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Conserved domains on  [gi|1958807461|ref|XP_038955692|]
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BCL-6 corepressor isoform X1 [Rattus norvegicus]

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, ...
 1203-1415 1.28e-95

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: 307.61  E-value: 1.28e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1203 GLHPKKQRHLLHLRERWEQQVSAAE-SKPGRQSRKEVTQAVQPEVTS---QGNNITEERPGRKKAEAKGNRGWSEESLKS 1278
Cdd:pfam15808    1 GLRLKKQRHLQHLRELWEQQVSPAEpSKPGRQSRKEKAEAVQPEVTArdrKVKDIAEEKPLRKRSEAKSNRSWSEESLKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1279 CDNEQGLPVFSASPPMKSLSSTNASGKKQTQPSCTPASRPPAKQQKIKESQKTDVLCTEEDEDCRAASPLQKYTDnIEKP 1358
Cdd:pfam15808   81 SDNEQGLPAFPPSPHMKSLSSANANGKKQTQPSCTPASRLSAKRQKLKESRKTDPSSPDEDEDCQAASLLQKHTD-SEKP 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1359 SGKRLCKTKHLIPQDSRRSVQITGE--YYVENTDTKMTV-RRFRKRPEPSTDYDLSPPAK 1415
Cdd:pfam15808  160 KGKRQCKTKHLSLQERRRGLSLTGDsaYELENADGKVTVkRRFRKRPESSSDYDSSPVKP 219
PUFD pfam16553
BCORL-PCGF1-binding domain; PUFD is the minimal domain at the C-terminus of BCORL (BCL6 ...
 1636-1749 4.33e-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: 230.35  E-value: 4.33e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1636 SDMFEFEFAESSLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNMEIVSIAEAEFYRQVSTSLLFSCPKDL 1715
Cdd:pfam16553    1 SDVFEFEFSDKPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRARFPHFEVVTIAEAEFYKQVSLSQLLSPPEDL 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958807461 1716 EAFNPEGKELLDLVEFTNELQTLLGSSVEWLHPS 1749
Cdd:pfam16553   81 EAFNPDSKELVELVEFTPELQTLLGSSVEFLHPS 114
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1463-1596 5.38e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 5.38e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1463 NAGETLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN 1542
Cdd:COG0666    118 KDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807461 1543 DHLEIVRLLLSYGADPTLATYSGRT----IMKMTHSELMEKFLTDYLNDLQGRSEEDT 1596
Cdd:COG0666    197 GHLEIVKLLLEAGADVNAKDNDGKTaldlAAENGNLEIVKLLLEAGADLNAKDKDGLT 254
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 257-672 9.60e-09

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: 60.32  E-value: 9.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461  257 IPSSLASPMRLSTPSASAaipPLVHCSDKSLPWKMGVNPG-NPVDSHTYPHIQ--NSKQPRVTSAKAVNSGLPGDAALLL 333
Cdd:pfam05109  448 LPSSTHVPTNLTAPASTG---PTVSTADVTSPTPAGTTSGaSPVTPSPSPRDNgtESKAPDMTSPTSAVTTPTPNATSPT 524

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461  334 PPSPRPSTRVHLPTQPAAESYSEFHKHYPR-ISTSPSVTLTKPYMTASSEFPTARLSSGKYPKAldgGDCAPSMSGHSRK 412
Cdd:pfam05109  525 PAVTTPTPNATSPTLGKTSPTSAVTTPTPNaTSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTP---NATSPTVGETSPQ 601

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461  413 TTVQDRKDGGSppllekqTVTKDVTDKPLDLSSKVV----DVDTSKTDHMKkMAPTVLVHSRATSGLVLSGSEIPKETSP 488
Cdd:pfam05109  602 ANTTNHTLGGT-------SSTPVVTSPPKNATSAVTtgqhNITSSSTSSMS-LRPSSISETLSPSTSDNSTSHMPLLTSA 673

