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Conserved domains on  [gi|1039798530|ref|XP_017174110|]
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BCL-6 corepressor isoform X2 [Mus musculus]

Protein Classification

BCOR and PUFD domain-containing protein( domain architecture ID 13557854)

BCOR and PUFD domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BCOR pfam15808
BCL-6 co-repressor, non-ankyrin-repeat region; BCOR is a domain family found in eukaryotes, ...
 1205-1417 1.30e-97

BCL-6 co-repressor, non-ankyrin-repeat region; BCOR is a domain family found in eukaryotes, and is approximately 220 amino acids in length. This domain lies just upstream of the ankyrin-repeat region at the C-terminus of BCL-6 co-repressor proteins. The function of this region is not known.


:

Pssm-ID: 434953  Cd Length: 219  Bit Score: 313.39  E-value: 1.30e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1205 GLHPKKQRHLLHLRERWEQQVSAAE-SKPGRQSRKEVAQAVQPEVTS---QGTNITEEKPGRKKAEAKGNRGWSEESLKS 1280
Cdd:pfam15808    1 GLRLKKQRHLQHLRELWEQQVSPAEpSKPGRQSRKEKAEAVQPEVTArdrKVKDIAEEKPLRKRSEAKSNRSWSEESLKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1281 CDNEQGLPVLSGSPPMKSLSSTNASGKKQTQPSCTPASRLPAKQQKIKESQKTDVLCTGEDEDCQAASPLQKYTDnIEKP 1360
Cdd:pfam15808   81 SDNEQGLPAFPPSPHMKSLSSANANGKKQTQPSCTPASRLSAKRQKLKESRKTDPSSPDEDEDCQAASLLQKHTD-SEKP 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1361 SGKRLCKTKHLIPQESRRSLQITGD--YYVENTDTKMTV-RRFRKRPEPSSDYDLSPPAK 1417
Cdd:pfam15808  160 KGKRQCKTKHLSLQERRRGLSLTGDsaYELENADGKVTVkRRFRKRPESSSDYDSSPVKP 219
PUFD pfam16553
BCORL-PCGF1-binding domain; PUFD is the minimal domain at the C-terminus of BCORL (BCL6 ...
 1638-1751 2.75e-70

BCORL-PCGF1-binding domain; PUFD is the minimal domain at the C-terminus of BCORL (BCL6 corepressor) that is needed for binding and giving specificity to some of the PCGF proteins, polycomb-group RING finger homologs. PUFD binds to the RAWUL (RING finger- and WD40-associated ubiquitin-like) domain of the particular PCGF PCGF1, pfam16207. Polycomb group proteins form repressive complexes (PRC) that mediate epigenetic modifications of histones. In humans there are many different PCGF homologs whose functions all vary, but the direct binding partner of PCGF1 is BCOR. BCOR has emerged as an important player in development and health.


:

Pssm-ID: 465171  Cd Length: 114  Bit Score: 230.73  E-value: 2.75e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1638 SDLFEFEFAESSLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRSNFPNLEIVTIAEAEFYRQVSTSLLFSCPKDL 1717
Cdd:pfam16553    1 SDVFEFEFSDKPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRARFPHFEVVTIAEAEFYKQVSLSQLLSPPEDL 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1039798530 1718 EAFNPESKELLDLVEFTNELQTLLGSSVEWLHPS 1751
Cdd:pfam16553   81 EAFNPDSKELVELVEFTPELQTLLGSSVEFLHPS 114
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1465-1598 4.72e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.98  E-value: 4.72e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1465 NAGETLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN 1544
Cdd:COG0666    118 KDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039798530 1545 DHLEIVRLLLSYGADPTLATYSGRT----IMKMTHSELMEKFLTDYLNDLQGRSEDDT 1598
Cdd:COG0666    197 GHLEIVKLLLEAGADVNAKDNDGKTaldlAAENGNLEIVKLLLEAGADLNAKDKDGLT 254
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 257-674 3.68e-06

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


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 51.84  E-value: 3.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530  257 IPSSLASPMRLSTPSASAaipPLVHCSDKSLPWKMGVNPG-NPVDSHSYPHIQ--NSKQPRVTS-AKAVNSGLPGDTAll 332
Cdd:pfam05109  448 LPSSTHVPTNLTAPASTG---PTVSTADVTSPTPAGTTSGaSPVTPSPSPRDNgtESKAPDMTSpTSAVTTPTPNATS-- 522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530  333 lpPSP---RPSARVHLPTQPAAETYSEFHKHYPR-ISTSPSVTLTKPYMTANSEFSTSRLSNGKYPKAldggDCAQSMPG 408
Cdd:pfam05109  523 --PTPavtTPTPNATSPTLGKTSPTSAVTTPTPNaTSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTP----NATSPTVG 596

