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Conserved domains on  [gi|19114115|ref|NP_593203|]
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RNA-binding protein [Schizosaccharomyces pombe]

Protein Classification

KH domain-containing protein( domain architecture ID 16909965)

K homology (KH) domain-containing protein may bind single-stranded RNA or DNA

Gene Ontology:  GO:0003723|GO:0005681

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KH-I_KHDC4_rpt2 cd22386
first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ...
287-387 4.35e-48

first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein 4 (KHDC4) and similar proteins; KHDC4, also called Brings lots of money 7 (Blom7), or pre-mRNA splicing factor protein KHDC4, is an RNA-binding protein involved in pre-mRNA splicing. It interacts with the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome. KHDC4 binds preferentially RNA with A/C rich sequences and poly-C stretches. KHDC4 contains two type I K homology (KH) RNA-binding domains. The model corresponds to the second one.


:

Pssm-ID: 411814 [Multi-domain]  Cd Length: 102  Bit Score: 161.96  E-value: 4.35e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115 287 KWLEEKVYINLTPS-RGFHLRQAIVGPQGAYVKHIQQETRTRVQIKGQGSAFIEPSTNRESDEPIHLCIMSHDPNAIQRA 365
Cdd:cd22386   1 KYYQEKVFVGLEHApPGFNVRGKLIGPGGSNVKHIQQETGAKVQLRGKGSGFIEPASGREADEPLHLLISHPDPEGLQQA 80
                        90       100
                ....*....|....*....|..
gi 19114115 366 KVLCEDLIASVHQQYKAWKSQP 387
Cdd:cd22386  81 KKLCEDLLQTVHQEYGEFQQQP 102
KH-I_KHDC4_rpt1 cd22385
first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ...
162-241 3.36e-26

first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein 4 (KHDC4) and similar proteins; KHDC4, also called Brings lots of money 7 (Blom7), or pre-mRNA splicing factor protein KHDC4, is an RNA-binding protein involved in pre-mRNA splicing. It interacts with the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome. KHDC4 binds preferentially RNA with A/C rich sequences and poly-C stretches. KHDC4 contains two type I K homology (KH) RNA-binding domains. The model corresponds to the first one. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif.


:

Pssm-ID: 411813  Cd Length: 84  Bit Score: 101.90  E-value: 3.36e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115 162 GDGVFMQDVEINNVRN--RYILVRASTLSEIENKSGVQLFSKGRYYPNKALAT--DKDPPLYLHIVSHNRKDLTVALQEI 237
Cdd:cd22385   1 GDDLYVAEIEINDLPNtcRNLLTKGSTQEEIQKESGAAVSTRGRYMPPEEKATfnPGERPLYLHVQAPTKEAVDRAVNKI 80

                ....
gi 19114115 238 ESWI 241
Cdd:cd22385  81 NEII 84
U2AF_lg super family cl36941
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
4-80 1.75e-04

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


The actual alignment was detected with superfamily member TIGR01642:

Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 44.11  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115     4 SRQNSQREDNYSRDRRSRfteDSYSRRDSQ-----RSGNEAPRESRYYRKEEHLQERSRSRSPARDSRWKSSSSGFAPAH 78
Cdd:TIGR01642  41 SRERSYREDSRPRDRRRY---DSRSPRSLRyssvrRSRDRPRRRSRSVRSIEQHRRRLRDRSPSNQWRKDDKKRSLWDIK 117

                  ..
gi 19114115    79 PP 80
Cdd:TIGR01642 118 PP 119
PHA03247 super family cl33720
large tegument protein UL36; Provisional
390-504 2.08e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115   390 RDQNQGNRAYNPPNRNQAFSARD--------SRQEKTQPTNASPAPLVTPSLPVPSIP-----AVPGMEAMAMPPGVTSS 456
Cdd:PHA03247 2668 RRLGRAAQASSPPQRPRRRAARPtvgsltslADPPPPPPTPEPAPHALVSATPLPPGPaaarqASPALPAAPAPPAVPAG 2747
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 19114115   457 IAVPTTSSMPlqGMPTMFGAPGVSAPGTEAPGTGTPGLTTPGVDPYAA 504
Cdd:PHA03247 2748 PATPGGPARP--ARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSE 2793
 
