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Conserved domains on  [gi|183396785|ref|NP_001116856|]
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BCL-6 corepressor isoform b [Homo sapiens]

Protein Classification

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, ...
 1150-1362 2.42e-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: 306.84  E-value: 2.42e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  1150 GLHPKKQRHLLHLRERWEQQVSAAD-GKPGRQSRKEVTQATQPEAI---PQGTNITEEKPGRKRAEAKGNRSWSEESLKP 1225
Cdd:pfam15808    1 GLRLKKQRHLQHLRELWEQQVSPAEpSKPGRQSRKEKAEAVQPEVTardRKVKDIAEEKPLRKRSEAKSNRSWSEESLKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  1226 SDNEQGLPVFSGSPPMKSLSSTSAGGKKQAQPSCAPASRPPAKQQKIKENQKTDVLCADEEEDCQAASLLQKYTDnSEKP 1305
Cdd:pfam15808   81 SDNEQGLPAFPPSPHMKSLSSANANGKKQTQPSCTPASRLSAKRQKLKESRKTDPSSPDEDEDCQAASLLQKHTD-SEKP 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  1306 SGKRLCKTKHLIPQESRRGLPLTGE--YYVENADGKVTV-RRFRKRPEPSSDYDLSPAKQ 1362
Cdd:pfam15808  160 KGKRQCKTKHLSLQERRRGLSLTGDsaYELENADGKVTVkRRFRKRPESSSDYDSSPVKP 219
PUFD pfam16553
BCORL-PCGF1-binding domain; PUFD is the minimal domain at the C-terminus of BCORL (BCL6 ...
 1582-1695 6.97e-72

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: 235.35  E-value: 6.97e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  1582 SDVFEFEFSETPLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNVEIVTIAEAEFYRQVSASLLFSCSKDL 1661
Cdd:pfam16553    1 SDVFEFEFSDKPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRARFPHFEVVTIAEAEFYKQVSLSQLLSPPEDL 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 183396785  1662 EAFNPESKELLDLVEFTNEIQTLLGSSVEWLHPS 1695
Cdd:pfam16553   81 EAFNPDSKELVELVEFTPELQTLLGSSVEFLHPS 114
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1409-1541 3.42e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.37  E-value: 3.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1409 NAGETLLQRAARLGYEEVVLYCLENKIcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN 1488
Cdd:COG0666   118 KDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 183396785 1489 DHLEIVRLLLSYGADPTLATYSGRT----IMKMTHSELMEKFLTDYLNDLQGRNDDD 1541
Cdd:COG0666   197 GHLEIVKLLLEAGADVNAKDNDGKTaldlAAENGNLEIVKLLLEAGADLNAKDKDGL 253
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 257-673 3.12e-07

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: 55.31  E-value: 3.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785   257 IPSSLASPMRLSTPSASPaipPLVHCADKSLPWKMGVSPG-NPVDSHAYPHiQNSKQPRVPSAKAVTSGLPGDTALLLPp 335
Cdd:pfam05109  448 LPSSTHVPTNLTAPASTG---PTVSTADVTSPTPAGTTSGaSPVTPSPSPR-DNGTESKAPDMTSPTSAVTTPTPNATS- 522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785   336 sprpsprvhlPTqPAADTYSEFHKHYARISTSPSVALSKPYMTVSSEFPAARLS--NGKYP---KAPEGGEGAQPVPGHA 410
Cdd:pfam05109  523 ----------PT-PAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPtpNATIPtlgKTSPTSAVTTPTPNAT 591

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785   411 RKTAVQDRKDGSSPP-LLEKQTVTKDVTDKPLDLSSKVV----DVDASKADHMKkMAPTVLVHSRAGSGLVLSGSEIPKE 485
Cdd:pfam05109  592 SPTVGETSPQANTTNhTLGGTSSTPVVTSPPKNATSAVTtgqhNITSSSTSSMS-LRPSSISETLSPSTSDNSTSHMPLL 670

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785   486 TLSPPGNGCAIYRSEIISTAPSSWVVPGPSPNEENNGKSMSLKNkaldwaipqqrSSSCPRMGGTDAvitnvsgsvsSAG 565
Cdd:pfam05109  671 TSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGN-----------SSTSTKPGEVNV----------TKG 729