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530  409 HTR-KTTVQDRKDGGSppllekqTVTKDVTDKPLDLSSKVvdadaSKGDHMkkmaptvlVHSRAASGLVLSGSEIpKETL 487
Cdd:pfam05109  597 ETSpQANTTNHTLGGT-------SSTPVVTSPPKNATSAV-----TTGQHN--------ITSSSTSSMSLRPSSI-SETL 655

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530  488 SPPGNGCSIYRSEIISTAPSSwvvpGPSPNEENNGKSLSLKNKALDWAIPQQRSSSCPRMGGTDAVVTNVSGSVSSSGRP 567
Cdd:pfam05109  656 SPSTSDNSTSHMPLLTSAHPT----GGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTP 731

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530  568 ASASPAPNANAnadGTKTSrssvdtTPSVIQHVGQPSSTPAK-----HGGSTSSK------GAKANPEPSFKASENGLPP 636
Cdd:pfam05109  732 PKNATSPQAPS---GQKTA------VPTVTSTGGKANSTTGGkhttgHGARTSTEpttdygGDSTTPRTRYNATTYLPPS 802

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1039798530  637 TSIFLSPNEAFRSPAIPYPRSYLPYAAPEGIALSPLSL 674
Cdd:pfam05109  803 TSSKLRPRWTFTSPPVTTAQATVPVPPTSQPRFSNLSM 840
 
Name Accession Description Interval E-value
BCOR pfam15808
BCL-6 co-repressor, non-ankyrin-repeat region; BCOR is a domain family found in eukaryotes, ...
 1205-1417 1.30e-97

BCL-6 co-repressor, non-ankyrin-repeat region; BCOR is a domain family found in eukaryotes, and is approximately 220 amino acids in length. This domain lies just upstream of the ankyrin-repeat region at the C-terminus of BCL-6 co-repressor proteins. The function of this region is not known.


Pssm-ID: 434953  Cd Length: 219  Bit Score: 313.39  E-value: 1.30e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1205 GLHPKKQRHLLHLRERWEQQVSAAE-SKPGRQSRKEVAQAVQPEVTS---QGTNITEEKPGRKKAEAKGNRGWSEESLKS 1280
Cdd:pfam15808    1 GLRLKKQRHLQHLRELWEQQVSPAEpSKPGRQSRKEKAEAVQPEVTArdrKVKDIAEEKPLRKRSEAKSNRSWSEESLKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1281 CDNEQGLPVLSGSPPMKSLSSTNASGKKQTQPSCTPASRLPAKQQKIKESQKTDVLCTGEDEDCQAASPLQKYTDnIEKP 1360
Cdd:pfam15808   81 SDNEQGLPAFPPSPHMKSLSSANANGKKQTQPSCTPASRLSAKRQKLKESRKTDPSSPDEDEDCQAASLLQKHTD-SEKP 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1361 SGKRLCKTKHLIPQESRRSLQITGD--YYVENTDTKMTV-RRFRKRPEPSSDYDLSPPAK 1417
Cdd:pfam15808  160 KGKRQCKTKHLSLQERRRGLSLTGDsaYELENADGKVTVkRRFRKRPESSSDYDSSPVKP 219
PUFD pfam16553
BCORL-PCGF1-binding domain; PUFD is the minimal domain at the C-terminus of BCORL (BCL6 ...
 1638-1751 2.75e-70

BCORL-PCGF1-binding domain; PUFD is the minimal domain at the C-terminus of BCORL (BCL6 corepressor) that is needed for binding and giving specificity to some of the PCGF proteins, polycomb-group RING finger homologs. PUFD binds to the RAWUL (RING finger- and WD40-associated ubiquitin-like) domain of the particular PCGF PCGF1, pfam16207. Polycomb group proteins form repressive complexes (PRC) that mediate epigenetic modifications of histones. In humans there are many different PCGF homologs whose functions all vary, but the direct binding partner of PCGF1 is BCOR. BCOR has emerged as an important player in development and health.


Pssm-ID: 465171  Cd Length: 114  Bit Score: 230.73  E-value: 2.75e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1638 SDLFEFEFAESSLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRSNFPNLEIVTIAEAEFYRQVSTSLLFSCPKDL 1717
Cdd:pfam16553    1 SDVFEFEFSDKPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRARFPHFEVVTIAEAEFYKQVSLSQLLSPPEDL 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1039798530 1718 EAFNPESKELLDLVEFTNELQTLLGSSVEWLHPS 1751
Cdd:pfam16553   81 EAFNPDSKELVELVEFTPELQTLLGSSVEFLHPS 114
PUFD cd14261
PCGF Ub-like fold discriminator of BCOR; The PUFD domain binds the RAWUL (RING finger and ...
 1634-1750 8.08e-67

PCGF Ub-like fold discriminator of BCOR; The PUFD domain binds the RAWUL (RING finger and WD40-associated ubiquitin-like) domain of the polycomb-group RING finger homologs PCGF1 and PCGF3. PUFD was characterized as a domain of the BCL6 corepressor BCOR. It does not appear to bind to PCGF2 and PCGF4. PCGF1 is a component of the Polycomb group (PcG) multi-protein BCOR complex, which is involved in repressing the transcription of BCL6 and CDKN1A. The BCL-6 corepressor (BCOR) is a transcriptional repressor required for germinal center formation and is possibly involved in apoptosis.


