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Conserved domains on  [gi|1002232352|ref|XP_015616412|]
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homeobox-DDT domain protein RLT2 isoform X1 [Oryza sativa Japonica Group]

Protein Classification

homeobox domain-containing protein( domain architecture ID 11079024)

homeobox domain-containing protein similar to double homeobox protein that may act as a transcription factor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WSD pfam15613
Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined ...
 1207-1281 3.76e-23

Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined alpha-helical module found in diverse eukaryotic chromatin proteins. Based on the Ioc3 structure, the N-terminus of this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The acidic residue from the GxD signature at the N-terminus is a major determinant of the interaction between the ISWI and WHIM motifs. The N-terminal portion also contacts the inter-nucleosomal linker DNA. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognizing and DNA binding domains, some of which discriminate methylated DNA. The WSD module constitutes the inter-nucleosomal linker DNA binding site in the major groove of DNA, and was first identified as WSD, the D-TOX E motif of plant homeodomains homologous with the mutant transcription factor causing Williams-Beuren syndrome in association with the DDT-domain.


:

Pssm-ID: 464775 [Multi-domain]  Cd Length: 69  Bit Score: 94.52  E-value: 3.76e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232352 1207 YRSLPLGQDRRRNRYWQFstsaspnDPGSGRIFFE-CRDGYWRVLDTEEAFDSLVASLDTRGSREAQLHSMLQRIE 1281
Cdd:pfam15613    1 IRSLPLGRDRRYNRYWWF-------DPGTGRLFVEsPSDGEWGVYSSKEQLDALIASLNPRGVRESALKEALEKIK 69
DDT pfam02791
DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription ...
 632-687 1.45e-17

DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription factors) and is approximately 60 residues in length. Along with the WHIM motifs, it comprises an entirely alpha helical module found in diverse eukaryotic chromatin proteins. Based on the structure of Ioc3, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. In particular, the DDT domain, in combination with the WHIM1 and WHIM2 motifs form the SLIDE domain binding pocket.


:

Pssm-ID: 460696  Cd Length: 58  Bit Score: 78.32  E-value: 1.45e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232352  632 DNVGNLLMVWKFSITFADVLGLSSVTFDEFVQSLHDYD--SRLLGELHIALLKSIIKD 687
Cdd:pfam02791    1 EAFGDLLMVWEFLNSFGEVLGLSPFTLDDFEEALLCTEepSELLDEIHCALLKALVRD 58
Homeodomain pfam00046
Homeodomain;
49-103 1.81e-16

Homeodomain;


:

Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 74.84  E-value: 1.81e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1002232352   49 KRMMKSPYQLEVLEKTYAVEQYPSETLRAELSAKIGLSDRQLQMWFCHRRLKDRK 103
Cdd:pfam00046    3 KRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
HARE-HTH pfam05066
HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in ...
 807-875 7.20e-15

HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in the plant HB1, vertebrate ASXL, the H. pylori restriction endonuclease HpyAIII(HgrA), the RNA polymerase delta subunit(RpoE) of Gram positive bacteria and several restriction endonucleases. The domain is distinguished by the presence of a conserved one-turn helix between helix-3 and the preceding conserved turn. Its diverse architectures in eukaryotic species with extensive gene body methylation is suggestive of a chromatin function. The genetic interaction of the HARE-HTH containing ASXL with the methyl cytosine hydroxylating Tet2 protein is suggestive of a role for the domain in discriminating sequences with DNA modifications such as hmC. Bacterial versions include fusions to diverse restriction endonucleases, and a DNA glycosylase where it may play a similar role in detecting modified DNA. Certain bacterial version of the HARE-HTH domain show fusions to the helix-hairpin-helix domain of the RNA polymerase alpha subunit and the HTH domains found in regions 3 and 4 of the sigma factors. These versions are predicted to function as a novel inhibitor of the binding of RNA polymerase to transcription start sites, similar to the Bacillus delta protein.


:

Pssm-ID: 461541  Cd Length: 71  Bit Score: 70.80  E-value: 7.20e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232352  807 GTVKFAAFHVLSLEGsKGLTILEVAERIQKSGLRDlTTSKTPEASIAAALSRDTK---LFERTAPSTYCVKS 875
Cdd:pfam05066    1 GTLKEAAFQVLEEEG-RPLHFKEIAEEIQEKGLIS-LSGKTPEATLAAQLYTDIKedsLFVRVGPGTFGLRS 70
WHIM1 pfam15612
WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and ...
 1027-1072 5.43e-07

WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and WHIM3 motifs, and the DDT domain comprise an alpha helical module found in diverse eukaryotic chromatin proteins.Based on the Ioc3 structure, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The conserved basic residue in WHIM1 is involved in packing with the DDT motif. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognising and DNA binding domains, some of which discriminate methylated DNA.


