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Conserved domains on  [gi|21071037|ref|NP_060215|]
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BCL-6 corepressor isoform a [Homo sapiens]

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, ...
 1168-1380 1.40e-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: 1.40e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   1168 GLHPKKQRHLLHLRERWEQQVSAAD-GKPGRQSRKEVTQATQPEAI---PQGTNITEEKPGRKRAEAKGNRSWSEESLKP 1243
Cdd:pfam15808    1 GLRLKKQRHLQHLRELWEQQVSPAEpSKPGRQSRKEKAEAVQPEVTardRKVKDIAEEKPLRKRSEAKSNRSWSEESLKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   1244 SDNEQGLPVFSGSPPMKSLSSTSAGGKKQAQPSCAPASRPPAKQQKIKENQKTDVLCADEEEDCQAASLLQKYTDnSEKP 1323
Cdd:pfam15808   81 SDNEQGLPAFPPSPHMKSLSSANANGKKQTQPSCTPASRLSAKRQKLKESRKTDPSSPDEDEDCQAASLLQKHTD-SEKP 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   1324 SGKRLCKTKHLIPQESRRGLPLTGE--YYVENADGKVTV-RRFRKRPEPSSDYDLSPAKQ 1380
Cdd:pfam15808  160 KGKRQCKTKHLSLQERRRGLSLTGDsaYELENADGKVTVkRRFRKRPESSSDYDSSPVKP 219
PUFD pfam16553
BCORL-PCGF1-binding domain; PUFD is the minimal domain at the C-terminus of BCORL (BCL6 ...
 1600-1713 7.39e-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: 7.39e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   1600 SDVFEFEFSETPLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNVEIVTIAEAEFYRQVSASLLFSCSKDL 1679
Cdd:pfam16553    1 SDVFEFEFSDKPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRARFPHFEVVTIAEAEFYKQVSLSQLLSPPEDL 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 21071037   1680 EAFNPESKELLDLVEFTNEIQTLLGSSVEWLHPS 1713
Cdd:pfam16553   81 EAFNPDSKELVELVEFTPELQTLLGSSVEFLHPS 114
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1427-1559 3.46e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.37  E-value: 3.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037 1427 NAGETLLQRAARLGYEEVVLYCLENKIcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN 1506
Cdd:COG0666  118 KDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 21071037 1507 DHLEIVRLLLSYGADPTLATYSGRT----IMKMTHSELMEKFLTDYLNDLQGRNDDD 1559
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 2.16e-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: 56.08  E-value: 2.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037    257 IPSSLASPMRLSTPSASPaipPLVHCADKSLPWKMGVSPG-NPVDSHAYPHiQNSKQPRVPSAKAVTSGLPGDTALLLPp 335
Cdd:pfam05109  448 LPSSTHVPTNLTAPASTG---PTVSTADVTSPTPAGTTSGaSPVTPSPSPR-DNGTESKAPDMTSPTSAVTTPTPNATS- 522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037    336 sprpsprvhlPTqPAADTYSEFHKHYARISTSPSVALSKPYMTVSSEFPAARLS--NGKYP---KAPEGGEGAQPVPGHA 410
Cdd:pfam05109  523 ----------PT-PAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPtpNATIPtlgKTSPTSAVTTPTPNAT 591

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037    411 RKTAVQDRKDGSSPP-LLEKQTVTKDVTDKPLDLSSKVV----DVDASKADHMKkMAPTVLVHSRAGSGLVLSGSEIPKE 485
Cdd:pfam05109  592 SPTVGETSPQANTTNhTLGGTSSTPVVTSPPKNATSAVTtgqhNITSSSTSSMS-LRPSSISETLSPSTSDNSTSHMPLL 670

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037    486 TLSPPGNGCAIYRSEIISTAPSSWVVPGPSPNEENNGKSMSLKNkaldwaipqqrSSSCPRMGGTDAvitnvsgsvsSAG 565
Cdd:pfam05109  671 TSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGN-----------SSTSTKPGEVNV----------TKG 729

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037    566 RPASASPAPNANAdGTKTSrssvetTPSVIQHVGQPPATPA-KHSSS---------TSSKGAKASNPEPSFKANENGLPP 635
Cdd:pfam05109  730 TPPKNATSPQAPS-GQKTA------VPTVTSTGGKANSTTGgKHTTGhgartstepTTDYGGDSTTPRTRYNATTYLPPS 802