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461  489 -PGNGCSIYRSEIISTAPSSWVVPGPSPNEENNGKSLSLKNkaldwaipqqrSSSCPRMGGTDAVITNVSGSVSSSGRPA 567
Cdd:pfam05109  674 hPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGN-----------SSTSTKPGEVNVTKGTPPKNATSPQAPS 742

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461  568 SASPA-PNANADGTKTSrsSVDTTPSVIQHVGQPPSTPakhsgsTSSKGAKASNPEPSFKASENGLPPTSIFLSPNEAFR 646
Cdd:pfam05109  743 GQKTAvPTVTSTGGKAN--STTGGKHTTGHGARTSTEP------TTDYGGDSTTPRTRYNATTYLPPSTSSKLRPRWTFT 814

                          410       420
                   ....*....|....*....|....*.
gi 1958807461  647 SPPIPYPRSYLPYPAPEGIALSPLSL 672
Cdd:pfam05109  815 SPPVTTAQATVPVPPTSQPRFSNLSM 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, ...
 1203-1415 1.28e-95

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: 307.61  E-value: 1.28e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1203 GLHPKKQRHLLHLRERWEQQVSAAE-SKPGRQSRKEVTQAVQPEVTS---QGNNITEERPGRKKAEAKGNRGWSEESLKS 1278
Cdd:pfam15808    1 GLRLKKQRHLQHLRELWEQQVSPAEpSKPGRQSRKEKAEAVQPEVTArdrKVKDIAEEKPLRKRSEAKSNRSWSEESLKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1279 CDNEQGLPVFSASPPMKSLSSTNASGKKQTQPSCTPASRPPAKQQKIKESQKTDVLCTEEDEDCRAASPLQKYTDnIEKP 1358
Cdd:pfam15808   81 SDNEQGLPAFPPSPHMKSLSSANANGKKQTQPSCTPASRLSAKRQKLKESRKTDPSSPDEDEDCQAASLLQKHTD-SEKP 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1359 SGKRLCKTKHLIPQDSRRSVQITGE--YYVENTDTKMTV-RRFRKRPEPSTDYDLSPPAK 1415
Cdd:pfam15808  160 KGKRQCKTKHLSLQERRRGLSLTGDsaYELENADGKVTVkRRFRKRPESSSDYDSSPVKP 219
PUFD pfam16553
BCORL-PCGF1-binding domain; PUFD is the minimal domain at the C-terminus of BCORL (BCL6 ...
 1636-1749 4.33e-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: 230.35  E-value: 4.33e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1636 SDMFEFEFAESSLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNMEIVSIAEAEFYRQVSTSLLFSCPKDL 1715
Cdd:pfam16553    1 SDVFEFEFSDKPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRARFPHFEVVTIAEAEFYKQVSLSQLLSPPEDL 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958807461 1716 EAFNPEGKELLDLVEFTNELQTLLGSSVEWLHPS 1749
Cdd:pfam16553   81 EAFNPDSKELVELVEFTPELQTLLGSSVEFLHPS 114
PUFD cd14261
PCGF Ub-like fold discriminator of BCOR; The PUFD domain binds the RAWUL (RING finger and ...
 1632-1748 1.79e-66

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: 220.10  E-value: 1.79e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1632 EDAYSDMFEFEFAESSLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNMEIVSIAEAEFYRQVSTSLLFSC 1711
Cdd:cd14261      1 DDAYSDVFEFEFSDRPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRCNFPNVEVVTIAEAEFYRQVSLSQLFSC 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1958807461 1712 PKDLEAFNPEGKELLDLVEFTNELQTLLGSSVEWLHP 1748
Cdd:cd14261     81 PKDLEAFNPDSKELLDLVEFTNELQTLLGSSLEWLHP 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1463-1596 5.38e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 5.38e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1463 NAGETLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN 1542
Cdd:COG0666    118 KDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807461 1543 DHLEIVRLLLSYGADPTLATYSGRT----IMKMTHSELMEKFLTDYLNDLQGRSEEDT 1596
Cdd:COG0666    197 GHLEIVKLLLEAGADVNAKDNDGKTaldlAAENGNLEIVKLLLEAGADLNAKDKDGLT 254
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1469-1560 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 1958807461 1469 LQRAARLGYEEVVLYCLENKvCDVNHRDNAGYCALHEACARGWLNIVRHLLEYgADVNCSAQDGTrPLHDAVENDHLEIV 1548
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRT-ALHYAARSGHLEIV 77