:

Pssm-ID: 464774 [Multi-domain]  Cd Length: 46  Bit Score: 47.88  E-value: 5.43e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1002232352 1027 SNQGESWVHGLAEGDYCDLSVEERLNALVALVSVANEGNFIRAVLE 1072
Cdd:pfam15612    1 REDLPGLLETLKKGGYYELSPEEKLKILKALCDLLLSSSAIRDEIE 46
TPH super family cl38442
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 439-579 2.50e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


The actual alignment was detected with superfamily member pfam13868:

Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 51.84  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  439 RVDRKRKHNEEAKIAKEVEAHERRIRKElEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQERFLREQRREH 518
Cdd:pfam13868  195 KAQDEKAERDELRAKLYQEEQERKERQK-EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAED 273

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232352  519 ERMEKfMQKQSRRAEKQRQKEEL-------RKEKEAARQKAANERATARRIAREYMELVEDECLELME 579
Cdd:pfam13868  274 EEIEQ-EEAEKRRMKRLEHRRELekqieerEEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
 
Name Accession Description Interval E-value
WSD pfam15613
Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined ...
 1207-1281 3.76e-23

Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined alpha-helical module found in diverse eukaryotic chromatin proteins. Based on the Ioc3 structure, the N-terminus of this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The acidic residue from the GxD signature at the N-terminus is a major determinant of the interaction between the ISWI and WHIM motifs. The N-terminal portion also contacts the inter-nucleosomal linker DNA. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognizing and DNA binding domains, some of which discriminate methylated DNA. The WSD module constitutes the inter-nucleosomal linker DNA binding site in the major groove of DNA, and was first identified as WSD, the D-TOX E motif of plant homeodomains homologous with the mutant transcription factor causing Williams-Beuren syndrome in association with the DDT-domain.


Pssm-ID: 464775 [Multi-domain]  Cd Length: 69  Bit Score: 94.52  E-value: 3.76e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232352 1207 YRSLPLGQDRRRNRYWQFstsaspnDPGSGRIFFE-CRDGYWRVLDTEEAFDSLVASLDTRGSREAQLHSMLQRIE 1281
Cdd:pfam15613    1 IRSLPLGRDRRYNRYWWF-------DPGTGRLFVEsPSDGEWGVYSSKEQLDALIASLNPRGVRESALKEALEKIK 69
DDT pfam02791
DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription ...
 632-687 1.45e-17

DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription factors) and is approximately 60 residues in length. Along with the WHIM motifs, it comprises an entirely alpha helical module found in diverse eukaryotic chromatin proteins. Based on the structure of Ioc3, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. In particular, the DDT domain, in combination with the WHIM1 and WHIM2 motifs form the SLIDE domain binding pocket.


Pssm-ID: 460696  Cd Length: 58  Bit Score: 78.32  E-value: 1.45e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232352  632 DNVGNLLMVWKFSITFADVLGLSSVTFDEFVQSLHDYD--SRLLGELHIALLKSIIKD 687
Cdd:pfam02791    1 EAFGDLLMVWEFLNSFGEVLGLSPFTLDDFEEALLCTEepSELLDEIHCALLKALVRD 58
Homeodomain pfam00046
Homeodomain;
49-103 1.81e-16

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 74.84  E-value: 1.81e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1002232352   49 KRMMKSPYQLEVLEKTYAVEQYPSETLRAELSAKIGLSDRQLQMWFCHRRLKDRK 103
Cdd:pfam00046    3 KRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
HARE-HTH pfam05066
HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in ...
 807-875 7.20e-15

HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in the plant HB1, vertebrate ASXL, the H. pylori restriction endonuclease HpyAIII(HgrA), the RNA polymerase delta subunit(RpoE) of Gram positive bacteria and several restriction endonucleases. The domain is distinguished by the presence of a conserved one-turn helix between helix-3 and the preceding conserved turn. Its diverse architectures in eukaryotic species with extensive gene body methylation is suggestive of a chromatin function. The genetic interaction of the HARE-HTH containing ASXL with the methyl cytosine hydroxylating Tet2 protein is suggestive of a role for the domain in discriminating sequences with DNA modifications such as hmC. Bacterial versions include fusions to diverse restriction endonucleases, and a DNA glycosylase where it may play a similar role in detecting modified DNA. Certain bacterial version of the HARE-HTH domain show fusions to the helix-hairpin-helix domain of the RNA polymerase alpha subunit and the HTH domains found in regions 3 and 4 of the sigma factors. These versions are predicted to function as a novel inhibitor of the binding of RNA polymerase to transcription start sites, similar to the Bacillus delta protein.


