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Conserved domains on  [gi|1377605360|dbj|GBG27189|]
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Pumilio-like 1 [Hondaea fermentalgiana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Pumilio cd07920
Pumilio-family RNA binding domain; Puf repeats (also labelled PUM-HD or Pumilio homology ...
447-825 1.19e-110

Pumilio-family RNA binding domain; Puf repeats (also labelled PUM-HD or Pumilio homology domain) mediate sequence specific RNA binding in fly Pumilio, worm FBF-1 and FBF-2, and many other proteins such as vertebrate Pumilio. These proteins function as translational repressors in early embryonic development by binding to sequences in the 3' UTR of target mRNAs, such as the nanos response element (NRE) in fly Hunchback mRNA, or the point mutation element (PME) in worm fem-3 mRNA. Other proteins that contain Puf domains are also plausible RNA binding proteins. Yeast PUF1 (JSN1), for instance, appears to contain a single RNA-recognition motif (RRM) domain. Puf repeat proteins have been observed to function asymmetrically and may be responsible for creating protein gradients involved in the specification of cell fate and differentiation. Puf domains usually occur as a tandem repeat of 8 domains. This model encompasses all 8 tandem repeats. Some proteins may have fewer (canonical) repeats.


:

Pssm-ID: 153420 [Multi-domain]  Cd Length: 322  Bit Score: 355.36  E-value: 1.19e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  447 LRSIR-GQVVEFAKDQHGSRFLQTQLDSTTvsDEDKENLVAEILPDAQRLCADVFGNYTIQKLLTHGasTPAQQEQLVKE 525
Cdd:cd07920      4 LQDIKaGHIVEFAKDQHGSRFLQQKLEEAT--PEEKELIFDEILPHVVELMVDPFGNYVIQKLFEHG--TEEQRLQLLEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  526 AIEnHMVEHSNGSYSCRVIQKMIECIfsedgekvarslkpgepgstlySVEYQDQLLRELDGHVTKCACSNNANHVLQKL 605
Cdd:cd07920     80 ILG-HVVRLSLDMYGCRVIQKLLESI----------------------SEEQISLLVKELRGHVVELVKDQNGNHVIQKC 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  606 LECVRPlSRIDFIFDAFKGKMVELSTQAYACRVAQRAMENAEDDRLEPLLAEIMENVEILIQDSFGNYVTQHIIQHGDPE 685
Cdd:cd07920    137 IEKFPP-EDLQFIIDAFKGNCVALSTHPYGCRVIQRCLEHCSEEQREPLLEEILEHALELVQDQFGNYVVQHVLELGDPD 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  686 shdsclsrHRAELISIVKTNLLRFSQHKFSSNVVERCLESGNREERRMLIAKMLGPaesvktsnatsarqpssnaqpggg 765
Cdd:cd07920    216 --------DTSRIIEKLLGNIVQLSCHKFASNVVEKCLKHASKEERELIIDEILAS------------------------ 263
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  766 nGATKTLLEVMMTDQFANYVIQKALEVAEPDQREQIVIVIQRNANALKRLTYGRHILNRL 825
Cdd:cd07920    264 -GNETSALDTLMKDQYGNYVIQTALDVAKEEQRELLVEAIRPHLPSLRKSPYGKHILAKL 322
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
1665-1741 2.12e-42

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


:

Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 150.01  E-value: 2.12e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1377605360 1665 KPFCYYCDREFIDENQLIQHQKARHFRCLSCSRKFVSAPAMGVHLRQMHGQDLETVPNALPGRESPSVSVSGMRGVP 1741
Cdd:cd20908      1 KPWCYYCDREFDDEKILIQHQKAKHFKCHICHKKLYTAGGLAVHCLQVHKETLTKVPNALPGRDDPEIEIFGMEGIP 77
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1874-2092 1.09e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.60  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360 1874 SAGSGQRTASAEPPQSQQTSQETQPVLATPS---NVTAASAPEKnTKPSSGELKPVPAAAAVEDAKAKlLKTNETQPSVv 1950
Cdd:pfam05109  463 STGPTVSTADVTSPTPAGTTSGASPVTPSPSprdNGTESKAPDM-TSPTSAVTTPTPNATSPTPAVTT-PTPNATSPTL- 539
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360 1951 mpaAIAVPVGASTSPVPQASATVQSLApSPAQPQQADTVQESKEGAAQDSSSANAAKPYSASQAGAIATSKQSSGSEGPI 2030
Cdd:pfam05109  540 ---GKTSPTSAVTTPTPNATSPTPAVT-TPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSST 615
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360 2031 PTFN----DAFSASKLEKANSGMANPSESAFGDQSGHQHLAqghyPSASANHET--PTITAARQ--GQNV 2092
Cdd:pfam05109  616 PVVTsppkNATSAVTTGQHNITSSSTSSMSLRPSSISETLS----PSTSDNSTShmPLLTSAHPtgGENI 681
SEC14 super family cl49604
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
1182-1317 5.64e-03