Pssm-ID: 271224  Cd Length: 117  Bit Score: 220.87  E-value: 8.08e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1634 EDTYSDLFEFEFAESSLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRSNFPNLEIVTIAEAEFYRQVSTSLLFSC 1713
Cdd:cd14261      1 DDAYSDVFEFEFSDRPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRCNFPNVEVVTIAEAEFYRQVSLSQLFSC 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1039798530 1714 PKDLEAFNPESKELLDLVEFTNELQTLLGSSVEWLHP 1750
Cdd:cd14261     81 PKDLEAFNPDSKELLDLVEFTNELQTLLGSSLEWLHP 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1465-1598 4.72e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.98  E-value: 4.72e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1465 NAGETLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN 1544
Cdd:COG0666    118 KDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039798530 1545 DHLEIVRLLLSYGADPTLATYSGRT----IMKMTHSELMEKFLTDYLNDLQGRSEDDT 1598
Cdd:COG0666    197 GHLEIVKLLLEAGADVNAKDNDGKTaldlAAENGNLEIVKLLLEAGADLNAKDKDGLT 254
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1471-1562 2.85e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 2.85e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1471 LQRAARLGYEEVVLYCLENKvCDVNHRDNAGYCALHEACARGWLNIVRHLLEYgADVNCSAQDGTrPLHDAVENDHLEIV 1550
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRT-ALHYAARSGHLEIV 77

                           90
                   ....*....|..
gi 1039798530 1551 RLLLSYGADPTL 1562
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1468-1589 1.45e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.54  E-value: 1.45e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1468 ETLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHL 1547
Cdd:PHA03100   160 KLLIDKGVDINAKNRVNYLLSYGV-PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039798530 1548 EIVRLLLSYGAD-----PTL-----ATYSGRTIMKMTHSELMEKFLTD---YLND 1589
Cdd:PHA03100   239 EIFKLLLNNGPSiktiiETLlyfkdKDLNTITKIKMLKKSIMYMFLLDpgfYKNR 293
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 257-674 3.68e-06

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 51.84  E-value: 3.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530  257 IPSSLASPMRLSTPSASAaipPLVHCSDKSLPWKMGVNPG-NPVDSHSYPHIQ--NSKQPRVTS-AKAVNSGLPGDTAll 332
Cdd:pfam05109  448 LPSSTHVPTNLTAPASTG---PTVSTADVTSPTPAGTTSGaSPVTPSPSPRDNgtESKAPDMTSpTSAVTTPTPNATS-- 522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530  333 lpPSP---RPSARVHLPTQPAAETYSEFHKHYPR-ISTSPSVTLTKPYMTANSEFSTSRLSNGKYPKAldggDCAQSMPG 408
Cdd:pfam05109  523 --PTPavtTPTPNATSPTLGKTSPTSAVTTPTPNaTSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTP----NATSPTVG 596

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530  409 HTR-KTTVQDRKDGGSppllekqTVTKDVTDKPLDLSSKVvdadaSKGDHMkkmaptvlVHSRAASGLVLSGSEIpKETL 487
Cdd:pfam05109  597 ETSpQANTTNHTLGGT-------SSTPVVTSPPKNATSAV-----TTGQHN--------ITSSSTSSMSLRPSSI-SETL 655

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530  488 SPPGNGCSIYRSEIISTAPSSwvvpGPSPNEENNGKSLSLKNKALDWAIPQQRSSSCPRMGGTDAVVTNVSGSVSSSGRP 567
Cdd:pfam05109  656 SPSTSDNSTSHMPLLTSAHPT----GGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTP 731

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530  568 ASASPAPNANAnadGTKTSrssvdtTPSVIQHVGQPSSTPAK-----HGGSTSSK------GAKANPEPSFKASENGLPP 636
Cdd:pfam05109  732 PKNATSPQAPS---GQKTA------VPTVTSTGGKANSTTGGkhttgHGARTSTEpttdygGDSTTPRTRYNATTYLPPS 802

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1039798530  637 TSIFLSPNEAFRSPAIPYPRSYLPYAAPEGIALSPLSL 674
Cdd:pfam05109  803 TSSKLRPRWTFTSPPVTTAQATVPVPPTSQPRFSNLSM 840
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1537-1562 9.32e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 9.32e-05
                            10        20
                    ....*....|....*....|....*.
gi 1039798530  1537 PLHDAVENDHLEIVRLLLSYGADPTL 1562
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1467-1573 1.85e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.16  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1467 GETLLQRAARLGYEEVVLYCLENKVCDVNHRDN----AGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGT------- 1535
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpk 130

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1039798530 1536 -------RPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKM 1573
Cdd:cd22192    131 nliyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
 
Name Accession Description Interval E-value
BCOR pfam15808
BCL-6 co-repressor, non-ankyrin-repeat region; BCOR is a domain family found in eukaryotes, ...
 1205-1417 1.30e-97

BCL-6 co-repressor, non-ankyrin-repeat region; BCOR is a domain family found in eukaryotes, and is approximately 220 amino acids in length. This domain lies just upstream of the ankyrin-repeat region at the C-terminus of BCL-6 co-repressor proteins. The function of this region is not known.