Pssm-ID: 461541  Cd Length: 71  Bit Score: 70.80  E-value: 7.20e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232352  807 GTVKFAAFHVLSLEGsKGLTILEVAERIQKSGLRDlTTSKTPEASIAAALSRDTK---LFERTAPSTYCVKS 875
Cdd:pfam05066    1 GTLKEAAFQVLEEEG-RPLHFKEIAEEIQEKGLIS-LSGKTPEATLAAQLYTDIKedsLFVRVGPGTFGLRS 70
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 49-104 1.29e-13

Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.


Pssm-ID: 238039 [Multi-domain]  Cd Length: 59  Bit Score: 66.88  E-value: 1.29e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232352   49 KRMMKSPYQLEVLEKTYAVEQYPSETLRAELSAKIGLSDRQLQMWFCHRRLKDRKP 104
Cdd:cd00086      3 KRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
DDT smart00571
domain in different transcription and chromosome remodeling factors;
631-690 3.22e-13

domain in different transcription and chromosome remodeling factors;


Pssm-ID: 214726  Cd Length: 63  Bit Score: 66.12  E-value: 3.22e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002232352   631 EDNVGNLLMVWKFSITFADVLGLS--SVTFDEFVQSLHDYDSR-LLGELHIALLKSIIKDIED 690
Cdd:smart00571    1 NEAFGDLLMVYEFLRSFGKVLGLSpfRATLEDFIAALKCRDQNgLLTEVHVVLLRAILKDEGE 63
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 49-102 3.89e-13

Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes


Pssm-ID: 197696 [Multi-domain]  Cd Length: 57  Bit Score: 65.73  E-value: 3.89e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1002232352    49 KRMMKSPYQLEVLEKTYAVEQYPSETLRAELSAKIGLSDRQLQMWFCHRRLKDR 102
Cdd:smart00389    4 KRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
42-103 4.54e-07

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 51.28  E-value: 4.54e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232352   42 GSGEKTVKRMMKSPYQLEVLEKTYAVEQYPSETLRAELSAKIGLSDRQLQMWFCHRRLKDRK 103
Cdd:COG5576     47 GSSPPKSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKK 108
WHIM1 pfam15612
WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and ...
 1027-1072 5.43e-07

WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and WHIM3 motifs, and the DDT domain comprise an alpha helical module found in diverse eukaryotic chromatin proteins.Based on the Ioc3 structure, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The conserved basic residue in WHIM1 is involved in packing with the DDT motif. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognising and DNA binding domains, some of which discriminate methylated DNA.


Pssm-ID: 464774 [Multi-domain]  Cd Length: 46  Bit Score: 47.88  E-value: 5.43e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1002232352 1027 SNQGESWVHGLAEGDYCDLSVEERLNALVALVSVANEGNFIRAVLE 1072
Cdd:pfam15612    1 REDLPGLLETLKKGGYYELSPEEKLKILKALCDLLLSSSAIRDEIE 46
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 439-579 2.50e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 51.84  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  439 RVDRKRKHNEEAKIAKEVEAHERRIRKElEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQERFLREQRREH 518
Cdd:pfam13868  195 KAQDEKAERDELRAKLYQEEQERKERQK-EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAED 273

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232352  519 ERMEKfMQKQSRRAEKQRQKEEL-------RKEKEAARQKAANERATARRIAREYMELVEDECLELME 579
Cdd:pfam13868  274 EEIEQ-EEAEKRRMKRLEHRRELekqieerEEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
PTZ00121 PTZ00121
MAEBL; Provisional
 435-573 2.99e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 2.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  435 EDGSRVDRKRKhNEEAKIAKEVEAHERRiRKELEKQDMMKRKRE-----EQMRKEMERHDRERRKEEERLLRERQREQER 509
Cdd:PTZ00121  1543 EEKKKADELKK-AEELKKAEEKKKAEEA-KKAEEDKNMALRKAEeakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002232352  510 FLREQRREHERMEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYMELVEDE 573
Cdd:PTZ00121  1621 KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
 
Name Accession Description Interval E-value
WSD pfam15613
Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined ...
 1207-1281 3.76e-23

Williams-Beuren syndrome DDT (WSD), D-TOX E motif; This family represents the combined alpha-helical module found in diverse eukaryotic chromatin proteins. Based on the Ioc3 structure, the N-terminus of this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The acidic residue from the GxD signature at the N-terminus is a major determinant of the interaction between the ISWI and WHIM motifs. The N-terminal portion also contacts the inter-nucleosomal linker DNA. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognizing and DNA binding domains, some of which discriminate methylated DNA. The WSD module constitutes the inter-nucleosomal linker DNA binding site in the major groove of DNA, and was first identified as WSD, the D-TOX E motif of plant homeodomains homologous with the mutant transcription factor causing Williams-Beuren syndrome in association with the DDT-domain.