Name Accession Description Interval E-value
KH-I_KHDC4_rpt2 cd22386
first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ...
287-387 4.35e-48

first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein 4 (KHDC4) and similar proteins; KHDC4, also called Brings lots of money 7 (Blom7), or pre-mRNA splicing factor protein KHDC4, is an RNA-binding protein involved in pre-mRNA splicing. It interacts with the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome. KHDC4 binds preferentially RNA with A/C rich sequences and poly-C stretches. KHDC4 contains two type I K homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411814 [Multi-domain]  Cd Length: 102  Bit Score: 161.96  E-value: 4.35e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115 287 KWLEEKVYINLTPS-RGFHLRQAIVGPQGAYVKHIQQETRTRVQIKGQGSAFIEPSTNRESDEPIHLCIMSHDPNAIQRA 365
Cdd:cd22386   1 KYYQEKVFVGLEHApPGFNVRGKLIGPGGSNVKHIQQETGAKVQLRGKGSGFIEPASGREADEPLHLLISHPDPEGLQQA 80
                        90       100
                ....*....|....*....|..
gi 19114115 366 KVLCEDLIASVHQQYKAWKSQP 387
Cdd:cd22386  81 KKLCEDLLQTVHQEYGEFQQQP 102
KH-I_KHDC4_rpt1 cd22385
first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ...
162-241 3.36e-26

first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein 4 (KHDC4) and similar proteins; KHDC4, also called Brings lots of money 7 (Blom7), or pre-mRNA splicing factor protein KHDC4, is an RNA-binding protein involved in pre-mRNA splicing. It interacts with the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome. KHDC4 binds preferentially RNA with A/C rich sequences and poly-C stretches. KHDC4 contains two type I K homology (KH) RNA-binding domains. The model corresponds to the first one. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411813  Cd Length: 84  Bit Score: 101.90  E-value: 3.36e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115 162 GDGVFMQDVEINNVRN--RYILVRASTLSEIENKSGVQLFSKGRYYPNKALAT--DKDPPLYLHIVSHNRKDLTVALQEI 237
Cdd:cd22385   1 GDDLYVAEIEINDLPNtcRNLLTKGSTQEEIQKESGAAVSTRGRYMPPEEKATfnPGERPLYLHVQAPTKEAVDRAVNKI 80

                ....
gi 19114115 238 ESWI 241
Cdd:cd22385  81 NEII 84
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
4-80 1.75e-04

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 44.11  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115     4 SRQNSQREDNYSRDRRSRfteDSYSRRDSQ-----RSGNEAPRESRYYRKEEHLQERSRSRSPARDSRWKSSSSGFAPAH 78
Cdd:TIGR01642  41 SRERSYREDSRPRDRRRY---DSRSPRSLRyssvrRSRDRPRRRSRSVRSIEQHRRRLRDRSPSNQWRKDDKKRSLWDIK 117

                  ..
gi 19114115    79 PP 80
Cdd:TIGR01642 118 PP 119
KH smart00322
K homology RNA-binding domain;
308-373 7.60e-04

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 38.05  E-value: 7.60e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114115    308 AIVGPQGAYVKHIQQETRTRVQIkgqgsafiepstnRESDEPIHLCIMSHDPNAIQRAKVLCEDLI 373
Cdd:smart00322  16 LIIGKGGSTIKKIEEETGVKIDI-------------PGPGSEERVVEITGPPENVEKAAELILEIL 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
390-504 2.08e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115   390 RDQNQGNRAYNPPNRNQAFSARD--------SRQEKTQPTNASPAPLVTPSLPVPSIP-----AVPGMEAMAMPPGVTSS 456
Cdd:PHA03247 2668 RRLGRAAQASSPPQRPRRRAARPtvgsltslADPPPPPPTPEPAPHALVSATPLPPGPaaarqASPALPAAPAPPAVPAG 2747
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 19114115   457 IAVPTTSSMPlqGMPTMFGAPGVSAPGTEAPGTGTPGLTTPGVDPYAA 504
Cdd:PHA03247 2748 PATPGGPARP--ARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSE 2793
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
304-371 2.46e-03