Pssm-ID: 434953  Cd Length: 219  Bit Score: 313.39  E-value: 1.30e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1205 GLHPKKQRHLLHLRERWEQQVSAAE-SKPGRQSRKEVAQAVQPEVTS---QGTNITEEKPGRKKAEAKGNRGWSEESLKS 1280
Cdd:pfam15808    1 GLRLKKQRHLQHLRELWEQQVSPAEpSKPGRQSRKEKAEAVQPEVTArdrKVKDIAEEKPLRKRSEAKSNRSWSEESLKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1281 CDNEQGLPVLSGSPPMKSLSSTNASGKKQTQPSCTPASRLPAKQQKIKESQKTDVLCTGEDEDCQAASPLQKYTDnIEKP 1360
Cdd:pfam15808   81 SDNEQGLPAFPPSPHMKSLSSANANGKKQTQPSCTPASRLSAKRQKLKESRKTDPSSPDEDEDCQAASLLQKHTD-SEKP 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1361 SGKRLCKTKHLIPQESRRSLQITGD--YYVENTDTKMTV-RRFRKRPEPSSDYDLSPPAK 1417
Cdd:pfam15808  160 KGKRQCKTKHLSLQERRRGLSLTGDsaYELENADGKVTVkRRFRKRPESSSDYDSSPVKP 219
PUFD pfam16553
BCORL-PCGF1-binding domain; PUFD is the minimal domain at the C-terminus of BCORL (BCL6 ...
 1638-1751 2.75e-70

BCORL-PCGF1-binding domain; PUFD is the minimal domain at the C-terminus of BCORL (BCL6 corepressor) that is needed for binding and giving specificity to some of the PCGF proteins, polycomb-group RING finger homologs. PUFD binds to the RAWUL (RING finger- and WD40-associated ubiquitin-like) domain of the particular PCGF PCGF1, pfam16207. Polycomb group proteins form repressive complexes (PRC) that mediate epigenetic modifications of histones. In humans there are many different PCGF homologs whose functions all vary, but the direct binding partner of PCGF1 is BCOR. BCOR has emerged as an important player in development and health.


Pssm-ID: 465171  Cd Length: 114  Bit Score: 230.73  E-value: 2.75e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1638 SDLFEFEFAESSLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRSNFPNLEIVTIAEAEFYRQVSTSLLFSCPKDL 1717
Cdd:pfam16553    1 SDVFEFEFSDKPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRARFPHFEVVTIAEAEFYKQVSLSQLLSPPEDL 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1039798530 1718 EAFNPESKELLDLVEFTNELQTLLGSSVEWLHPS 1751
Cdd:pfam16553   81 EAFNPDSKELVELVEFTPELQTLLGSSVEFLHPS 114
PUFD cd14261
PCGF Ub-like fold discriminator of BCOR; The PUFD domain binds the RAWUL (RING finger and ...
 1634-1750 8.08e-67

PCGF Ub-like fold discriminator of BCOR; The PUFD domain binds the RAWUL (RING finger and WD40-associated ubiquitin-like) domain of the polycomb-group RING finger homologs PCGF1 and PCGF3. PUFD was characterized as a domain of the BCL6 corepressor BCOR. It does not appear to bind to PCGF2 and PCGF4. PCGF1 is a component of the Polycomb group (PcG) multi-protein BCOR complex, which is involved in repressing the transcription of BCL6 and CDKN1A. The BCL-6 corepressor (BCOR) is a transcriptional repressor required for germinal center formation and is possibly involved in apoptosis.


Pssm-ID: 271224  Cd Length: 117  Bit Score: 220.87  E-value: 8.08e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1634 EDTYSDLFEFEFAESSLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRSNFPNLEIVTIAEAEFYRQVSTSLLFSC 1713
Cdd:cd14261      1 DDAYSDVFEFEFSDRPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRCNFPNVEVVTIAEAEFYRQVSLSQLFSC 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1039798530 1714 PKDLEAFNPESKELLDLVEFTNELQTLLGSSVEWLHP 1750
Cdd:cd14261     81 PKDLEAFNPDSKELLDLVEFTNELQTLLGSSLEWLHP 117
PUFD_like cd14259
PCGF Ub-like fold discriminator and related domains; The PUFD domain binds the RAWUL (RING ...
 1639-1746 3.73e-37

PCGF Ub-like fold discriminator and related domains; The PUFD domain binds the RAWUL (RING finger and WD40-associated ubiquitin-like) domain of the polycomb-group RING finger homologs PCGF1 and PCGF3. PUFD was characterized as a domain of the BCL6 corepressor BCOR. It does not appear to bind to PCGF2 and PCGF4. PCGF1 is a component of the Polycomb group (PcG) multi-protein BCOR complex, which is involved in repressing the transcription of BCL6 and CDKN1A. The BCL-6 corepressor (BCOR) is a transcriptional repressor required for germinal center formation and is possibly involved in apoptosis.