Pssm-ID: 464775 [Multi-domain]  Cd Length: 69  Bit Score: 94.52  E-value: 3.76e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232352 1207 YRSLPLGQDRRRNRYWQFstsaspnDPGSGRIFFE-CRDGYWRVLDTEEAFDSLVASLDTRGSREAQLHSMLQRIE 1281
Cdd:pfam15613    1 IRSLPLGRDRRYNRYWWF-------DPGTGRLFVEsPSDGEWGVYSSKEQLDALIASLNPRGVRESALKEALEKIK 69
DDT pfam02791
DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription ...
 632-687 1.45e-17

DDT domain; The DDT domain is named after (DNA binding homeobox and Different Transcription factors) and is approximately 60 residues in length. Along with the WHIM motifs, it comprises an entirely alpha helical module found in diverse eukaryotic chromatin proteins. Based on the structure of Ioc3, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. In particular, the DDT domain, in combination with the WHIM1 and WHIM2 motifs form the SLIDE domain binding pocket.


Pssm-ID: 460696  Cd Length: 58  Bit Score: 78.32  E-value: 1.45e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232352  632 DNVGNLLMVWKFSITFADVLGLSSVTFDEFVQSLHDYD--SRLLGELHIALLKSIIKD 687
Cdd:pfam02791    1 EAFGDLLMVWEFLNSFGEVLGLSPFTLDDFEEALLCTEepSELLDEIHCALLKALVRD 58
Homeodomain pfam00046
Homeodomain;
49-103 1.81e-16

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 74.84  E-value: 1.81e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1002232352   49 KRMMKSPYQLEVLEKTYAVEQYPSETLRAELSAKIGLSDRQLQMWFCHRRLKDRK 103
Cdd:pfam00046    3 KRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
HARE-HTH pfam05066
HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in ...
 807-875 7.20e-15

HB1, ASXL, restriction endonuclease HTH domain; A winged helix-turn-helix domain present in the plant HB1, vertebrate ASXL, the H. pylori restriction endonuclease HpyAIII(HgrA), the RNA polymerase delta subunit(RpoE) of Gram positive bacteria and several restriction endonucleases. The domain is distinguished by the presence of a conserved one-turn helix between helix-3 and the preceding conserved turn. Its diverse architectures in eukaryotic species with extensive gene body methylation is suggestive of a chromatin function. The genetic interaction of the HARE-HTH containing ASXL with the methyl cytosine hydroxylating Tet2 protein is suggestive of a role for the domain in discriminating sequences with DNA modifications such as hmC. Bacterial versions include fusions to diverse restriction endonucleases, and a DNA glycosylase where it may play a similar role in detecting modified DNA. Certain bacterial version of the HARE-HTH domain show fusions to the helix-hairpin-helix domain of the RNA polymerase alpha subunit and the HTH domains found in regions 3 and 4 of the sigma factors. These versions are predicted to function as a novel inhibitor of the binding of RNA polymerase to transcription start sites, similar to the Bacillus delta protein.


Pssm-ID: 461541  Cd Length: 71  Bit Score: 70.80  E-value: 7.20e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232352  807 GTVKFAAFHVLSLEGsKGLTILEVAERIQKSGLRDlTTSKTPEASIAAALSRDTK---LFERTAPSTYCVKS 875
Cdd:pfam05066    1 GTLKEAAFQVLEEEG-RPLHFKEIAEEIQEKGLIS-LSGKTPEATLAAQLYTDIKedsLFVRVGPGTFGLRS 70
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
 49-104 1.29e-13

Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.


