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Conserved domains on  [gi|1845974109|ref|NP_001370528|]
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KH domain-containing protein akap-1 [Caenorhabditis elegans]

Protein Classification

A-kinase anchoring protein 1( domain architecture ID 16910147)

A-kinase anchoring protein 1 (AKAP1) anchors protein kinase A to the mitochondrial outer membrane which brings various molecules from the cytosol to mitochondria and that it regulates factors associated with mitochondrial physiological activities

Gene Ontology:  GO:0003723|GO:0005681|GO:0005739|GO:0060090
PubMed:  8696973|25625331

Graphical summary

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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; ...
 686-761 4.99e-38

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: 136.18  E-value: 4.99e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845974109 686 LPIPCQNGLLCAAPVGNAWFRAVTVQYFDETDEVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRP 761
Cdd:cd20407     1 LPEPIEVGVICAAPVMNAWYRAQVVGVFEETDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATECYLANIEP 76
KH-I_AKAP1 cd22395
type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 ...
 530-600 3.61e-26

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: 102.21  E-value: 3.61e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845974109 530 MYEFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETdkvKTHQICQVRGKRDEINHCLQMLRRRFP 600
Cdd:cd22395     1 VYEFEVPSELVGRLIGKQGRNVKQLKQKSGAKIYIKPHPYT---QNFQICSIEGTQQQIDKALKLIRKKFP 68
PTZ00121 super family cl31754
MAEBL; Provisional
 183-477 2.92e-04

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109  183 QKQQQKDEDEKTQKKDAVQNEKPSIDKK--QPKSQAPTEKKEEKTVEIHTETEETDHVAAGDSGVVSEHKEH--DKKTKQ 258
Cdd:PTZ00121  1296 KKAEEKKKADEAKKKAEEAKKADEAKKKaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaaEKKKEE 1375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109  259 KNDEPVSIDKKSEEIEVPKQAGVVNEEPKKQSEETVVEEQFVKKEEPKLKSAPTPLLTMPSKKKVLENEQIPEepTPTKM 338
Cdd:PTZ00121  1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADE--AKKKA 1453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109  339 NDATSPLSLDIAAQMSPASFSWSEEMEKSFNEEEfrLNESSDIDRSPASPLRHLQQQHNK----NRSSQKRKGGRVNGRD 414
Cdd:PTZ00121  1454 EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE--AKKKAEEAKKKADEAKKAAEAKKKadeaKKAEEAKKADEAKKAE 1531

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845974109  415 GVHQPQQQHQQQKKEEQGQIKKGQ--RRLTKEKSVEETPEKSQKRVVLKHHENEAGDAAHAQIIE 477
Cdd:PTZ00121  1532 EAKKADEAKKAEEKKKADELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
 
Name Accession Description Interval E-value
Tudor_AKAP1 cd20407
Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; ...
 686-761 4.99e-38

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: 136.18  E-value: 4.99e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845974109 686 LPIPCQNGLLCAAPVGNAWFRAVTVQYFDETDEVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRP 761
Cdd:cd20407     1 LPEPIEVGVICAAPVMNAWYRAQVVGVFEETDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATECYLANIEP 76
TUDOR pfam00567
Tudor domain;
638-758 8.22e-27

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 105.51  E-value: 8.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 638 IKCEVAVSSIISASHFFIQQptHPSFASLRHLDMYMGSLYGEQSNlPELPIPCQNGLLCAAPVGNAWFRAVtVQYFDETD 717
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQP--KSDSKKLEKLTEELQEYYASKPP-ESLPPAVGDGCVAAFSEDGKWYRAK-ITESLDDG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1845974109 718 EVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAH 758
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 ...
 530-600 3.61e-26

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: 102.21  E-value: 3.61e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845974109 530 MYEFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETdkvKTHQICQVRGKRDEINHCLQMLRRRFP 600
Cdd:cd22395     1 VYEFEVPSELVGRLIGKQGRNVKQLKQKSGAKIYIKPHPYT---QNFQICSIEGTQQQIDKALKLIRKKFP 68
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 531-596 2.34e-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: 56.91  E-value: 2.34e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845974109 531 YEFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHhetDKVKTHQICQVRGKRDEINHCLQMLR 596
Cdd:pfam00013   2 VEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPS---ESEGNERIVTITGTPEAVEAAKALIE 64
KH smart00322
K homology RNA-binding domain;
532-598 1.50e-09

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 54.61  E-value: 1.50e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845974109  532 EFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETDKVKThqicqVRGKRDEINHCLQMLRRR 598
Cdd:smart00322   6 EVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVE-----ITGPPENVEKAAELILEI 67
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 693-744 9.00e-08