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785   566 RPASASPAPNANAdGTKTSrssvetTPSVIQHVGQPPATPA-KHSSS---------TSSKGAKASNPEPSFKANENGLPP 635
Cdd:pfam05109  730 TPPKNATSPQAPS-GQKTA------VPTVTSTGGKANSTTGgKHTTGhgartstepTTDYGGDSTTPRTRYNATTYLPPS 802

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 183396785   636 SSIFLSPNEAFRSPPIPYPRSYLPYPAPEGIAVSPLSL 673
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, ...
 1150-1362 2.42e-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: 306.84  E-value: 2.42e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  1150 GLHPKKQRHLLHLRERWEQQVSAAD-GKPGRQSRKEVTQATQPEAI---PQGTNITEEKPGRKRAEAKGNRSWSEESLKP 1225
Cdd:pfam15808    1 GLRLKKQRHLQHLRELWEQQVSPAEpSKPGRQSRKEKAEAVQPEVTardRKVKDIAEEKPLRKRSEAKSNRSWSEESLKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  1226 SDNEQGLPVFSGSPPMKSLSSTSAGGKKQAQPSCAPASRPPAKQQKIKENQKTDVLCADEEEDCQAASLLQKYTDnSEKP 1305
Cdd:pfam15808   81 SDNEQGLPAFPPSPHMKSLSSANANGKKQTQPSCTPASRLSAKRQKLKESRKTDPSSPDEDEDCQAASLLQKHTD-SEKP 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  1306 SGKRLCKTKHLIPQESRRGLPLTGE--YYVENADGKVTV-RRFRKRPEPSSDYDLSPAKQ 1362
Cdd:pfam15808  160 KGKRQCKTKHLSLQERRRGLSLTGDsaYELENADGKVTVkRRFRKRPESSSDYDSSPVKP 219
PUFD pfam16553
BCORL-PCGF1-binding domain; PUFD is the minimal domain at the C-terminus of BCORL (BCL6 ...
 1582-1695 6.97e-72

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: 235.35  E-value: 6.97e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  1582 SDVFEFEFSETPLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNVEIVTIAEAEFYRQVSASLLFSCSKDL 1661
Cdd:pfam16553    1 SDVFEFEFSDKPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRARFPHFEVVTIAEAEFYKQVSLSQLLSPPEDL 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 183396785  1662 EAFNPESKELLDLVEFTNEIQTLLGSSVEWLHPS 1695
Cdd:pfam16553   81 EAFNPDSKELVELVEFTPELQTLLGSSVEFLHPS 114
PUFD cd14261
PCGF Ub-like fold discriminator of BCOR; The PUFD domain binds the RAWUL (RING finger and ...
 1580-1694 1.27e-68

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: 226.27  E-value: 1.27e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1580 AYSDVFEFEFSETPLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNVEIVTIAEAEFYRQVSASLLFSCSK 1659
Cdd:cd14261     3 AYSDVFEFEFSDRPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRCNFPNVEVVTIAEAEFYRQVSLSQLFSCPK 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 183396785 1660 DLEAFNPESKELLDLVEFTNEIQTLLGSSVEWLHP 1694
Cdd:cd14261    83 DLEAFNPDSKELLDLVEFTNELQTLLGSSLEWLHP 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1409-1541 3.42e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.37  E-value: 3.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1409 NAGETLLQRAARLGYEEVVLYCLENKIcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN 1488
Cdd:COG0666   118 KDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 183396785 1489 DHLEIVRLLLSYGADPTLATYSGRT----IMKMTHSELMEKFLTDYLNDLQGRNDDD 1541
Cdd:COG0666   197 GHLEIVKLLLEAGADVNAKDNDGKTaldlAAENGNLEIVKLLLEAGADLNAKDKDGL 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1415-1506 2.76e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 2.76e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  1415 LQRAARLGYEEVVLYCLENKiCDVNHRDNAGYCALHEACARGWLNIVRHLLEYgADVNCSAQDGTrPLHDAVENDHLEIV 1494
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRT-ALHYAARSGHLEIV 77

