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Conserved domains on  [gi|22831735|gb|AAF46032|]
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spoonbill, isoform A [Drosophila melanogaster]

Protein Classification

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List of domain hits

Name Accession Description Interval E-value
Tudor_AKAP1 cd20407
Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; ...
441-517 3.55e-35

Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope, where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. It contains a C-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


:

Pssm-ID: 410478  Cd Length: 76  Bit Score: 126.94  E-value: 3.55e-35
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22831735 441 LLPSLELSAVCVIPINDVWYRVQIVDTDPEDEErCVIKFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTECILSNIEP 517
Cdd:cd20407   1 LPEPIEVGVICAAPVMNAWYRAQVVGVFEETDE-VEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATECYLANIEP 76
KH-I super family cl00098
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
289-356 2.92e-19

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 cd22395:

Pssm-ID: 469614 [Multi-domain]  Cd Length: 68  Bit Score: 81.80  E-value: 2.92e-19
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22831735 289 TYEFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGKNPYSGKVRICTIEGTESEIDAALAMIRQRLP 356
Cdd:cd22395   1 VYEFEVPSELVGRLIGKQGRNVKQLKQKSGAKIYIKPHPYTQNFQICSIEGTQQQIDKALKLIRKKFP 68
 
Name Accession Description Interval E-value
Tudor_AKAP1 cd20407
Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; ...
441-517 3.55e-35

Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope, where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. It contains a C-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410478  Cd Length: 76  Bit Score: 126.94  E-value: 3.55e-35
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22831735 441 LLPSLELSAVCVIPINDVWYRVQIVDTDPEDEErCVIKFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTECILSNIEP 517
Cdd:cd20407   1 LPEPIEVGVICAAPVMNAWYRAQVVGVFEETDE-VEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATECYLANIEP 76
TUDOR pfam00567
Tudor domain;
395-514 1.12e-26

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 104.74  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831735   395 INNDVVVSAVLSGSHIFIQHplHPSHPSLPLLQKQLYDSYSTMEAPLL-PSLELSAVCVIPINDVWYRVQIvdTDPEDEE 473
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQP--KSDSKKLEKLTEELQEYYASKPPESLpPAVGDGCVAAFSEDGKWYRAKI--TESLDDG 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 22831735   474 RCVIKFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTECILSN 514
Cdd:pfam00567  77 LVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLAG 117
KH-I_AKAP1 cd22395
type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 ...
289-356 2.92e-19

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: 81.80  E-value: 2.92e-19
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22831735 289 TYEFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGKNPYSGKVRICTIEGTESEIDAALAMIRQRLP 356
Cdd:cd22395   1 VYEFEVPSELVGRLIGKQGRNVKQLKQKSGAKIYIKPHPYTQNFQICSIEGTQQQIDKALKLIRKKFP 68
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
289-353 4.67e-10

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: 55.75  E-value: 4.67e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22831735   289 TYEFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGKNPYSGKVRICTIEGTESEIDAALAMIRQ 353
Cdd:pfam00013   1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTITGTPEAVEAAKALIEE 65
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
443-500 3.12e-04

Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 38.79  E-value: 3.12e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 22831735    443 PSLELSAVCVIPIND-VWYRVQIVDTDPEDEerCVIKFLDFGGYMNVGFNTLRQIRTDF 500
Cdd:smart00333   1 PTFKVGDKVAARWEDgEWYRARIVKVDGEQL--YEVFFIDYGNEEVVPPSDLRQLPEEL 57
 
Name Accession Description Interval E-value
Tudor_AKAP1 cd20407
Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; ...
441-517 3.55e-35

Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope, where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. It contains a C-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410478  Cd Length: 76  Bit Score: 126.94  E-value: 3.55e-35
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22831735 441 LLPSLELSAVCVIPINDVWYRVQIVDTDPEDEErCVIKFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTECILSNIEP 517
Cdd:cd20407   1 LPEPIEVGVICAAPVMNAWYRAQVVGVFEETDE-VEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATECYLANIEP 76
TUDOR pfam00567
Tudor domain;
395-514 1.12e-26

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 104.74  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831735   395 INNDVVVSAVLSGSHIFIQHplHPSHPSLPLLQKQLYDSYSTMEAPLL-PSLELSAVCVIPINDVWYRVQIvdTDPEDEE 473
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQP--KSDSKKLEKLTEELQEYYASKPPESLpPAVGDGCVAAFSEDGKWYRAKI--TESLDDG 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 22831735   474 RCVIKFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTECILSN 514
Cdd:pfam00567  77 LVEVLFIDYGNTETVPLSDLRPLPPELESLPPQAIKCQLAG 117
KH-I_AKAP1 cd22395
type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 ...
289-356 2.92e-19