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


The actual alignment was detected with superfamily member cd00170:

Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 39.62  E-value: 5.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360 1182 RLIREEDLLKCALYLAERSLLLLESISNRVgrvhelTILCDARGSPdePGLLLFMRMLKSVCESLS-HYPLRPKlilwkp 1260
Cdd:cd00170     35 KLLDLEELLRYLVYLLEKALRELEEQVEGF------VVIIDLKGFS--LSNLSDLSLLKKLLKILQdHYPERLK------ 100
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1377605360 1261 saelaelvraypSVHVVNSTKMLRILLSVE--CIPEELSGELRF--GKQSEMLSKVDPWQL 1317
Cdd:cd00170    101 ------------KIYIVNAPWIFSALWKIVkpFLSEKTRKKIVFlgSDLEELLEYIDPDQL 149
 
Name Accession Description Interval E-value
Pumilio cd07920
Pumilio-family RNA binding domain; Puf repeats (also labelled PUM-HD or Pumilio homology ...
447-825 1.19e-110

Pumilio-family RNA binding domain; Puf repeats (also labelled PUM-HD or Pumilio homology domain) mediate sequence specific RNA binding in fly Pumilio, worm FBF-1 and FBF-2, and many other proteins such as vertebrate Pumilio. These proteins function as translational repressors in early embryonic development by binding to sequences in the 3' UTR of target mRNAs, such as the nanos response element (NRE) in fly Hunchback mRNA, or the point mutation element (PME) in worm fem-3 mRNA. Other proteins that contain Puf domains are also plausible RNA binding proteins. Yeast PUF1 (JSN1), for instance, appears to contain a single RNA-recognition motif (RRM) domain. Puf repeat proteins have been observed to function asymmetrically and may be responsible for creating protein gradients involved in the specification of cell fate and differentiation. Puf domains usually occur as a tandem repeat of 8 domains. This model encompasses all 8 tandem repeats. Some proteins may have fewer (canonical) repeats.


Pssm-ID: 153420 [Multi-domain]  Cd Length: 322  Bit Score: 355.36  E-value: 1.19e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  447 LRSIR-GQVVEFAKDQHGSRFLQTQLDSTTvsDEDKENLVAEILPDAQRLCADVFGNYTIQKLLTHGasTPAQQEQLVKE 525
Cdd:cd07920      4 LQDIKaGHIVEFAKDQHGSRFLQQKLEEAT--PEEKELIFDEILPHVVELMVDPFGNYVIQKLFEHG--TEEQRLQLLEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  526 AIEnHMVEHSNGSYSCRVIQKMIECIfsedgekvarslkpgepgstlySVEYQDQLLRELDGHVTKCACSNNANHVLQKL 605
Cdd:cd07920     80 ILG-HVVRLSLDMYGCRVIQKLLESI----------------------SEEQISLLVKELRGHVVELVKDQNGNHVIQKC 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  606 LECVRPlSRIDFIFDAFKGKMVELSTQAYACRVAQRAMENAEDDRLEPLLAEIMENVEILIQDSFGNYVTQHIIQHGDPE 685
Cdd:cd07920    137 IEKFPP-EDLQFIIDAFKGNCVALSTHPYGCRVIQRCLEHCSEEQREPLLEEILEHALELVQDQFGNYVVQHVLELGDPD 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  686 shdsclsrHRAELISIVKTNLLRFSQHKFSSNVVERCLESGNREERRMLIAKMLGPaesvktsnatsarqpssnaqpggg 765
Cdd:cd07920    216 --------DTSRIIEKLLGNIVQLSCHKFASNVVEKCLKHASKEERELIIDEILAS------------------------ 263
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  766 nGATKTLLEVMMTDQFANYVIQKALEVAEPDQREQIVIVIQRNANALKRLTYGRHILNRL 825
Cdd:cd07920    264 -GNETSALDTLMKDQYGNYVIQTALDVAKEEQRELLVEAIRPHLPSLRKSPYGKHILAKL 322
COG5099 COG5099
RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal ...
459-835 3.21e-64

RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227430 [Multi-domain]  Cd Length: 777  Bit Score: 235.41  E-value: 3.21e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  459 KDQHGSRFLQTQLDSTtvSDEDKENLVAEILPDAQRLCADVFGNYTIQKLLTHGasTPAQQEQLVKeAIENHMVEHSNGS 538
Cdd:COG5099    448 KDQHGSRFLQKLLDSN--SSPEIEVIFNEILDQLVELSSDYFGNYLIQKLFEYG--SEIQKSIMLS-KSSKHLVSLSVHK 522
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  539 YSCRVIQKMIECIFSEDgekvarslkpgepgstlysveyQ-DQLLRELDGHVTKCACSNNANHVLQKLLECVRPlSRIDF 617
Cdd:COG5099    523 YGTRVLQKAIDIVSTDI----------------------QiSLLVEELRPYCLQLIKDQNGNHVIQKCIEKFNK-EKNQF 579
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  618 IFDAFKGKMVELSTQAYACRVAQRAMENAEDDRLEPLLAEIMENVEILIQDSFGNYVTQHIIQHGdpeshdSCLSRHRaE 697
Cdd:COG5099    580 IFDSINENLYDLSTHRYGSRVVQRCLENCNSEDKENLVEEIISNSKYLSQDQYGNYVVQHILDNG------AEPNKER-I 652
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  698 LISIVKTNLLRFSQHKFSSNVVERCLESGNREERRMLIAKmlgpaesvktsnatsarqpsSNAQPGGGNgatKTLLEVMM 777
Cdd:COG5099    653 IIKLLSKRVVELSTHKFASNVVEKCIKYASDSFKRSRILN--------------------ELTNRGIEK---PGFLMLIL 709
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1377605360  778 TDQFANYVIQKALEVAEPDQREQIVIVIQRNANALKRLTYGRHILNRLE-LNNKSGGSR 835
Cdd:COG5099    710 DDQYANYVIQYLLDVSPEIQRSLLARAIKKVIPSLKKSMYGQHILALLEkVGSSSQSSI 768
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
1665-1741 2.12e-42

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 150.01  E-value: 2.12e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1377605360 1665 KPFCYYCDREFIDENQLIQHQKARHFRCLSCSRKFVSAPAMGVHLRQMHGQDLETVPNALPGRESPSVSVSGMRGVP 1741
Cdd:cd20908      1 KPWCYYCDREFDDEKILIQHQKAKHFKCHICHKKLYTAGGLAVHCLQVHKETLTKVPNALPGRDDPEIEIFGMEGIP 77
Pumilio smart00025
Pumilio-like repeats; Pumilio-like repeats that bind RNA.
773-802 2.32e-07

Pumilio-like repeats; Pumilio-like repeats that bind RNA.


Pssm-ID: 214475 [Multi-domain]  Cd Length: 36  Bit Score: 48.58  E-value: 2.32e-07
                            10        20        30
                    ....*....|....*....|....*....|
gi 1377605360   773 LEVMMTDQFANYVIQKALEVAEPDQREQIV 802
Cdd:smart00025    6 LLELSKDQYGNRVVQKLLEHASESQREQII 35
PUF pfam00806
Pumilio-family RNA binding repeat; Puf repeats (aka PUM-HD, Pumilio homology domain) are ...
453-489 8.02e-07

Pumilio-family RNA binding repeat; Puf repeats (aka PUM-HD, Pumilio homology domain) are necessary and sufficient for sequence specific RNA binding in fly Pumilio and worm FBF-1 and FBF-2. Both proteins function as translational repressors in early embryonic development by binding sequences in the 3' UTR of target mRNAs (e.g. the nanos response element (NRE) in fly Hunchback mRNA, or the point mutation element (PME) in worm fem-3 mRNA). Other proteins that contain Puf domains are also plausible RNA binding proteins. Swiss:P47135, for instance, appears to also contain a single RRM domain by HMM analysis. Puf domains usually occur as a tandem repeat of 8 domains. The Pfam model does not necessarily recognize all 8 repeats in all sequences; some sequences appear to have 5 or 6 repeats on initial analysis, but further analysis suggests the presence of additional divergent repeats. Structures of PUF repeat proteins show they consist of a two helix structure.