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: 49.58  E-value: 9.00e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1845974109  693 GLLCAAPVGN-AWFRAVTVQYfDETDEVFVKFVDYGGYSKMARQDLRQIRTDL 744
Cdd:smart00333   6 GDKVAARWEDgEWYRARIVKV-DGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
PTZ00121 PTZ00121
MAEBL; Provisional
 183-477 2.92e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109  183 QKQQQKDEDEKTQKKDAVQNEKPSIDKK--QPKSQAPTEKKEEKTVEIHTETEETDHVAAGDSGVVSEHKEH--DKKTKQ 258
Cdd:PTZ00121  1296 KKAEEKKKADEAKKKAEEAKKADEAKKKaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaaEKKKEE 1375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109  259 KNDEPVSIDKKSEEIEVPKQAGVVNEEPKKQSEETVVEEQFVKKEEPKLKSAPTPLLTMPSKKKVLENEQIPEepTPTKM 338
Cdd:PTZ00121  1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADE--AKKKA 1453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109  339 NDATSPLSLDIAAQMSPASFSWSEEMEKSFNEEEfrLNESSDIDRSPASPLRHLQQQHNK----NRSSQKRKGGRVNGRD 414
Cdd:PTZ00121  1454 EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE--AKKKAEEAKKKADEAKKAAEAKKKadeaKKAEEAKKADEAKKAE 1531

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845974109  415 GVHQPQQQHQQQKKEEQGQIKKGQ--RRLTKEKSVEETPEKSQKRVVLKHHENEAGDAAHAQIIE 477
Cdd:PTZ00121  1532 EAKKADEAKKAEEKKKADELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
Caldesmon pfam02029
Caldesmon;
172-332 7.45e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 39.85  E-value: 7.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 172 NGDVQSSIGVSQKQQQKDEDEKTQKKDAVQNEKPSiDKKQPKSQAPTEKKEEKTVEIHTETEETDHVAAGDSGVVSEHKE 251
Cdd:pfam02029  93 IADEKESVAERKENNEEEENSSWEKEEKRDSRLGR-YKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPT 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 252 HDKKTKQKNDEPVSIDKK-SEEIEVPKQAGVVNEEPKKQSEETVVEEQFVkKEEPKLKSAPTPLLTMPSKKKVLENEQIP 330
Cdd:pfam02029 172 ENFAKEEVKDEKIKKEKKvKYESKVFLDQKRGHPEVKSQNGEEEVTKLKV-TTKRRQGGLSQSQEREEEAEVFLEAEQKL 250


                  ..
gi 1845974109 331 EE 332
Cdd:pfam02029 251 EE 252
 
Name Accession Description Interval E-value
Tudor_AKAP1 cd20407
Tudor domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; ...
 686-761 4.99e-38

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: 136.18  E-value: 4.99e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845974109 686 LPIPCQNGLLCAAPVGNAWFRAVTVQYFDETDEVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRP 761
Cdd:cd20407     1 LPEPIEVGVICAAPVMNAWYRAQVVGVFEETDEVEIKYLDYGGYERVPVDDLRQIRSDFMTLPFQATECYLANIEP 76
TUDOR pfam00567
Tudor domain;
638-758 8.22e-27

Tudor domain;


Pssm-ID: 425754 [Multi-domain]  Cd Length: 117  Bit Score: 105.51  E-value: 8.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 638 IKCEVAVSSIISASHFFIQQptHPSFASLRHLDMYMGSLYGEQSNlPELPIPCQNGLLCAAPVGNAWFRAVtVQYFDETD 717
Cdd:pfam00567   1 STIDVVVSHIESPSTFYIQP--KSDSKKLEKLTEELQEYYASKPP-ESLPPAVGDGCVAAFSEDGKWYRAK-ITESLDDG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1845974109 718 EVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAH 758
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 ...
 530-600 3.61e-26

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: 102.21  E-value: 3.61e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845974109 530 MYEFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETdkvKTHQICQVRGKRDEINHCLQMLRRRFP 600
Cdd:cd22395     1 VYEFEVPSELVGRLIGKQGRNVKQLKQKSGAKIYIKPHPYT---QNFQICSIEGTQQQIDKALKLIRKKFP 68
Tudor_TDRD12_rpt2 cd20435
second Tudor domain found in Tudor domain-containing protein 12 (TDRD12) and similar proteins; ...
 649-768 1.09e-11

