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Conserved domains on  [gi|1980307245|gb|KAG2496717|]
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hypothetical protein HYH03_005130 [Edaphochlamys debaryana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00018 PTZ00018
histone H3; Provisional
 1-135 9.92e-97

histone H3; Provisional


:

Pssm-ID: 185400 [Multi-domain]  Cd Length: 136  Bit Score: 304.91  E-value: 9.92e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245    1 MARTKQTARKSTGGKAPRKQLATKAARKT-PATGGVKKPHRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFK 79
Cdd:PTZ00018     1 MARTKQTARKSTGGKAPRKQLASKAARKSaPVTGGIKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1980307245   80 TDLRFQSQAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA 135
Cdd:PTZ00018    81 TDLRFQSSAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERS 136
Pumilio super family cl46378
Pumilio-family RNA binding domain; Puf repeats (also labelled PUM-HD or Pumilio homology ...
 666-986 3.17e-63

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.


The actual alignment was detected with superfamily member cd07920:

Pssm-ID: 480718 [Multi-domain]  Cd Length: 322  Bit Score: 218.23  E-value: 3.17e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  666 LSCDQQGSRVVQRLLCSAHGEQVGRCLDELMPCLVEVACHPYGNYVVQQLLVVGGSRHKLRMGGALAGRIPELSFDPFGC 745
Cdd:cd07920     15 FAKDQHGSRFLQQKLEEATPEEKELIFDEILPHVVELMVDPFGNYVIQKLFEHGTEEQRLQLLEKILGHVVRLSLDMYGC 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  746 RVVQKLLEVIPEQQAAAAVGELDGCVMRCVRDKCAHHVLRAALHHVPHHRQPFLLDALQAALPALARHPYGCRLVQSLLQ 825
Cdd:cd07920     95 RVIQKLLESISEEQISLLVKELRGHVVELVKDQNGNHVIQKCIEKFPPEDLQFIIDAFKGNCVALSTHPYGCRVIQRCLE 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  826 TVSEPERWRVISfDLLQDATQLGGHEYGNYVMQTLAQVAAPAVRTALAASLAAQGVRLACCRHGSPVLEAVLKYGSDDDR 905
Cdd:cd07920    175 HCSEEQREPLLE-EILEHALELVQDQFGNYVVQHVLELGDPDDTSRIIEKLLGNIVQLSCHKFASNVVEKCLKHASKEER 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  906 ETLLTALLGPPetdhaplGGADPLgaggsggggvmgagvcraLRLACDPFGNYVLQRCFQVCGPAHQARLAACLLPAIPE 985
Cdd:cd07920    254 ELIIDEILASG-------NETSAL------------------DTLMKDQYGNYVIQTALDVAKEEQRELLVEAIRPHLPS 308


                   .
gi 1980307245  986 L 986
Cdd:cd07920    309 L 309
 
Name Accession Description Interval E-value
PTZ00018 PTZ00018
histone H3; Provisional
 1-135 9.92e-97

histone H3; Provisional


Pssm-ID: 185400 [Multi-domain]  Cd Length: 136  Bit Score: 304.91  E-value: 9.92e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245    1 MARTKQTARKSTGGKAPRKQLATKAARKT-PATGGVKKPHRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFK 79
Cdd:PTZ00018     1 MARTKQTARKSTGGKAPRKQLASKAARKSaPVTGGIKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1980307245   80 TDLRFQSQAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA 135
Cdd:PTZ00018    81 TDLRFQSSAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERS 136
HFD_H3 cd22911
histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component ...
 39-132 7.50e-67

histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component of the nucleosome, which wraps and compacts DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication, and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called the histone code, and nucleosome remodeling. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.