                           90
                   ....*....|..
gi 183396785  1495 RLLLSYGADPTL 1506
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1412-1533 2.13e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.15  E-value: 2.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1412 ETLLQRAARLGYEEVVLYCLENKiCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHL 1491
Cdd:PHA03100  160 KLLIDKGVDINAKNRVNYLLSYG-VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 183396785 1492 EIVRLLLSYGAD-----PTL-----ATYSGRTIMKMTHSELMEKFLTD---YLND 1533
Cdd:PHA03100  239 EIFKLLLNNGPSiktiiETLlyfkdKDLNTITKIKMLKKSIMYMFLLDpgfYKNR 293
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 257-673 3.12e-07

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: 55.31  E-value: 3.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785   257 IPSSLASPMRLSTPSASPaipPLVHCADKSLPWKMGVSPG-NPVDSHAYPHiQNSKQPRVPSAKAVTSGLPGDTALLLPp 335
Cdd:pfam05109  448 LPSSTHVPTNLTAPASTG---PTVSTADVTSPTPAGTTSGaSPVTPSPSPR-DNGTESKAPDMTSPTSAVTTPTPNATS- 522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785   336 sprpsprvhlPTqPAADTYSEFHKHYARISTSPSVALSKPYMTVSSEFPAARLS--NGKYP---KAPEGGEGAQPVPGHA 410
Cdd:pfam05109  523 ----------PT-PAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPtpNATIPtlgKTSPTSAVTTPTPNAT 591

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785   411 RKTAVQDRKDGSSPP-LLEKQTVTKDVTDKPLDLSSKVV----DVDASKADHMKkMAPTVLVHSRAGSGLVLSGSEIPKE 485
Cdd:pfam05109  592 SPTVGETSPQANTTNhTLGGTSSTPVVTSPPKNATSAVTtgqhNITSSSTSSMS-LRPSSISETLSPSTSDNSTSHMPLL 670

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785   486 TLSPPGNGCAIYRSEIISTAPSSWVVPGPSPNEENNGKSMSLKNkaldwaipqqrSSSCPRMGGTDAvitnvsgsvsSAG 565
Cdd:pfam05109  671 TSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGN-----------SSTSTKPGEVNV----------TKG 729

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785   566 RPASASPAPNANAdGTKTSrssvetTPSVIQHVGQPPATPA-KHSSS---------TSSKGAKASNPEPSFKANENGLPP 635
Cdd:pfam05109  730 TPPKNATSPQAPS-GQKTA------VPTVTSTGGKANSTTGgKHTTGhgartstepTTDYGGDSTTPRTRYNATTYLPPS 802

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 183396785   636 SSIFLSPNEAFRSPPIPYPRSYLPYPAPEGIAVSPLSL 673
Cdd:pfam05109  803 TSSKLRPRWTFTSPPVTTAQATVPVPPTSQPRFSNLSM 840
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1481-1506 9.02e-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: 9.02e-05
                            10        20
                    ....*....|....*....|....*.
gi 183396785   1481 PLHDAVENDHLEIVRLLLSYGADPTL 1506
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1411-1517 2.02e-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: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1411 GETLLQRAARLGYEEVVLYCLENKICDVNHRDN----AGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGT------- 1479
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpk 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 183396785 1480 -------RPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKM 1517
Cdd:cd22192   131 nliyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
503-720 4.09e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.79  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  503 STAPSSWVVPGPSPNEENNGKSMSLKNKALdwaiPQQRSSSCPRMGGTDAVITNVSGSVSSAGRPASASPAPNANADGTK 582
Cdd:PRK12323  404 AAPAAAPAAAAAARAVAAAPARRSPAPEAL----AAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAA 479

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  583 TSRSsvettpsviqhvgQPPATPAKHSSSTSS-KGAKASNPEPSFKANENGLPPSSIFLSPNEAFRSPPIPYPRsylPYP 661
Cdd:PRK12323  480 PARA-------------APAAAPAPADDDPPPwEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFET---LAP 543

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  662 APEGIAVSPLSLHGKGPVYPHPVLLPNGSLFPGHLAPKPGLPYGLP-TGRPEFVTYQDAL 720
Cdd:PRK12323  544 APAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPALAARLPvRGLAQQLARQSEL 603
 
