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Conserved domains on  [gi|1002273012|ref|XP_015640815|]
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KH domain-containing protein At1g09660/At1g09670 isoform X1 [Oryza sativa Japonica Group]

Protein Classification

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 ...
139-239 3.86e-62

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 cd22467:

Pssm-ID: 469614  Cd Length: 101  Bit Score: 191.55  E-value: 3.86e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002273012 139 KKVVRIDVPVDKYPNYNFVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVKDSVKEDKLRDKPGYEHLNDPLHVLVEAEFP 218
Cdd:cd22467     1 KKVLRLDVPVDKYPNFNFVGRILGPRGNSLKRVEATTGCRVFIRGRGSIKDTAKEEKLRDKPGYEHLNEPLHVLIEAELP 80
                          90       100
                  ....*....|....*....|.
gi 1002273012 219 SDIVDVRLNQAVAILEDLLKP 239
Cdd:cd22467    81 ANIIDARLQHAQEIIEDLLKP 101
STAR_dimer super family cl24943
Homodimerization region of STAR domain protein; This family is the homodimerization domain of ...
38-81 3.91e-09

Homodimerization region of STAR domain protein; This family is the homodimerization domain of quaking proteins. Quaking-dimer is a helix-turn-helix dimer with an additional helix in the turn region. dimerization is required for adequate RNA-binding. Quaking is a prototypical member of the STAR (signal transducer and activator of RNA) protein family, which plays key roles in post-transcriptional gene regulation by controlling mRNA translation, stability and splicing. STAR_dimer is the homodimerization domain, Qua1 of the STAR domain of a series of proteins referred to as STAR/GSG, or Signal Transduction and Activation of RNA/GRP33, Sam68, GLD-1 family. These are conserved in higher eukaryotes and are RNA-binding transcriptional regulators. The STAR domain is a KH domain flanked by two homologous regions, Qua1 and Qua2. Qua1, this family, is the homodimerization domain, and the KH plus Qua2 is the RNA-binding region.


The actual alignment was detected with superfamily member pfam16544:

Pssm-ID: 435414  Cd Length: 52  Bit Score: 51.56  E-value: 3.91e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1002273012  38 YLAELLAERQKLAPFMQVLPFCNRLLNQEILRASSLPPNPNFVE 81
Cdd:pfam16544   8 YLAQLLKDKKQLAAFPNVFPHLERLLDEEISRVRGDLFNKGFGD 51
 
Name Accession Description Interval E-value
KH-I_SPIN1_like cd22467
type I K homology (KH) RNA-binding domain found in Oryza sativa SPL11-interacting protein 1 ...
139-239 3.86e-62

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: 191.55  E-value: 3.86e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002273012 139 KKVVRIDVPVDKYPNYNFVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVKDSVKEDKLRDKPGYEHLNDPLHVLVEAEFP 218
Cdd:cd22467     1 KKVLRLDVPVDKYPNFNFVGRILGPRGNSLKRVEATTGCRVFIRGRGSIKDTAKEEKLRDKPGYEHLNEPLHVLIEAELP 80
                          90       100
                  ....*....|....*....|.
gi 1002273012 219 SDIVDVRLNQAVAILEDLLKP 239
Cdd:cd22467    81 ANIIDARLQHAQEIIEDLLKP 101
MSL5 COG5176
Splicing factor (branch point binding protein) [RNA processing and modification];
77-265 8.59e-25

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


Pssm-ID: 227503 [Multi-domain]  Cd Length: 269  Bit Score: 100.04  E-value: 8.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002273012  77 PNFVEPERVNHG--SPLRLTGHPMNGQPMDLEGWSGMQTEQMGVLQSP--SMGWNVAPGVAGSPVVKKVvRIDVPVDKYP 152
Cdd:COG5176    82 PDGVPSKRELRSpsPPPRYDEIGRRLNTREARYNKKLEDERLWLKERAqkILPRFVLPNDYIRPSKYQN-KIYIPVQEYP 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002273012 153 NYNFVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVKDSVKEDKLrdKPGYEHLNDPLHVLVEAEFPSDIVDVRLNQAVAI 232
Cdd:COG5176   161 ESNFVGLLIGPRGSTLKQLERISRAKIAIRGSGSVKEGKISSDT--PESLKNAEAVLHCLIEADSEDKICRLIKSQLNAI 238
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1002273012 233 LEDLLKPvdESMDYYKKQQLRELAILNGTLREE 265
Cdd:COG5176   239 REARRNP--EGQNDLKRFQLRWLAHLNGTLRAD 269
STAR_dimer pfam16544
Homodimerization region of STAR domain protein; This family is the homodimerization domain of ...
38-81 3.91e-09