Pssm-ID: 467036  Cd Length: 95  Bit Score: 219.72  E-value: 7.50e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245   39 HRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKT-DLRFQSQAVLALQEAAEAYLVGLFEDTNLCAIHAKRV 117
Cdd:cd22911      1 RRYRPGTVALREIRRYQKSTELLIPKLPFQRLVREIAQDFKTkDLRFQSSALLALQEAAEAYLVGLFEDSNLCAIHAKRV 80

                           90
                   ....*....|....*
gi 1980307245  118 TIMPKDIQLARRIRG 132
Cdd:cd22911     81 TLMPKDMQLARRIRG 95
H3 smart00428
Histone H3;
33-135 1.09e-65

Histone H3;


Pssm-ID: 128705 [Multi-domain]  Cd Length: 105  Bit Score: 216.93  E-value: 1.09e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245    33 GGVKKPHRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKT--DLRFQSQAVLALQEAAEAYLVGLFEDTNLC 110
Cdd:smart00428    1 GGKTKHRRYRPGQVALREIRKYQKSTDLLIRKAPFQRLVREIAQKFTTgvDLRFQSSAIMALQEAAEAYLVGLFEDTNLL 80

                            90       100
                    ....*....|....*....|....*
gi 1980307245   111 AIHAKRVTIMPKDIQLARRIRGERA 135
Cdd:smart00428   81 AIHAKRVTIMPKDIQLARRIRGERL 105
Pumilio cd07920
Pumilio-family RNA binding domain; Puf repeats (also labelled PUM-HD or Pumilio homology ...
 666-986 3.17e-63

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: 218.23  E-value: 3.17e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  666 LSCDQQGSRVVQRLLCSAHGEQVGRCLDELMPCLVEVACHPYGNYVVQQLLVVGGSRHKLRMGGALAGRIPELSFDPFGC 745
Cdd:cd07920     15 FAKDQHGSRFLQQKLEEATPEEKELIFDEILPHVVELMVDPFGNYVIQKLFEHGTEEQRLQLLEKILGHVVRLSLDMYGC 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  746 RVVQKLLEVIPEQQAAAAVGELDGCVMRCVRDKCAHHVLRAALHHVPHHRQPFLLDALQAALPALARHPYGCRLVQSLLQ 825
Cdd:cd07920     95 RVIQKLLESISEEQISLLVKELRGHVVELVKDQNGNHVIQKCIEKFPPEDLQFIIDAFKGNCVALSTHPYGCRVIQRCLE 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  826 TVSEPERWRVISfDLLQDATQLGGHEYGNYVMQTLAQVAAPAVRTALAASLAAQGVRLACCRHGSPVLEAVLKYGSDDDR 905
Cdd:cd07920    175 HCSEEQREPLLE-EILEHALELVQDQFGNYVVQHVLELGDPDDTSRIIEKLLGNIVQLSCHKFASNVVEKCLKHASKEER 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  906 ETLLTALLGPPetdhaplGGADPLgaggsggggvmgagvcraLRLACDPFGNYVLQRCFQVCGPAHQARLAACLLPAIPE 985
Cdd:cd07920    254 ELIIDEILASG-------NETSAL------------------DTLMKDQYGNYVIQTALDVAKEEQRELLVEAIRPHLPS 308


                   .
gi 1980307245  986 L 986
Cdd:cd07920    309 L 309
Histone pfam00125
Core histone H2A/H2B/H3/H4;
1-131 1.14e-59

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 200.35  E-value: 1.14e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245    1 MARTKQTARKSTGGKAPRKQLATKAARKTPatggvKKPHRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKT 80
Cdd:pfam00125    1 MARNKNKANPRRGGTAPEKKISQKSSSSSK-----KKTRRYRPGTVALKEIRKYQSSTDLLIYKLPFARVVREVVQSTKT 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1980307245   81 DLRFQSQAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIR 131
Cdd:pfam00125   76 DLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
COG5099 COG5099
RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal ...
 665-962 6.39e-25