Name Accession Description Interval E-value
BCOR pfam15808
BCL-6 co-repressor, non-ankyrin-repeat region; BCOR is a domain family found in eukaryotes, ...
 1150-1362 2.42e-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: 306.84  E-value: 2.42e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  1150 GLHPKKQRHLLHLRERWEQQVSAAD-GKPGRQSRKEVTQATQPEAI---PQGTNITEEKPGRKRAEAKGNRSWSEESLKP 1225
Cdd:pfam15808    1 GLRLKKQRHLQHLRELWEQQVSPAEpSKPGRQSRKEKAEAVQPEVTardRKVKDIAEEKPLRKRSEAKSNRSWSEESLKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  1226 SDNEQGLPVFSGSPPMKSLSSTSAGGKKQAQPSCAPASRPPAKQQKIKENQKTDVLCADEEEDCQAASLLQKYTDnSEKP 1305
Cdd:pfam15808   81 SDNEQGLPAFPPSPHMKSLSSANANGKKQTQPSCTPASRLSAKRQKLKESRKTDPSSPDEDEDCQAASLLQKHTD-SEKP 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  1306 SGKRLCKTKHLIPQESRRGLPLTGE--YYVENADGKVTV-RRFRKRPEPSSDYDLSPAKQ 1362
Cdd:pfam15808  160 KGKRQCKTKHLSLQERRRGLSLTGDsaYELENADGKVTVkRRFRKRPESSSDYDSSPVKP 219
PUFD pfam16553
BCORL-PCGF1-binding domain; PUFD is the minimal domain at the C-terminus of BCORL (BCL6 ...
 1582-1695 6.97e-72

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: 235.35  E-value: 6.97e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  1582 SDVFEFEFSETPLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNVEIVTIAEAEFYRQVSASLLFSCSKDL 1661
Cdd:pfam16553    1 SDVFEFEFSDKPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRARFPHFEVVTIAEAEFYKQVSLSQLLSPPEDL 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 183396785  1662 EAFNPESKELLDLVEFTNEIQTLLGSSVEWLHPS 1695
Cdd:pfam16553   81 EAFNPDSKELVELVEFTPELQTLLGSSVEFLHPS 114
PUFD cd14261
PCGF Ub-like fold discriminator of BCOR; The PUFD domain binds the RAWUL (RING finger and ...
 1580-1694 1.27e-68

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: 226.27  E-value: 1.27e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1580 AYSDVFEFEFSETPLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNVEIVTIAEAEFYRQVSASLLFSCSK 1659
Cdd:cd14261     3 AYSDVFEFEFSDRPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRCNFPNVEVVTIAEAEFYRQVSLSQLFSCPK 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 183396785 1660 DLEAFNPESKELLDLVEFTNEIQTLLGSSVEWLHP 1694
Cdd:cd14261    83 DLEAFNPDSKELLDLVEFTNELQTLLGSSLEWLHP 117
PUFD_like cd14259
PCGF Ub-like fold discriminator and related domains; The PUFD domain binds the RAWUL (RING ...
 1583-1690 2.70e-40

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: 144.77  E-value: 2.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1583 DVFEFEFSETPLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNVEIVTIAEAEFYRQVSASLLFSCSKDLe 1662
Cdd:cd14259     1 DDFEFEFSDEPLPPLYNLRISPNDGPRNWHLLSDVLTRLKLKSRDFLLKQICLELTSIPIEDFLEQASCLQLLCAGEKL- 79

                          90       100
                  ....*....|....*....|....*...
gi 183396785 1663 aFNPESKELLDLVEFTNEIQTLLGSSVE 1690
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 ...
 1582-1690 1.39e-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: 134.59  E-value: 1.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1582 SDVFEFEFSETPLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNVEIVTIAEAEFYRQVSASLLFSCSKDL 1661
Cdd:cd14260     3 EDDFMFEFSDKPLLPCYNLQVSVSRGPCNWFLFSDVLKRLKLSSRIFQARFPHFEIATMPKAEFYRQVLSSQLLTPAERP 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 183396785 1662 EAFN----PESKELLDLVEFTNEIQTLLGSSVE 1690
Cdd:cd14260    83 GGLDdrspQGSSETVELVRYEPELLRLLGSAVE 115
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1409-1541 3.42e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.37  E-value: 3.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1409 NAGETLLQRAARLGYEEVVLYCLENKIcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN 1488
Cdd:COG0666   118 KDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 183396785 1489 DHLEIVRLLLSYGADPTLATYSGRT----IMKMTHSELMEKFLTDYLNDLQGRNDDD 1541
Cdd:COG0666   197 GHLEIVKLLLEAGADVNAKDNDGKTaldlAAENGNLEIVKLLLEAGADLNAKDKDGL 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1404-1513 2.52e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.98  E-value: 2.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1404 LIVNKNAGETLLQRAARLGYEEVVLYCLENKIcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLH 1483
Cdd:COG0666    80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158