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: 81.80  E-value: 2.92e-19
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22831735 289 TYEFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGKNPYSGKVRICTIEGTESEIDAALAMIRQRLP 356
Cdd:cd22395   1 VYEFEVPSELVGRLIGKQGRNVKQLKQKSGAKIYIKPHPYTQNFQICSIEGTQQQIDKALKLIRKKFP 68
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
289-353 4.67e-10

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: 55.75  E-value: 4.67e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22831735   289 TYEFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGKNPYSGKVRICTIEGTESEIDAALAMIRQ 353
Cdd:pfam00013   1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNERIVTITGTPEAVEAAKALIEE 65
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
291-352 5.60e-10

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: 55.38  E-value: 5.60e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22831735 291 EFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGKNPYSGKVRICTIEGTESEIDAALAMIR 352
Cdd:cd00105   2 EIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGERVVTITGTPEAVEKAKELIE 63
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
456-517 1.77e-07

second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410486  Cd Length: 96  Bit Score: 49.36  E-value: 1.77e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22831735 456 NDVWYRVQIVDTdpEDEERCVIKFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTECILSNIEP 517
Cdd:cd20415  37 DGAWYRARIIGL--PGHREVEVKYVDFGNTATVTIKHVRKIKDDFLSLPEKARECRLAFIEP 96
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
418-518 5.00e-07

second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; TDRD12, also called ES cell-associated transcript 8 protein (ECAT8), is a putative ATP-dependent DEAD-like RNA helicase that is essential for germ cell development and maintenance. It acts as a unique piRNA biogenesis factor essential for secondary PIWI interacting RNA (piRNA) biogenesis. TDRD12 contains two Tudor domains, one at the N-terminus and the other at the C-terminal end. The model corresponds to the second/C-terminal one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410506  Cd Length: 134  Bit Score: 49.17  E-value: 5.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831735 418 PSHPSLPLLQKQLYDSYSTMEAP-LLPSLELSAVCVI-PINDVWYRVQ---IVDTDPEDEERCV-IKFLDFGGYMNVGFN 491
Cdd:cd20435  22 SMSSTYLKLSMKLNMYYSDPSNRiLHGKVKVGDLCAVeDENNLYHRVKvleITEKDDKTKPREVlVKFIDEGRVETVVVS 101
                        90       100
                ....*....|....*....|....*..
gi 22831735 492 TLRQIRTDFMNVPFQSTECILSNIEPI 518
Cdd:cd20435 102 QLLELPEELKSLPPQAVEVFLCNVKPV 128
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
457-517 9.70e-07

first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; TDRD7, also called PCTAIRE2-binding protein, or Tudor repeat associator with PCTAIRE-2 (Trap), is a component of specific cytoplasmic RNA granules involved in post-transcriptional regulation of specific genes: probably acts by binding to specific mRNAs and regulating their translation. It is required for lens transparency during lens development, by regulating translation of genes such as CRYBB3 and HSPB1 in the developing lens. It is also essential for dynamic ribonucleoprotein (RNP) remodeling of chromatoid bodies during spermatogenesis. TDRD7 contains three Tudor domains. The model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410498  Cd Length: 98  Bit Score: 47.42  E-value: 9.70e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22831735 457 DVWYRVQIVDTDpedEERCVIKFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTECILSNIEP 517
Cdd:cd20427  36 DAWLRAQVIEVE---EDKVKVYYVDHGFSEVVERSKLFKLNKQFYSLPFQATKCKLAGLEP 93
Tudor_TDRD2 cd20412
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, ...
459-510 1.83e-06

Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, also called Tudor and KH domain-containing protein (TDRKH), participates in the primary piwi-interacting RNA (piRNA) biogenesis pathway and is required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for germline integrity. The family also includes the TDRD2 homolog found in Drosophila melanogaster (dTDRKH), which is also called partner of PIWIs protein, or PAPI, and is involved in Zucchini-mediated piRNA 3'-end maturation. TDRD2 contains two KH domains and one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410483  Cd Length: 95  Bit Score: 46.52  E-value: 1.83e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 22831735 459 WYRVQIVDTDPEDEERcvIKFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTEC 510
Cdd:cd20412  45 WYRARVLGFLENGNLD--LYFVDYGDSGYVPLEDLRALRSDFLSLPFQAIEC 94
KH-I_PCBP_rpt3 cd22439
third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
288-354 7.85e-06