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: 63.04  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 649 SASHFFIQ---------QPTHPSFASLRHLDMYMGSLYGEQSNLPELPIPCQNGLLCAAPVGNAWFRaVTVQYFDETD-- 717
Cdd:cd20435     1 DATHYSARilehrssdgEVTKSMSSTYLKLSMKLNMYYSDPSNRILHGKVKVGDLCAVEDENNLYHR-VKVLEITEKDdk 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1845974109 718 ----EVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRPVDGTTNW 768
Cdd:cd20435    80 tkprEVLVKFIDEGRVETVVVSQLLELPEELKSLPPQAVEVFLCNVKPVDNDTEW 134
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 532-596 1.75e-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: 57.31  E-value: 1.75e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845974109 532 EFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETDkvkTHQICQVRGKRDEINHCLQMLR 596
Cdd:cd00105     2 EIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGS---GERVVTITGTPEAVEKAKELIE 63
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 531-596 2.34e-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: 56.91  E-value: 2.34e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845974109 531 YEFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHhetDKVKTHQICQVRGKRDEINHCLQMLR 596
Cdd:pfam00013   2 VEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPS---ESEGNERIVTITGTPEAVEAAKALIE 64
Tudor_TDRD2 cd20412
Tudor domain found in Tudor domain-containing protein 2 (TDRD2) and similar proteins; TDRD2, ...
 673-753 4.59e-10

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: 57.31  E-value: 4.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 673 MGSLYGEQSNLPELPIPcQNGLLCAAPV--GNAWFRAVTVQyFDETDEVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQ 750
Cdd:cd20412    13 MTQYYESEENRHTLLTV-QVGDIVAAPFrhDGSWYRARVLG-FLENGNLDLYFVDYGDSGYVPLEDLRALRSDFLSLPFQ 90


                  ...
gi 1845974109 751 STE 753
Cdd:cd20412    91 AIE 93
KH smart00322
K homology RNA-binding domain;
532-598 1.50e-09

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 54.61  E-value: 1.50e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845974109  532 EFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETDKVKThqicqVRGKRDEINHCLQMLRRR 598
Cdd:smart00322   6 EVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVE-----ITGPPENVEKAAELILEI 67
Tudor_TDRD1_rpt1 cd20408
first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; ...
 642-773 2.34e-08

first Tudor domain found in Tudor domain-containing protein 1 (TDRD1) and similar proteins; TDRD1, also called cancer/testis antigen 41.1 (CT41.1), plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for germline integrity. It acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins, and governs the methylation and subsequent repression of transposons. TDRD1 contains four 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: 410479  Cd Length: 130  Bit Score: 53.53  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 642 VAVSSIISASHFFIQQPTHPSFASLRHLDMYMGSLYgEQSNLPELPIPCQnGLLCAA--PVGNAWFRAV--TVQYFDETD 717
Cdd:cd20408     1 GTVTEFKNPGEFYIQIYTLEVLESLVKLTSQLKKTY-ASVNNHKEYIPEV-GEVCVAkySEDQNWYRALvqTVDVQQKKA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1845974109 718 EVFvkFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRPVDGttNWSDAAM 773
Cdd:cd20408    79 GVF--YIDYGNEETVPLNRIQPLKKDIELFPPCAIKCCLANVKPPSG--SWSEECI 130
Tudor_TDRD9 cd20431
Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is ...
 645-748 8.21e-08

Tudor domain found in Tudor domain-containing protein 9 (TDRD9) and similar proteins; TDRD9 is an ATP-dependent DEAD-like RNA helicase required during spermatogenesis. It is involved in the biosynthesis of PIWI-interacting RNAs (piRNAs). A recessive deleterious mutation mutation in TDRD9 causes non-obstructive azoospermia in infertile men. TDRD9 contains an N-terminal HrpA-like RNA helicase module and a 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: 410502  Cd Length: 101  Bit Score: 50.85  E-value: 8.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 645 SSIISASHFFIQQPTHPSFASLRHLDMYMgslygEQSNLPELPIPCQNGLLCAAPVGNA----WFRAVTVQYFDETDEVF 720
Cdd:cd20431     1 TEVVEVGHFWGYRIDENSSEILQQLTAEI-----NQRQLVPLTTKPVPNLLCLAPFTDAdmkkYYRAKILYVSGSSAEVF 75

                          90       100
                  ....*....|....*....|....*...
gi 1845974109 721 vkFVDYGGYSKMARQDLRQIRTDLMSLP 748
Cdd:cd20431    76 --FVDYGNTSQVPSSLLREIPETLLTLP 101
TUDOR smart00333
Tudor domain; Domain of unknown function present in several RNA-binding proteins. 10 copies in ...
 693-744 9.00e-08

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: 49.58  E-value: 9.00e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1845974109  693 GLLCAAPVGN-AWFRAVTVQYfDETDEVFVKFVDYGGYSKMARQDLRQIRTDL 744
Cdd:smart00333   6 GDKVAARWEDgEWYRARIVKV-DGEQLYEVFFIDYGNEEVVPPSDLRQLPEEL 57
KH-I_RCF3_like_rpt5 cd22463
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
 528-599 2.62e-07

fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein RCF3 and similar protein; 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 contains five K-homology (KH) RNA-binding domains. The model corresponds to the KH5 domain of RCF3.