Pssm-ID: 459944 [Multi-domain]  Cd Length: 35  Bit Score: 47.30  E-value: 8.02e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1377605360  453 QVVEFAKDQHGSRFLQTQLDstTVSDEDKENLVAEIL 489
Cdd:pfam00806    1 HVVELATDQYGCRVIQKCLE--HATEEQREQILDEIL 35
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1874-2092 1.09e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.60  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360 1874 SAGSGQRTASAEPPQSQQTSQETQPVLATPS---NVTAASAPEKnTKPSSGELKPVPAAAAVEDAKAKlLKTNETQPSVv 1950
Cdd:pfam05109  463 STGPTVSTADVTSPTPAGTTSGASPVTPSPSprdNGTESKAPDM-TSPTSAVTTPTPNATSPTPAVTT-PTPNATSPTL- 539
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360 1951 mpaAIAVPVGASTSPVPQASATVQSLApSPAQPQQADTVQESKEGAAQDSSSANAAKPYSASQAGAIATSKQSSGSEGPI 2030
Cdd:pfam05109  540 ---GKTSPTSAVTTPTPNATSPTPAVT-TPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSST 615
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360 2031 PTFN----DAFSASKLEKANSGMANPSESAFGDQSGHQHLAqghyPSASANHET--PTITAARQ--GQNV 2092
Cdd:pfam05109  616 PVVTsppkNATSAVTTGQHNITSSSTSSMSLRPSSISETLS----PSTSDNSTShmPLLTSAHPtgGENI 681
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
1665-1686 5.63e-03

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 35.99  E-value: 5.63e-03
                           10        20
                   ....*....|....*....|..
gi 1377605360 1665 KPFCYYCDREFIDENQLIQHQK 1686
Cdd:pfam12171    1 QFYCVLCDKYFKSENALQNHLK 22
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
1182-1317 5.64e-03

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 39.62  E-value: 5.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360 1182 RLIREEDLLKCALYLAERSLLLLESISNRVgrvhelTILCDARGSPdePGLLLFMRMLKSVCESLS-HYPLRPKlilwkp 1260
Cdd:cd00170     35 KLLDLEELLRYLVYLLEKALRELEEQVEGF------VVIIDLKGFS--LSNLSDLSLLKKLLKILQdHYPERLK------ 100
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1377605360 1261 saelaelvraypSVHVVNSTKMLRILLSVE--CIPEELSGELRF--GKQSEMLSKVDPWQL 1317
Cdd:cd00170    101 ------------KIYIVNAPWIFSALWKIVkpFLSEKTRKKIVFlgSDLEELLEYIDPDQL 149
 
Name Accession Description Interval E-value
Pumilio cd07920
Pumilio-family RNA binding domain; Puf repeats (also labelled PUM-HD or Pumilio homology ...
447-825 1.19e-110

Pumilio-family RNA binding domain; Puf repeats (also labelled PUM-HD or Pumilio homology domain) mediate sequence specific RNA binding in fly Pumilio, worm FBF-1 and FBF-2, and many other proteins such as vertebrate Pumilio. These proteins function as translational repressors in early embryonic development by binding to sequences in the 3' UTR of target mRNAs, such as the nanos response element (NRE) in fly Hunchback mRNA, or the point mutation element (PME) in worm fem-3 mRNA. Other proteins that contain Puf domains are also plausible RNA binding proteins. Yeast PUF1 (JSN1), for instance, appears to contain a single RNA-recognition motif (RRM) domain. Puf repeat proteins have been observed to function asymmetrically and may be responsible for creating protein gradients involved in the specification of cell fate and differentiation. Puf domains usually occur as a tandem repeat of 8 domains. This model encompasses all 8 tandem repeats. Some proteins may have fewer (canonical) repeats.