Pssm-ID: 238039 [Multi-domain]  Cd Length: 59  Bit Score: 66.88  E-value: 1.29e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232352   49 KRMMKSPYQLEVLEKTYAVEQYPSETLRAELSAKIGLSDRQLQMWFCHRRLKDRKP 104
Cdd:cd00086      3 KRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
DDT smart00571
domain in different transcription and chromosome remodeling factors;
631-690 3.22e-13

domain in different transcription and chromosome remodeling factors;


Pssm-ID: 214726  Cd Length: 63  Bit Score: 66.12  E-value: 3.22e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002232352   631 EDNVGNLLMVWKFSITFADVLGLS--SVTFDEFVQSLHDYDSR-LLGELHIALLKSIIKDIED 690
Cdd:smart00571    1 NEAFGDLLMVYEFLRSFGKVLGLSpfRATLEDFIAALKCRDQNgLLTEVHVVLLRAILKDEGE 63
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
 49-102 3.89e-13

Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes


Pssm-ID: 197696 [Multi-domain]  Cd Length: 57  Bit Score: 65.73  E-value: 3.89e-13
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1002232352    49 KRMMKSPYQLEVLEKTYAVEQYPSETLRAELSAKIGLSDRQLQMWFCHRRLKDR 102
Cdd:smart00389    4 KRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
42-103 4.54e-07

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 51.28  E-value: 4.54e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232352   42 GSGEKTVKRMMKSPYQLEVLEKTYAVEQYPSETLRAELSAKIGLSDRQLQMWFCHRRLKDRK 103
Cdd:COG5576     47 GSSPPKSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKK 108
WHIM1 pfam15612
WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and ...
 1027-1072 5.43e-07

WSTF, HB1, Itc1p, MBD9 motif 1; A conserved alpha helical motif that along with the WHIM2 and WHIM3 motifs, and the DDT domain comprise an alpha helical module found in diverse eukaryotic chromatin proteins.Based on the Ioc3 structure, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes. The conserved basic residue in WHIM1 is involved in packing with the DDT motif. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognising and DNA binding domains, some of which discriminate methylated DNA.


Pssm-ID: 464774 [Multi-domain]  Cd Length: 46  Bit Score: 47.88  E-value: 5.43e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1002232352 1027 SNQGESWVHGLAEGDYCDLSVEERLNALVALVSVANEGNFIRAVLE 1072
Cdd:pfam15612    1 REDLPGLLETLKKGGYYELSPEEKLKILKALCDLLLSSSAIRDEIE 46
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 439-579 2.50e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 51.84  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  439 RVDRKRKHNEEAKIAKEVEAHERRIRKElEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQERFLREQRREH 518
Cdd:pfam13868  195 KAQDEKAERDELRAKLYQEEQERKERQK-EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAED 273

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232352  519 ERMEKfMQKQSRRAEKQRQKEEL-------RKEKEAARQKAANERATARRIAREYMELVEDECLELME 579
Cdd:pfam13868  274 EEIEQ-EEAEKRRMKRLEHRRELekqieerEEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
PTZ00121 PTZ00121
MAEBL; Provisional
 435-573 2.99e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 2.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  435 EDGSRVDRKRKhNEEAKIAKEVEAHERRiRKELEKQDMMKRKRE-----EQMRKEMERHDRERRKEEERLLRERQREQER 509
Cdd:PTZ00121  1543 EEKKKADELKK-AEELKKAEEKKKAEEA-KKAEEDKNMALRKAEeakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002232352  510 FLREQRREHERMEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYMELVEDE 573
Cdd:PTZ00121  1621 KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 373-585 4.07e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 51.49  E-value: 4.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  373 SGSGHLPQ-SGRREVLPAVPTDYEMIQSNSDLNSVPvegqygiSQVAGIENSLLPSERRAYHDEDGSRVDRKRKHNEEAK 451
Cdd:pfam15709  264 SERGAFSSdSVVEDPWLSSKYDAEESQVSIDGRSSP-------TQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRD 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  452 IAKEVEAHERRI-----RKELEKQDMMKRK---REEQMRKEMERHDRERRKEEERLLRERqrEQerflREQRREHERMEK 523
Cdd:pfam15709  337 RLRAERAEMRRLeverkRREQEEQRRLQQEqleRAEKMREELELEQQRRFEEIRLRKQRL--EE----ERQRQEEEERKQ 410

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232352  524 FMQKQSRRAEKQRQKEELRK---EKEAARQKAANERATA--RRIAREYMELVEdECLELMELAAQSK 585
Cdd:pfam15709  411 RLQLQAAQERARQQQEEFRRklqELQRKKQQEEAERAEAekQRQKELEMQLAE-EQKRLMEMAEEER 476
PTZ00121 PTZ00121
MAEBL; Provisional
 435-572 7.80e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 7.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  435 EDGSRVDRKRKHNEEAKIAKEVEAHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQERFLREQ 514
Cdd:PTZ00121  1197 EDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE 1276