Pssm-ID: 271222  Cd Length: 106  Bit Score: 135.52  E-value: 3.73e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1639 DLFEFEFAESSLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRSNFPNLEIVTIAEAEFYRQVSTSLLFSCPKDLe 1718
Cdd:cd14259      1 DDFEFEFSDEPLPPLYNLRISPNDGPRNWHLLSDVLTRLKLKSRDFLLKQICLELTSIPIEDFLEQASCLQLLCAGEKL- 79

                           90       100
                   ....*....|....*....|....*...
gi 1039798530 1719 aFNPESKELLDLVEFTNELQTLLGSSVE 1746
Cdd:cd14259     80 -TNNVSSSKVELVEYNDSLRSLLGIEVE 106
PUFD_like_1 cd14260
PCGF Ub-like fold discriminator of BCOR-like 1; The PUFD domain binds the RAWUL (RING finger ...
 1636-1746 5.08e-36

PCGF Ub-like fold discriminator of BCOR-like 1; The PUFD domain binds the RAWUL (RING finger and WD40-associated ubiquitin-like) domain of the polycomb-group RING finger homologs PCGF1 and PCGF3. PUFD was characterized as a domain of the BCL6 corepressor BCOR. It does not appear to bind to PCGF2 and PCGF4. PCGF1 is a component of the Polycomb group (PcG) multi-protein BCOR complex, which is involved in repressing the transcription of BCL6 and CDKN1A. The BCL-6 corepressor-like protein 1 (BCoR-L1) is largely uncharacterized; it contains ankyrin repeats.


Pssm-ID: 271223  Cd Length: 115  Bit Score: 132.67  E-value: 5.08e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1636 TYSDLFEFEFAESSLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRSNFPNLEIVTIAEAEFYRQVSTSLLFSCPK 1715
Cdd:cd14260      1 TEEDDFMFEFSDKPLLPCYNLQVSVSRGPCNWFLFSDVLKRLKLSSRIFQARFPHFEIATMPKAEFYRQVLSSQLLTPAE 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1039798530 1716 DLEAFN----PESKELLDLVEFTNELQTLLGSSVE 1746
Cdd:cd14260     81 RPGGLDdrspQGSSETVELVRYEPELLRLLGSAVE 115
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1465-1598 4.72e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.98  E-value: 4.72e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1465 NAGETLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN 1544
Cdd:COG0666    118 KDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039798530 1545 DHLEIVRLLLSYGADPTLATYSGRT----IMKMTHSELMEKFLTDYLNDLQGRSEDDT 1598
Cdd:COG0666    197 GHLEIVKLLLEAGADVNAKDNDGKTaldlAAENGNLEIVKLLLEAGADLNAKDKDGLT 254
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1460-1569 2.76e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.59  E-value: 2.76e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1460 LIVNKNAGETLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLH 1539
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158

                           90       100       110
                   ....*....|....*....|....*....|
gi 1039798530 1540 DAVENDHLEIVRLLLSYGADPTLATYSGRT 1569
Cdd:COG0666    159 LAAANGNLEIVKLLLEAGADVNARDNDGET 188
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1455-1597 6.79e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.10  E-value: 6.79e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1455 PEARRLIVNKNA--------GETLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGAD 1526
Cdd:COG0666    133 LEIVKLLLEAGAdvnaqdndGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039798530 1527 VNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKMTHSELMEKFLTDYLNDLQGRSEDD 1597
Cdd:COG0666    212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1471-1562 2.85e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 2.85e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1471 LQRAARLGYEEVVLYCLENKvCDVNHRDNAGYCALHEACARGWLNIVRHLLEYgADVNCSAQDGTrPLHDAVENDHLEIV 1550
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRT-ALHYAARSGHLEIV 77

                           90
                   ....*....|..
gi 1039798530 1551 RLLLSYGADPTL 1562
Cdd:pfam12796   78 KLLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1460-1569 2.03e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.78  E-value: 2.03e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1460 LIVNKNAGETLLQRAARLGYEEVVLYCLENKVCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLH 1539
Cdd:COG0666     46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLH 125

                           90       100       110
                   ....*....|....*....|....*....|
gi 1039798530 1540 DAVENDHLEIVRLLLSYGADPTLATYSGRT 1569
Cdd:COG0666    126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1465-1571 4.43e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.91  E-value: 4.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1465 NAGETLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN 1544
Cdd:COG0666    184 NDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAA 262