Pssm-ID: 153420 [Multi-domain]  Cd Length: 322  Bit Score: 355.36  E-value: 1.19e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  447 LRSIR-GQVVEFAKDQHGSRFLQTQLDSTTvsDEDKENLVAEILPDAQRLCADVFGNYTIQKLLTHGasTPAQQEQLVKE 525
Cdd:cd07920      4 LQDIKaGHIVEFAKDQHGSRFLQQKLEEAT--PEEKELIFDEILPHVVELMVDPFGNYVIQKLFEHG--TEEQRLQLLEK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  526 AIEnHMVEHSNGSYSCRVIQKMIECIfsedgekvarslkpgepgstlySVEYQDQLLRELDGHVTKCACSNNANHVLQKL 605
Cdd:cd07920     80 ILG-HVVRLSLDMYGCRVIQKLLESI----------------------SEEQISLLVKELRGHVVELVKDQNGNHVIQKC 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  606 LECVRPlSRIDFIFDAFKGKMVELSTQAYACRVAQRAMENAEDDRLEPLLAEIMENVEILIQDSFGNYVTQHIIQHGDPE 685
Cdd:cd07920    137 IEKFPP-EDLQFIIDAFKGNCVALSTHPYGCRVIQRCLEHCSEEQREPLLEEILEHALELVQDQFGNYVVQHVLELGDPD 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  686 shdsclsrHRAELISIVKTNLLRFSQHKFSSNVVERCLESGNREERRMLIAKMLGPaesvktsnatsarqpssnaqpggg 765
Cdd:cd07920    216 --------DTSRIIEKLLGNIVQLSCHKFASNVVEKCLKHASKEERELIIDEILAS------------------------ 263
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  766 nGATKTLLEVMMTDQFANYVIQKALEVAEPDQREQIVIVIQRNANALKRLTYGRHILNRL 825
Cdd:cd07920    264 -GNETSALDTLMKDQYGNYVIQTALDVAKEEQRELLVEAIRPHLPSLRKSPYGKHILAKL 322
COG5099 COG5099
RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal ...
459-835 3.21e-64

RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227430 [Multi-domain]  Cd Length: 777  Bit Score: 235.41  E-value: 3.21e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  459 KDQHGSRFLQTQLDSTtvSDEDKENLVAEILPDAQRLCADVFGNYTIQKLLTHGasTPAQQEQLVKeAIENHMVEHSNGS 538
Cdd:COG5099    448 KDQHGSRFLQKLLDSN--SSPEIEVIFNEILDQLVELSSDYFGNYLIQKLFEYG--SEIQKSIMLS-KSSKHLVSLSVHK 522
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  539 YSCRVIQKMIECIFSEDgekvarslkpgepgstlysveyQ-DQLLRELDGHVTKCACSNNANHVLQKLLECVRPlSRIDF 617
Cdd:COG5099    523 YGTRVLQKAIDIVSTDI----------------------QiSLLVEELRPYCLQLIKDQNGNHVIQKCIEKFNK-EKNQF 579
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  618 IFDAFKGKMVELSTQAYACRVAQRAMENAEDDRLEPLLAEIMENVEILIQDSFGNYVTQHIIQHGdpeshdSCLSRHRaE 697
Cdd:COG5099    580 IFDSINENLYDLSTHRYGSRVVQRCLENCNSEDKENLVEEIISNSKYLSQDQYGNYVVQHILDNG------AEPNKER-I 652
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360  698 LISIVKTNLLRFSQHKFSSNVVERCLESGNREERRMLIAKmlgpaesvktsnatsarqpsSNAQPGGGNgatKTLLEVMM 777
Cdd:COG5099    653 IIKLLSKRVVELSTHKFASNVVEKCIKYASDSFKRSRILN--------------------ELTNRGIEK---PGFLMLIL 709
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1377605360  778 TDQFANYVIQKALEVAEPDQREQIVIVIQRNANALKRLTYGRHILNRLE-LNNKSGGSR 835
Cdd:COG5099    710 DDQYANYVIQYLLDVSPEIQRSLLARAIKKVIPSLKKSMYGQHILALLEkVGSSSQSSI 768
SUF4-like cd20908
N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), ...
1665-1741 2.12e-42

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.