                           90
                   ....*....|..
gi 1958807461 1549 RLLLSYGADPTL 1560
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1466-1587 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 1958807461 1466 ETLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHL 1545
Cdd:PHA03100   160 KLLIDKGVDINAKNRVNYLLSYGV-PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807461 1546 EIVRLLLSYGAD-----PTL-----ATYSGRTIMKMTHSELMEKFLTD---YLND 1587
Cdd:PHA03100   239 EIFKLLLNNGPSiktiiETLlyfkdKDLNTITKIKMLKKSIMYMFLLDpgfYKNR 293
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 257-672 9.60e-09

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: 60.32  E-value: 9.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461  257 IPSSLASPMRLSTPSASAaipPLVHCSDKSLPWKMGVNPG-NPVDSHTYPHIQ--NSKQPRVTSAKAVNSGLPGDAALLL 333
Cdd:pfam05109  448 LPSSTHVPTNLTAPASTG---PTVSTADVTSPTPAGTTSGaSPVTPSPSPRDNgtESKAPDMTSPTSAVTTPTPNATSPT 524

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461  334 PPSPRPSTRVHLPTQPAAESYSEFHKHYPR-ISTSPSVTLTKPYMTASSEFPTARLSSGKYPKAldgGDCAPSMSGHSRK 412
Cdd:pfam05109  525 PAVTTPTPNATSPTLGKTSPTSAVTTPTPNaTSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTP---NATSPTVGETSPQ 601

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461  413 TTVQDRKDGGSppllekqTVTKDVTDKPLDLSSKVV----DVDTSKTDHMKkMAPTVLVHSRATSGLVLSGSEIPKETSP 488
Cdd:pfam05109  602 ANTTNHTLGGT-------SSTPVVTSPPKNATSAVTtgqhNITSSSTSSMS-LRPSSISETLSPSTSDNSTSHMPLLTSA 673

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461  489 -PGNGCSIYRSEIISTAPSSWVVPGPSPNEENNGKSLSLKNkaldwaipqqrSSSCPRMGGTDAVITNVSGSVSSSGRPA 567
Cdd:pfam05109  674 hPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGN-----------SSTSTKPGEVNVTKGTPPKNATSPQAPS 742

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461  568 SASPA-PNANADGTKTSrsSVDTTPSVIQHVGQPPSTPakhsgsTSSKGAKASNPEPSFKASENGLPPTSIFLSPNEAFR 646
Cdd:pfam05109  743 GQKTAvPTVTSTGGKAN--STTGGKHTTGHGARTSTEP------TTDYGGDSTTPRTRYNATTYLPPSTSSKLRPRWTFT 814

                          410       420
                   ....*....|....*....|....*.
gi 1958807461  647 SPPIPYPRSYLPYPAPEGIALSPLSL 672
Cdd:pfam05109  815 SPPVTTAQATVPVPPTSQPRFSNLSM 840
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1535-1560 9.31e-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: 9.31e-05
                            10        20
                    ....*....|....*....|....*.
gi 1958807461  1535 PLHDAVENDHLEIVRLLLSYGADPTL 1560
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1465-1571 1.84e-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: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1465 GETLLQRAARLGYEEVVLYCLENKVCDVNHRDN----AGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGT------- 1533
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpk 130