third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411867 [Multi-domain]  Cd Length: 68  Bit Score: 43.76  E-value: 7.85e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22831735 288 TTYEFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGKNPYSGKVRICTIEGTESEIDAALAMIRQR 354
Cdd:cd22439   2 TTQEITIPNDLIGCIIGKGGTKINEIRQLSGATIKIANSEDGSTERSVTITGTPEAVSLAQYLINAR 68
KH-I_HEN4_like_rpt5 cd22462
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH ...
290-351 6.51e-05

fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH domain-containing protein HEN4 and similar protein; 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. HEN4 contains five K-homology (KH) RNA-binding domains. The model corresponds to the KH5 domain of HEN4.


Pssm-ID: 411890 [Multi-domain]  Cd Length: 66  Bit Score: 41.08  E-value: 6.51e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22831735 290 YEFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGKNPYSGKVRICTIEGTESEIDAALAMI 351
Cdd:cd22462   1 IEILIPAHAVGSVIGRGGSNINQIREISGAKVEVLKPDSATGERIVLISGTPDQARHAQNLI 62
Tudor_TDRD6_rpt7 cd20426
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
442-538 7.48e-05

seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the seventh one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410497  Cd Length: 140  Bit Score: 42.87  E-value: 7.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831735 442 LPSLELSAVCVIPIND--VWYRVQIVDTDpedEERCVIKFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTECILSNIEPIG 519
Cdd:cd20426  44 IPSIYVGDPCIVKYSEdnHWYRALVTKIN---DNLVSVRFVDYGNEEDVVREQVRALPSELLKIPVQAFPCCLSGFNLSE 120
                        90       100
                ....*....|....*....|
gi 22831735 520 GTWSIEAAE-ILNKLTKGIV 538
Cdd:cd20426 121 GLWSDEANDyFYEIVTEDLL 140
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
450-496 8.31e-05

Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar proteins; dTUD is required during oogenesis for the formation of primordial germ cells and for normal abdominal segmentation. It contains 11 Tudor domains. The family also includes mitochondrial A-kinase anchor protein 1 (AKAP1) and Tudor domain-containing proteins (TDRDs). AKAP1, also called A-kinase anchor protein 149 kDa (AKAP 149), or dual specificity A-kinase-anchoring protein 1 (D-AKAP-1), or protein kinase A-anchoring protein 1 (PRKA1), or Spermatid A-kinase anchor protein 84 (S-AKAP84), is found in mitochondria and in the endoplasmic reticulum-nuclear envelope where it anchors protein kinases, phosphatases, and a phosphodiesterase. It regulates multiple cellular processes governing mitochondrial homeostasis and cell viability. AKAP1 binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. TDRDs have diverse biological functions and may contain one or more copies of the Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410450  Cd Length: 50  Bit Score: 40.19  E-value: 8.31e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 22831735 450 VCV-IPINDVWYRVQIVDTDPEDEerCVIKFLDFGGYMNVGFNTLRQI 496
Cdd:cd20379   5 CAAkYEEDGKWYRARVLEVLSNDK--VEVFFVDYGNTETVPLSDLRPL 50
KH-I_PCBP1_2_rpt3 cd22521
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) ...
288-359 8.75e-05

third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) and similar proteins; The family includes PCBP1 (also called alpha-CP1, or heterogeneous nuclear ribonucleoprotein E1, or hnRNP E1, or nucleic acid-binding protein SUB2.3) and PCBP2 (also called alpha-CP2, or heterogeneous nuclear ribonucleoprotein E2, or hnRNP E2). They are single-stranded nucleic acid binding proteins that bind preferentially to oligo dC. They act as iron chaperones for ferritin. In case of infection by poliovirus, PCBP1 plays a role in initiation of viral RNA replication in concert with the viral protein 3CD. PCBP2 is a major cellular poly(rC)-binding protein. It also binds poly(rU). PCBP2 negatively regulates cellular antiviral responses mediated by MAVS signaling. It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation. PCBP2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer. Both PCBP1 and PCBP2 contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411949  Cd Length: 76  Bit Score: 41.19  E-value: 8.75e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22831735 288 TTYEFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGkNPYSGKV-RICTIEGTESEIDAALAMIRQRLPAKR 359
Cdd:cd22521   5 TSHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIA-NPVEGSTdRQVTITGSAASISLAQYLINARLSSEK 76
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
288-353 1.62e-04

