NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1002233957|ref|XP_015621181|]
View 

KH domain-containing protein At1g09660/At1g09670 [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 4.99e-63

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: 193.86  E-value: 4.99e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233957 139 KKVVRLDVPVDKYPNYNFVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVKDSVKEDKLRDKPGYEHLNEPLHVLVEAEFP 218
Cdd:cd22467     1 KKVLRLDVPVDKYPNFNFVGRILGPRGNSLKRVEATTGCRVFIRGRGSIKDTAKEEKLRDKPGYEHLNEPLHVLIEAELP 80
                          90       100
                  ....*....|....*....|.
gi 1002233957 219 ADIIDTRLNQAVTILEDLLKP 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 6.31e-10

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: 53.87  E-value: 6.31e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1002233957  38 YLAELLAERQKLAPFVQVLPFCTRLLNQEILRASSLPPNHNFVD 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 4.99e-63

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: 193.86  E-value: 4.99e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233957 139 KKVVRLDVPVDKYPNYNFVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVKDSVKEDKLRDKPGYEHLNEPLHVLVEAEFP 218
Cdd:cd22467     1 KKVLRLDVPVDKYPNFNFVGRILGPRGNSLKRVEATTGCRVFIRGRGSIKDTAKEEKLRDKPGYEHLNEPLHVLIEAELP 80
                          90       100
                  ....*....|....*....|.
gi 1002233957 219 ADIIDTRLNQAVTILEDLLKP 239
Cdd:cd22467    81 ANIIDARLQHAQEIIEDLLKP 101
MSL5 COG5176
Splicing factor (branch point binding protein) [RNA processing and modification];
146-265 2.60e-22

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


Pssm-ID: 227503 [Multi-domain]  Cd Length: 269  Bit Score: 93.50  E-value: 2.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233957 146 VPVDKYPNYNFVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVKDSVKEDKLrdKPGYEHLNEPLHVLVEAEFPADIIDTR 225
Cdd:COG5176   154 IPVQEYPESNFVGLLIGPRGSTLKQLERISRAKIAIRGSGSVKEGKISSDT--PESLKNAEAVLHCLIEADSEDKICRLI 231
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002233957 226 LNQAVTILEDLLKPidESMDYYKKQQLRELAILNGTLREE 265
Cdd:COG5176   232 KSQLNAIREARRNP--EGQNDLKRFQLRWLAHLNGTLRAD 269
STAR_dimer pfam16544
Homodimerization region of STAR domain protein; This family is the homodimerization domain of ...
38-81 6.31e-10

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: 53.87  E-value: 6.31e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1002233957  38 YLAELLAERQKLAPFVQVLPFCTRLLNQEILRASSLPPNHNFVD 81
Cdd:pfam16544   8 YLAQLLKDKKQLAAFPNVFPHLERLLDEEISRVRGDLFNKGFGD 51
KH smart00322
K homology RNA-binding domain;
139-191 2.48e-04

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 38.82  E-value: 2.48e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1002233957  139 KKVVRLDVPVDKypnynfVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVKDSV 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 6.07e-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: 34.56  E-value: 6.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002233957 141 VVRLDVPVDKypnynfVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVKDS 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 4.99e-63

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: 193.86  E-value: 4.99e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233957 139 KKVVRLDVPVDKYPNYNFVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVKDSVKEDKLRDKPGYEHLNEPLHVLVEAEFP 218
Cdd:cd22467     1 KKVLRLDVPVDKYPNFNFVGRILGPRGNSLKRVEATTGCRVFIRGRGSIKDTAKEEKLRDKPGYEHLNEPLHVLIEAELP 80
                          90       100
                  ....*....|....*....|.
gi 1002233957 219 ADIIDTRLNQAVTILEDLLKP 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 2.06e-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: 159.06  E-value: 2.06e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233957 139 KKVVRLDVPVDKYPNYNFVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVKDSVKEDKLRDKPGYEHLNEPLHVLVEAEFP 218
Cdd:cd22383     1 KLSEKVYVPVDEYPDYNFVGRILGPRGMTAKQLEQDTGCKIMIRGKGSMRDKKKEEANRGKPNWEHLNDDLHVLITVEDT 80
                          90       100
                  ....*....|....*....|.
gi 1002233957 219 ADIIDTRLNQAVTILEDLLKP 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 4.07e-31