Homodimerization region of STAR domain protein; This family is the homodimerization domain of quaking proteins. Quaking-dimer is a helix-turn-helix dimer with an additional helix in the turn region. dimerization is required for adequate RNA-binding. Quaking is a prototypical member of the STAR (signal transducer and activator of RNA) protein family, which plays key roles in post-transcriptional gene regulation by controlling mRNA translation, stability and splicing. STAR_dimer is the homodimerization domain, Qua1 of the STAR domain of a series of proteins referred to as STAR/GSG, or Signal Transduction and Activation of RNA/GRP33, Sam68, GLD-1 family. These are conserved in higher eukaryotes and are RNA-binding transcriptional regulators. The STAR domain is a KH domain flanked by two homologous regions, Qua1 and Qua2. Qua1, this family, is the homodimerization domain, and the KH plus Qua2 is the RNA-binding region.


Pssm-ID: 435414  Cd Length: 52  Bit Score: 51.56  E-value: 3.91e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1002273012  38 YLAELLAERQKLAPFMQVLPFCNRLLNQEILRASSLPPNPNFVE 81
Cdd:pfam16544   8 YLAQLLKDKKQLAAFPNVFPHLERLLDEEISRVRGDLFNKGFGD 51
KH smart00322
K homology RNA-binding domain;
139-191 4.93e-05

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 40.74  E-value: 4.93e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1002273012  139 KKVVRIDVPVDKypnynfVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVKDSV 191
Cdd:smart00322   2 PVTIEVLIPADK------VGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVV 48
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
141-190 2.52e-03

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: 35.72  E-value: 2.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002273012 141 VVRIDVPVDKypnynfVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVKDS 190
Cdd:pfam00013   1 TVEILVPSSL------VGLIIGKGGSNIKEIREETGAKIQIPPSESEGNE 44
 
Name Accession Description Interval E-value
KH-I_SPIN1_like cd22467
type I K homology (KH) RNA-binding domain found in Oryza sativa SPL11-interacting protein 1 ...
139-239 3.86e-62

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: 191.55  E-value: 3.86e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002273012 139 KKVVRIDVPVDKYPNYNFVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVKDSVKEDKLRDKPGYEHLNDPLHVLVEAEFP 218
Cdd:cd22467     1 KKVLRLDVPVDKYPNFNFVGRILGPRGNSLKRVEATTGCRVFIRGRGSIKDTAKEEKLRDKPGYEHLNEPLHVLIEAELP 80
                          90       100
                  ....*....|....*....|.
gi 1002273012 219 SDIVDVRLNQAVAILEDLLKP 239
Cdd:cd22467    81 ANIIDARLQHAQEIIEDLLKP 101
KH-I_Hqk_like cd22383
type I K homology (KH) RNA-binding domain found in protein quaking (Hqk) family; The Hqk ...
139-239 3.89e-49

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: 158.29  E-value: 3.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002273012 139 KKVVRIDVPVDKYPNYNFVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVKDSVKEDKLRDKPGYEHLNDPLHVLVEAEFP 218
Cdd:cd22383     1 KLSEKVYVPVDEYPDYNFVGRILGPRGMTAKQLEQDTGCKIMIRGKGSMRDKKKEEANRGKPNWEHLNDDLHVLITVEDT 80
                          90       100
                  ....*....|....*....|.
gi 1002273012 219 SDIVDVRLNQAVAILEDLLKP 239
Cdd:cd22383    81 ENRAHIKLAKAVEEVKKLLIP 101
KH-I_KHDRBS cd22384
type I K homology (KH) RNA-binding domain found in the KH domain-containing, RNA-binding, ...
138-231 7.41e-32

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: 113.92  E-value: 7.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002273012 138 VKKVVRIDVPVDKYPNYNFVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVKDSVKEDKLR--DKPGYEHLNDPLHVLVEA 215
Cdd:cd22384     3 IKLSEKVLIPVKEFPKFNFVGKLLGPRGNTLKRLQEETGTKMSILGKGSMRDKAKEEELRksGDPKYAHLNEDLHVLIEA 82
                          90
                  ....*....|....*.
gi 1002273012 216 EFPSDIVDVRLNQAVA 231
Cdd:cd22384    83 FAPPAEAYARLAHALA 98
KH-I_HOW cd22466
type I K homology (KH) RNA-binding domain found in Drosophila protein held out wings (how) and ...
136-239 1.95e-30

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: 110.40  E-value: 1.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002273012 136 PVVKKVVRIDVPVDKYPNYNFVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVKDSVKEDKLRDKPGYEHLNDPLHVLVEA 215
Cdd:cd22466     2 PSVTLSEKVYVPVKEHPDYNFVGRILGPRGMTAKQLEQETGCKIMVRGKGSMRDKKKEDLNRGKPNWEHLNDELHVLITV 81
                          90       100
                  ....*....|....*....|....
gi 1002273012 216 EFPSDIVDVRLNQAVAILEDLLKP 239
Cdd:cd22466    82 EDTENRAKVKLQRAVEEVRKLLVP 105
KH-I_Hqk cd22465
type I K homology (KH) RNA-binding domain found in protein quaking (Hqk) and similar proteins; ...
146-239 8.89e-30