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 36.49  E-value: 2.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114115   304 HLRQAIVGPQGAYVKHIQQETRTRVQIKGQGSafiePSTNREsdepihlCIMSHDPNAIQRAKVLCED 371
Cdd:pfam00013   9 SLVGLIIGKGGSNIKEIREETGAKIQIPPSES----EGNERI-------VTITGTPEAVEAAKALIEE 65
MSL5 COG5176
Splicing factor (branch point binding protein) [RNA processing and modification];
290-373 3.86e-03

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


Pssm-ID: 227503 [Multi-domain]  Cd Length: 269  Bit Score: 39.18  E-value: 3.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115 290 EEKVYINLTPSRGFHLRQAIVGPQGAYVKHIQQETRTRVQIKGQGS------AFIEPSTNRESDEPIHLCIMSHDPNAIQ 363
Cdd:COG5176 149 QNKIYIPVQEYPESNFVGLLIGPRGSTLKQLERISRAKIAIRGSGSvkegkiSSDTPESLKNAEAVLHCLIEADSEDKIC 228
                        90
                ....*....|
gi 19114115 364 RAKVLCEDLI 373
Cdd:COG5176 229 RLIKSQLNAI 238
 
Name Accession Description Interval E-value
KH-I_KHDC4_rpt2 cd22386
first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ...
287-387 4.35e-48

first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein 4 (KHDC4) and similar proteins; KHDC4, also called Brings lots of money 7 (Blom7), or pre-mRNA splicing factor protein KHDC4, is an RNA-binding protein involved in pre-mRNA splicing. It interacts with the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome. KHDC4 binds preferentially RNA with A/C rich sequences and poly-C stretches. KHDC4 contains two type I K homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411814 [Multi-domain]  Cd Length: 102  Bit Score: 161.96  E-value: 4.35e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115 287 KWLEEKVYINLTPS-RGFHLRQAIVGPQGAYVKHIQQETRTRVQIKGQGSAFIEPSTNRESDEPIHLCIMSHDPNAIQRA 365
Cdd:cd22386   1 KYYQEKVFVGLEHApPGFNVRGKLIGPGGSNVKHIQQETGAKVQLRGKGSGFIEPASGREADEPLHLLISHPDPEGLQQA 80
                        90       100
                ....*....|....*....|..
gi 19114115 366 KVLCEDLIASVHQQYKAWKSQP 387
Cdd:cd22386  81 KKLCEDLLQTVHQEYGEFQQQP 102
KH-I_KHDC4_rpt1 cd22385
first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein ...
162-241 3.36e-26

first type I K homology (KH) RNA-binding domain found in KH homology domain-containing protein 4 (KHDC4) and similar proteins; KHDC4, also called Brings lots of money 7 (Blom7), or pre-mRNA splicing factor protein KHDC4, is an RNA-binding protein involved in pre-mRNA splicing. It interacts with the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome. KHDC4 binds preferentially RNA with A/C rich sequences and poly-C stretches. KHDC4 contains two type I K homology (KH) RNA-binding domains. The model corresponds to the first one. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411813  Cd Length: 84  Bit Score: 101.90  E-value: 3.36e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115 162 GDGVFMQDVEINNVRN--RYILVRASTLSEIENKSGVQLFSKGRYYPNKALAT--DKDPPLYLHIVSHNRKDLTVALQEI 237
Cdd:cd22385   1 GDDLYVAEIEINDLPNtcRNLLTKGSTQEEIQKESGAAVSTRGRYMPPEEKATfnPGERPLYLHVQAPTKEAVDRAVNKI 80

                ....
gi 19114115 238 ESWI 241
Cdd:cd22385  81 NEII 84
KH-I_RIK_like_rpt2 cd22472
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein RIK and ...
293-382 4.63e-15

second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein RIK and similar proteins; RIK, also called rough sheath 2-interacting KH domain protein, or RS2-interacting KH domain protein, is a RNA binding protein that acts together with RS2/AS1 in the recruitment of HIRA. RIK contains two type I K homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411900  Cd Length: 96  Bit Score: 70.94  E-value: 4.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115 293 VYINLTPSRGFHLRQAIVGPQGAYVKHIQQETRTRVQIKGQGSAFIEpstnrESDEPIHLCIMSHDPNAIQRAKVLCEDL 372
Cdd:cd22472   7 LYVGIEAPPSFNLAGRIRGPNNSYLQHIASATGATVALRGRGSGGAP-----EGPEPLHLFLSASDPKALEEARGLAENL 81
                        90
                ....*....|
gi 19114115 373 IASVHQQYKA 382
Cdd:cd22472  82 IDTVRADFKA 91
KH-I_RIK_like_rpt1 cd22471
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein RIK and ...
162-222 5.12e-11