                          90       100       110
                  ....*....|....*....|....*....|
gi 183396785 1484 DAVENDHLEIVRLLLSYGADPTLATYSGRT 1513
Cdd:COG0666   159 LAAANGNLEIVKLLLEAGADVNARDNDGET 188
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1399-1548 2.38e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.26  E-value: 2.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1399 PEARRLIVNKNA--------GETLLQRAARLGYEEVVLYCLENKiCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGAD 1470
Cdd:COG0666   133 LEIVKLLLEAGAdvnaqdndGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 183396785 1471 VNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKMTHSELMEKFLTDYLNDLQGRNDDDASGTWDF 1548
Cdd:COG0666   212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1415-1506 2.76e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 2.76e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  1415 LQRAARLGYEEVVLYCLENKiCDVNHRDNAGYCALHEACARGWLNIVRHLLEYgADVNCSAQDGTrPLHDAVENDHLEIV 1494
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRT-ALHYAARSGHLEIV 77

                           90
                   ....*....|..
gi 183396785  1495 RLLLSYGADPTL 1506
Cdd:pfam12796   78 KLLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1404-1513 1.52e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.17  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1404 LIVNKNAGETLLQRAARLGYEEVVLYCLENKICDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLH 1483
Cdd:COG0666    46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLH 125

                          90       100       110
                  ....*....|....*....|....*....|
gi 183396785 1484 DAVENDHLEIVRLLLSYGADPTLATYSGRT 1513
Cdd:COG0666   126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1449-1515 4.21e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 4.21e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 183396785  1449 LHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGAdpTLATYSGRTIM 1515
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTAL 65
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1412-1533 2.13e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.15  E-value: 2.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1412 ETLLQRAARLGYEEVVLYCLENKiCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHL 1491
Cdd:PHA03100  160 KLLIDKGVDINAKNRVNYLLSYG-VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 183396785 1492 EIVRLLLSYGAD-----PTL-----ATYSGRTIMKMTHSELMEKFLTD---YLND 1533
Cdd:PHA03100  239 EIFKLLLNNGPSiktiiETLlyfkdKDLNTITKIKMLKKSIMYMFLLDpgfYKNR 293
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1406-1472 1.66e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 1.66e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 183396785  1406 VNKNAGETLLQRAARLGYEEVVLYCLENkiCDVNHRDNaGYCALHEACARGWLNIVRHLLEYGADVN 1472
Cdd:pfam12796   25 LQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADIN 88
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1346-1500 3.46e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.92  E-value: 3.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1346 RKRPEPSSDYDLSPAKQEpkpFDRLQQLLPASQSTQLPCSSSPQETTQSRPMPPearrlIVNKNAGETLLQRAArlGYEE 1425
Cdd:PTZ00322   26 KRRAKPISFERMAAIQEE---IARIDTHLEALEATENKDATPDHNLTTEEVIDP-----VVAHMLTVELCQLAA--SGDA 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 183396785 1426 VVLYCLENKICDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSY 1500
Cdd:PTZ00322   96 VGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1400-1513 2.05e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1400 EARRLIVNKNAGETLLQRAARLGYEEVVLYCLENKICDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGT 1479
Cdd:COG0666     9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                          90       100       110
                  ....*....|....*....|....*....|....
gi 183396785 1480 RPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT 1513
Cdd:COG0666    89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGET 122
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1399-1513 2.68e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 2.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1399 PEARRLIVNKNA--------GETLLQRAA--RLGYEEVVLYcLENKICDVNHRDNAGYCALHEA--CARGWLNIVRHLLE 1466
Cdd:PHA03100   86 KEIVKLLLEYGAnvnapdnnGITPLLYAIskKSNSYSIVEY-LLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLID 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 183396785 1467 YGADVNcsAQD------------------GTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT 1513
Cdd:PHA03100  165 KGVDIN--AKNrvnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1461-1517 5.26e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 5.26e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 183396785 1461 VRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKM 1517
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
Ank_4 pfam13637
Ankyrin repeats (many copies);
1448-1498 2.48e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 2.48e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 183396785  1448 ALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLL 1498
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1437-1513 4.96e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 4.96e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 183396785 1437 DVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT 1513
Cdd:PHA02874  116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1415-1514 5.79e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.34  E-value: 5.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1415 LQRAARLGYEEVVLYCleNKICDVNHRDNAGYCALH-------EACARgwlnIVRHLLEYGADVNCSAQDGTRPLHDAVE 1487
Cdd:PHA03095   19 LLNASNVTVEEVRRLL--AAGADVNFRGEYGKTPLHlylhyssEKVKD----IVRLLLEAGADVNAPERCGFTPLHLYLY 92