first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411824 [Multi-domain]  Cd Length: 68  Bit Score: 39.93  E-value: 1.62e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22831735 288 TTYEFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGKNPYSGKVRICTIEGTESEIDAALAMIRQ 353
Cdd:cd22396   1 VTEEYKVPDKMVGLIIGRGGEQINRLQAESGAKIQIAPDSGGLPERPCTLTGTPDAIETAKRLIDQ 66
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
459-520 2.95e-04

fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410494  Cd Length: 80  Bit Score: 39.77  E-value: 2.95e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22831735 459 WYRVQIVDTDPEDEERCVIkFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTECILSNIEPIGG 520
Cdd:cd20423  19 WCRALIDNVYEPVEMVEVT-YVDYGNKELVSLKNLRSISEEFLKLKAQAFRCSLYNLIQPSG 79
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
443-500 3.12e-04

Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in the Drosophila Tudor protein. Initial proposal that the survival motor neuron gene product contain a Tudor domain are corroborated by more recent database search techniques such as PSI-BLAST (unpublished).


Pssm-ID: 197660  Cd Length: 57  Bit Score: 38.79  E-value: 3.12e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 22831735    443 PSLELSAVCVIPIND-VWYRVQIVDTDPEDEerCVIKFLDFGGYMNVGFNTLRQIRTDF 500
Cdd:smart00333   1 PTFKVGDKVAARWEDgEWYRARIVKVDGEQL--YEVFFIDYGNEEVVPPSDLRQLPEEL 57
Tudor_TDRD15_rpt2 cd20437
second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
394-513 3.27e-04

second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410508  Cd Length: 120  Bit Score: 40.48  E-value: 3.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831735 394 GINNDVVVSAVLSGSHIFIQhpLHPSHPSLPLLQKQLYDSYSTMEAPLLPSLE-LSAVCVIPIND-VWYRvQIVDTDPED 471
Cdd:cd20437   2 GTTEKVKITAAVSPSKFYCQ--LLSWEPELSKLTTQMTLHYESVSKELNPSCEnFGLLCAAKGKDgQWHR-GFLQQLLPP 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 22831735 472 EERCVIkFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTECILS 513
Cdd:cd20437  79 SQVKVW-FIDYGNSEAVSSHSVLKLPPDFFSLPLMSFPCSLS 119
Tudor_TDRD15_rpt4 cd20439
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
398-515 3.29e-04

fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the fourth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410510  Cd Length: 125  Bit Score: 40.94  E-value: 3.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831735 398 DVVVSAVLSGSHIFIQhpLHPSHPSLPLLQKQLYDSYSTMEAPLLPSlelSAVCVIP-IND-VWYRVQIVDTDPEDEERC 475
Cdd:cd20439  13 DVKCSYVNSPGDFWCQ--LQTKSSELKSLMKQIQSYYLIHNDPYKHG---QIACVAKySKDgKWYRAAVLKQVSAKEVDV 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 22831735 476 VikFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTECILSNI 515
Cdd:cd20439  88 I--FVDYGNQERVLISDLRAIKPQFLLLEGQAFRCSLNNF 125
Tudor_TDRD6_rpt3 cd20422
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
430-526 3.96e-04

third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; TDRD6, also called antigen NY-CO-45 or cancer/testis antigen 41.2 (CT41.2), is a testis-specific expressed protein that was localized to the chromatoid bodies in germ cells, and is involved in spermiogenesis, chromatoid body formation, and for proper precursor and mature miRNA expression. Mutations in TDRD6 may be associated with human male infertility and early embryonic lethality. TDRD6 contains seven Tudor domains. This model corresponds to the third one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410493  Cd Length: 135  Bit Score: 40.96  E-value: 3.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831735 430 LYDSYSTMEAPLLPSLELSAVCVIPINDVWYRVQIVDTDPEDEErcvIKFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTE 509
Cdd:cd20422  36 FYSQASKLDGVVLKPQPGQLCCAKWKEDRYYRAIVTAVKGKMVE---VFLVDRGNTEMVDWYDVKKLLPQFRELPALALK 112
                        90
                ....*....|....*..
gi 22831735 510 CILSNIEPIGGTWSIEA 526
Cdd:cd20422 113 CCLADICPLGERWSPEA 129
KH-I_PCBP3_rpt3 cd22522
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) ...
282-354 5.24e-04