Pssm-ID: 411891 [Multi-domain]  Cd Length: 71  Bit Score: 48.58  E-value: 2.62e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845974109 528 LPMYEFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETDKvKTHQICQVRGKRDEINHCLQMLRRRF 599
Cdd:cd22463     1 RSKIEFQIPEAVVGLIIGKSGNTIKQISERSGAFVAIVQDRYPLE-ETQKILRISGTEEQLKRAQSLVEGLI 71
Tudor_TDRD5 cd20419
Tudor domain found in Tudor domain-containing protein 5 (TDRD5) and similar proteins; TDRD5 is ...
 644-756 3.88e-07

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: 49.37  E-value: 3.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 644 VSSIISASHFFIQ---QPTHPSF----ASLRHLdmYMGSLYGEQSNLPELPIpCQNGLLCAAPVGNAWF-RAVTVQYFDE 715
Cdd:cd20419     2 VEYIESPSQFYVRfysKDTSEMLedmmIEMRRC--YSNEHVSERYVMPEAFI-QPGQVCCVRIPEDVWWyRVIIHQVLNK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1845974109 716 tDEVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVML 756
Cdd:cd20419    79 -QEVEVFYPDFGDIGTVQKSRLRFLKCCYSKLPAQAIPASL 118
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
 530-598 1.32e-06

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: 46.54  E-value: 1.32e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845974109 530 MYEFEIPNSLVGLIIGVKGKTIKELSVRTNVRmlIRQHHETDKVKTHQIcQVRGKRDEINHCLQMLRRR 598
Cdd:cd22454     5 TIEVVIPNADVGKVIGKGGETIKRIEALTDTV--ITFERVNGGSPNREV-QITGSPDNVAAAKRLIEDT 70
Tudor_TDRD6_rpt4 cd20423
fourth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 704-764 2.16e-06

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: 46.32  E-value: 2.16e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845974109 704 WFRAVTVQYFDETDEVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRPVDG 764
Cdd:cd20423    19 WCRALIDNVYEPVEMVEVTYVDYGNKELVSLKNLRSISEEFLKLKAQAFRCSLYNLIQPSG 79
Tudor_TDRD4_rpt2 cd20415
second Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 678-761 3.11e-06

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: 46.27  E-value: 3.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 678 GEQSNLpELPIPCQNGLLCAAPVGNAWFRAVTVQyFDETDEVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLA 757
Cdd:cd20415    15 GDDGGL-EILCPVQGQACVALFEDGAWYRARIIG-LPGHREVEVKYVDFGNTATVTIKHVRKIKDDFLSLPEKARECRLA 92


                  ....
gi 1845974109 758 HVRP 761
Cdd:cd20415    93 FIEP 96
Tudor_TDRD6_rpt7 cd20426
seventh Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 640-776 4.46e-06

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: 47.11  E-value: 4.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 640 CEVAVSSIISASHFFIQQPThpsfASLRHLDMYMGSLyGEQSNLPELPIPC---QNGLLCAAPVGNAWFRAVTVQYFDet 716
Cdd:cd20426     1 IEAYATAVDSPEYFWCQFAT----EKIQCLAVKVQEA-GEQVADRGNFIPSiyvGDPCIVKYSEDNHWYRALVTKIND-- 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 717 DEVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRPVDGTtnWSDAAMQKF 776
Cdd:cd20426    74 NLVSVRFVDYGNEEDVVREQVRALPSELLKIPVQAFPCCLSGFNLSEGL--WSDEANDYF 131
Tudor_TDRD7_rpt1 cd20427
first Tudor domain found in Tudor domain-containing protein 7 (TDRD7) and similar proteins; ...
 673-761 1.88e-05

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: 43.96  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 673 MGSLYGEQSNLPELPIPCQNGLLCAAPVGNAWFRAVTVQYfdETDEVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQST 752
Cdd:cd20427     7 MKEFYSKSSTAMCLRSPSVGQLVAVKAEEDAWLRAQVIEV--EEDKVKVYYVDHGFSEVVERSKLFKLNKQFYSLPFQAT 84