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1958807461 1534 -------RPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKM 1571
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, ...
 1203-1415 1.28e-95

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: 307.61  E-value: 1.28e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1203 GLHPKKQRHLLHLRERWEQQVSAAE-SKPGRQSRKEVTQAVQPEVTS---QGNNITEERPGRKKAEAKGNRGWSEESLKS 1278
Cdd:pfam15808    1 GLRLKKQRHLQHLRELWEQQVSPAEpSKPGRQSRKEKAEAVQPEVTArdrKVKDIAEEKPLRKRSEAKSNRSWSEESLKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1279 CDNEQGLPVFSASPPMKSLSSTNASGKKQTQPSCTPASRPPAKQQKIKESQKTDVLCTEEDEDCRAASPLQKYTDnIEKP 1358
Cdd:pfam15808   81 SDNEQGLPAFPPSPHMKSLSSANANGKKQTQPSCTPASRLSAKRQKLKESRKTDPSSPDEDEDCQAASLLQKHTD-SEKP 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1359 SGKRLCKTKHLIPQDSRRSVQITGE--YYVENTDTKMTV-RRFRKRPEPSTDYDLSPPAK 1415
Cdd:pfam15808  160 KGKRQCKTKHLSLQERRRGLSLTGDsaYELENADGKVTVkRRFRKRPESSSDYDSSPVKP 219
PUFD pfam16553
BCORL-PCGF1-binding domain; PUFD is the minimal domain at the C-terminus of BCORL (BCL6 ...
 1636-1749 4.33e-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: 230.35  E-value: 4.33e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1636 SDMFEFEFAESSLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNMEIVSIAEAEFYRQVSTSLLFSCPKDL 1715
Cdd:pfam16553    1 SDVFEFEFSDKPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRARFPHFEVVTIAEAEFYKQVSLSQLLSPPEDL 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958807461 1716 EAFNPEGKELLDLVEFTNELQTLLGSSVEWLHPS 1749
Cdd:pfam16553   81 EAFNPDSKELVELVEFTPELQTLLGSSVEFLHPS 114
PUFD cd14261
PCGF Ub-like fold discriminator of BCOR; The PUFD domain binds the RAWUL (RING finger and ...
 1632-1748 1.79e-66

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: 220.10  E-value: 1.79e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1632 EDAYSDMFEFEFAESSLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNMEIVSIAEAEFYRQVSTSLLFSC 1711
Cdd:cd14261      1 DDAYSDVFEFEFSDRPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRCNFPNVEVVTIAEAEFYRQVSLSQLFSC 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1958807461 1712 PKDLEAFNPEGKELLDLVEFTNELQTLLGSSVEWLHP 1748
Cdd:cd14261     81 PKDLEAFNPDSKELLDLVEFTNELQTLLGSSLEWLHP 117
PUFD_like cd14259
PCGF Ub-like fold discriminator and related domains; The PUFD domain binds the RAWUL (RING ...
 1637-1744 9.26e-36

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: 131.67  E-value: 9.26e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1637 DMFEFEFAESSLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNMEIVSIAEAEFYRQVSTSLLFSCPKDLe 1716
Cdd:cd14259      1 DDFEFEFSDEPLPPLYNLRISPNDGPRNWHLLSDVLTRLKLKSRDFLLKQICLELTSIPIEDFLEQASCLQLLCAGEKL- 79

                           90       100
                   ....*....|....*....|....*...
gi 1958807461 1717 aFNPEGKELLDLVEFTNELQTLLGSSVE 1744
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 ...
 1636-1744 6.76e-35