first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein RIK and similar proteins; RIK, also called rough sheath 2-interacting KH domain protein, or RS2-interacting KH domain protein, is a RNA binding protein that acts together with RS2/AS1 in the recruitment of HIRA. RIK contains two type I K homology (KH) RNA-binding domains. The model corresponds to the first one. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411899  Cd Length: 91  Bit Score: 59.02  E-value: 5.12e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19114115 162 GDGVFMQDVEINNV--RNRYILVRASTLSEIENKSGVQLFSKGRYYPNKALATDKDPPLYLHI 222
Cdd:cd22471   1 AESSIAREIVINDAppSVRHHLTKRSTQDEIQSKTGVVVVTRGRYYPPGTPPPDNEKPLYLHI 63
KH-I_BBP cd02395
type I K homology (KH) RNA-binding domain found in yeast branchpoint-bridging protein (BBP) ...
291-373 1.69e-07

type I K homology (KH) RNA-binding domain found in yeast branchpoint-bridging protein (BBP) and similar proteins; Yeast BBP, also called mud synthetic-lethal 5 protein, or splicing factor 1, or zinc finger protein BBP, is a mammalian splicing factor SF1 ortholog. It is involved in protein-protein interactions that bridge the 3' and 5' splice-site ends of the intron during the early steps of yeast pre-mRNA splicing. BBP interacts specifically with the pre-mRNA branchpoint sequence UACUAAC.


Pssm-ID: 411805 [Multi-domain]  Cd Length: 92  Bit Score: 49.14  E-value: 1.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115 291 EKVYINLTPSRGFHLRQAIVGPQGAYVKHIQQETRTRVQIKGQGSA-----FIEPSTNRESDEPIHLCIMSHDPNAIQRA 365
Cdd:cd02395   4 RKIYIPVDEYPDYNFIGLIIGPRGNTQKRMEKESGAKIAIRGKGSVkegkgRSDPQPDPDEEEDLHVLITADTEEKVDKA 83

                ....*...
gi 19114115 366 KVLCEDLI 373
Cdd:cd02395  84 AKLIEKLL 91
KH-I_DDX46_like cd22387
type I K homology (KH) RNA-binding domain found in the family of DEAD box protein 46 (DDX46); ...
162-239 3.75e-06

type I K homology (KH) RNA-binding domain found in the family of DEAD box protein 46 (DDX46); The DDX46 family includes DEAD box protein 46 (DDX46), fungal pre-mRNA-processing ATP-dependent RNA helicase PRP5, Arabidopsis thaliana DEAD-box ATP-dependent RNA helicase RH42 and similar proteins. DDX46, also called PRP5 homolog, is an ATP-dependent RNA helicase that plays an essential role in splicing, either prior to, or during splicing A complex formation. It inhibits antiviral innate responses by entrapping selected antiviral transcripts in the nucleus. It is also involved in the development of several tumors. PRP5 is an ATP-dependent RNA helicase involved spliceosome assembly and in nuclear splicing. It catalyzes an ATP-dependent conformational change of U2 snRNP. PRP5 interacts with the U2 snRNP and HSH155. RH42, also called DEAD-box RNA helicase RCF1, or REGULATOR OF CBF GENE EXPRESSION 1, is a helicase required for pre-mRNA splicing, cold-responsive gene regulation and cold tolerance. Members in this family contain a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411815  Cd Length: 82  Bit Score: 44.96  E-value: 3.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115 162 GDGVFMQDVEINNVRN--RYILVRASTLSEIENKSGVQLFSKGRYYPNKALATDKDPPLYLHIVSHNRKDLTVALQEIES 239
Cdd:cd22387   1 NNGNFVEEFEINDYPQiaRLKVTSKEVLNSIMEETGATITIKGQYYPPGKKPKPGERKLYLLIEGATEESVQSARNEIKR 80
KH-I_PRP5_like cd22474
type I K homology (KH) RNA-binding domain found in fungal pre-mRNA-processing ATP-dependent ...
170-239 3.59e-05