                  ....*....
gi 1845974109 753 EVMLAHVRP 761
Cdd:cd20427    85 KCKLAGLEP 93
Tudor_dTUD-like cd20379
Tudor domain found in Drosophila melanogaster maternal protein Tudor (dTUD) and similar ...
 693-740 1.95e-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: 42.50  E-value: 1.95e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1845974109 693 GLLCAA--PVGNAWFRAVtVQYFDETDEVFVKFVDYGGYSKMARQDLRQI 740
Cdd:cd20379     2 GDLCAAkyEEDGKWYRAR-VLEVLSNDKVEVFFVDYGNTETVPLSDLRPL 50
Tudor_TDRD15_rpt7 cd20442
seventh Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 679-751 2.44e-05

seventh 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 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: 410513  Cd Length: 160  Bit Score: 45.42  E-value: 2.44e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845974109 679 EQSNLPELPIpcQNGLLCAAPV--GNAWFRAVTVQYFDETDEVFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQS 751
Cdd:cd20442    41 KCKFVPVEDI--KEGLECLAKSkkNLKWYRAVVEHLYPETEKMLVFFVDHGITEVVSMGNIKQLSNDLLQIPRQA 113
Tudor_TDRD4_rpt5 cd20418
fifth Tudor domain found in Tudor domain-containing protein 4 (TDRD4) and similar proteins; ...
 704-773 3.79e-05

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: 43.55  E-value: 3.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 704 WFRAVTVQyFDETDEV--FVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRP--VDGTTN-------WSDAA 772
Cdd:cd20418    19 WYRAKLLS-ILEFNPVkiLVRHVDYGSTAALPTSRLRQIPAELMQYPCQAIKVKLAGFKPplNDSETEripycpeWSMKA 97


                  .
gi 1845974109 773 M 773
Cdd:cd20418    98 L 98
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
 532-595 4.95e-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: 41.86  E-value: 4.95e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1845974109 532 EFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETDKVKthqICQVRGKRDEINHCLQML 595
Cdd:cd22396     4 EYKVPDKMVGLIIGRGGEQINRLQAESGAKIQIAPDSGGLPER---PCTLTGTPDAIETAKRLI 64
Tudor_TDRD6_rpt6 cd20425
sixth Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 639-748 7.15e-05

sixth 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 sixth 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: 410496  Cd Length: 115  Bit Score: 42.83  E-value: 7.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 639 KCEVAVSSIISASHFFIQQPTHPSFASLRHLDMYMGSLYGEQSNLPELpipcQNG-LLCAA-PVGNAWFRAV-TVQYFDe 715
Cdd:cd20425     1 KTEVYVSHVNSPSDFYVQLAQDEDELSMISEKLNASKANDEEVECESL----QLGdLICAEyPEDGLWYRAVvKEKIPN- 75

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1845974109 716 tDEVFVKFVDYGGYSKMARQDLRQIRTDLMSLP 748
Cdd:cd20425    76 -NLVSVQFIDYGNTSVVQPSKIHRLPKELLSIP 107
KH-I_FUBP_rpt2 cd22397
second type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
 532-566 8.20e-05

second 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 second one.


Pssm-ID: 411825 [Multi-domain]  Cd Length: 69  Bit Score: 41.46  E-value: 8.20e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1845974109 532 EFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQ 566
Cdd:cd22397     3 EIMIPGNKVGLIIGKGGETIKQLQERAGVKMVMIQ 37
Tudor_TDRD15_rpt2 cd20437
second Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 641-751 9.35e-05

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: 42.79  E-value: 9.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 641 EVAVSSIISASHFFIQQPThpSFASLRHLDMYMGSLYGEQSNlpELPIPCQN-GLLCAAPVGNA-WFRAVtVQYFDETDE 718
Cdd:cd20437     6 KVKITAAVSPSKFYCQLLS--WEPELSKLTTQMTLHYESVSK--ELNPSCENfGLLCAAKGKDGqWHRGF-LQQLLPPSQ 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1845974109 719 VFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQS 751
Cdd:cd20437    81 VKVWFIDYGNSEAVSSHSVLKLPPDFFSLPLMS 113
Tudor_TDRD15_rpt4 cd20439
fourth Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 641-759 1.19e-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: 42.48  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 641 EVAVSSIISASHFFIQQPTHPSfaSLRHLDMYMGSLYGEQSNLPElpiPCQNGLLCAAPVGNAWFRAVTVQYFDEtDEVF 720
Cdd:cd20439    13 DVKCSYVNSPGDFWCQLQTKSS--ELKSLMKQIQSYYLIHNDPYK---HGQIACVAKYSKDGKWYRAAVLKQVSA-KEVD 86