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: 108.49  E-value: 8.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002273012 146 VPVDKYPNYNFVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVKDSVKEDKLRDKPGYEHLNDPLHVLVEAEFPSDIVDVR 225
Cdd:cd22465     8 VPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRAEIK 87
                          90
                  ....*....|....
gi 1002273012 226 LNQAVAILEDLLKP 239
Cdd:cd22465    88 LKRAVEEVKKLLVP 101
KH-I_BBP cd02395
type I K homology (KH) RNA-binding domain found in yeast branchpoint-bridging protein (BBP) ...
139-237 4.45e-28

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: 103.83  E-value: 4.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002273012 139 KKVVRIDVPVDKYPNYNFVGRLLGPRGNSLKRVEATTQCRVYIRGRGsvkdSVKEDKLRDKPGYE-HLNDPLHVLVEAEF 217
Cdd:cd02395     1 KKQRKIYIPVDEYPDYNFIGLIIGPRGNTQKRMEKESGAKIAIRGKG----SVKEGKGRSDPQPDpDEEEDLHVLITADT 76
                          90       100
                  ....*....|....*....|
gi 1002273012 218 PSDIvdvrlNQAVAILEDLL 237
Cdd:cd02395    77 EEKV-----DKAAKLIEKLL 91
MSL5 COG5176
Splicing factor (branch point binding protein) [RNA processing and modification];
77-265 8.59e-25

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


Pssm-ID: 227503 [Multi-domain]  Cd Length: 269  Bit Score: 100.04  E-value: 8.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002273012  77 PNFVEPERVNHG--SPLRLTGHPMNGQPMDLEGWSGMQTEQMGVLQSP--SMGWNVAPGVAGSPVVKKVvRIDVPVDKYP 152
Cdd:COG5176    82 PDGVPSKRELRSpsPPPRYDEIGRRLNTREARYNKKLEDERLWLKERAqkILPRFVLPNDYIRPSKYQN-KIYIPVQEYP 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002273012 153 NYNFVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVKDSVKEDKLrdKPGYEHLNDPLHVLVEAEFPSDIVDVRLNQAVAI 232
Cdd:COG5176   161 ESNFVGLLIGPRGSTLKQLERISRAKIAIRGSGSVKEGKISSDT--PESLKNAEAVLHCLIEADSEDKICRLIKSQLNAI 238
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1002273012 233 LEDLLKPvdESMDYYKKQQLRELAILNGTLREE 265
Cdd:COG5176   239 REARRNP--EGQNDLKRFQLRWLAHLNGTLRAD 269
KH-I_KHDRBS2 cd22469
type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal ...
138-239 1.63e-21

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: 87.49  E-value: 1.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002273012 138 VKKVVRIDVPVDKYPNYNFVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVKDSVKEDKLR--DKPGYEHLNDPLHVLVEA 215
Cdd:cd22469     5 IKLSERVLIPVKQYPKFNFVGKLLGPRGNSLKRLQEETGAKMSILGKGSMRDKAKEEELRksGEAKYAHLSDELHVLIEV 84
                          90       100
                  ....*....|....*....|....
gi 1002273012 216 EFPSDIVDVRLNQAVAILEDLLKP 239
Cdd:cd22469    85 FAPPGEAYSRMSHALEEIKKFLVP 108
KH-I_SF1 cd22382
type I K homology (KH) RNA-binding domain found in splicing factor 1 (SF1) and similar ...
143-215 4.10e-21

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: 85.44  E-value: 4.10e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002273012 143 RIDVPVDKYPNYNFVGRLLGPRGNSLKRVEATTQCRVYIRGRGsvkdSVKEDKLRDKPG--YEHLNDPLHVLVEA 215
Cdd:cd22382     5 KVMIPQEEYPDINFVGLLIGPRGNTLKKIEKETGAKIMIRGKG----SVKEGKVGRKDGqpLPGEDEPLHALVTA 75
KH-I_KHDRBS1 cd22468
type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal ...
143-239 5.95e-21

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: 85.45  E-value: 5.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002273012 143 RIDVPVDKYPNYNFVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVKDSVKEDKLRD--KPGYEHLNDPLHVLVEAEFPSD 220
Cdd:cd22468     8 RILIPVKQYPKFNFVGKILGPQGNTIKRLQEETGAKISVLGKGSMRDKAKEEELRKggDPKYAHLNMDLHVFIEVFGPPC 87
                          90
                  ....*....|....*....
gi 1002273012 221 IVDVRLNQAVAILEDLLKP 239
Cdd:cd22468    88 EAYARMAHAMEEVKKFLVP 106
KH-I_KHDRBS3 cd22470
type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal ...
143-239 8.99e-20