third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) and similar proteins; PCBP3, also called alpha-CP3, or PCBP3-overlapping transcript, or PCBP3-overlapping transcript 1, or heterogeneous nuclear ribonucleoprotein E3, or hnRNP E3, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It can function as a repressor dependent on binding to single-strand and double-stranded poly(C) sequences. PCBP3 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411950 [Multi-domain]  Cd Length: 75  Bit Score: 38.94  E-value: 5.24e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22831735 282 EATRVKTTYEFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGKNPYSGKVRICTIEGTESEIDAALAMIRQR 354
Cdd:cd22522   3 DASPPASTHELTIPNDLIGCIIGRQGTKINEIRQMSGAQIKIANATEGSSERQITITGSPANISLAQYLINAR 75
KH-I_PEPPER_rpt1_like cd22459
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
287-341 6.02e-04

first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER, flowering locus K homology domain protein (FLK), RNA-binding KH domain-containing protein RCF3 and KH domain-containing protein HEN4. PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 and HEN4 contain five KH RNA-binding domains. The model corresponds to the KH1 domain of PEPPER and FLK, as well as KH1 and KH3 domains of RCF3 and HEN4.


Pssm-ID: 411887 [Multi-domain]  Cd Length: 69  Bit Score: 38.36  E-value: 6.02e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22831735 287 KTTYEFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGKNPYSGKVRICTIEGTE 341
Cdd:cd22459   1 EVVFRLLCPVSKAGSVIGKGGEIIKQLRQETGARIKVEDGVPGTEERVITISSSE 55
KH-I_NOVA_rpt2 cd22436
second type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
293-355 8.98e-04

second 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 second one.


Pssm-ID: 411864 [Multi-domain]  Cd Length: 70  Bit Score: 37.98  E-value: 8.98e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22831735 293 LFPISLIGHLYGRKRAFINQIKAKTLASVSVGKNPYSGKV--RICTIEGTESEIDAALAMIRQRL 355
Cdd:cd22436   6 LVPNSTAGMIIGKGGATIKAIMEQSGARVQISQKPESINLqeRVVTVTGEPEANRKAVSLILQKI 70
Tudor_TDRD15_rpt1 cd20436
first Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
458-526 1.61e-03

first Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; TDRD15 is an uncharacterized Tudor domain-containing protein that contains seven Tudor domains. This model corresponds to the first one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410507  Cd Length: 147  Bit Score: 39.33  E-value: 1.61e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831735 458 VWYRVQIvdTDPEDEERCVikFL-DFGGYMNVGFNTLRQIRTDFMNVPFQSTECILSNIEPIGGTWSIEA 526
Cdd:cd20436  62 EWYRGRV--LEKIDEKYEV--FLiDRGEVLNVHATNMASASGELFQLPPKAVCGIFANILPIGEKWSSTA 127
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
459-526 3.20e-03

fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; TDRD4, also called RING finger protein 17 (RNF17), is a component of the mammalian germ cell nuage and is essential for spermiogenesis. It seems to be involved in the regulation of transcriptional activity of MYC. In vitro, TDRD4 inhibits the DNA-binding activity of Mad-MAX heterodimers. It can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. TDRD4 also acts as a potential cancer/testis antigen in liver cancer. TDRD4 contains a RING finger and five Tudor domains. This model corresponds to the fifth one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410489  Cd Length: 105  Bit Score: 37.39  E-value: 3.20e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22831735 459 WYRVQIVDTDPEDEERCVIKFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTECILSNIEPI---GGT--------WSIEA 526
Cdd:cd20418  19 WYRAKLLSILEFNPVKILVRHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPPlndSETeripycpeWSMKA 97
Tudor_TDRD7_rpt2 cd20428
second Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
398-526 3.83e-03

second Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; TDRD7, also called PCTAIRE2-binding protein, or Tudor repeat associator with PCTAIRE-2 (Trap), is a component of specific cytoplasmic RNA granules involved in post-transcriptional regulation of specific genes: probably acts by binding to specific mRNAs and regulating their translation. It is required for lens transparency during lens development, by regulating translation of genes such as CRYBB3 and HSPB1 in the developing lens. It is also essential for dynamic ribonucleoprotein (RNP) remodeling of chromatoid bodies during spermatogenesis. TDRD7 contains three Tudor domains. The model corresponds to the second one. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410499  Cd Length: 140  Bit Score: 38.19  E-value: 3.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831735 398 DVVVSAVLSGSHIFIQHPLHPSHPSLPLLQK-QLYDSYSTMEAPLLPSLELSA-VCVIPINDVWYRVQIVDTDpedEERC 475
Cdd:cd20428   3 NVRVTNVCSDGTLYCQVPSKGLSKLNEILDKiEYYFHSRQMTSEYFVSLPFCGkICLARYKGKWARVEITNVH---SSRA 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 22831735 476 V-IKFLDFGGYMNVGFNTLRQIRTDFM----NVPFQSTECILSNIEPIGGTWSIEA 526
Cdd:cd20428  80 LdVHFLDTGTVASVKVSELREIPPPFLreliSIPPQALKCCLADLPLNIGMWTPDA 135
KH-I_PCBP4_rpt3 cd22523
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ...
288-351 4.13e-03