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


Pssm-ID: 227430 [Multi-domain]  Cd Length: 777  Bit Score: 112.15  E-value: 6.39e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  665 GLSC-DQQGSRVVQRLLCSAHGEQVGRCLDELMPCLVEVACHPYGNYVVQQLLVVGGSRHKLRMGGALAGRIPELSFDPF 743
Cdd:COG5099    444 IVSCkDQHGSRFLQKLLDSNSSPEIEVIFNEILDQLVELSSDYFGNYLIQKLFEYGSEIQKSIMLSKSSKHLVSLSVHKY 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  744 GCRVVQKLLEVIPE-QQAAAAVGELDGCVMRCVRDKCAHHVLRAALHHVPHHRQPFLLDALQAALPALARHPYGCRLVQS 822
Cdd:COG5099    524 GTRVLQKAIDIVSTdIQISLLVEELRPYCLQLIKDQNGNHVIQKCIEKFNKEKNQFIFDSINENLYDLSTHRYGSRVVQR 603

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  823 LLQTVSEpERWRVISFDLLQDATQLGGHEYGNYVMQTLAQVAAPAVRTA-LAASLAAQGVRLACCRHGSPVLEAVLKYGS 901
Cdd:COG5099    604 CLENCNS-EDKENLVEEIISNSKYLSQDQYGNYVVQHILDNGAEPNKERiIIKLLSKRVVELSTHKFASNVVEKCIKYAS 682

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1980307245  902 DDD-RETLLTALLGPPETDHAPLggadplgaggsggggvmgagvcraLRLACDPFGNYVLQR 962
Cdd:COG5099    683 DSFkRSRILNELTNRGIEKPGFL------------------------MLILDDQYANYVIQY 720
PUF pfam00806
Pumilio-family RNA binding repeat; Puf repeats (aka PUM-HD, Pumilio homology domain) are ...
 948-975 8.62e-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: 43.44  E-value: 8.62e-06
                           10        20
                   ....*....|....*....|....*...
gi 1980307245  948 LRLACDPFGNYVLQRCFQVCGPAHQARL 975
Cdd:pfam00806    3 VELATDQYGCRVIQKCLEHATEEQREQI 30
Pumilio smart00025
Pumilio-like repeats; Pumilio-like repeats that bind RNA.
 733-759 3.11e-05

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


Pssm-ID: 214475 [Multi-domain]  Cd Length: 36  Bit Score: 42.04  E-value: 3.11e-05
                            10        20
                    ....*....|....*....|....*..
gi 1980307245   733 GRIPELSFDPFGCRVVQKLLEVIPEQQ 759
Cdd:smart00025    4 GHLLELSKDQYGNRVVQKLLEHASESQ 30
HHT1 COG2036
Archaeal histone H3/H4 [Chromatin structure and dynamics];
66-130 2.07e-03

Archaeal histone H3/H4 [Chromatin structure and dynamics];


Pssm-ID: 441639  Cd Length: 67  Bit Score: 37.89  E-value: 2.07e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1980307245   66 PFQRLVREIaqdfkTDLRFQSQAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRI 130
Cdd:COG2036      6 PVDRIIKKA-----GAERVSEDAVEALAEILEEYAEEIAKEAVELAKHAGRKTVKAEDIELAAKL 65
 
Name Accession Description Interval E-value
PTZ00018 PTZ00018
histone H3; Provisional
 1-135 9.92e-97

histone H3; Provisional


Pssm-ID: 185400 [Multi-domain]  Cd Length: 136  Bit Score: 304.91  E-value: 9.92e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245    1 MARTKQTARKSTGGKAPRKQLATKAARKT-PATGGVKKPHRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFK 79
Cdd:PTZ00018     1 MARTKQTARKSTGGKAPRKQLASKAARKSaPVTGGIKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1980307245   80 TDLRFQSQAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA 135
Cdd:PTZ00018    81 TDLRFQSSAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERS 136
PLN00121 PLN00121
histone H3; Provisional
 1-135 1.37e-89

histone H3; Provisional


Pssm-ID: 177733 [Multi-domain]  Cd Length: 136  Bit Score: 285.41  E-value: 1.37e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245    1 MARTKQTARKSTGGKAPRKQLATKAARKT-PATGGVKKPHRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFK 79
Cdd:PLN00121     1 MARTKQTARKSTGGKAPRKQLATKAARKSaPATGGVKKPHRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1980307245   80 TDLRFQSQAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA 135
Cdd:PLN00121    81 TDLRFQSSAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA 136
HFD_H3 cd22911
histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component ...
 39-132 7.50e-67

histone-fold domain found in histone H3 and similar proteins; Histone H3 is a core component of the nucleosome, which wraps and compacts DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication, and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called the histone code, and nucleosome remodeling. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.