                          90       100
                  ....*....|....*....|....*...
gi 183396785 1488 NDH-LEIVRLLLSYGADPTLATYSGRTI 1514
Cdd:PHA03095   93 NATtLDVIKLLIKAGADVNAKDKVGRTP 120
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 257-673 3.12e-07

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: 55.31  E-value: 3.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785   257 IPSSLASPMRLSTPSASPaipPLVHCADKSLPWKMGVSPG-NPVDSHAYPHiQNSKQPRVPSAKAVTSGLPGDTALLLPp 335
Cdd:pfam05109  448 LPSSTHVPTNLTAPASTG---PTVSTADVTSPTPAGTTSGaSPVTPSPSPR-DNGTESKAPDMTSPTSAVTTPTPNATS- 522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785   336 sprpsprvhlPTqPAADTYSEFHKHYARISTSPSVALSKPYMTVSSEFPAARLS--NGKYP---KAPEGGEGAQPVPGHA 410
Cdd:pfam05109  523 ----------PT-PAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPtpNATIPtlgKTSPTSAVTTPTPNAT 591

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785   411 RKTAVQDRKDGSSPP-LLEKQTVTKDVTDKPLDLSSKVV----DVDASKADHMKkMAPTVLVHSRAGSGLVLSGSEIPKE 485
Cdd:pfam05109  592 SPTVGETSPQANTTNhTLGGTSSTPVVTSPPKNATSAVTtgqhNITSSSTSSMS-LRPSSISETLSPSTSDNSTSHMPLL 670

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785   486 TLSPPGNGCAIYRSEIISTAPSSWVVPGPSPNEENNGKSMSLKNkaldwaipqqrSSSCPRMGGTDAvitnvsgsvsSAG 565
Cdd:pfam05109  671 TSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGN-----------SSTSTKPGEVNV----------TKG 729

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785   566 RPASASPAPNANAdGTKTSrssvetTPSVIQHVGQPPATPA-KHSSS---------TSSKGAKASNPEPSFKANENGLPP 635
Cdd:pfam05109  730 TPPKNATSPQAPS-GQKTA------VPTVTSTGGKANSTTGgKHTTGhgartstepTTDYGGDSTTPRTRYNATTYLPPS 802

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 183396785   636 SSIFLSPNEAFRSPPIPYPRSYLPYPAPEGIAVSPLSL 673
Cdd:pfam05109  803 TSSKLRPRWTFTSPPVTTAQATVPVPPTSQPRFSNLSM 840
Ank_5 pfam13857
Ankyrin repeats (many copies);
1464-1517 5.50e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 5.50e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 183396785  1464 LLEYG-ADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKM 1517
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1411-1524 9.18e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 9.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1411 GETLLQRAARLGYEEVVLYCLENKiCDVNHRDNAGYCALHEACA-------------------------------RGWLN 1459
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAISakhhkifrilyhfasisdphaagdllctaakRNDLT 636

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 183396785 1460 IVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATysgrTIMKMTHSELME 1524
Cdd:PLN03192  637 AMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN----TDDDFSPTELRE 697
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1423-1517 7.37e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 7.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1423 YEEVVLYCLENKiCDVNHRDNAGYCALH-----EACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN--DHLEIVR 1495
Cdd:PHA03100   47 NIDVVKILLDNG-ADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVE 125