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: 82.40  E-value: 8.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002273012 143 RIDVPVDKYPNYNFVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVKDSVKEDKLRD--KPGYEHLNDPLHVLVEAEFPSD 220
Cdd:cd22470    12 KVLIPVKQFPKFNFVGKLLGPRGNSLKRLQEETLTKMSILGKGSMRDKAKEEELRKsgEAKYFHLNDDLHVLIEVFAPPA 91
                          90
                  ....*....|....*....
gi 1002273012 221 IVDVRLNQAVAILEDLLKP 239
Cdd:cd22470    92 EAYARMGHALEEIKKFLIP 110
KH-I_KHDC4_rpt2 cd22386
first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ...
152-251 9.75e-15

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: 68.74  E-value: 9.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002273012 152 PNYNFVGRLLGPRGNSLKRVEATTQCRVYIRGRGSvkdsvkeDKLRDKPGYEHlNDPLHVLVEAEFPsdivdVRLNQAVA 231
Cdd:cd22386    16 PGFNVRGKLIGPGGSNVKHIQQETGAKVQLRGKGS-------GFIEPASGREA-DEPLHLLISHPDP-----EGLQQAKK 82
                          90       100
                  ....*....|....*....|
gi 1002273012 232 ILEDLLKPVDESMDYYKKQQ 251
Cdd:cd22386    83 LCEDLLQTVHQEYGEFQQQP 102
STAR_dimer pfam16544
Homodimerization region of STAR domain protein; This family is the homodimerization domain of ...
38-81 3.91e-09

Homodimerization region of STAR domain protein; This family is the homodimerization domain of quaking proteins. Quaking-dimer is a helix-turn-helix dimer with an additional helix in the turn region. dimerization is required for adequate RNA-binding. Quaking is a prototypical member of the STAR (signal transducer and activator of RNA) protein family, which plays key roles in post-transcriptional gene regulation by controlling mRNA translation, stability and splicing. STAR_dimer is the homodimerization domain, Qua1 of the STAR domain of a series of proteins referred to as STAR/GSG, or Signal Transduction and Activation of RNA/GRP33, Sam68, GLD-1 family. These are conserved in higher eukaryotes and are RNA-binding transcriptional regulators. The STAR domain is a KH domain flanked by two homologous regions, Qua1 and Qua2. Qua1, this family, is the homodimerization domain, and the KH plus Qua2 is the RNA-binding region.


Pssm-ID: 435414  Cd Length: 52  Bit Score: 51.56  E-value: 3.91e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1002273012  38 YLAELLAERQKLAPFMQVLPFCNRLLNQEILRASSLPPNPNFVE 81
Cdd:pfam16544   8 YLAQLLKDKKQLAAFPNVFPHLERLLDEEISRVRGDLFNKGFGD 51
KH-I_RIK_like_rpt2 cd22472
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein RIK and ...
144-240 3.31e-06

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: 44.74  E-value: 3.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002273012 144 IDVPVDKYPNYNFVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVkdSVKEDKlrdkpgyehlnDPLHVLVEAEFPSdivd 223
Cdd:cd22472     7 LYVGIEAPPSFNLAGRIRGPNNSYLQHIASATGATVALRGRGSG--GAPEGP-----------EPLHLFLSASDPK---- 69
                          90
                  ....*....|....*..
gi 1002273012 224 vRLNQAVAILEDLLKPV 240
Cdd:cd22472    70 -ALEEARGLAENLIDTV 85
KH smart00322
K homology RNA-binding domain;
139-191 4.93e-05

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 40.74  E-value: 4.93e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1002273012  139 KKVVRIDVPVDKypnynfVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVKDSV 191
Cdd:smart00322   2 PVTIEVLIPADK------VGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVV 48
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
142-190 1.90e-04

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: 38.82  E-value: 1.90e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002273012 142 VRIDVPVDkypnynFVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVKDS 190
Cdd:cd00105     1 EEIEVPSE------LVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGE 43
KH-I_IGF2BP1_rpt2 cd22493
second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ...
145-181 6.51e-04

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: 38.11  E-value: 6.51e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1002273012 145 DVPVDKYPNYNFVGRLLGPRGNSLKRVEATTQCRVYI 181
Cdd:cd22493     4 EVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITI 40
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
141-190 2.52e-03

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: 35.72  E-value: 2.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002273012 141 VVRIDVPVDKypnynfVGRLLGPRGNSLKRVEATTQCRVYIRGRGSVKDS 190
Cdd:pfam00013   1 TVEILVPSSL------VGLIIGKGGSNIKEIREETGAKIQIPPSESEGNE 44
 
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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