type I K homology (KH) RNA-binding domain found in fungal pre-mRNA-processing ATP-dependent RNA helicase PRP5 and similar proteins; PRP5 is an ATP-dependent RNA helicase involved spliceosome assembly and in nuclear splicing. It catalyzes an ATP-dependent conformational change of U2 snRNP. PRP5 interacts with the U2 snRNP and HSH155. Members in this subfamily contain a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411902  Cd Length: 89  Bit Score: 42.31  E-value: 3.59e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114115 170 VEINNV--RNRYILVRASTLSEIENKSGVQLFSKGRYYP-NKALATDKDPP-LYLHIVSHNRKDLTVALQEIES 239
Cdd:cd22474   9 VEINDLpqKARWEATNNTSLSKIIEETGCSITNKGNFYPpGKEPQPNNDEPkLYLLIEGTTEKAVRLAIELLRR 82
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
308-370 9.30e-05

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: 40.36  E-value: 9.30e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19114115 308 AIVGPQGAYVKHIQQETRTRVQIKGqgsafiepstnRESDEPIHLCIMSHDPNAIQRAKVLCE 370
Cdd:cd00105  12 LIIGKGGSTIKEIEEETGARIQIPK-----------EGEGSGERVVTITGTPEAVEKAKELIE 63
KH-I_SF1 cd22382
type I K homology (KH) RNA-binding domain found in splicing factor 1 (SF1) and similar ...
309-365 9.34e-05

type I K homology (KH) RNA-binding domain found in splicing factor 1 (SF1) and similar proteins; SF1, also called branch point-binding protein, or BBP, or transcription factor ZFM1, or zinc finger gene in MEN1 locus, or zinc finger protein 162, is necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. It may act as transcription repressor.


Pssm-ID: 411810 [Multi-domain]  Cd Length: 93  Bit Score: 41.53  E-value: 9.34e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114115 309 IVGPQGAYVKHIQQETRTRVQIKGQGSAfIEPSTNR-------ESDEPIHLCIMSHDPNAIQRA 365
Cdd:cd22382  22 LIGPRGNTLKKIEKETGAKIMIRGKGSV-KEGKVGRkdgqplpGEDEPLHALVTANTAESVKKA 84
KH-I_DDX46_like cd22387
type I K homology (KH) RNA-binding domain found in the family of DEAD box protein 46 (DDX46); ...
290-373 1.11e-04

type I K homology (KH) RNA-binding domain found in the family of DEAD box protein 46 (DDX46); The DDX46 family includes DEAD box protein 46 (DDX46), fungal pre-mRNA-processing ATP-dependent RNA helicase PRP5, Arabidopsis thaliana DEAD-box ATP-dependent RNA helicase RH42 and similar proteins. DDX46, also called PRP5 homolog, is an ATP-dependent RNA helicase that plays an essential role in splicing, either prior to, or during splicing A complex formation. It inhibits antiviral innate responses by entrapping selected antiviral transcripts in the nucleus. It is also involved in the development of several tumors. PRP5 is an ATP-dependent RNA helicase involved spliceosome assembly and in nuclear splicing. It catalyzes an ATP-dependent conformational change of U2 snRNP. PRP5 interacts with the U2 snRNP and HSH155. RH42, also called DEAD-box RNA helicase RCF1, or REGULATOR OF CBF GENE EXPRESSION 1, is a helicase required for pre-mRNA splicing, cold-responsive gene regulation and cold tolerance. Members in this family contain a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411815  Cd Length: 82  Bit Score: 40.72  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115 290 EEKVYINLTPSrgfHLRQAIVgpQGAYVKHIQQETRTRVQIKGQgsaFIEPSTNRESDE-PIHLCIMSHDPNAIQRAKVL 368
Cdd:cd22387   6 VEEFEINDYPQ---IARLKVT--SKEVLNSIMEETGATITIKGQ---YYPPGKKPKPGErKLYLLIEGATEESVQSARNE 77

                ....*
gi 19114115 369 CEDLI 373
Cdd:cd22387  78 IKRVL 82
KH-I_TDRKH_rpt1 cd22428
first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
308-366 1.55e-04

first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the first one.