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232352  515 RREHERMekfmqkqsRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYMELVED 572
Cdd:PTZ00121  1277 ARKADEL--------KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
PTZ00121 PTZ00121
MAEBL; Provisional
 434-573 1.39e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  434 DEDGSRVDRKRKHNEEAKIAKEVEA----HERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQEr 509
Cdd:PTZ00121  1643 AEEKKKAEELKKAEEENKIKAAEEAkkaeEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL- 1721

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232352  510 flreQRREHERMEKFMQKQSRRAEKQRQKEELRK---EKEAARQKAANERATARRIAREYMELVEDE 573
Cdd:PTZ00121  1722 ----KKAEEENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
PTZ00121 PTZ00121
MAEBL; Provisional
 420-573 1.44e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  420 IENSLLPSERRAYHDEDGSRVDRKRKHNEEAKIAKEV--EAHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEE 497
Cdd:PTZ00121  1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  498 RLLRERQREQERFLREQ---------RREHERMEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYME 568
Cdd:PTZ00121  1669 KAEEDKKKAEEAKKAEEdekkaaealKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748


                   ....*
gi 1002232352  569 LVEDE 573
Cdd:PTZ00121  1749 AKKDE 1753
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 441-558 2.35e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 49.35  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  441 DRKRKHNE---EAKIAKEVEAHERRI-RKELE--KQDMMKRKREEQM-RKEMERHDRERRKEEERLLRERQREQERFLRE 513
Cdd:pfam17380  471 ERKRKKLElekEKRDRKRAEEQRRKIlEKELEerKQAMIEEERKRKLlEKEMEERQKAIYEEERRREAEEERRKQQEMEE 550

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1002232352  514 QRREHERMEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERAT 558
Cdd:pfam17380  551 RRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATT 595
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 442-583 5.53e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 47.61  E-value: 5.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  442 RKRKHNEEAKIAKEVEAHERRIRKELEKQDMMKRKREEQMRKEmerhdrerrkeeerllrerqreqerfLREQRREHERm 521
Cdd:pfam13868   35 KAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQE--------------------------LEEQIEEREQ- 87

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232352  522 EKFMQKQSRRAEKQRQKEELRKEKEAARQKAAnERATARRIAREYMELVEDECLELMELAAQ 583
Cdd:pfam13868   88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAE-EKLEKQRQLREEIDEFNEEQAEWKELEKE 148
PTZ00121 PTZ00121
MAEBL; Provisional
 435-587 1.10e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  435 EDGSRVDRKRKHNEEAKIAKEVE--AHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQERflr 512
Cdd:PTZ00121  1454 EEAKKAEEAKKKAEEAKKADEAKkkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA--- 1530

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232352  513 EQRREHERMEKFMQKqsRRAEKQRQKEELRKEKEAAR----QKAANERATARRIAREYMELVEDECLELMELAAQSKGL 587
Cdd:PTZ00121  1531 EEAKKADEAKKAEEK--KKADELKKAEELKKAEEKKKaeeaKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
PTZ00121 PTZ00121
MAEBL; Provisional
 428-568 1.35e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  428 ERRAYHDEDGSRVDRKRKHNEEAKIAKEV--EAHERRIRKELE--KQDMMKRKREEQMRKEMERHDRERRKEEERllrer 503
Cdd:PTZ00121  1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELkkAEEENKIKAAEEakKAEEDKKKAEEAKKAEEDEKKAAEALKKEA----- 1698

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232352  504 qreqerflrEQRREHERMEKFMQKQSRRAEKQRQKEELRKEK-EAARQKAANERATARRIAREYME 568
Cdd:PTZ00121  1699 ---------EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKaEEAKKEAEEDKKKAEEAKKDEEE 1755
PTZ00121 PTZ00121
MAEBL; Provisional
 428-565 1.65e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  428 ERRAYHDEDGSRVDRKRKHNEEAKIAKEVE--AHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQR 505
Cdd:PTZ00121  1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKkkAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE 1474

