predicted protein [Candida tropicalis MYA-3404]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| MSL5 super family | cl34926 | Splicing factor (branch point binding protein) [RNA processing and modification]; |
43-279 | 6.05e-62 | ||||
Splicing factor (branch point binding protein) [RNA processing and modification]; The actual alignment was detected with superfamily member COG5176: Pssm-ID: 227503 [Multi-domain] Cd Length: 269 Bit Score: 200.97 E-value: 6.05e-62
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| Name | Accession | Description | Interval | E-value | ||||
| MSL5 | COG5176 | Splicing factor (branch point binding protein) [RNA processing and modification]; |
43-279 | 6.05e-62 | ||||
Splicing factor (branch point binding protein) [RNA processing and modification]; Pssm-ID: 227503 [Multi-domain] Cd Length: 269 Bit Score: 200.97 E-value: 6.05e-62
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| SF1-HH | pfam16275 | Splicing factor 1 helix-hairpin domain; This domain, approximately 100 residues in length, is ... |
25-153 | 1.22e-41 | ||||
Splicing factor 1 helix-hairpin domain; This domain, approximately 100 residues in length, is mainly found in splicing factor 1 from yeast to human. It is a helix-hairpin domain, which forms a secondary, hydrophobic interface with U2AF65(UHM) to lock the orientation of the two subunits, which is essential for cooperative formation of the ternary SF1-U2AF65-RNA complex. In this domain, it contains a highly conserved SPSP motif in its C terminal and phophorylation of SPSP motif induces a disorder-to-order transition within a novel SF1/U2AF65 interface, indicating a phosphorylation-dependent control of pre-mRNA splicing factors. Pssm-ID: 465080 Cd Length: 114 Bit Score: 142.75 E-value: 1.22e-41
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| KH-I_BBP | cd02395 | type I K homology (KH) RNA-binding domain found in yeast branchpoint-bridging protein (BBP) ... |
158-250 | 5.00e-41 | ||||
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: 140.43 E-value: 5.00e-41
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| KH | smart00322 | K homology RNA-binding domain; |
158-249 | 3.04e-07 | ||||
K homology RNA-binding domain; Pssm-ID: 197652 [Multi-domain] Cd Length: 68 Bit Score: 47.29 E-value: 3.04e-07
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| Name | Accession | Description | Interval | E-value | ||||
| MSL5 | COG5176 | Splicing factor (branch point binding protein) [RNA processing and modification]; |
43-279 | 6.05e-62 | ||||
Splicing factor (branch point binding protein) [RNA processing and modification]; Pssm-ID: 227503 [Multi-domain] Cd Length: 269 Bit Score: 200.97 E-value: 6.05e-62
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| SF1-HH | pfam16275 | Splicing factor 1 helix-hairpin domain; This domain, approximately 100 residues in length, is ... |
25-153 | 1.22e-41 | ||||
Splicing factor 1 helix-hairpin domain; This domain, approximately 100 residues in length, is mainly found in splicing factor 1 from yeast to human. It is a helix-hairpin domain, which forms a secondary, hydrophobic interface with U2AF65(UHM) to lock the orientation of the two subunits, which is essential for cooperative formation of the ternary SF1-U2AF65-RNA complex. In this domain, it contains a highly conserved SPSP motif in its C terminal and phophorylation of SPSP motif induces a disorder-to-order transition within a novel SF1/U2AF65 interface, indicating a phosphorylation-dependent control of pre-mRNA splicing factors. Pssm-ID: 465080 Cd Length: 114 Bit Score: 142.75 E-value: 1.22e-41
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| KH-I_BBP | cd02395 | type I K homology (KH) RNA-binding domain found in yeast branchpoint-bridging protein (BBP) ... |
158-250 | 5.00e-41 | ||||
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: 140.43 E-value: 5.00e-41
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| KH-I_SF1 | cd22382 | type I K homology (KH) RNA-binding domain found in splicing factor 1 (SF1) and similar ... |
161-249 | 3.26e-28 | ||||
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: 106.62 E-value: 3.26e-28
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| KH-I_Hqk_like | cd22383 | type I K homology (KH) RNA-binding domain found in protein quaking (Hqk) family; The Hqk ... |
158-253 | 1.86e-26 | ||||
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: 102.05 E-value: 1.86e-26
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| KH-I_Hqk | cd22465 | type I K homology (KH) RNA-binding domain found in protein quaking (Hqk) and similar proteins; ... |
161-253 | 1.79e-22 | ||||
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: 91.15 E-value: 1.79e-22
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| KH-I_KHDRBS | cd22384 | type I K homology (KH) RNA-binding domain found in the KH domain-containing, RNA-binding, ... |
155-242 | 6.44e-22 | ||||
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: 89.65 E-value: 6.44e-22
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| KH-I_HOW | cd22466 | type I K homology (KH) RNA-binding domain found in Drosophila protein held out wings (how) and ... |
161-253 | 2.40e-21 | ||||
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: 88.05 E-value: 2.40e-21
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| KH-I_KHDRBS1 | cd22468 | type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal ... |
158-230 | 1.26e-17 | ||||
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: 77.75 E-value: 1.26e-17
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| KH-I_KHDRBS2 | cd22469 | type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal ... |
158-230 | 9.83e-17 | ||||
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: 75.93 E-value: 9.83e-17
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| KH-I_SPIN1_like | cd22467 | type I K homology (KH) RNA-binding domain found in Oryza sativa SPL11-interacting protein 1 ... |
158-253 | 1.52e-16 | ||||
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: 74.84 E-value: 1.52e-16
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| KH-I_KHDRBS3 | cd22470 | type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal ... |
158-230 | 1.17e-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: 67.00 E-value: 1.17e-13
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| KH-I_KHDC4_rpt2 | cd22386 | first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ... |
161-252 | 1.06e-12 | ||||
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: 63.73 E-value: 1.06e-12