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1845974109 721 VKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHV 759
Cdd:cd20439    87 VIFVDYGNQERVLISDLRAIKPQFLLLEGQAFRCSLNNF 125
Tudor_TDRD6_rpt3 cd20422
third Tudor domain found in Tudor domain-containing protein 6 (TDRD6) and similar proteins; ...
 640-777 1.48e-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: 42.50  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 640 CEVAVSSIISASHFFIQQPTHPSfaSLRHLDMYMGSLYGEQSNLPELPIPCQNGLLCAAPVG-NAWFRAVTVQYFDETDE 718
Cdd:cd20422     2 YDAQVEFVKDPSEFWIRLGEHAV--PFSKLMRSMTAFYSQASKLDGVVLKPQPGQLCCAKWKeDRYYRAIVTAVKGKMVE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1845974109 719 VFvkFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRPVDGTtnWSDAAMQKFR 777
Cdd:cd20422    80 VF--LVDRGNTEMVDWYDVKKLLPQFRELPALALKCCLADICPLGER--WSPEAISAFK 134
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
 533-574 2.54e-04

type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box protein 53 (DDX53) and similar proteins; DDX43 (also called cancer/testis antigen 13, or DEAD box protein HAGE, or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 (also called cancer-associated gene protein, or cancer/testis antigen 26, or DEAD box protein CAGE) shows high expression level in various tumors and is involved in anti-cancer drug resistance. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation.


Pssm-ID: 411858 [Multi-domain]  Cd Length: 66  Bit Score: 39.96  E-value: 2.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1845974109 533 FEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETDKVK 574
Cdd:cd22430     4 FKIDSSLVGAVIGRGGSKIRELEESTGSKIKIIKGGQEAEVK 45
PTZ00121 PTZ00121
MAEBL; Provisional
 183-477 2.92e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109  183 QKQQQKDEDEKTQKKDAVQNEKPSIDKK--QPKSQAPTEKKEEKTVEIHTETEETDHVAAGDSGVVSEHKEH--DKKTKQ 258
Cdd:PTZ00121  1296 KKAEEKKKADEAKKKAEEAKKADEAKKKaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaaEKKKEE 1375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109  259 KNDEPVSIDKKSEEIEVPKQAGVVNEEPKKQSEETVVEEQFVKKEEPKLKSAPTPLLTMPSKKKVLENEQIPEepTPTKM 338
Cdd:PTZ00121  1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADE--AKKKA 1453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109  339 NDATSPLSLDIAAQMSPASFSWSEEMEKSFNEEEfrLNESSDIDRSPASPLRHLQQQHNK----NRSSQKRKGGRVNGRD 414
Cdd:PTZ00121  1454 EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE--AKKKAEEAKKKADEAKKAAEAKKKadeaKKAEEAKKADEAKKAE 1531

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845974109  415 GVHQPQQQHQQQKKEEQGQIKKGQ--RRLTKEKSVEETPEKSQKRVVLKHHENEAGDAAHAQIIE 477
Cdd:PTZ00121  1532 EAKKADEAKKAEEKKKADELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
KH-I_FUBP3_rpt2 cd22483
second type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
 532-566 5.41e-04

second type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 3 (FUBP3) and similar proteins; 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. FUBP3 contains four K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411911 [Multi-domain]  Cd Length: 83  Bit Score: 39.51  E-value: 5.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1845974109 532 EFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQ 566
Cdd:cd22483     8 EILIPASKVGLVIGKGGETIKQLQERTGVKMIMIQ 42
KH-I_FUBP_rpt4 cd22399
fourth type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
 531-598 5.41e-04

fourth 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 fourth one.


Pssm-ID: 411827 [Multi-domain]  Cd Length: 67  Bit Score: 39.13  E-value: 5.41e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845974109 531 YEFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETDKVKthQICQVRGKRDEINHCLQMLRRR 598
Cdd:cd22399     2 VTFLVPANKCGLVIGKGGETIRQINQQSGAHVELDRNPPPNPNE--KLFIIRGNPQQIEHAKQLIREK 67
KH-I_FUBP_rpt3 cd22398
third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
 530-596 8.39e-04

third 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 third one.


Pssm-ID: 411826 [Multi-domain]  Cd Length: 67  Bit Score: 38.39  E-value: 8.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845974109 530 MYEFEIPNSLVGLIIGVKGKTIKELSVRTNVRMlirQHHETDKVKTHQICQVRGKRDEINHCLQMLR 596
Cdd:cd22398     1 GMEVPVPRFAVGVVIGKGGEMIKKIQNETGARV---QFKPDDGNSPDRICVITGPPDQVQHAARMIQ 64
Tudor_TDRD15_rpt3 cd20438
third Tudor domain found in Tudor domain-containing protein 15 (TDRD15) and similar proteins; ...
 644-777 1.09e-03