                           90       100
                   ....*....|....*....|....*..
gi 1039798530 1545 DHLEIVRLLLSYGADPTLATYSGRTIM 1571
Cdd:COG0666    263 GAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1505-1571 4.35e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 4.35e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039798530 1505 LHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGAdpTLATYSGRTIM 1571
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTAL 65
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1468-1589 1.45e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.54  E-value: 1.45e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1468 ETLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHL 1547
Cdd:PHA03100   160 KLLIDKGVDINAKNRVNYLLSYGV-PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039798530 1548 EIVRLLLSYGAD-----PTL-----ATYSGRTIMKMTHSELMEKFLTD---YLND 1589
Cdd:PHA03100   239 EIFKLLLNNGPSiktiiETLlyfkdKDLNTITKIKMLKKSIMYMFLLDpgfYKNR 293
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1462-1528 1.72e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 1.72e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039798530 1462 VNKNAGETLLQRAARLGYEEVVLYCLENkvCDVNHRDNaGYCALHEACARGWLNIVRHLLEYGADVN 1528
Cdd:pfam12796   25 LQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADIN 88
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1401-1556 9.43e-10

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.38  E-value: 9.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1401 RKRPEPSSDYDLSppAKQEPkpFDRLQQLLPATQATQLPRSNSPQETTQSRPMPPearrlIVNKNAGETLLQRAArlGYE 1480
Cdd:PTZ00322    26 KRRAKPISFERMA--AIQEE--IARIDTHLEALEATENKDATPDHNLTTEEVIDP-----VVAHMLTVELCQLAA--SGD 94

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039798530 1481 EVVLYCLENKVCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSY 1556
Cdd:PTZ00322    95 AVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1455-1569 2.36e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.60  E-value: 2.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1455 PEARRLIVNKNA--------GETLLQRAA--RLGYEEVVLYcLENKVCDVNHRDNAGYCALHEA--CARGWLNIVRHLLE 1522
Cdd:PHA03100    86 KEIVKLLLEYGAnvnapdnnGITPLLYAIskKSNSYSIVEY-LLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLID 164

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039798530 1523 YGADVNcsAQD------------------GTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT 1569
Cdd:PHA03100   165 KGVDIN--AKNrvnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1456-1569 2.98e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.35  E-value: 2.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1456 EARRLIVNKNAGETLLQRAARLGYEEVVLYCLENKVCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGT 1535
Cdd:COG0666      9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1039798530 1536 RPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT 1569
Cdd:COG0666     89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGET 122
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1517-1573 5.56e-09

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 5.56e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039798530 1517 VRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKM 1573
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
Ank_4 pfam13637
Ankyrin repeats (many copies);
1504-1554 2.56e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 2.56e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039798530 1504 ALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLL 1554
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1493-1569 5.14e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 5.14e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039798530 1493 DVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT 1569
Cdd:PHA02874   116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1493-1570 1.80e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.80  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1493 DVNHRDNAGYCALH-------EACARgwlnIVRHLLEYGADVNCSAQDGTRPLHDAVENDH-LEIVRLLLSYGADPTLAT 1564
Cdd:PHA03095    39 DVNFRGEYGKTPLHlylhyssEKVKD----IVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKD 114


                   ....*.
gi 1039798530 1565 YSGRTI 1570
Cdd:PHA03095   115 KVGRTP 120
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1467-1640 3.78e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.26  E-value: 3.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1467 GETLLQRAARLGYEEVVLYCLENkVCDVNHRDNAGYCALHEACA-------------------------------RGWLN 1515
Cdd:PLN03192   558 GRTPLHIAASKGYEDCVLVLLKH-ACNVHIRDANGNTALWNAISakhhkifrilyhfasisdphaagdllctaakRNDLT 636

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1516 IVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADptlatysgrtimkMTHSELMEKFLTDYLNDLQGRSE 1595
Cdd:PLN03192   637 AMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD-------------VDKANTDDDFSPTELRELLQKRE 703

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1039798530 1596 ddtsgawefYGSSVCEPDDESGYDVLANPPGPEDPDEEEDTYSDL 1640
Cdd:PLN03192   704 ---------LGHSITIVDSVPADEPDLGRDGGSRPGRLQGTSSDN 739
Ank_5 pfam13857
Ankyrin repeats (many copies);
1520-1573 5.69e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 5.69e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039798530 1520 LLEYG-ADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKM 1573
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 257-674 3.68e-06

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 51.84  E-value: 3.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530  257 IPSSLASPMRLSTPSASAaipPLVHCSDKSLPWKMGVNPG-NPVDSHSYPHIQ--NSKQPRVTS-AKAVNSGLPGDTAll 332
Cdd:pfam05109  448 LPSSTHVPTNLTAPASTG---PTVSTADVTSPTPAGTTSGaSPVTPSPSPRDNgtESKAPDMTSpTSAVTTPTPNATS-- 522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530  333 lpPSP---RPSARVHLPTQPAAETYSEFHKHYPR-ISTSPSVTLTKPYMTANSEFSTSRLSNGKYPKAldggDCAQSMPG 408
Cdd:pfam05109  523 --PTPavtTPTPNATSPTLGKTSPTSAVTTPTPNaTSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTP----NATSPTVG 596