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: 129.58  E-value: 6.76e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1636 SDMFEFEFAESSLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNMEIVSIAEAEFYRQVSTSLLFSCPKDL 1715
Cdd:cd14260      3 EDDFMFEFSDKPLLPCYNLQVSVSRGPCNWFLFSDVLKRLKLSSRIFQARFPHFEIATMPKAEFYRQVLSSQLLTPAERP 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958807461 1716 EAFN----PEGKELLDLVEFTNELQTLLGSSVE 1744
Cdd:cd14260     83 GGLDdrspQGSSETVELVRYEPELLRLLGSAVE 115
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1463-1596 5.38e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 5.38e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1463 NAGETLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN 1542
Cdd:COG0666    118 KDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807461 1543 DHLEIVRLLLSYGADPTLATYSGRT----IMKMTHSELMEKFLTDYLNDLQGRSEEDT 1596
Cdd:COG0666    197 GHLEIVKLLLEAGADVNAKDNDGKTaldlAAENGNLEIVKLLLEAGADLNAKDKDGLT 254
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1458-1567 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 1958807461 1458 LIVNKNAGETLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLH 1537
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958807461 1538 DAVENDHLEIVRLLLSYGADPTLATYSGRT 1567
Cdd:COG0666    159 LAAANGNLEIVKLLLEAGADVNARDNDGET 188
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1469-1560 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 1958807461 1469 LQRAARLGYEEVVLYCLENKvCDVNHRDNAGYCALHEACARGWLNIVRHLLEYgADVNCSAQDGTrPLHDAVENDHLEIV 1548
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRT-ALHYAARSGHLEIV 77

                           90
                   ....*....|..
gi 1958807461 1549 RLLLSYGADPTL 1560
Cdd:pfam12796   78 KLLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1458-1567 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 1958807461 1458 LIVNKNAGETLLQRAARLGYEEVVLYCLENKVCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLH 1537
Cdd:COG0666     46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLH 125

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958807461 1538 DAVENDHLEIVRLLLSYGADPTLATYSGRT 1567
Cdd:COG0666    126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1463-1569 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 1958807461 1463 NAGETLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN 1542
Cdd:COG0666    184 NDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAA 262

                           90       100
                   ....*....|....*....|....*..
gi 1958807461 1543 DHLEIVRLLLSYGADPTLATYSGRTIM 1569
Cdd:COG0666    263 GAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1503-1569 4.34e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 4.34e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807461 1503 LHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGAdpTLATYSGRTIM 1569
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTAL 65
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1466-1587 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 1958807461 1466 ETLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHL 1545
Cdd:PHA03100   160 KLLIDKGVDINAKNRVNYLLSYGV-PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807461 1546 EIVRLLLSYGAD-----PTL-----ATYSGRTIMKMTHSELMEKFLTD---YLND 1587
Cdd:PHA03100   239 EIFKLLLNNGPSiktiiETLlyfkdKDLNTITKIKMLKKSIMYMFLLDpgfYKNR 293
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1460-1526 1.71e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 1.71e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807461 1460 VNKNAGETLLQRAARLGYEEVVLYCLENkvCDVNHRDNaGYCALHEACARGWLNIVRHLLEYGADVN 1526
Cdd:pfam12796   25 LQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADIN 88
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1491-1554 1.37e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 1.37e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807461 1491 DVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSY 1554
Cdd:PTZ00322   107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1453-1567 2.35e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.60  E-value: 2.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1453 PEARRLIVNKNA--------GETLLQRAA--RLGYEEVVLYcLENKVCDVNHRDNAGYCALHEA--CARGWLNIVRHLLE 1520
Cdd:PHA03100    86 KEIVKLLLEYGAnvnapdnnGITPLLYAIskKSNSYSIVEY-LLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLID 164

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807461 1521 YGADVNcsAQD------------------GTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT 1567
Cdd:PHA03100   165 KGVDIN--AKNrvnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1454-1567 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 1958807461 1454 EARRLIVNKNAGETLLQRAARLGYEEVVLYCLENKVCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGT 1533
Cdd:COG0666      9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958807461 1534 RPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT 1567
Cdd:COG0666     89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGET 122
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1515-1571 5.60e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 5.60e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807461 1515 VRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKM 1571
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 257-672 9.60e-09