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: 111.99  E-value: 4.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233957 138 VKKVVRLDVPVDKYPNYNFVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVKDSVKEDKLR--DKPGYEHLNEPLHVLVEA 215
Cdd:cd22384     3 IKLSEKVLIPVKEFPKFNFVGKLLGPRGNTLKRLQEETGTKMSILGKGSMRDKAKEEELRksGDPKYAHLNEDLHVLIEA 82
                          90
                  ....*....|....*.
gi 1002233957 216 EFPADIIDTRLNQAVT 231
Cdd:cd22384    83 FAPPAEAYARLAHALA 98
KH-I_Hqk cd22465
type I K homology (KH) RNA-binding domain found in protein quaking (Hqk) and similar proteins; ...
143-239 3.33e-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: 109.64  E-value: 3.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233957 143 RLDVPVDKYPNYNFVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVKDSVKEDKLRDKPGYEHLNEPLHVLVEAEFPADII 222
Cdd:cd22465     5 KLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRA 84
                          90
                  ....*....|....*..
gi 1002233957 223 DTRLNQAVTILEDLLKP 239
Cdd:cd22465    85 EIKLKRAVEEVKKLLVP 101
KH-I_HOW cd22466
type I K homology (KH) RNA-binding domain found in Drosophila protein held out wings (how) and ...
136-239 6.73e-29

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: 106.16  E-value: 6.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233957 136 PVVKKVVRLDVPVDKYPNYNFVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVKDSVKEDKLRDKPGYEHLNEPLHVLVEA 215
Cdd:cd22466     2 PSVTLSEKVYVPVKEHPDYNFVGRILGPRGMTAKQLEQETGCKIMVRGKGSMRDKKKEDLNRGKPNWEHLNDELHVLITV 81
                          90       100
                  ....*....|....*....|....
gi 1002233957 216 EFPADIIDTRLNQAVTILEDLLKP 239
Cdd:cd22466    82 EDTENRAKVKLQRAVEEVRKLLVP 105
KH-I_BBP cd02395
type I K homology (KH) RNA-binding domain found in yeast branchpoint-bridging protein (BBP) ...
139-237 3.76e-27

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: 101.14  E-value: 3.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233957 139 KKVVRLDVPVDKYPNYNFVGRLLGPRGNSLKRVEASTQCRVYIRGRGsvkdSVKEDKLRDKPGYE-HLNEPLHVLVEAEF 217
Cdd:cd02395     1 KKQRKIYIPVDEYPDYNFIGLIIGPRGNTQKRMEKESGAKIAIRGKG----SVKEGKGRSDPQPDpDEEEDLHVLITADT 76
                          90       100
                  ....*....|....*....|
gi 1002233957 218 PADIidtrlNQAVTILEDLL 237
Cdd:cd02395    77 EEKV-----DKAAKLIEKLL 91
MSL5 COG5176
Splicing factor (branch point binding protein) [RNA processing and modification];
146-265 2.60e-22