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530  409 HTR-KTTVQDRKDGGSppllekqTVTKDVTDKPLDLSSKVvdadaSKGDHMkkmaptvlVHSRAASGLVLSGSEIpKETL 487
Cdd:pfam05109  597 ETSpQANTTNHTLGGT-------SSTPVVTSPPKNATSAV-----TTGQHN--------ITSSSTSSMSLRPSSI-SETL 655

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530  488 SPPGNGCSIYRSEIISTAPSSwvvpGPSPNEENNGKSLSLKNKALDWAIPQQRSSSCPRMGGTDAVVTNVSGSVSSSGRP 567
Cdd:pfam05109  656 SPSTSDNSTSHMPLLTSAHPT----GGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTP 731

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530  568 ASASPAPNANAnadGTKTSrssvdtTPSVIQHVGQPSSTPAK-----HGGSTSSK------GAKANPEPSFKASENGLPP 636
Cdd:pfam05109  732 PKNATSPQAPS---GQKTA------VPTVTSTGGKANSTTGGkhttgHGARTSTEpttdygGDSTTPRTRYNATTYLPPS 802

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1039798530  637 TSIFLSPNEAFRSPAIPYPRSYLPYAAPEGIALSPLSL 674
Cdd:pfam05109  803 TSSKLRPRWTFTSPPVTTAQATVPVPPTSQPRFSNLSM 840
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1479-1573 7.64e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 7.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1479 YEEVVLYCLENKvCDVNHRDNAGYCALH-----EACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN--DHLEIVR 1551
Cdd:PHA03100    47 NIDVVKILLDNG-ADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVE 125

                           90       100
                   ....*....|....*....|..
gi 1039798530 1552 LLLSYGADPTLATYSGRTIMKM 1573
Cdd:PHA03100   126 YLLDNGANVNIKNSDGENLLHL 147
Ank_4 pfam13637
Ankyrin repeats (many copies);
1469-1521 1.08e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 1.08e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039798530 1469 TLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLL 1521
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
1487-1539 1.23e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 1.23e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039798530 1487 LENKVCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLH 1539
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1439-1559 3.54e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 3.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1439 PRSNSPQETTQSRPMPPEARRLI-VN-KN-AGETLLQRAARLGYEEVVLYCLENKVCDVNHRDNAGYCALHEACARG-WL 1514
Cdd:PHA02876   276 PLHHASQAPSLSRLVPKLLERGAdVNaKNiKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNK 355

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1039798530 1515 NIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGAD 1559
Cdd:PHA02876   356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1516-1560 3.62e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 3.62e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1039798530 1516 IVRHLLEYGADVNCSAQD-GTRPLHDAVENDHLEIVRLLLSYGADP 1560
Cdd:PHA02878   149 ITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANV 194
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1515-1583 3.98e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.12  E-value: 3.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1515 NIVRHLLEYGADVNCSAQDGTRPLH-----DAVENDHLEIVRLLLSYGADPTLATYSGRTIM------KMTHSELMEKFL 1583
Cdd:PHA03100    49 DVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLlyaiskKSNSYSIVEYLL 128
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1493-1570 4.70e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.10  E-value: 4.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1493 DVNHRDNAGYCALHeACARG-WLN--IVRHLLEYGADVNCSAQDGTRPLHDAVENDH--LEIVRLLLSYGADPTLATYSG 1567
Cdd:PHA03095   109 DVNAKDKVGRTPLH-VYLSGfNINpkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRF 187


                   ...
gi 1039798530 1568 RTI 1570
Cdd:PHA03095   188 RSL 190
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1447-1569 8.29e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 8.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1447 TTQSRPMPPEARRLI-----VN--KNAGETLLQRAARLGYEEV--VLYCLENKVCDVNHRDNAGYCALH-EACARGWLNI 1516
Cdd:PHA03095    20 LNASNVTVEEVRRLLaagadVNfrGEYGKTPLHLYLHYSSEKVkdIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDV 99

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039798530 1517 VRHLLEYGADVNCSAQDGTRPLHD--AVENDHLEIVRLLLSYGADPTLATYSGRT 1569
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMT 154
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1537-1562 9.32e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 9.32e-05
                            10        20
                    ....*....|....*....|....*.
gi 1039798530  1537 PLHDAVENDHLEIVRLLLSYGADPTL 1562
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1501-1529 1.66e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.32  E-value: 1.66e-04
                           10        20
                   ....*....|....*....|....*....
gi 1039798530 1501 GYCALHEACARGWLNIVRHLLEYGADVNC 1529
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1467-1573 1.85e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.16  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1467 GETLLQRAARLGYEEVVLYCLENKVCDVNHRDN----AGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGT------- 1535
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpk 130

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1039798530 1536 -------RPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKM 1573
Cdd:cd22192    131 nliyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1460-1559 1.86e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.16  E-value: 1.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1460 LIVNKNAGETLLQRAARLGYEEVVLYCLENKVCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGAD-VN----CSAQDG 1534
Cdd:cd22192     10 LLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNepmtSDLYQG 89

                           90       100
                   ....*....|....*....|....*
gi 1039798530 1535 TRPLHDAVENDHLEIVRLLLSYGAD 1559
Cdd:cd22192     90 ETALHIAVVNQNLNLVRELIARGAD 114
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1487-1578 1.98e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1487 LENKVCdVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDG-TRPLHDAVENDHLEIVRLLLSYGADPTLATy 1565
Cdd:PHA02875   155 IDHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF- 232

                           90
                   ....*....|...
gi 1039798530 1566 sgrTIMKMTHSEL 1578
Cdd:PHA02875   233 ---MIEGEECTIL 242
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1505-1564 2.52e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 2.52e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039798530 1505 LHEACARGWLNIVRHLLEYGADVN-CSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLAT 1564
Cdd:PHA02875    72 LHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPN 132
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1471-1573 2.65e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.64  E-value: 2.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1471 LQRAARLGYEEVVLYCLENKvCDVNHRDNAGYCALHEACARGW-LNIVRHLLEYGADVNC-SAQDGTRPLHDAVENDhlE 1548
Cdd:PHA02878   205 LHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCKdYDILKLLLEHGVDVNAkSYILGLTALHSSIKSE--R 281

                           90       100
                   ....*....|....*....|....*
gi 1039798530 1549 IVRLLLSYGADPTLATYSGRTIMKM 1573
Cdd:PHA02878   282 KLKLLLEYGADINSLNSYKLTPLSS 306
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1533-1564 3.42e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 3.42e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1039798530 1533 DGTRPLHDAVE-NDHLEIVRLLLSYGADPTLAT 1564
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1492-1569 3.63e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 3.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1492 CDVNHRDNAGYCALHEA-----CARGwlnIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYS 1566
Cdd:PHA03095   213 CDPAATDMLGNTPLHSMatgssCKRS---LVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD 289


                   ...
gi 1039798530 1567 GRT 1569
Cdd:PHA03095   290 GNT 292
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1468-1557 3.72e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 3.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1468 ETLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHL 1547
Cdd:PHA02874   125 KTFLHYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDY 203

                           90
                   ....*....|
gi 1039798530 1548 EIVRLLLSYG 1557
Cdd:PHA02874   204 ACIKLLIDHG 213
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1493-1555 4.65e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 4.65e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039798530 1493 DVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLS 1555
Cdd:PHA03095   249 SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1514-1572 4.89e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 4.89e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039798530 1514 LNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMK 1572
Cdd:PHA02876   158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLE 216
Ank_4 pfam13637
Ankyrin repeats (many copies);
1534-1583 5.28e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 5.28e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039798530 1534 GTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIM----KMTHSELMEKFL 1583
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALhfaaSNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1501-1529 7.22e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 7.22e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039798530 1501 GYCALHEACAR-GWLNIVRHLLEYGADVNC 1529
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNA 31
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1493-1569 8.80e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 8.80e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039798530 1493 DVNHRD-NAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT 1569
Cdd:PHA02878   159 DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1461-1589 1.37e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.33  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1461 IVNKNAGETLLQRAARLGYEEVVLYCLeNKVCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHD 1540
Cdd:PHA02878   162 MKDRHKGNTALHYATENKDQRLTELLL-SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHI 240

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039798530 1541 AVEN-DHLEIVRLLLSYGADPTLATY-SGRTIMKMT-HSELMEKFLTDYLND 1589
Cdd:PHA02878   241 SVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSiKSERKLKLLLEYGAD 292
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 1501-1560 1.69e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.33  E-value: 1.69e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039798530 1501 GYCALHEACARGWLNIVRHLLEYGADVNCSAQD-------------GTRPLHDAVENDHLEIVRLLLSYGADP 1560
Cdd:cd21882     73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQP 145
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1493-1554 5.99e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 5.99e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039798530 1493 DVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLL 1554
Cdd:PHA02876   170 DVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 1481-1569 6.41e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 41.44  E-value: 6.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039798530 1481 EVVLYCLENKVcDVNHRDNAGYCALHEACARGWLN--IVRHLLEYGADVNCSAQDGTRPLH-------------DAVEND 1545
Cdd:PHA02716   298 SVVYSFLQPGV-KLHYKDSAGRTCLHQYILRHNIStdIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvnildPETDND 376

                           90       100
                   ....*....|....*....|....*
gi 1039798530 1546 -HLEIVRLLLSYGADPTLATYSGRT 1569
Cdd:PHA02716   377 iRLDVIQCLISLGADITAVNCLGYT 401
 
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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