Pssm-ID: 467036  Cd Length: 95  Bit Score: 219.72  E-value: 7.50e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245   39 HRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKT-DLRFQSQAVLALQEAAEAYLVGLFEDTNLCAIHAKRV 117
Cdd:cd22911      1 RRYRPGTVALREIRRYQKSTELLIPKLPFQRLVREIAQDFKTkDLRFQSSALLALQEAAEAYLVGLFEDSNLCAIHAKRV 80

                           90
                   ....*....|....*
gi 1980307245  118 TIMPKDIQLARRIRG 132
Cdd:cd22911     81 TLMPKDMQLARRIRG 95
H3 smart00428
Histone H3;
33-135 1.09e-65

Histone H3;


Pssm-ID: 128705 [Multi-domain]  Cd Length: 105  Bit Score: 216.93  E-value: 1.09e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245    33 GGVKKPHRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKT--DLRFQSQAVLALQEAAEAYLVGLFEDTNLC 110
Cdd:smart00428    1 GGKTKHRRYRPGQVALREIRKYQKSTDLLIRKAPFQRLVREIAQKFTTgvDLRFQSSAIMALQEAAEAYLVGLFEDTNLL 80

                            90       100
                    ....*....|....*....|....*
gi 1980307245   111 AIHAKRVTIMPKDIQLARRIRGERA 135
Cdd:smart00428   81 AIHAKRVTIMPKDIQLARRIRGERL 105
Pumilio cd07920
Pumilio-family RNA binding domain; Puf repeats (also labelled PUM-HD or Pumilio homology ...
 666-986 3.17e-63

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: 218.23  E-value: 3.17e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  666 LSCDQQGSRVVQRLLCSAHGEQVGRCLDELMPCLVEVACHPYGNYVVQQLLVVGGSRHKLRMGGALAGRIPELSFDPFGC 745
Cdd:cd07920     15 FAKDQHGSRFLQQKLEEATPEEKELIFDEILPHVVELMVDPFGNYVIQKLFEHGTEEQRLQLLEKILGHVVRLSLDMYGC 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  746 RVVQKLLEVIPEQQAAAAVGELDGCVMRCVRDKCAHHVLRAALHHVPHHRQPFLLDALQAALPALARHPYGCRLVQSLLQ 825
Cdd:cd07920     95 RVIQKLLESISEEQISLLVKELRGHVVELVKDQNGNHVIQKCIEKFPPEDLQFIIDAFKGNCVALSTHPYGCRVIQRCLE 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  826 TVSEPERWRVISfDLLQDATQLGGHEYGNYVMQTLAQVAAPAVRTALAASLAAQGVRLACCRHGSPVLEAVLKYGSDDDR 905
Cdd:cd07920    175 HCSEEQREPLLE-EILEHALELVQDQFGNYVVQHVLELGDPDDTSRIIEKLLGNIVQLSCHKFASNVVEKCLKHASKEER 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  906 ETLLTALLGPPetdhaplGGADPLgaggsggggvmgagvcraLRLACDPFGNYVLQRCFQVCGPAHQARLAACLLPAIPE 985
Cdd:cd07920    254 ELIIDEILASG-------NETSAL------------------DTLMKDQYGNYVIQTALDVAKEEQRELLVEAIRPHLPS 308


                   .
gi 1980307245  986 L 986
Cdd:cd07920    309 L 309
Histone pfam00125
Core histone H2A/H2B/H3/H4;
1-131 1.14e-59

Core histone H2A/H2B/H3/H4;


Pssm-ID: 459682 [Multi-domain]  Cd Length: 126  Bit Score: 200.35  E-value: 1.14e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245    1 MARTKQTARKSTGGKAPRKQLATKAARKTPatggvKKPHRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKT 80
Cdd:pfam00125    1 MARNKNKANPRRGGTAPEKKISQKSSSSSK-----KKTRRYRPGTVALKEIRKYQSSTDLLIYKLPFARVVREVVQSTKT 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1980307245   81 DLRFQSQAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIR 131
Cdd:pfam00125   76 DLRISADAVVALQEAVEDFLVELFEEANLLAIHAKRVTLTPKDIQLARRLR 126
PLN00161 PLN00161
histone H3; Provisional
 1-138 2.65e-54

histone H3; Provisional


Pssm-ID: 215082 [Multi-domain]  Cd Length: 135  Bit Score: 185.59  E-value: 2.65e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245    1 MARTKQtARKSTGGKAPRKQLATKAARKTPatggvKKPHRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKT 80
Cdd:PLN00161     1 MARRLQ-GKRFRKGKKPQKEASGVTRQELD-----KKPHRYRPGTVALREIRKYQKSTELLIRKLPFARLVREISNEMLR 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1980307245   81 D-LRFQSQAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERAGSS 138
Cdd:PLN00161    75 EpFRWTAEALLALQEATEDFLVHLFEDCNLCAIHAKRVTIMPKDMQLARRIRGPIYGIS 133
PLN00160 PLN00160
histone H3; Provisional
 42-133 1.32e-41

histone H3; Provisional


Pssm-ID: 165727  Cd Length: 97  Bit Score: 147.89  E-value: 1.32e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245   42 RPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDF-KTDLRFQSQAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIM 120
Cdd:PLN00160     2 RPGEKALKEIKMYQKSTDLLIRRLPFARLVREIQMEMsREAYRWQGSAILALQEAAEAHLVGLFEDSNLCAIHGKRVTIM 81

                           90
                   ....*....|...
gi 1980307245  121 PKDIQLARRIRGE 133
Cdd:PLN00160    82 PKDMQLARRIRGQ 94
COG5099 COG5099
RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal ...
 665-962 6.39e-25

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


Pssm-ID: 227430 [Multi-domain]  Cd Length: 777  Bit Score: 112.15  E-value: 6.39e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  665 GLSC-DQQGSRVVQRLLCSAHGEQVGRCLDELMPCLVEVACHPYGNYVVQQLLVVGGSRHKLRMGGALAGRIPELSFDPF 743
Cdd:COG5099    444 IVSCkDQHGSRFLQKLLDSNSSPEIEVIFNEILDQLVELSSDYFGNYLIQKLFEYGSEIQKSIMLSKSSKHLVSLSVHKY 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  744 GCRVVQKLLEVIPE-QQAAAAVGELDGCVMRCVRDKCAHHVLRAALHHVPHHRQPFLLDALQAALPALARHPYGCRLVQS 822
Cdd:COG5099    524 GTRVLQKAIDIVSTdIQISLLVEELRPYCLQLIKDQNGNHVIQKCIEKFNKEKNQFIFDSINENLYDLSTHRYGSRVVQR 603

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  823 LLQTVSEpERWRVISFDLLQDATQLGGHEYGNYVMQTLAQVAAPAVRTA-LAASLAAQGVRLACCRHGSPVLEAVLKYGS 901
Cdd:COG5099    604 CLENCNS-EDKENLVEEIISNSKYLSQDQYGNYVVQHILDNGAEPNKERiIIKLLSKRVVELSTHKFASNVVEKCIKYAS 682

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1980307245  902 DDD-RETLLTALLGPPETDHAPLggadplgaggsggggvmgagvcraLRLACDPFGNYVLQR 962
Cdd:COG5099    683 DSFkRSRILNELTNRGIEKPGFL------------------------MLILDDQYANYVIQY 720
Pumilio cd07920
Pumilio-family RNA binding domain; Puf repeats (also labelled PUM-HD or Pumilio homology ...
 659-896 5.16e-22

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: 98.43  E-value: 5.16e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  659 LYGRLTGLSCDQQGSRVVQRLLCSAHGEQVGRCLDELMPCLVEVACHPYGNYVVQQLLVVGGSRHKLRMGGALAGRIPEL 738
Cdd:cd07920    152 FKGNCVALSTHPYGCRVIQRCLEHCSEEQREPLLEEILEHALELVQDQFGNYVVQHVLELGDPDDTSRIIEKLLGNIVQL 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1980307245  739 SFDPFGCRVVQKLLevipeqqaaaavgeldgcvmrcvrdKCAHHVLRAalhhvphhrqpflldalqaalpalarhpygcR 818
Cdd:cd07920    232 SCHKFASNVVEKCL-------------------------KHASKEERE-------------------------------L 255

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1980307245  819 LVQSLLqtVSEPERWRVIsfDLLQDatqlgghEYGNYVMQTLAQVAAPAVRTALAASLAAQGVRLACCRHGSPVLEAV 896
Cdd:cd07920    256 IIDEIL--ASGNETSALD--TLMKD-------QYGNYVIQTALDVAKEEQRELLVEAIRPHLPSLRKSPYGKHILAKL 322
PUF pfam00806
Pumilio-family RNA binding repeat; Puf repeats (aka PUM-HD, Pumilio homology domain) are ...
 948-975 8.62e-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: 43.44  E-value: 8.62e-06
                           10        20
                   ....*....|....*....|....*...
gi 1980307245  948 LRLACDPFGNYVLQRCFQVCGPAHQARL 975
Cdd:pfam00806    3 VELATDQYGCRVIQKCLEHATEEQREQI 30
PUF pfam00806
Pumilio-family RNA binding repeat; Puf repeats (aka PUM-HD, Pumilio homology domain) are ...
 734-767 1.25e-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: 43.06  E-value: 1.25e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1980307245  734 RIPELSFDPFGCRVVQKLLEVIPEQQAAAAVGEL 767
Cdd:pfam00806    1 HVVELATDQYGCRVIQKCLEHATEEQREQILDEI 34
Pumilio smart00025
Pumilio-like repeats; Pumilio-like repeats that bind RNA.
 733-759 3.11e-05

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


Pssm-ID: 214475 [Multi-domain]  Cd Length: 36  Bit Score: 42.04  E-value: 3.11e-05
                            10        20
                    ....*....|....*....|....*..
gi 1980307245   733 GRIPELSFDPFGCRVVQKLLEVIPEQQ 759
Cdd:smart00025    4 GHLLELSKDQYGNRVVQKLLEHASESQ 30
HFD_archaea_histone-like cd22909
histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription ...
 64-129 8.80e-05

histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription regulators and similar proteins; The family includes many archaeal histone-fold proteins and histone-like transcription regulators, which may bind and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. They can increase the resistance of DNA to thermal denaturation.


Pssm-ID: 467034  Cd Length: 64  Bit Score: 41.76  E-value: 8.80e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1980307245   64 KLPFQRLVREIaqdfkTDLRFQSQAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARR 129
Cdd:cd22909      4 KAPVKRIIKKA-----GAERVSEDAAEELAKLLEEIAEEIAEEAVKLAKHAGRKTVKAEDIELAVK 64
PUF pfam00806
Pumilio-family RNA binding repeat; Puf repeats (aka PUM-HD, Pumilio homology domain) are ...
 666-696 1.07e-04

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: 40.36  E-value: 1.07e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1980307245  666 LSCDQQGSRVVQRLLCSAHGEQVGRCLDELM 696
Cdd:pfam00806    5 LATDQYGCRVIQKCLEHATEEQREQILDEIL 35
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 67-127 1.24e-04

histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally conserved interaction motif involved in heterodimerization of the core histones and their assembly into the nucleosome octamer. Histone fold heterodimers play crucial roles in gene regulation. The minimal HFD consists of three alpha helices connected by two short, unstructured loops. The HFD is found in core histones, TATA box-binding protein-associated factors (TAFs), and many other transcription factors. HFD plays a role in the nucleosomal core particle by conserving histone interactions; these contain more than one HFD. The structure of the nucleosome core particle has two modes that have the largest interaction surfaces, and these are the H3-H4 and H2A-H2B heterodimer interactions. Several TAFs interact via histone-fold (HF) motifs. Five HF-containing TAF pairs have been described in transcription factor II D (TFIID): TAF6-TAF9, TAF4-TAF12, TAF11-TAF13, TAF8-TAF10 and TAF3-TAF10.