Pssm-ID: 411856 [Multi-domain]  Cd Length: 74  Bit Score: 40.01  E-value: 1.55e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19114115 308 AIVGPQGAYVKHIQQETRTRVQIKGQGSafiepstnrESDEPIHLCIMSHDPNAIQRAK 366
Cdd:cd22428  18 LIIGRQGATIKQIQKETGARIDFKDEGS---------GGELPERVLLIQGNPVQAQRAE 67
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
4-80 1.75e-04

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 44.11  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115     4 SRQNSQREDNYSRDRRSRfteDSYSRRDSQ-----RSGNEAPRESRYYRKEEHLQERSRSRSPARDSRWKSSSSGFAPAH 78
Cdd:TIGR01642  41 SRERSYREDSRPRDRRRY---DSRSPRSLRyssvrRSRDRPRRRSRSVRSIEQHRRRLRDRSPSNQWRKDDKKRSLWDIK 117

                  ..
gi 19114115    79 PP 80
Cdd:TIGR01642 118 PP 119
KH-I_MEX3_rpt2 cd22424
second type I K homology (KH) RNA-binding domain found in the family of MEX-3 RNA-binding ...
309-374 2.69e-04

second type I K homology (KH) RNA-binding domain found in the family of MEX-3 RNA-binding proteins; The MEX-3 protein family includes four members, MEX3A/RKHD4, MEX3B/RKHD3/RNF195, MEX3C/ RKHD2/RNF194, and MEX3D/RKHD1/RNF193/TINO. They are homologous of Caenorhabditis elegans MEX-3 protein, a translational regulator that specifies the posterior blastomere identity in the early embryo and contributes to the maintenance of the germline totipotency. Mex-3 proteins are RNA-binding phosphoproteins involved in post-transcriptional regulatory mechanisms. They are characterized by containing two K-homology (KH) RNA-binding domains and a C-terminal RING finger. They bind RNA through their KH domains and shuttle between the nucleus and the cytoplasm via the CRM1-dependent export pathway. The model corresponds to the second KH domain.


Pssm-ID: 411852 [Multi-domain]  Cd Length: 72  Bit Score: 39.63  E-value: 2.69e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114115 309 IVGPQGAYVKHIQQETRTRVqikgqgsafIEPSTNResdEPIHlcIMSHDPNAIQRAKVLCEDLIA 374
Cdd:cd22424  18 VVGPKGATIKRIQQQTHTYI---------VTPSRDK---EPVF--EVTGMPENVERAREEIEAHIA 69
KH-I_Hqk_like cd22383
type I K homology (KH) RNA-binding domain found in protein quaking (Hqk) family; The Hqk ...
289-367 5.40e-04

type I K homology (KH) RNA-binding domain found in protein quaking (Hqk) family; The Hqk family includes Hqk and protein held out wings (how) found in Drosophila. Hqk, also called HqkI, is an RNA-binding protein that plays a central role in myelinization. It binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core sequence and regulates target mRNA stability. It acts by regulating pre-mRNA splicing, mRNA export and protein translation. Hqk is a regulator of oligodendrocyte differentiation and maturation in the brain that may play a role in myelin and oligodendrocyte dysfunction in schizophrenia. How, also called KH domain protein KH93F, or protein muscle-specific, or protein Struthio, or protein wings held out (who), or Quaking-related 93F (qkr93F), is an RNA-binding protein involved in the control of muscular and cardiac activity. It is required for integrin-mediated cell-adhesion in wing blade. It plays essential roles during embryogenesis, in late stages of somatic muscle development, for myotube migration and during metamorphosis for muscle reorganization.


Pssm-ID: 411811 [Multi-domain]  Cd Length: 101  Bit Score: 39.26  E-value: 5.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115 289 LEEKVYI--NLTPSRGFHLRqaIVGPQGAYVKHIQQETRTRVQIKGQGS--------AFIEPSTNRESDEPIHLCIMSHD 358
Cdd:cd22383   2 LSEKVYVpvDEYPDYNFVGR--ILGPRGMTAKQLEQDTGCKIMIRGKGSmrdkkkeeANRGKPNWEHLNDDLHVLITVED 79

                ....*....
gi 19114115 359 PNAIQRAKV 367
Cdd:cd22383  80 TENRAHIKL 88
KH smart00322
K homology RNA-binding domain;
308-373 7.60e-04