third 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 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: 410509  Cd Length: 141  Bit Score: 40.15  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 644 VSSIISASHFFIQQPTHPS-FASLRH--LDMYmgSLYGEQSNLPELPIPcqnGLLCAAPVGN--AWFRAVTVQYFDetDE 718
Cdd:cd20438    11 VEYVLNPSNFWIRTDEYNNeFQALMKniADIY--NLCGNDEELLKKPEP---GLLCCARYSKdrHYYRAVITEVLD--LK 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1845974109 719 VFVKFVDYGGYSKMARQDLRQIRTDLMSLPFQSTEVMLAHVRPVDGTtnWSDAAMQKFR 777
Cdd:cd20438    84 VSVYFLDFGNTDTVPFYDVKTLLPEFSELPALAMCCSLAHVFPVEEV--WTKNANDFFK 140
KH-I_BTR1_rpt2 cd22437
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 ...
 535-588 1.12e-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: 38.35  E-value: 1.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1845974109 535 IPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETDKVKTHQICQVRGKRDEI 588
Cdd:cd22437     5 VPNSSCGLIIGKGGSTIKELREDSNANIKISPKDQLLPGSSERIVTITGSFDQV 58
KH-I_BTR1_rpt3 cd22514
third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and ...
 535-598 1.16e-03

third 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 third one.


Pssm-ID: 411942 [Multi-domain]  Cd Length: 71  Bit Score: 38.17  E-value: 1.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1845974109 535 IPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETDKVKTHQICQVRGKRDEINHCLQMLRRR 598
Cdd:cd22514     7 VPDEHIGAILGRGGRTINEIQQHSGARIKISDRGDFVSGTRNRKVTITGPQDAVQMAQYLLEQK 70
KH-I_HNRNPK_rpt2 cd22433
second type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ...
 538-592 1.24e-03

second type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ribonucleoprotein K (hnRNP K) and similar proteins; hnRNP K, also called transformation up-regulated nuclear protein (TUNP), is a pre-mRNA binding protein that binds tenaciously to poly(C) sequences. It may be involved in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. It can also bind poly(C) single-stranded DNA. hnRNP K plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. hnRNP K contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411861 [Multi-domain]  Cd Length: 70  Bit Score: 38.00  E-value: 1.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1845974109 538 SLVGLIIGVKGKTIKELSVRTNVRMLIRQH---HETDKVkthqiCQVRGKRDEINHCL 592
Cdd:cd22433    11 SQAGCIIGRAGFKIKELREKTGATIKVYSEccpRSTDRV-----VQIGGKPDKVVECI 63
KH-I_FUBP1_rpt2 cd22481
second type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
 530-566 2.22e-03

second type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 1 (FUBP1) and similar proteins; 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. FUBP1 contains four K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411909 [Multi-domain]  Cd Length: 71  Bit Score: 37.68  E-value: 2.22e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1845974109 530 MYEFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQ 566
Cdd:cd22481     3 VQEIMIPASKAGLVIGKGGETIKQLQERAGVKMVMIQ 39
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 533-564 4.81e-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: 37.00  E-value: 4.81e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1845974109 533 FEIPNSLVGLIIGVKGKTIKELSVRTNVRMLI 564
Cdd:cd22446    11 ISVPSSVRGAIIGSRGKNLKSIQDKTGTKIQI 42
KH-I_FUBP1_rpt4 cd22487
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
 528-598 5.23e-03

fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 1 (FUBP1) and similar proteins; 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. FUBP1 contains four K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411915  Cd Length: 72  Bit Score: 36.47  E-value: 5.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845974109 528 LPMYEFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETDKVKTHQICQVRGKRDEINHCLQMLRRR 598
Cdd:cd22487     1 LQEFNFIVPTGKTGLIIGKGGETIKSISQQSGARIELQRNPPPNADPNMKLFTIRGSPQQIDYARQLIEEK 71
KH-I_PCBP_rpt1 cd22438
first type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
 540-599 6.25e-03

first 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 first one.


Pssm-ID: 411866 [Multi-domain]  Cd Length: 67  Bit Score: 36.08  E-value: 6.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 540 VGLIIGVKGKTIKELSVRTNVRMLIrqhheTDKVKTHQICQVRGKRDEINHCLQMLRRRF 599
Cdd:cd22438    10 VGSIIGKKGETIKKFREESGARINI-----SDGSCPERIVTVTGTTDAVFKAFELICRKL 64
PTZ00121 PTZ00121
MAEBL; Provisional
 183-488 6.74e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 6.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109  183 QKQQQKDEDEKTQ--KKDAVQNEKPSIDKKQPKSQAPTEKKEEKTVEIHTETEETDHVAAGDSGVVSEHKEHDKKTKQKN 260
Cdd:PTZ00121  1494 EAKKKADEAKKAAeaKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109  261 DEPVSIDKKSEEIEVPKQAGVVNEEPKKQSEETVVEEQFVKKEEPKLKSapTPLLTMPSKKKVLENEQIPEEPTPTKmnd 340
Cdd:PTZ00121  1574 EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKAEEEKKKVEQLKKKEAEEKKK--- 1648