Pssm-ID: 411020 [Multi-domain]  Cd Length: 82  Bit Score: 150.01  E-value: 2.12e-42
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1377605360 1665 KPFCYYCDREFIDENQLIQHQKARHFRCLSCSRKFVSAPAMGVHLRQMHGQDLETVPNALPGRESPSVSVSGMRGVP 1741
Cdd:cd20908      1 KPWCYYCDREFDDEKILIQHQKAKHFKCHICHKKLYTAGGLAVHCLQVHKETLTKVPNALPGRDDPEIEIFGMEGIP 77
Pumilio smart00025
Pumilio-like repeats; Pumilio-like repeats that bind RNA.
773-802 2.32e-07

Pumilio-like repeats; Pumilio-like repeats that bind RNA.


Pssm-ID: 214475 [Multi-domain]  Cd Length: 36  Bit Score: 48.58  E-value: 2.32e-07
                            10        20        30
                    ....*....|....*....|....*....|
gi 1377605360   773 LEVMMTDQFANYVIQKALEVAEPDQREQIV 802
Cdd:smart00025    6 LLELSKDQYGNRVVQKLLEHASESQREQII 35
PUF pfam00806
Pumilio-family RNA binding repeat; Puf repeats (aka PUM-HD, Pumilio homology domain) are ...
453-489 8.02e-07

Pumilio-family RNA binding repeat; Puf repeats (aka PUM-HD, Pumilio homology domain) are necessary and sufficient for sequence specific RNA binding in fly Pumilio and worm FBF-1 and FBF-2. Both proteins function as translational repressors in early embryonic development by binding sequences in the 3' UTR of target mRNAs (e.g. the nanos response element (NRE) in fly Hunchback mRNA, or the point mutation element (PME) in worm fem-3 mRNA). Other proteins that contain Puf domains are also plausible RNA binding proteins. Swiss:P47135, for instance, appears to also contain a single RRM domain by HMM analysis. Puf domains usually occur as a tandem repeat of 8 domains. The Pfam model does not necessarily recognize all 8 repeats in all sequences; some sequences appear to have 5 or 6 repeats on initial analysis, but further analysis suggests the presence of additional divergent repeats. Structures of PUF repeat proteins show they consist of a two helix structure.


Pssm-ID: 459944 [Multi-domain]  Cd Length: 35  Bit Score: 47.30  E-value: 8.02e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1377605360  453 QVVEFAKDQHGSRFLQTQLDstTVSDEDKENLVAEIL 489
Cdd:pfam00806    1 HVVELATDQYGCRVIQKCLE--HATEEQREQILDEIL 35
PUF pfam00806
Pumilio-family RNA binding repeat; Puf repeats (aka PUM-HD, Pumilio homology domain) are ...
776-805 1.94e-06

Pumilio-family RNA binding repeat; Puf repeats (aka PUM-HD, Pumilio homology domain) are necessary and sufficient for sequence specific RNA binding in fly Pumilio and worm FBF-1 and FBF-2. Both proteins function as translational repressors in early embryonic development by binding sequences in the 3' UTR of target mRNAs (e.g. the nanos response element (NRE) in fly Hunchback mRNA, or the point mutation element (PME) in worm fem-3 mRNA). Other proteins that contain Puf domains are also plausible RNA binding proteins. Swiss:P47135, for instance, appears to also contain a single RRM domain by HMM analysis. Puf domains usually occur as a tandem repeat of 8 domains. The Pfam model does not necessarily recognize all 8 repeats in all sequences; some sequences appear to have 5 or 6 repeats on initial analysis, but further analysis suggests the presence of additional divergent repeats. Structures of PUF repeat proteins show they consist of a two helix structure.