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  506 EQERflREQRREHERMEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIARE 565
Cdd:PTZ00121  1475 AKKK--AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
PTZ00121 PTZ00121
MAEBL; Provisional
 435-573 2.18e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 2.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  435 EDGSRVDRKRKHNEE-------AKIAKEVEahERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQ 507
Cdd:PTZ00121  1561 EEKKKAEEAKKAEEDknmalrkAEEAKKAE--EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232352  508 ERFLREQRREHERMEKFMQKQSRRAEKQRQK--------EELRKEKEAARQK--AANERATARRIAREYMELVEDE 573
Cdd:PTZ00121  1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKaeedkkkaEEAKKAEEDEKKAaeALKKEAEEAKKAEELKKKEAEE 1714
PTZ00121 PTZ00121
MAEBL; Provisional
 421-565 2.78e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 2.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  421 ENSLLPSERRAYHDEDGSRVDRKRKHNEEAKIAKEV---EAHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEE 497
Cdd:PTZ00121  1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAlkkEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232352  498 RLLRERQREqerflREQRREHERMEKFmqkQSRRAEKQRQKEELRKEKEAARQKAANERATARRIARE 565
Cdd:PTZ00121  1738 EAEEDKKKA-----EEAKKDEEEKKKI---AHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 445-568 4.10e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.50  E-value: 4.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  445 KHNEEAKIAKEVEAHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQErfLREQR-REHERMEK 523
Cdd:pfam17380  376 RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR--LEEERaREMERVRL 453

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1002232352  524 FMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYME 568
Cdd:pfam17380  454 EEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE 498
PLN02316 PLN02316
synthase/transferase
 511-567 1.14e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 44.09  E-value: 1.14e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232352  511 LREQRREHERMEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYM 567
Cdd:PLN02316   251 LEEKRRELEKLAKEEAERERQAEEQRRREEEKAAMEADRAQAKAEVEKRREKLQNLL 307
PTZ00121 PTZ00121
MAEBL; Provisional
 435-565 1.18e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  435 EDGSRVDRKRKhNEEAKIAKEV-EAHERRIRKELEKQDMMkRKREEQMRKEMERHDRERRKEEERLLRERQREQERFLRE 513
Cdd:PTZ00121  1519 EEAKKADEAKK-AEEAKKADEAkKAEEKKKADELKKAEEL-KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232352  514 QRREHERMEKFMQKQSRRAEKQRQK-------EELRKEKEAARQKAANERATARRIARE 565
Cdd:PTZ00121  1597 VMKLYEEEKKMKAEEAKKAEEAKIKaeelkkaEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 424-589 1.24e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.57  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  424 LLPSERRAYHDEDGSRVDRKRKHNEEAK------IAKEVEAHERRIR-KELEKQDMMKRKRE-EQMRKEMERHDRERRKE 495
Cdd:pfam17380  406 ILEEERQRKIQQQKVEMEQIRAEQEEARqrevrrLEEERAREMERVRlEEQERQQQVERLRQqEEERKRKKLELEKEKRD 485

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  496 EERLLRERQREQERFLREQRR---EHERMEKFMQK-----QSRRAEKQRQK---EELRKEKEAARQKAANE---RATARR 561
Cdd:pfam17380  486 RKRAEEQRRKILEKELEERKQamiEEERKRKLLEKemeerQKAIYEEERRReaeEERRKQQEMEERRRIQEqmrKATEER 565

                          170       180
                   ....*....|....*....|....*...
gi 1002232352  562 IAREYMELVEDECLELMELAAQSKGLPS 589
Cdd:pfam17380  566 SRLEAMEREREMMRQIVESEKARAEYEA 593
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 422-579 1.61e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.42  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  422 NSLLPSERRAYHDEDGSRVDRKRKHNEEAKIAKEV-EAHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLL 500
Cdd:pfam02463  652 VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAEsELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232352  501 RERQREQERFLREQRREHERMEKFmqKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYMELVEDECLELME 579
Cdd:pfam02463  732 DKINEELKLLKQKIDEEEEEEEKS--RLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEE 808
PTZ00121 PTZ00121
MAEBL; Provisional
 435-565 2.56e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 2.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  435 EDGSRVDRKRKHNEEAKIAKEVE--AHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQReqerflr 512
Cdd:PTZ00121  1428 EEKKKADEAKKKAEEAKKADEAKkkAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD------- 1500

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1002232352  513 EQRREHErmEKFMQKQSRRAEKQRQKEELRKEKEAARQKAAnERATARRIARE 565
Cdd:PTZ00121  1501 EAKKAAE--AKKKADEAKKAEEAKKADEAKKAEEAKKADEA-KKAEEKKKADE 1550
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 430-569 2.58e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  430 RAYHDEDGSRVDRKRKHNE-----EAKIAKEVEAHERRIRKELEKQDMMKRKREEQMRKEMerhdrerrkeeerllrerq 504
Cdd:pfam17380  302 RQEKEEKAREVERRRKLEEaekarQAEMDRQAAIYAEQERMAMERERELERIRQEERKREL------------------- 362