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: 60.32  E-value: 9.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461  257 IPSSLASPMRLSTPSASAaipPLVHCSDKSLPWKMGVNPG-NPVDSHTYPHIQ--NSKQPRVTSAKAVNSGLPGDAALLL 333
Cdd:pfam05109  448 LPSSTHVPTNLTAPASTG---PTVSTADVTSPTPAGTTSGaSPVTPSPSPRDNgtESKAPDMTSPTSAVTTPTPNATSPT 524

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461  334 PPSPRPSTRVHLPTQPAAESYSEFHKHYPR-ISTSPSVTLTKPYMTASSEFPTARLSSGKYPKAldgGDCAPSMSGHSRK 412
Cdd:pfam05109  525 PAVTTPTPNATSPTLGKTSPTSAVTTPTPNaTSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTP---NATSPTVGETSPQ 601

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461  413 TTVQDRKDGGSppllekqTVTKDVTDKPLDLSSKVV----DVDTSKTDHMKkMAPTVLVHSRATSGLVLSGSEIPKETSP 488
Cdd:pfam05109  602 ANTTNHTLGGT-------SSTPVVTSPPKNATSAVTtgqhNITSSSTSSMS-LRPSSISETLSPSTSDNSTSHMPLLTSA 673

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461  489 -PGNGCSIYRSEIISTAPSSWVVPGPSPNEENNGKSLSLKNkaldwaipqqrSSSCPRMGGTDAVITNVSGSVSSSGRPA 567
Cdd:pfam05109  674 hPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGN-----------SSTSTKPGEVNVTKGTPPKNATSPQAPS 742

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461  568 SASPA-PNANADGTKTSrsSVDTTPSVIQHVGQPPSTPakhsgsTSSKGAKASNPEPSFKASENGLPPTSIFLSPNEAFR 646
Cdd:pfam05109  743 GQKTAvPTVTSTGGKAN--STTGGKHTTGHGARTSTEP------TTDYGGDSTTPRTRYNATTYLPPSTSSKLRPRWTFT 814

                          410       420
                   ....*....|....*....|....*.
gi 1958807461  647 SPPIPYPRSYLPYPAPEGIALSPLSL 672
Cdd:pfam05109  815 SPPVTTAQATVPVPPTSQPRFSNLSM 840
Ank_4 pfam13637
Ankyrin repeats (many copies);
1502-1552 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 1958807461 1502 ALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLL 1552
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1491-1567 5.13e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 5.13e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807461 1491 DVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT 1567
Cdd:PHA02874   116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1491-1568 1.79e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.80  E-value: 1.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1491 DVNHRDNAGYCALH-------EACARgwlnIVRHLLEYGADVNCSAQDGTRPLHDAVENDH-LEIVRLLLSYGADPTLAT 1562
Cdd:PHA03095    39 DVNFRGEYGKTPLHlylhyssEKVKD----IVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKD 114


                   ....*.
gi 1958807461 1563 YSGRTI 1568
Cdd:PHA03095   115 KVGRTP 120
Ank_5 pfam13857
Ankyrin repeats (many copies);
1518-1571 5.68e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 5.68e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807461 1518 LLEYG-ADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKM 1571
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1465-1578 9.36e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 9.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1465 GETLLQRAARLGYEEVVLYCLENkVCDVNHRDNAGYCALHEACA-------------------------------RGWLN 1513
Cdd:PLN03192   558 GRTPLHIAASKGYEDCVLVLLKH-ACNVHIRDANGNTALWNAISakhhkifrilyhfasisdphaagdllctaakRNDLT 636

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807461 1514 IVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATysgrTIMKMTHSELME 1578
Cdd:PLN03192   637 AMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN----TDDDFSPTELRE 697
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1477-1571 7.63e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 7.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1477 YEEVVLYCLENKvCDVNHRDNAGYCALH-----EACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN--DHLEIVR 1549
Cdd:PHA03100    47 NIDVVKILLDNG-ADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVE 125