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


Pssm-ID: 227503 [Multi-domain]  Cd Length: 269  Bit Score: 93.50  E-value: 2.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233957 146 VPVDKYPNYNFVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVKDSVKEDKLrdKPGYEHLNEPLHVLVEAEFPADIIDTR 225
Cdd:COG5176   154 IPVQEYPESNFVGLLIGPRGSTLKQLERISRAKIAIRGSGSVKEGKISSDT--PESLKNAEAVLHCLIEADSEDKICRLI 231
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002233957 226 LNQAVTILEDLLKPidESMDYYKKQQLRELAILNGTLREE 265
Cdd:COG5176   232 KSQLNAIREARRNP--EGQNDLKRFQLRWLAHLNGTLRAD 269
KH-I_KHDRBS1 cd22468
type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal ...
143-239 1.86e-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: 86.61  E-value: 1.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233957 143 RLDVPVDKYPNYNFVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVKDSVKEDKLRD--KPGYEHLNEPLHVLVEAEFPAD 220
Cdd:cd22468     8 RILIPVKQYPKFNFVGKILGPQGNTIKRLQEETGAKISVLGKGSMRDKAKEEELRKggDPKYAHLNMDLHVFIEVFGPPC 87
                          90
                  ....*....|....*....
gi 1002233957 221 IIDTRLNQAVTILEDLLKP 239
Cdd:cd22468    88 EAYARMAHAMEEVKKFLVP 106
KH-I_SF1 cd22382
type I K homology (KH) RNA-binding domain found in splicing factor 1 (SF1) and similar ...
143-215 1.95e-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: 86.21  E-value: 1.95e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002233957 143 RLDVPVDKYPNYNFVGRLLGPRGNSLKRVEASTQCRVYIRGRGsvkdSVKEDKLRDKPG--YEHLNEPLHVLVEA 215
Cdd:cd22382     5 KVMIPQEEYPDINFVGLLIGPRGNTLKKIEKETGAKIMIRGKG----SVKEGKVGRKDGqpLPGEDEPLHALVTA 75
KH-I_KHDRBS2 cd22469
type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal ...
138-239 4.12e-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: 86.33  E-value: 4.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233957 138 VKKVVRLDVPVDKYPNYNFVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVKDSVKEDKLR--DKPGYEHLNEPLHVLVEA 215
Cdd:cd22469     5 IKLSERVLIPVKQYPKFNFVGKLLGPRGNSLKRLQEETGAKMSILGKGSMRDKAKEEELRksGEAKYAHLSDELHVLIEV 84
                          90       100
                  ....*....|....*....|....
gi 1002233957 216 EFPADIIDTRLNQAVTILEDLLKP 239
Cdd:cd22469    85 FAPPGEAYSRMSHALEEIKKFLVP 108
KH-I_KHDRBS3 cd22470
type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal ...
146-239 1.31e-19

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: 82.02  E-value: 1.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233957 146 VPVDKYPNYNFVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVKDSVKEDKLRD--KPGYEHLNEPLHVLVEAEFPADIID 223
Cdd:cd22470    15 IPVKQFPKFNFVGKLLGPRGNSLKRLQEETLTKMSILGKGSMRDKAKEEELRKsgEAKYFHLNDDLHVLIEVFAPPAEAY 94
                          90
                  ....*....|....*.
gi 1002233957 224 TRLNQAVTILEDLLKP 239
Cdd:cd22470    95 ARMGHALEEIKKFLIP 110
KH-I_KHDC4_rpt2 cd22386
first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ...
145-251 8.17e-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: 8.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233957 145 DVPVDKY--------PNYNFVGRLLGPRGNSLKRVEASTQCRVYIRGRGSvkdsvkeDKLRDKPGYEHlNEPLHVLVEAE 216
Cdd:cd22386     1 KYYQEKVfvglehapPGFNVRGKLIGPGGSNVKHIQQETGAKVQLRGKGS-------GFIEPASGREA-DEPLHLLISHP 72
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1002233957 217 FPadiidTRLNQAVTILEDLLKPIDESMDYYKKQQ 251
Cdd:cd22386    73 DP-----EGLQQAKKLCEDLLQTVHQEYGEFQQQP 102
STAR_dimer pfam16544
Homodimerization region of STAR domain protein; This family is the homodimerization domain of ...
38-81 6.31e-10

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: 53.87  E-value: 6.31e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1002233957  38 YLAELLAERQKLAPFVQVLPFCTRLLNQEILRASSLPPNHNFVD 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 ...
144-225 6.64e-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: 43.97  E-value: 6.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002233957 144 LDVPVDKYPNYNFVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVkdSVKEDKlrdkpgyehlnEPLHVLVEAEFPADIID 223
Cdd:cd22472     7 LYVGIEAPPSFNLAGRIRGPNNSYLQHIASATGATVALRGRGSG--GAPEGP-----------EPLHLFLSASDPKALEE 73

                  ..
gi 1002233957 224 TR 225
Cdd:cd22472    74 AR 75
KH smart00322
K homology RNA-binding domain;
139-191 2.48e-04

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 38.82  E-value: 2.48e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1002233957  139 KKVVRLDVPVDKypnynfVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVKDSV 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 4.43e-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: 37.66  E-value: 4.43e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002233957 142 VRLDVPVDkypnynFVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVKDS 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 5.26e-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: 38.50  E-value: 5.26e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1002233957 145 DVPVDKYPNYNFVGRLLGPRGNSLKRVEASTQCRVYI 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 6.07e-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: 34.56  E-value: 6.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002233957 141 VVRLDVPVDKypnynfVGRLLGPRGNSLKRVEASTQCRVYIRGRGSVKDS 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH