
Name Accession Description Interval E-value
AKAP7_NLS pfam10469
AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic ...
177-392 3.23e-56

AKAP7 2'5' RNA ligase-like domain; AKAP7_NLS is the N-terminal domain of the cyclic AMP-dependent protein kinase A, PKA, anchor protein AKAP7. This protein anchors PKA for its role in regulating PKA-mediated gene transcription in both somatic cells and oocytes. AKAP7_NLS carries the nuclear localization signal (NLS) KKRKK, that indicates the cellular destiny of this anchor protein. Binding to the regulatory subunits RI and RII of PKA is mediated via the family AKAP7_RIRII_bdg. at the C-terminus. This family represents a region that contains two 2'5' RNA ligase like domains pfam02834. Presumably this domain carried out some as yet unknown enzymatic function.


Pssm-ID: 402204 [Multi-domain]  Cd Length: 207  Bit Score: 183.24  E-value: 3.23e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204147  177 NHFVALPCDQHEVQENFNIFKQMVMESDhfdsSCKNSQLFTKPTRLHLTLSVARIFDDMDLQKAVGAFEILEKEIRQIKD 256
Cdd:pfam10469   2 THFLSIPLNSPELRKRLEEFQESVLKQL----PGLDESLFIPPEKLHITLLVLVLLDDEEVARAKEALRECREEIKDILN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204147  257 SKPLIADIQGIDMMNDDPSQVFVLYAKVKGD----KVQEVANYVNRRLIELGVSSKNEHDNgsdaVKLHMTLMNSRYVTQ 332
Cdd:pfam10469  78 GNPLSLRFKGLETFNDDPSAVRVLYAKVEEDdhspKLQELADRIIRRFQEAGLLVKENNSR----VKLHMTLMNTRYRKK 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204147  333 SEKSGKSKeaalFDAKQVLEDLKDSYFGTFELKEICLCPMSSNSQtSDGkFYDKLAIIKL 392
Cdd:pfam10469 154 KYAKSKES----FDAREILDEFKDFDFGTQKVSELHLCSMGSSDE-SDG-FYHVEASVKL 207
PLN00108 PLN00108
unknown protein; Provisional
178-366 2.05e-10

unknown protein; Provisional


Pssm-ID: 177724  Cd Length: 257  Bit Score: 60.85  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204147 178 HFVALPCDQH-EVQENFNIFKQMVMESDHFDSSCKNSQL---------FTKPTRLHLTLSVARIFDDMDLQKAVGAFEIL 247
Cdd:PLN00108  38 HFVSLPLAIYpDLKKNIEAFQNSVLGNNDKDPLKFQSTLaemgieksiFVSPKTFHLTVVMLKLENNESVVKAQNILKSI 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204147 248 EKEIRQIKDSKPLIADIQGIDMMNDDPSQVFVLYAKVkgDKVQEVANYVNRRLIELGvSSKNEHDNGSDA---VKLHMTL 324
Cdd:PLN00108 118 CSNVRQALKDRPVFIRLRGLDCMNGSLDKTRVLYAPV--EEVGHEGRLLNACHVIID-AFENAGFAGKDAksrLKLHATL 194
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 193204147 325 MNSRYvtqseKSGKSKEAALFDAKQVLEDLKDSYFGTFELKE 366
Cdd:PLN00108 195 MNASY-----RKDKSKKMDTFDAREIHKEFENKDWGTYLIRE 231
KH smart00322
K homology RNA-binding domain;
99-164 5.62e-06

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 43.82  E-value: 5.62e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193204147    99 KKWISSINVAPCFIGKLIGTNRRTLNSLENETQCRVKTPRRNENI-ACEISSivSLECVQRCLDRLE 164
Cdd:smart00322   1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEErVVEITG--PPENVEKAAELIL 65
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
104-164 3.43e-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: 41.13  E-value: 3.43e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193204147 104 SINVAPCFIGKLIGTNRRTLNSLENETQCRVKTPRRNENIA---CEISSivSLECVQRCLDRLE 164
Cdd:cd00105    2 EIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGervVTITG--TPEAVEKAKELIE 63
ThpR COG1514
RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and ...
179-393 2.43e-04

RNA 2',3'-cyclic phosphodiesterase (2'-5' RNA ligase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441123 [Multi-domain]  Cd Length: 181  Bit Score: 41.55  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204147 179 FVALPCDQhEVQENFNIFKQmvmesdHFDSSCKNSqlFTKPTRLHLTLSVARIFDDMDLQKAVgafEILEKEIRQIKdsk 258
Cdd:COG1514    4 FIALPPPE-ELREALAALRA------RLKAAPGGR--WVRPENLHLTLAFLGEVDEERLEALA---EALARAAAGAP--- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204147 259 PLIADIQGIDmmnddpsqVF------VLYAKVKG-DKVQEVANYVNRRLIELGVSSKNEhdngsdAVKLHMTLMNsryvt 331
Cdd:COG1514   69 PFELRLDGLG--------AFprprprVLWLGVEPsPELLALHRRLRAALARAGLPPERR------PFVPHVTLAR----- 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193204147 332 qseksGKSKEAALFDAkqvLEDLKDSYFGTFELKEICLcpMSSnSQTSDGKFYDKLAIIKLA 393
Cdd:COG1514  130 -----GKRPAPPLAPA---LAELRDFEFPEFTVDEFVL--YES-ELTPDGPRYEVLAEFPLG 180
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
111-164 4.83e-04

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: 38.03  E-value: 4.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 193204147  111 FIGKLIGTNRRTLNSLENETQCRVKTPRRNENIACEISSIV-SLECVQRCLDRLE 164
Cdd:pfam00013  10 LVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTITgTPEAVEAAKALIE 64
 
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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