                          90       100
                  ....*....|....*....|..
gi 183396785 1496 LLLSYGADPTLATYSGRTIMKM 1517
Cdd:PHA03100  126 YLLDNGANVNIKNSDGENLLHL 147
Ank_4 pfam13637
Ankyrin repeats (many copies);
1413-1465 1.23e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 1.23e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 183396785  1413 TLLQRAARLGYEEVVLYCLENKIcDVNHRDNAGYCALHEACARGWLNIVRHLL 1465
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
1431-1483 2.06e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 2.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 183396785  1431 LENKICDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLH 1483
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1460-1504 3.49e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 3.49e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 183396785 1460 IVRHLLEYGADVNCSAQD-GTRPLHDAVENDHLEIVRLLLSYGADP 1504
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANV 194
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1459-1527 3.84e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.12  E-value: 3.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1459 NIVRHLLEYGADVNCSAQDGTRPLH-----DAVENDHLEIVRLLLSYGADPTLATYSGRTIM------KMTHSELMEKFL 1527
Cdd:PHA03100   49 DVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLlyaiskKSNSYSIVEYLL 128
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1383-1503 4.01e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 4.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1383 PCSSSPQETTQSRPMPPEARRLI-VN-KN-AGETLLQRAARLGYEEVVLYCLENKICDVNHRDNAGYCALHEACARG-WL 1458
Cdd:PHA02876  276 PLHHASQAPSLSRLVPKLLERGAdVNaKNiKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNK 355

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 183396785 1459 NIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGAD 1503
Cdd:PHA02876  356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1437-1514 4.54e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.10  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1437 DVNHRDNAGYCALHeACARG-WLN--IVRHLLEYGADVNCSAQDGTRPLHDAVENDH--LEIVRLLLSYGADPTLATYSG 1511
Cdd:PHA03095  109 DVNAKDKVGRTPLH-VYLSGfNINpkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRF 187


                  ...
gi 183396785 1512 RTI 1514
Cdd:PHA03095  188 RSL 190
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1481-1506 9.02e-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: 9.02e-05
                            10        20
                    ....*....|....*....|....*.
gi 183396785   1481 PLHDAVENDHLEIVRLLLSYGADPTL 1506
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1391-1513 9.09e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 9.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1391 TTQSRPMPPEARRLI-----VN--KNAGETLLQRAARLGYEEV--VLYCLENKICDVNHRDNAGYCALH-EACARGWLNI 1460
Cdd:PHA03095   20 LNASNVTVEEVRRLLaagadVNfrGEYGKTPLHLYLHYSSEKVkdIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDV 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 183396785 1461 VRHLLEYGADVNCSAQDGTRPLHD--AVENDHLEIVRLLLSYGADPTLATYSGRT 1513
Cdd:PHA03095  100 IKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMT 154
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1445-1473 1.61e-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: 1.61e-04
                           10        20
                   ....*....|....*....|....*....
gi 183396785  1445 GYCALHEACARGWLNIVRHLLEYGADVNC 1473
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1411-1517 2.02e-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: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1411 GETLLQRAARLGYEEVVLYCLENKICDVNHRDN----AGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGT------- 1479
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpk 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 183396785 1480 -------RPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKM 1517
Cdd:cd22192   131 nliyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1404-1503 2.13e-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: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1404 LIVNKNAGETLLQRAARLGYEEVVLYCLENKICDVNHRDNAGYCALHEACARGWLNIVRHLLEYGAD-VN----CSAQDG 1478
Cdd:cd22192    10 LLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNepmtSDLYQG 89

                          90       100
                  ....*....|....*....|....*
gi 183396785 1479 TRPLHDAVENDHLEIVRLLLSYGAD 1503
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGAD 114
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1449-1508 2.43e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 2.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 183396785 1449 LHEACARGWLNIVRHLLEYGADVN-CSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLAT 1508
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPN 132
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1415-1517 2.56e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.64  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1415 LQRAARLGYEEVVLYCLENKiCDVNHRDNAGYCALHEACARGW-LNIVRHLLEYGADVNC-SAQDGTRPLHDAVENDhlE 1492
Cdd:PHA02878  205 LHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCKdYDILKLLLEHGVDVNAkSYILGLTALHSSIKSE--R 281

                          90       100
                  ....*....|....*....|....*
gi 183396785 1493 IVRLLLSYGADPTLATYSGRTIMKM 1517
Cdd:PHA02878  282 KLKLLLEYGADINSLNSYKLTPLSS 306
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1431-1522 2.69e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1431 LENKICdVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDG-TRPLHDAVENDHLEIVRLLLSYGADPTLATy 1509
Cdd:PHA02875  155 IDHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF- 232