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109  341 atsplsldiAAQMSPAsfswsEEMEKSFNEEEFRLNESsdiDRSPASPLRHLQQQHNKNRSSQKRKGGRVNGRDGVhqpq 420
Cdd:PTZ00121  1649 ---------AEELKKA-----EEENKIKAAEEAKKAEE---DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL---- 1707

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109  421 QQHQQQKKEEQGQIKKGQ--RRLTKEKSVEETPEKSQKRVVLKHHENEAGDAAHAQIIESPHHENASYEK 488
Cdd:PTZ00121  1708 KKKEAEEKKKAEELKKAEeeNKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
Caldesmon pfam02029
Caldesmon;
172-332 7.45e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 39.85  E-value: 7.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 172 NGDVQSSIGVSQKQQQKDEDEKTQKKDAVQNEKPSiDKKQPKSQAPTEKKEEKTVEIHTETEETDHVAAGDSGVVSEHKE 251
Cdd:pfam02029  93 IADEKESVAERKENNEEEENSSWEKEEKRDSRLGR-YKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPT 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 252 HDKKTKQKNDEPVSIDKK-SEEIEVPKQAGVVNEEPKKQSEETVVEEQFVkKEEPKLKSAPTPLLTMPSKKKVLENEQIP 330
Cdd:pfam02029 172 ENFAKEEVKDEKIKKEKKvKYESKVFLDQKRGHPEVKSQNGEEEVTKLKV-TTKRRQGGLSQSQEREEEAEVFLEAEQKL 250


                  ..
gi 1845974109 331 EE 332
Cdd:pfam02029 251 EE 252
DUF612 pfam04747
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ...
 182-387 7.61e-03

Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.


Pssm-ID: 282585 [Multi-domain]  Cd Length: 511  Bit Score: 39.66  E-value: 7.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 182 SQKQQQKDEDEKTQKKDAVQN--EKPSIDKKQPKSQAPTEKKEEKTVEIHTETEETDhvAAGDSGV---------VSEHK 250
Cdd:pfam04747 216 NKKNKKKSESEATAAPASVEQvvEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVP--AASETPVepvvettppASENQ 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109 251 EHDKKTKQKNdEPVSIDKKSEEIEVPKQAG-------------VVNEEPKKQSEET---VVEEQFVKKEEPKLKSAPTPL 314
Cdd:pfam04747 294 KKNKKDKKKS-ESEKVVEEPVQAEAPKSKKptaddnmdfldfvTAKEEPKDEPAETpaaPVEEVVENVVENVVEKSTTPP 372

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845974109 315 LTMPSK-----KKVLENEQIPEEPTPTkmndATSPLSLDIAAQMSPASFSWSEEMEKSFNEEEFRLNESSDIDRSPAS 387
Cdd:pfam04747 373 ATENKKknkkdKKKSESEKVTEQPVES----APAPPQVEQVVETTPPASENKKKNKKDKKKSESEKAVEEPVQAAPSS 446
PTZ00121 PTZ00121
MAEBL; Provisional
 184-306 8.18e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 8.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974109  184 KQQQKDEDEKTQKKDAVQNEKPSIDKKQPKSQAPTEKKEEKTVEIHTETEETDHVAAGDsgVVSEHKEHDKKTKQKNDEP 263
Cdd:PTZ00121  1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE--LKKAEEENKIKAEEAKKEA 1739

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1845974109  264 VSIDKKSEEIEVP-----KQAGVVNEEPKKQSE-----ETVVEEQFVKKEEPK 306
Cdd:PTZ00121  1740 EEDKKKAEEAKKDeeekkKIAHLKKEEEKKAEEirkekEAVIEEELDEEDEKR 1792
KH-I_FUBP2_rpt2 cd22482
second type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
 530-566 9.14e-03

second type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 2 (FUBP2) and similar proteins; 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. FUBP2 contains four K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411910 [Multi-domain]  Cd Length: 73  Bit Score: 35.66  E-value: 9.14e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1845974109 530 MYEFEIPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQ 566
Cdd:cd22482     3 VQEIMIPAGKAGLVIGKGGETIKQLQERAGVKMILIQ 39
KH-I_NOVA_rpt1 cd22435
first type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
 535-595 9.86e-03

first 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 first one.


Pssm-ID: 411863 [Multi-domain]  Cd Length: 73  Bit Score: 35.59  E-value: 9.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845974109 535 IPNSLVGLIIGVKGKTIKELSVRTNVRMLIRQHHETDKVKTHQICQVRGKRDEINHCLQML 595
Cdd:cd22435     8 VPNYAAGSIIGKGGQTIAQLQKETGARIKLSKNNDFYPGTTERVCLIQGEVEAVNAVLDFI 68
 
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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