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 38.05  E-value: 7.60e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114115    308 AIVGPQGAYVKHIQQETRTRVQIkgqgsafiepstnRESDEPIHLCIMSHDPNAIQRAKVLCEDLI 373
Cdd:smart00322  16 LIIGKGGSTIKKIEEETGVKIDI-------------PGPGSEERVVEITGPPENVEKAAELILEIL 68
KH-I_KHDRBS cd22384
type I K homology (KH) RNA-binding domain found in the KH domain-containing, RNA-binding, ...
289-335 1.00e-03

type I K homology (KH) RNA-binding domain found in the KH domain-containing, RNA-binding, signal transduction-associated protein (KHDRBS) family; The KHDRBS family includes three members, KHDRBS1-3. KHDRBS1, also called GAP-associated tyrosine phosphoprotein p62, or Src-associated in mitosis 68 kDa protein, or Sam68, or p21 Ras GTPase-activating protein-associated p62, or p68, is an RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. It binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. It also binds poly(A). KHDRBS1 acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. It is recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. KHDRBS2, also called Sam68-like mammalian protein 1, or SLM-1, is an RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. It binds both poly(A) and poly(U) homopolymers. KHDRBS2 may function as an adapter protein for Src kinases during mitosis. KHDRBS3, also called RNA-binding protein T-Star, or Sam68-like mammalian protein 2, or SLM-2, or Sam68-like phosphotyrosine protein, is an RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. It binds optimally to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. It also binds poly(A). KHDRBS3 may play a role as a negative regulator of cell growth.


Pssm-ID: 411812 [Multi-domain]  Cd Length: 102  Bit Score: 38.80  E-value: 1.00e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 19114115 289 LEEKVYINLTPSRGFHLRQAIVGPQGAYVKHIQQETRTRVQIKGQGS 335
Cdd:cd22384   5 LSEKVLIPVKEFPKFNFVGKLLGPRGNTLKRLQEETGTKMSILGKGS 51
KH-I_HOW cd22466
type I K homology (KH) RNA-binding domain found in Drosophila protein held out wings (how) and ...
289-378 1.04e-03

type I K homology (KH) RNA-binding domain found in Drosophila protein held out wings (how) and similar proteins; How, also called KH domain protein KH93F, or protein muscle-specific, or protein Struthio, or protein wings held out (who), or Quaking-related 93F (qkr93F), is an RNA-binding protein involved in the control of muscular and cardiac activity. It is required for integrin-mediated cell-adhesion in wing blade. It plays essential roles during embryogenesis, in late stages of somatic muscle development, for myotube migration and during metamorphosis for muscle reorganization.


Pssm-ID: 411894 [Multi-domain]  Cd Length: 105  Bit Score: 38.75  E-value: 1.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115 289 LEEKVYINLTPSRGFHLRQAIVGPQGAYVKHIQQETRTRVQIKGQGSAFI---------EPSTNRESDEpIHLCIMSHDP 359
Cdd:cd22466   6 LSEKVYVPVKEHPDYNFVGRILGPRGMTAKQLEQETGCKIMVRGKGSMRDkkkedlnrgKPNWEHLNDE-LHVLITVEDT 84
                        90
                ....*....|....*....
gi 19114115 360 NaiQRAKVLCEDLIASVHQ 378
Cdd:cd22466  85 E--NRAKVKLQRAVEEVRK 101
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
309-373 1.32e-03

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: 37.23  E-value: 1.32e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114115 309 IVGPQGAYVKHIQQETRTRVQIKgqgsafiepstnRESDE-PIHLCIMSHDPNAIQRAKVLCEDLI 373
Cdd:cd22396  15 IIGRGGEQINRLQAESGAKIQIA------------PDSGGlPERPCTLTGTPDAIETAKRLIDQIV 68
PHA03247 PHA03247
large tegument protein UL36; Provisional
390-504 2.08e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115   390 RDQNQGNRAYNPPNRNQAFSARD--------SRQEKTQPTNASPAPLVTPSLPVPSIP-----AVPGMEAMAMPPGVTSS 456
Cdd:PHA03247 2668 RRLGRAAQASSPPQRPRRRAARPtvgsltslADPPPPPPTPEPAPHALVSATPLPPGPaaarqASPALPAAPAPPAVPAG 2747
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 19114115   457 IAVPTTSSMPlqGMPTMFGAPGVSAPGTEAPGTGTPGLTTPGVDPYAA 504
Cdd:PHA03247 2748 PATPGGPARP--ARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSE 2793
KH-I_KHDRBS1 cd22468
type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal ...
289-335 2.14e-03