                          90
                  ....*....|...
gi 183396785 1510 sgrTIMKMTHSEL 1522
Cdd:PHA02875  233 ---MIEGEECTIL 242
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1477-1508 3.31e-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: 3.31e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 183396785  1477 DGTRPLHDAVE-NDHLEIVRLLLSYGADPTLAT 1508
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1436-1513 3.50e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1436 CDVNHRDNAGYCALHEA-----CARGwlnIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYS 1510
Cdd:PHA03095  213 CDPAATDMLGNTPLHSMatgssCKRS---LVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD 289


                  ...
gi 183396785 1511 GRT 1513
Cdd:PHA03095  290 GNT 292
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1412-1501 3.84e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 3.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1412 ETLLQRAARLGYEEVVLYCLENKiCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHL 1491
Cdd:PHA02874  125 KTFLHYAIKKGDLESIKMLFEYG-ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDY 203

                          90
                  ....*....|
gi 183396785 1492 EIVRLLLSYG 1501
Cdd:PHA02874  204 ACIKLLIDHG 213
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1437-1499 4.49e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 4.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 183396785 1437 DVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLS 1499
Cdd:PHA03095  249 SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1458-1516 4.72e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 4.72e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 183396785 1458 LNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMK 1516
Cdd:PHA02876  158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLE 216
Ank_4 pfam13637
Ankyrin repeats (many copies);
1478-1527 5.11e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 5.11e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 183396785  1478 GTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIM----KMTHSELMEKFL 1527
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALhfaaSNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1445-1473 6.99e-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: 6.99e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 183396785  1445 GYCALHEACAR-GWLNIVRHLLEYGADVNC 1473
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNA 31
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1437-1513 8.49e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 8.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 183396785 1437 DVNHRD-NAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT 1513
Cdd:PHA02878  159 DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1405-1540 8.94e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.72  E-value: 8.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1405 IVNKNAGETLLQRAARLGYEEVVLYCLeNKICDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHD 1484
Cdd:PHA02878  162 MKDRHKGNTALHYATENKDQRLTELLL-SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHI 240

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 183396785 1485 AVEN-DHLEIVRLLLSYGADPTLATY-SGRTIMKMT-HSELMEKFLTDYLNDLQGRNDD 1540
Cdd:PHA02878  241 SVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSiKSERKLKLLLEYGADINSLNSY 299
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 1445-1504 1.63e-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: 1.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 183396785 1445 GYCALHEACARGWLNIVRHLLEYGADVNCSAQD-------------GTRPLHDAVENDHLEIVRLLLSYGADP 1504
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQP 145
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
503-720 4.09e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.79  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  503 STAPSSWVVPGPSPNEENNGKSMSLKNKALdwaiPQQRSSSCPRMGGTDAVITNVSGSVSSAGRPASASPAPNANADGTK 582
Cdd:PRK12323  404 AAPAAAPAAAAAARAVAAAPARRSPAPEAL----AAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAA 479

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  583 TSRSsvettpsviqhvgQPPATPAKHSSSTSS-KGAKASNPEPSFKANENGLPPSSIFLSPNEAFRSPPIPYPRsylPYP 661
Cdd:PRK12323  480 PARA-------------APAAAPAPADDDPPPwEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFET---LAP 543

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785  662 APEGIAVSPLSLHGKGPVYPHPVLLPNGSLFPGHLAPKPGLPYGLP-TGRPEFVTYQDAL 720
Cdd:PRK12323  544 APAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPALAARLPvRGLAQQLARQSEL 603
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1437-1498 5.78e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 5.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 183396785 1437 DVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLL 1498
Cdd:PHA02876  170 DVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
PHA02946 PHA02946
ankyin-like protein; Provisional
 1443-1544 7.36e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 7.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 183396785 1443 NAGYCALHEACARGWLN--IVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT---IMKM 1517
Cdd:PHA02946   35 SGNYHILHAYCGIKGLDerFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTplyYLSG 114

                          90       100
                  ....*....|....*....|....*....
gi 183396785 1518 THSELMEK--FLTDYLNDLQGRNDDDASG 1544
Cdd:PHA02946  115 TDDEVIERinLLVQYGAKINNSVDEEGCG 143
 
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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