third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) and similar proteins; PCBP4, also called alpha-CP4, or heterogeneous nuclear ribonucleoprotein E4, or hnRNP E4, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It regulates both basal and stress-induced p21 expression through binding p21 3'-UTR and modulating p21 mRNA stability. It also plays a role in the cell cycle and is implicated in lung tumor suppression. PCBP4 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411951  Cd Length: 68  Bit Score: 36.03  E-value: 4.13e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22831735 288 TTYEFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGKNPYSGKVRICTIEGTESEIDAALAMI 351
Cdd:cd22523   2 SSQEFLIPNDLIGCVIGRQGSKISEIRQMSGAHIKIGNQTEGTSERHVTITGSPVSITLAQYLI 65
KH-I_PCBP_rpt2 cd02396
second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
287-356 4.85e-03

second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411806 [Multi-domain]  Cd Length: 72  Bit Score: 36.09  E-value: 4.85e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22831735 287 KTTYEFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGKN--PYSGKvRICTIEGTESEIDAALAMIRQRLP 356
Cdd:cd02396   1 PITLRLLVPASQCGSLIGKGGSKIKEIRESTGASVQVASEmlPNSTE-RAVTISGSPEAITKCVEQICCVML 71
KH-I_MER1_like cd22458
type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae meiotic ...
289-353 5.51e-03

type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae meiotic recombination 1 protein (MER1) and similar proteins; MER1 is required for chromosome pairing and genetic recombination. It may function to bring the axial elements of the synaptonemal complex corresponding to homologous chromosomes together by initiating recombination. MER1 might be responsible for regulating the MER2 gene and/or gene product.


Pssm-ID: 411886 [Multi-domain]  Cd Length: 65  Bit Score: 35.50  E-value: 5.51e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22831735 289 TYEFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGKNPYSgKVRICTIEGTESEIDAALAMIRQ 353
Cdd:cd22458   2 TWEIKLPQALCGRLIGAKGKNIKALSEKSGASIRLIPISNS-SQQTIHLSGTDKQIALAISSIEE 65
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
285-354 8.44e-03

type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic translation initiation factor 4E-binding protein Mextli and similar proteins; Mextli is a novel eukaryotic translation initiation factor 4E-binding protein that promotes translation in Drosophila melanogaster.


Pssm-ID: 411882 [Multi-domain]  Cd Length: 71  Bit Score: 35.37  E-value: 8.44e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831735 285 RVKTTYEFLFPISLIGHLYGRKRAFINQIKAKTLASVSVGKNPYSGKVRICTIEGTESEIDAALAMIRQR 354
Cdd:cd22454   1 TGQTTIEVVIPNADVGKVIGKGGETIKRIEALTDTVITFERVNGGSPNREVQITGSPDNVAAAKRLIEDT 70
Tudor_TDRD5 cd20419
Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is ...
401-512 8.68e-03

Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is an RNA-binding protein directly associated with piRNA precursors. It is required for retrotransposon silencing, chromatoid body assembly, and spermiogenesis. TDRD5 participates in the repression of transposable elements and prevents their mobilization, which is essential for germline integrity. TDRD5 contains three LOTUS domains and one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410490  Cd Length: 118  Bit Score: 36.66  E-value: 8.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22831735 401 VSAVLSGSHIFIQHPLHPSHPSLPLLQKQLYDSYST---MEAPLLPSLELS---AVCVIPINDV-WYRVQIVDTDPEDEE 473
Cdd:cd20419   2 VEYIESPSQFYVRFYSKDTSEMLEDMMIEMRRCYSNehvSERYVMPEAFIQpgqVCCVRIPEDVwWYRVIIHQVLNKQEV 81
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 22831735 474 RcvIKFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTECIL 512
Cdd:cd20419  82 E--VFYPDFGDIGTVQKSRLRFLKCCYSKLPAQAIPASL 118
 
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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