Pssm-ID: 459944 [Multi-domain]  Cd Length: 35  Bit Score: 46.14  E-value: 1.94e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1377605360  776 MMTDQFANYVIQKALEVAEPDQREQIVIVI 805
Cdd:pfam00806    5 LATDQYGCRVIQKCLEHATEEQREQILDEI 34
PUF pfam00806
Pumilio-family RNA binding repeat; Puf repeats (aka PUM-HD, Pumilio homology domain) are ...
705-739 3.81e-06

Pumilio-family RNA binding repeat; Puf repeats (aka PUM-HD, Pumilio homology domain) are necessary and sufficient for sequence specific RNA binding in fly Pumilio and worm FBF-1 and FBF-2. Both proteins function as translational repressors in early embryonic development by binding sequences in the 3' UTR of target mRNAs (e.g. the nanos response element (NRE) in fly Hunchback mRNA, or the point mutation element (PME) in worm fem-3 mRNA). Other proteins that contain Puf domains are also plausible RNA binding proteins. Swiss:P47135, for instance, appears to also contain a single RRM domain by HMM analysis. Puf domains usually occur as a tandem repeat of 8 domains. The Pfam model does not necessarily recognize all 8 repeats in all sequences; some sequences appear to have 5 or 6 repeats on initial analysis, but further analysis suggests the presence of additional divergent repeats. Structures of PUF repeat proteins show they consist of a two helix structure.


Pssm-ID: 459944 [Multi-domain]  Cd Length: 35  Bit Score: 45.37  E-value: 3.81e-06
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1377605360  705 NLLRFSQHKFSSNVVERCLESGNREERRMLIAKML 739
Cdd:pfam00806    1 HVVELATDQYGCRVIQKCLEHATEEQREQILDEIL 35
PUF pfam00806
Pumilio-family RNA binding repeat; Puf repeats (aka PUM-HD, Pumilio homology domain) are ...
625-659 2.84e-05

Pumilio-family RNA binding repeat; Puf repeats (aka PUM-HD, Pumilio homology domain) are necessary and sufficient for sequence specific RNA binding in fly Pumilio and worm FBF-1 and FBF-2. Both proteins function as translational repressors in early embryonic development by binding sequences in the 3' UTR of target mRNAs (e.g. the nanos response element (NRE) in fly Hunchback mRNA, or the point mutation element (PME) in worm fem-3 mRNA). Other proteins that contain Puf domains are also plausible RNA binding proteins. Swiss:P47135, for instance, appears to also contain a single RRM domain by HMM analysis. Puf domains usually occur as a tandem repeat of 8 domains. The Pfam model does not necessarily recognize all 8 repeats in all sequences; some sequences appear to have 5 or 6 repeats on initial analysis, but further analysis suggests the presence of additional divergent repeats. Structures of PUF repeat proteins show they consist of a two helix structure.


Pssm-ID: 459944 [Multi-domain]  Cd Length: 35  Bit Score: 42.67  E-value: 2.84e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1377605360  625 KMVELSTQAYACRVAQRAMENAEDDRLEPLLAEIM 659
Cdd:pfam00806    1 HVVELATDQYGCRVIQKCLEHATEEQREQILDEIL 35
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
1874-2092 1.09e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.60  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360 1874 SAGSGQRTASAEPPQSQQTSQETQPVLATPS---NVTAASAPEKnTKPSSGELKPVPAAAAVEDAKAKlLKTNETQPSVv 1950
Cdd:pfam05109  463 STGPTVSTADVTSPTPAGTTSGASPVTPSPSprdNGTESKAPDM-TSPTSAVTTPTPNATSPTPAVTT-PTPNATSPTL- 539
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360 1951 mpaAIAVPVGASTSPVPQASATVQSLApSPAQPQQADTVQESKEGAAQDSSSANAAKPYSASQAGAIATSKQSSGSEGPI 2030
Cdd:pfam05109  540 ---GKTSPTSAVTTPTPNATSPTPAVT-TPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSST 615
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360 2031 PTFN----DAFSASKLEKANSGMANPSESAFGDQSGHQHLAqghyPSASANHET--PTITAARQ--GQNV 2092
Cdd:pfam05109  616 PVVTsppkNATSAVTTGQHNITSSSTSSMSLRPSSISETLS----PSTSDNSTShmPLLTSAHPtgGENI 681
Pumilio smart00025
Pumilio-like repeats; Pumilio-like repeats that bind RNA.
701-735 6.32e-04

Pumilio-like repeats; Pumilio-like repeats that bind RNA.


Pssm-ID: 214475 [Multi-domain]  Cd Length: 36  Bit Score: 38.95  E-value: 6.32e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1377605360   701 IVKTNLLRFSQHKFSSNVVERCLESGNREERRMLI 735
Cdd:smart00025    1 LIKGHLLELSKDQYGNRVVQKLLEHASESQREQII 35
Pumilio smart00025
Pumilio-like repeats; Pumilio-like repeats that bind RNA.
487-524 2.93e-03

Pumilio-like repeats; Pumilio-like repeats that bind RNA.