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232352  505 reqerflrEQRREHE---RMEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYMEL 569
Cdd:pfam17380  363 --------ERIRQEEiamEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM 422
PTZ00121 PTZ00121
MAEBL; Provisional
 435-572 4.66e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 4.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  435 EDGSRVDRKRKHNEEAKIAKEVEAHERRIRKeleKQDMMKRKREEQMRK-EMERHDRERRKEEERLLRERQREQERFLRE 513
Cdd:PTZ00121  1299 EEKKKADEAKKKAEEAKKADEAKKKAEEAKK---KADAAKKKAEEAKKAaEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232352  514 QRREHERMEKFMQKQ------SRRAEKQRQKEELRKEKEAARQKA--ANERATARRIAREYMELVED 572
Cdd:PTZ00121  1376 AKKKADAAKKKAEEKkkadeaKKKAEEDKKKADELKKAAAAKKKAdeAKKKAEEKKKADEAKKKAEE 1442
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 440-565 7.31e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.67  E-value: 7.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  440 VDRKRKHNEEAKIAKEVEAhERRIRKELEKQdMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQERFLREQRREHE 519
Cdd:pfam13868  215 QERKERQKEREEAEKKARQ-RQELQQAREEQ-IELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR 292

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1002232352  520 R-MEKFMQ--KQSRRAEKQRQKEELRKEKEAARQKAANERATARRIARE 565
Cdd:pfam13868  293 ReLEKQIEerEEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
PTZ00121 PTZ00121
MAEBL; Provisional
 421-573 7.33e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 7.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  421 ENSLLPSERRAYHD----EDGSRVDRKRKHNEEAKIAKEVEAHErRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEE 496
Cdd:PTZ00121  1209 EEERKAEEARKAEDakkaEAVKKAEEAKKDAEEAKKAEEERNNE-EIRKFEEARMAHFARRQAAIKAEEARKADELKKAE 1287

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232352  497 ERLLRERQREQerflrEQRREHERMEKFMQKQSRRAEKQRQKEELRKEKEAARQKaANERATARRIAREYMELVEDE 573
Cdd:PTZ00121  1288 EKKKADEAKKA-----EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK-AEEAKKAAEAAKAEAEAAADE 1358
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
 439-572 7.59e-03

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 39.01  E-value: 7.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  439 RVDRKRKHNEEAK-IAKEVeaHERRIRKELEKQdmmKRKREEQMRKEmerhdrerrkeeeRLLrerqreqerflREQRRE 517
Cdd:pfam15236   47 RERKRQKALEHQNaIKKQL--EEKERQKKLEEE---RRRQEEQEEEE-------------RLR-----------REREEE 97

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1002232352  518 HERMEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIaREYMELVED 572
Cdd:pfam15236   98 QKQFEEERRKQKEKEEAMTRKTQALLQAMQKAQELAQRLKQEQRI-RELAEKGHD 151
PTZ00121 PTZ00121
MAEBL; Provisional
 439-573 8.97e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 8.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  439 RVDRKRKHNEEAKIAKEVEAHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEERLLRERQREQERFLREQRREh 518
Cdd:PTZ00121  1273 KAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE- 1351

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1002232352  519 ermEKFMQKQSRRAEKQRQKEELRKEKEAARQKAANERATARRIAREYMELVEDE 573
Cdd:PTZ00121  1352 ---AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 442-556 9.19e-03

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 38.90  E-value: 9.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  442 RKRKHNEEAKIAKEVEAHERRIRKELEKQDMMKRKREEQMRKEMERHDRERRKEEerllrerqreqerflREQRREHERM 521
Cdd:pfam11600    8 QSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEE---------------EKELKEKERR 72

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1002232352  522 EKFMQKQSRRAEKQRQKEELRKEKEAARQKAANER 556
Cdd:pfam11600   73 EKKEKDEKEKAEKLRLKEEKRKEKQEALEAKLEEK 107
PTZ00121 PTZ00121
MAEBL; Provisional
 428-572 9.84e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 9.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  428 ERRAYHDEDGSRVDRKRKHNEEAKIAKEV-EAHERRIRKELEKQDMMK---RKREEQMRKEMERHDRERRKEEERLLRER 503
Cdd:PTZ00121  1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAaKAEAEAAADEAEAAEEKAeaaEKKKEEAKKKADAAKKKAEEKKKADEAKK 1398

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232352  504 QREQERFLREQRREHERMEKFMQKQSRRAEKQRQKEELRKEKEAARQ-KAANERATARRIAREYMELVED 572
Cdd:PTZ00121  1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKAEEAKKKAEE 1468
 
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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