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| KH-I | cd00105 | K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ... |
161-246 | 1.33e-07 | ||||
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: 48.06 E-value: 1.33e-07
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| KH | smart00322 | K homology RNA-binding domain; |
158-249 | 3.04e-07 | ||||
K homology RNA-binding domain; Pssm-ID: 197652 [Multi-domain] Cd Length: 68 Bit Score: 47.29 E-value: 3.04e-07
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| KH_1 | pfam00013 | KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ... |
161-205 | 7.24e-06 | ||||
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia. Pssm-ID: 459630 [Multi-domain] Cd Length: 65 Bit Score: 43.42 E-value: 7.24e-06
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| KH-I_TDRKH_rpt1 | cd22428 | first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ... |
176-249 | 7.67e-06 | ||||
first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the first one. Pssm-ID: 411856 [Multi-domain] Cd Length: 74 Bit Score: 43.48 E-value: 7.67e-06
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| KH-I_ScSCP160_rpt2 | cd22447 | second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ... |
174-249 | 3.97e-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: 41.63 E-value: 3.97e-05
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| KH-I_FUBP_rpt1 | cd22396 | first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ... |
174-249 | 5.60e-05 | ||||
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: 41.09 E-value: 5.60e-05
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| KH-I_RIK_like_rpt2 | cd22472 | second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein RIK and ... |
163-250 | 6.04e-05 | ||||
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: 41.66 E-value: 6.04e-05
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| KH-I_NOVA_rpt3 | cd09031 | third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ... |
171-204 | 1.11e-04 | ||||
third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova); The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411807 [Multi-domain] Cd Length: 71 Bit Score: 40.25 E-value: 1.11e-04
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| KH-I_Vigilin_rpt3 | cd22407 | third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ... |
160-200 | 2.20e-04 | ||||
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: 39.11 E-value: 2.20e-04
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| KH-I_KHDC4_rpt1 | cd22385 | first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ... |
183-249 | 2.75e-04 | ||||
first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein 4 (KHDC4) and similar proteins; KHDC4, also called Brings lots of money 7 (Blom7), or pre-mRNA splicing factor protein KHDC4, is an RNA-binding protein involved in pre-mRNA splicing. It interacts with the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome. KHDC4 binds preferentially RNA with A/C rich sequences and poly-C stretches. KHDC4 contains two type I K homology (KH) RNA-binding domains. The model corresponds to the first one. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif. Pssm-ID: 411813 Cd Length: 84 Bit Score: 39.50 E-value: 2.75e-04
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| KH-I_PEPPER_rpt2_like | cd22460 | second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ... |
176-214 | 5.55e-04 | ||||
second 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 KH2 domain of PEPPER and FLK, as well as KH2 and KH4 domains of RCF3 and HEN4. Pssm-ID: 411888 [Multi-domain] Cd Length: 73 Bit Score: 38.37 E-value: 5.55e-04
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| KH-I_IGF2BP_rpt3 | cd22402 | third type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ... |
162-200 | 1.28e-03 | ||||
third type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/ CRD-BP/ VICKZ1, IGF2BP2/IMP-2/ VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain 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 third one. Pssm-ID: 411830 [Multi-domain] Cd Length: 66 Bit Score: 36.84 E-value: 1.28e-03
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| KH-I_BTR1_rpt2 | cd22437 | second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 ... |
175-249 | 2.94e-03 | ||||
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and similar proteins; BTR1, also called Binding to ToMV RNA 1, is a negative regulator of tomato mosaic virus (ToMV) multiplication but has no effect on the multiplication of cucumber mosaic virus (CMV). BTR1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one. Pssm-ID: 411865 [Multi-domain] Cd Length: 69 Bit Score: 36.04 E-value: 2.94e-03
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| KH-I_IGF2BP_rpt1 | cd22400 | first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ... |
162-203 | 3.75e-03 | ||||
first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/ CRD-BP/ VICKZ1, IGF2BP2/IMP-2/ VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain 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 first one. Pssm-ID: 411828 [Multi-domain] Cd Length: 68 Bit Score: 35.71 E-value: 3.75e-03
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| KH-I_ScSCP160_rpt1 | cd22446 | first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ... |
154-226 | 5.48e-03 | ||||
first 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 first one. Pssm-ID: 411874 [Multi-domain] Cd Length: 86 Bit Score: 35.84 E-value: 5.48e-03
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| KH-I_IGF2BP1_rpt2 | cd22493 | second type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ... |
165-200 | 8.36e-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: 8.36e-03
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| KH-I_IGF2BP_rpt2 | cd22401 | second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ... |
174-200 | 9.25e-03 | ||||
second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/ CRD-BP/ VICKZ1, IGF2BP2/IMP-2/ VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain 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: 411829 [Multi-domain] Cd Length: 72 Bit Score: 34.89 E-value: 9.25e-03
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| KH-I_AKAP1 | cd22395 | type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 ... |
174-201 | 9.42e-03 | ||||
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: 34.80 E-value: 9.42e-03
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