Pssm-ID: 214475 [Multi-domain]  Cd Length: 36  Bit Score: 37.03  E-value: 2.93e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1377605360   487 EILPDAQRLCADVFGNYTIQKLLTHGasTPAQQEQLVK 524
Cdd:smart00025    1 LIKGHLLELSKDQYGNRVVQKLLEHA--SESQREQIID 36
Pumilio smart00025
Pumilio-like repeats; Pumilio-like repeats that bind RNA.
584-620 3.27e-03

Pumilio-like repeats; Pumilio-like repeats that bind RNA.


Pssm-ID: 214475 [Multi-domain]  Cd Length: 36  Bit Score: 37.03  E-value: 3.27e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1377605360   584 ELDGHVTKCACSNNANHVLQKLLECVRPlSRIDFIFD 620
Cdd:smart00025    1 LIKGHLLELSKDQYGNRVVQKLLEHASE-SQREQIID 36
Pumilio smart00025
Pumilio-like repeats; Pumilio-like repeats that bind RNA.
449-485 4.02e-03

Pumilio-like repeats; Pumilio-like repeats that bind RNA.


Pssm-ID: 214475 [Multi-domain]  Cd Length: 36  Bit Score: 36.64  E-value: 4.02e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 1377605360   449 SIRGQVVEFAKDQHGSRFLQTQLDstTVSDEDKENLV 485
Cdd:smart00025    1 LIKGHLLELSKDQYGNRVVQKLLE--HASESQREQII 35
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
1665-1686 5.63e-03

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 35.99  E-value: 5.63e-03
                           10        20
                   ....*....|....*....|..
gi 1377605360 1665 KPFCYYCDREFIDENQLIQHQK 1686
Cdd:pfam12171    1 QFYCVLCDKYFKSENALQNHLK 22
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
1182-1317 5.64e-03

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 39.62  E-value: 5.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1377605360 1182 RLIREEDLLKCALYLAERSLLLLESISNRVgrvhelTILCDARGSPdePGLLLFMRMLKSVCESLS-HYPLRPKlilwkp 1260
Cdd:cd00170     35 KLLDLEELLRYLVYLLEKALRELEEQVEGF------VVIIDLKGFS--LSNLSDLSLLKKLLKILQdHYPERLK------ 100
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1377605360 1261 saelaelvraypSVHVVNSTKMLRILLSVE--CIPEELSGELRF--GKQSEMLSKVDPWQL 1317
Cdd:cd00170    101 ------------KIYIVNAPWIFSALWKIVkpFLSEKTRKKIVFlgSDLEELLEYIDPDQL 149
PUF pfam00806
Pumilio-family RNA binding repeat; Puf repeats (aka PUM-HD, Pumilio homology domain) are ...
495-525 8.18e-03

Pumilio-family RNA binding repeat; Puf repeats (aka PUM-HD, Pumilio homology domain) are necessary and sufficient for sequence specific RNA binding in fly Pumilio and worm FBF-1 and FBF-2. Both proteins function as translational repressors in early embryonic development by binding sequences in the 3' UTR of target mRNAs (e.g. the nanos response element (NRE) in fly Hunchback mRNA, or the point mutation element (PME) in worm fem-3 mRNA). Other proteins that contain Puf domains are also plausible RNA binding proteins. Swiss:P47135, for instance, appears to also contain a single RRM domain by HMM analysis. Puf domains usually occur as a tandem repeat of 8 domains. The Pfam model does not necessarily recognize all 8 repeats in all sequences; some sequences appear to have 5 or 6 repeats on initial analysis, but further analysis suggests the presence of additional divergent repeats. Structures of PUF repeat proteins show they consist of a two helix structure.


Pssm-ID: 459944 [Multi-domain]  Cd Length: 35  Bit Score: 35.74  E-value: 8.18e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1377605360  495 LCADVFGNYTIQKLLTHGasTPAQQEQLVKE 525
Cdd:pfam00806    5 LATDQYGCRVIQKCLEHA--TEEQREQILDE 33
 
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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