                           90       100
                   ....*....|....*....|..
gi 1958807461 1550 LLLSYGADPTLATYSGRTIMKM 1571
Cdd:PHA03100   126 YLLDNGANVNIKNSDGENLLHL 147
Ank_4 pfam13637
Ankyrin repeats (many copies);
1467-1519 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 1958807461 1467 TLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLL 1519
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
1485-1537 1.22e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 1.22e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958807461 1485 LENKVCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLH 1537
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1437-1557 3.53e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 3.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1437 PRSNSPQETTQSRPMPPEARRLI-VN-KN-AGETLLQRAARLGYEEVVLYCLENKVCDVNHRDNAGYCALHEACARG-WL 1512
Cdd:PHA02876   276 PLHHASQAPSLSRLVPKLLERGAdVNaKNiKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNK 355

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1958807461 1513 NIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGAD 1557
Cdd:PHA02876   356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1514-1558 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 1958807461 1514 IVRHLLEYGADVNCSAQD-GTRPLHDAVENDHLEIVRLLLSYGADP 1558
Cdd:PHA02878   149 ITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANV 194
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1513-1581 3.97e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.12  E-value: 3.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1513 NIVRHLLEYGADVNCSAQDGTRPLH-----DAVENDHLEIVRLLLSYGADPTLATYSGRTIM------KMTHSELMEKFL 1581
Cdd:PHA03100    49 DVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLlyaiskKSNSYSIVEYLL 128
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1491-1568 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 1958807461 1491 DVNHRDNAGYCALHeACARG-WLN--IVRHLLEYGADVNCSAQDGTRPLHDAVENDH--LEIVRLLLSYGADPTLATYSG 1565
Cdd:PHA03095   109 DVNAKDKVGRTPLH-VYLSGfNINpkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRF 187


                   ...
gi 1958807461 1566 RTI 1568
Cdd:PHA03095   188 RSL 190
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1445-1567 8.28e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 8.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1445 TTQSRPMPPEARRLI-----VN--KNAGETLLQRAARLGYEEV--VLYCLENKVCDVNHRDNAGYCALH-EACARGWLNI 1514
Cdd:PHA03095    20 LNASNVTVEEVRRLLaagadVNfrGEYGKTPLHLYLHYSSEKVkdIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDV 99

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807461 1515 VRHLLEYGADVNCSAQDGTRPLHD--AVENDHLEIVRLLLSYGADPTLATYSGRT 1567
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMT 154
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1535-1560 9.31e-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: 9.31e-05
                            10        20
                    ....*....|....*....|....*.
gi 1958807461  1535 PLHDAVENDHLEIVRLLLSYGADPTL 1560
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1499-1527 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 1958807461 1499 GYCALHEACARGWLNIVRHLLEYGADVNC 1527
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1465-1571 1.84e-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: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1465 GETLLQRAARLGYEEVVLYCLENKVCDVNHRDN----AGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGT------- 1533
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpk 130

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1958807461 1534 -------RPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKM 1571
Cdd:cd22192    131 nliyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1458-1557 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 1958807461 1458 LIVNKNAGETLLQRAARLGYEEVVLYCLENKVCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGAD-VN----CSAQDG 1532
Cdd:cd22192     10 LLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNepmtSDLYQG 89

                           90       100
                   ....*....|....*....|....*
gi 1958807461 1533 TRPLHDAVENDHLEIVRLLLSYGAD 1557
Cdd:cd22192     90 ETALHIAVVNQNLNLVRELIARGAD 114
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1485-1576 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 1958807461 1485 LENKVCdVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDG-TRPLHDAVENDHLEIVRLLLSYGADPTLATy 1563
Cdd:PHA02875   155 IDHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF- 232