Pssm-ID: 467021  Cd Length: 63  Bit Score: 41.05  E-value: 1.24e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1980307245   67 FQRLVREIAQDFKTDlRFQSQAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLA 127
Cdd:cd00076      2 LRSAVARILKSAGFD-SVSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELA 61
Pumilio cd07920
Pumilio-family RNA binding domain; Puf repeats (also labelled PUM-HD or Pumilio homology ...
 945-987 4.01e-04

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: 44.12  E-value: 4.01e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1980307245  945 CRALRLACDPFGNYVLQRCFQVCGPAHQARLAACLLPAIPELS 987
Cdd:cd07920     46 PHVVELMVDPFGNYVIQKLFEHGTEEQRLQLLEKILGHVVRLS 88
Pumilio smart00025
Pumilio-like repeats; Pumilio-like repeats that bind RNA.
 948-975 5.53e-04

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


Pssm-ID: 214475 [Multi-domain]  Cd Length: 36  Bit Score: 38.57  E-value: 5.53e-04
                            10        20
                    ....*....|....*....|....*...
gi 1980307245   948 LRLACDPFGNYVLQRCFQVCGPAHQARL 975
Cdd:smart00025    7 LELSKDQYGNRVVQKLLEHASESQREQI 34
HHT1 COG2036
Archaeal histone H3/H4 [Chromatin structure and dynamics];
66-130 2.07e-03

Archaeal histone H3/H4 [Chromatin structure and dynamics];


Pssm-ID: 441639  Cd Length: 67  Bit Score: 37.89  E-value: 2.07e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1980307245   66 PFQRLVREIaqdfkTDLRFQSQAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRI 130
Cdd:COG2036      6 PVDRIIKKA-----GAERVSEDAVEALAEILEEYAEEIAKEAVELAKHAGRKTVKAEDIELAAKL 65
Pumilio smart00025
Pumilio-like repeats; Pumilio-like repeats that bind RNA.
 697-727 2.59e-03

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


Pssm-ID: 214475 [Multi-domain]  Cd Length: 36  Bit Score: 36.64  E-value: 2.59e-03
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1980307245   697 PCLVEVACHPYGNYVVQQLLVVGGSRHKLRM 727
Cdd:smart00025    4 GHLLELSKDQYGNRVVQKLLEHASESQREQI 34
PUF pfam00806
Pumilio-family RNA binding repeat; Puf repeats (aka PUM-HD, Pumilio homology domain) are ...
 700-727 2.78e-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: 36.51  E-value: 2.78e-03
                           10        20
                   ....*....|....*....|....*...
gi 1980307245  700 VEVACHPYGNYVVQQLLVVGGSRHKLRM 727
Cdd:pfam00806    3 VELATDQYGCRVIQKCLEHATEEQREQI 30
HFD_CENP-T cd22920
histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also ...
 69-131 6.89e-03

histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also called interphase centromere complex protein 22 (ICEN22), is a component of the CENPA-NAC (nucleosome-associated) complex, which plays a central role in the assembly of kinetochore proteins, mitotic progression, and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENP-T is also part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Moreover, CENP-T is a component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENP-T has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. It is required for normal chromosome organization and normal progress through mitosis.


Pssm-ID: 467045  Cd Length: 94  Bit Score: 37.15  E-value: 6.89e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1980307245   69 RLVREIAQdFKTDLRFQSQAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKD-IQLARRIR 131
Cdd:cd22920      6 SLVKKLFK-HFLKRRVSKEALEALEEISEEFFEQLSDDLEAYADHAGRKTINEKDvELLMKRQR 68
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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