type I K homology (KH) RNA-binding domain found in KH domain-containing, RNA-binding, signal transduction-associated protein 1 (KHDRBS1) and similar proteins; KHDRBS1, also called GAP-associated tyrosine phosphoprotein p62, or Src-associated in mitosis 68 kDa protein, or Sam68, or p21 Ras GTPase-activating protein-associated p62, or p68, is an RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. It binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. It also binds poly(A). KHDRBS1 acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. It is recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors.


Pssm-ID: 411896 [Multi-domain]  Cd Length: 106  Bit Score: 38.07  E-value: 2.14e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 19114115 289 LEEKVYINLTPSRGFHLRQAIVGPQGAYVKHIQQETRTRVQIKGQGS 335
Cdd:cd22468   5 LKERILIPVKQYPKFNFVGKILGPQGNTIKRLQEETGAKISVLGKGS 51
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
304-371 2.46e-03

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 36.49  E-value: 2.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114115   304 HLRQAIVGPQGAYVKHIQQETRTRVQIKGQGSafiePSTNREsdepihlCIMSHDPNAIQRAKVLCED 371
Cdd:pfam00013   9 SLVGLIIGKGGSNIKEIREETGAKIQIPPSES----EGNERI-------VTITGTPEAVEAAKALIEE 65
KH-I_NOVA_rpt3 cd09031
third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
308-368 3.45e-03

third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova); The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411807 [Multi-domain]  Cd Length: 71  Bit Score: 36.40  E-value: 3.45e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114115 308 AIVGPQGAYVKHIQQETRTRVQIKGQGSaFIEPSTNREsdepihlCIMSHDPNAIQRAKVL 368
Cdd:cd09031  14 AILGKGGKTLVEIQELTGARIQISKKGE-FVPGTRNRK-------VTITGTPAAVQAAQYL 66
MSL5 COG5176
Splicing factor (branch point binding protein) [RNA processing and modification];
290-373 3.86e-03

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


Pssm-ID: 227503 [Multi-domain]  Cd Length: 269  Bit Score: 39.18  E-value: 3.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115 290 EEKVYINLTPSRGFHLRQAIVGPQGAYVKHIQQETRTRVQIKGQGS------AFIEPSTNRESDEPIHLCIMSHDPNAIQ 363
Cdd:COG5176 149 QNKIYIPVQEYPESNFVGLLIGPRGSTLKQLERISRAKIAIRGSGSvkegkiSSDTPESLKNAEAVLHCLIEADSEDKIC 228
                        90
                ....*....|
gi 19114115 364 RAKVLCEDLI 373
Cdd:COG5176 229 RLIKSQLNAI 238
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
295-374 4.80e-03

second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411875 [Multi-domain]  Cd Length: 80  Bit Score: 36.24  E-value: 4.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114115 295 INLTPSRGFHLRQAIVGPQGAYVKHIQQETRTRVQIKGQGSAfiEPSTNRESDEPIHLCImSHDPNAIQRAKVLCEDLIA 374
Cdd:cd22447   4 QNLTVPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDAD--AAPADEDDDTMVEVTI-TGDEFNVQHAKQRIEEIIS 80
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
304-373 7.59e-03

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: 35.34  E-value: 7.59e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114115 304 HLRQAIVGPQGAYVKHIQQETRTRVQI-KGQGSAFIepstnresdepihlCIMShDPNAIQRAKVLCEDLI 373
Cdd:cd22430   9 SLVGAVIGRGGSKIRELEESTGSKIKIiKGGQEAEV--------------KIFG-SDEAQQKAKELIDELV 64
KH-I_FUBP_rpt3 cd22398
third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
306-373 9.36e-03

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: 34.93  E-value: 9.36e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114115 306 RQA---IVGPQGAYVKHIQQETRTRVQikgqgsaFIEPSTNresdEPIHLCIMSHDPNAIQRAKVLCEDLI 373
Cdd:cd22398   8 RFAvgvVIGKGGEMIKKIQNETGARVQ-------FKPDDGN----SPDRICVITGPPDQVQHAARMIQELI 67
 
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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