                           90
                   ....*....|...
gi 1958807461 1564 sgrTIMKMTHSEL 1576
Cdd:PHA02875   233 ---MIEGEECTIL 242
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1503-1562 2.51e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 2.51e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958807461 1503 LHEACARGWLNIVRHLLEYGADVN-CSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLAT 1562
Cdd:PHA02875    72 LHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPN 132
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1469-1571 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 1958807461 1469 LQRAARLGYEEVVLYCLENKvCDVNHRDNAGYCALHEACARGW-LNIVRHLLEYGADVNC-SAQDGTRPLHDAVENDhlE 1546
Cdd:PHA02878   205 LHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCKdYDILKLLLEHGVDVNAkSYILGLTALHSSIKSE--R 281

                           90       100
                   ....*....|....*....|....*
gi 1958807461 1547 IVRLLLSYGADPTLATYSGRTIMKM 1571
Cdd:PHA02878   282 KLKLLLEYGADINSLNSYKLTPLSS 306
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1531-1562 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 1958807461 1531 DGTRPLHDAVE-NDHLEIVRLLLSYGADPTLAT 1562
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1490-1567 3.62e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 3.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1490 CDVNHRDNAGYCALHEA-----CARGwlnIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYS 1564
Cdd:PHA03095   213 CDPAATDMLGNTPLHSMatgssCKRS---LVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD 289


                   ...
gi 1958807461 1565 GRT 1567
Cdd:PHA03095   290 GNT 292
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1466-1555 3.71e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1466 ETLLQRAARLGYEEVVLYCLENKVcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHL 1545
Cdd:PHA02874   125 KTFLHYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDY 203

                           90
                   ....*....|
gi 1958807461 1546 EIVRLLLSYG 1555
Cdd:PHA02874   204 ACIKLLIDHG 213
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1491-1553 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 1958807461 1491 DVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLS 1553
Cdd:PHA03095   249 SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1512-1570 4.88e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 4.88e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807461 1512 LNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMK 1570
Cdd:PHA02876   158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLE 216
Ank_4 pfam13637
Ankyrin repeats (many copies);
1532-1581 5.27e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 5.27e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958807461 1532 GTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIM----KMTHSELMEKFL 1581
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALhfaaSNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1499-1527 7.21e-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: 7.21e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958807461 1499 GYCALHEACAR-GWLNIVRHLLEYGADVNC 1527
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNA 31
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1491-1567 8.79e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 8.79e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807461 1491 DVNHRD-NAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT 1567
Cdd:PHA02878   159 DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1459-1596 1.33e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.33  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1459 IVNKNAGETLLQRAARLGYEEVVLYCLeNKVCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHD 1538
Cdd:PHA02878   162 MKDRHKGNTALHYATENKDQRLTELLL-SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHI 240

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807461 1539 AVEN-DHLEIVRLLLSYGADPTLATY-SGRTIMKMT-HSELMEKFLTDYLNDLQG-RSEEDT 1596
Cdd:PHA02878   241 SVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSiKSERKLKLLLEYGADINSlNSYKLT 302
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 1499-1558 1.68e-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: 1.68e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807461 1499 GYCALHEACARGWLNIVRHLLEYGADVNCSAQD-------------GTRPLHDAVENDHLEIVRLLLSYGADP 1558
Cdd:cd21882     73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQP 145
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1491-1552 5.98e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 5.98e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807461 1491 DVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLL 1552
Cdd:PHA02876   170 DVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 1479-1567 6.40e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 41.44  E-value: 6.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807461 1479 EVVLYCLENKVcDVNHRDNAGYCALHEACARGWLN--IVRHLLEYGADVNCSAQDGTRPLH-------------DAVEND 1543
Cdd:PHA02716   298 SVVYSFLQPGV-KLHYKDSAGRTCLHQYILRHNIStdIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvnildPETDND 376

                           90       100
                   ....*....|....*....|....*
gi 1958807461 1544 -HLEIVRLLLSYGADPTLATYSGRT 1567
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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