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 21071037    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, ...
 1168-1380 1.40e-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: 1.40e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   1168 GLHPKKQRHLLHLRERWEQQVSAAD-GKPGRQSRKEVTQATQPEAI---PQGTNITEEKPGRKRAEAKGNRSWSEESLKP 1243
Cdd:pfam15808    1 GLRLKKQRHLQHLRELWEQQVSPAEpSKPGRQSRKEKAEAVQPEVTardRKVKDIAEEKPLRKRSEAKSNRSWSEESLKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   1244 SDNEQGLPVFSGSPPMKSLSSTSAGGKKQAQPSCAPASRPPAKQQKIKENQKTDVLCADEEEDCQAASLLQKYTDnSEKP 1323
Cdd:pfam15808   81 SDNEQGLPAFPPSPHMKSLSSANANGKKQTQPSCTPASRLSAKRQKLKESRKTDPSSPDEDEDCQAASLLQKHTD-SEKP 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   1324 SGKRLCKTKHLIPQESRRGLPLTGE--YYVENADGKVTV-RRFRKRPEPSSDYDLSPAKQ 1380
Cdd:pfam15808  160 KGKRQCKTKHLSLQERRRGLSLTGDsaYELENADGKVTVkRRFRKRPESSSDYDSSPVKP 219
PUFD pfam16553
BCORL-PCGF1-binding domain; PUFD is the minimal domain at the C-terminus of BCORL (BCL6 ...
 1600-1713 7.39e-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: 7.39e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   1600 SDVFEFEFSETPLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNVEIVTIAEAEFYRQVSASLLFSCSKDL 1679
Cdd:pfam16553    1 SDVFEFEFSDKPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRARFPHFEVVTIAEAEFYKQVSLSQLLSPPEDL 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 21071037   1680 EAFNPESKELLDLVEFTNEIQTLLGSSVEWLHPS 1713
Cdd:pfam16553   81 EAFNPDSKELVELVEFTPELQTLLGSSVEFLHPS 114
PUFD cd14261
PCGF Ub-like fold discriminator of BCOR; The PUFD domain binds the RAWUL (RING finger and ...
 1598-1712 1.50e-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: 225.88  E-value: 1.50e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037 1598 AYSDVFEFEFSETPLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNVEIVTIAEAEFYRQVSASLLFSCSK 1677
Cdd:cd14261    3 AYSDVFEFEFSDRPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRCNFPNVEVVTIAEAEFYRQVSLSQLFSCPK 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 21071037 1678 DLEAFNPESKELLDLVEFTNEIQTLLGSSVEWLHP 1712
Cdd:cd14261   83 DLEAFNPDSKELLDLVEFTNELQTLLGSSLEWLHP 117
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1427-1559 3.46e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.37  E-value: 3.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037 1427 NAGETLLQRAARLGYEEVVLYCLENKIcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN 1506
Cdd:COG0666  118 KDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 21071037 1507 DHLEIVRLLLSYGADPTLATYSGRT----IMKMTHSELMEKFLTDYLNDLQGRNDDD 1559
Cdd:COG0666  197 GHLEIVKLLLEAGADVNAKDNDGKTaldlAAENGNLEIVKLLLEAGADLNAKDKDGL 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1433-1524 2.79e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 2.79e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   1433 LQRAARLGYEEVVLYCLENKiCDVNHRDNAGYCALHEACARGWLNIVRHLLEYgADVNCSAQDGTrPLHDAVENDHLEIV 1512
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRT-ALHYAARSGHLEIV 77

                           90
                   ....*....|..
gi 21071037   1513 RLLLSYGADPTL 1524
Cdd:pfam12796   78 KLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1430-1551 2.16e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.15  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037  1430 ETLLQRAARLGYEEVVLYCLENKiCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHL 1509
Cdd:PHA03100  160 KLLIDKGVDINAKNRVNYLLSYG-VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21071037  1510 EIVRLLLSYGAD-----PTL-----ATYSGRTIMKMTHSELMEKFLTD---YLND 1551
Cdd:PHA03100  239 EIFKLLLNNGPSiktiiETLlyfkdKDLNTITKIKMLKKSIMYMFLLDpgfYKNR 293
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 257-673 2.16e-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: 56.08  E-value: 2.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037    257 IPSSLASPMRLSTPSASPaipPLVHCADKSLPWKMGVSPG-NPVDSHAYPHiQNSKQPRVPSAKAVTSGLPGDTALLLPp 335
Cdd:pfam05109  448 LPSSTHVPTNLTAPASTG---PTVSTADVTSPTPAGTTSGaSPVTPSPSPR-DNGTESKAPDMTSPTSAVTTPTPNATS- 522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037    336 sprpsprvhlPTqPAADTYSEFHKHYARISTSPSVALSKPYMTVSSEFPAARLS--NGKYP---KAPEGGEGAQPVPGHA 410
Cdd:pfam05109  523 ----------PT-PAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPtpNATIPtlgKTSPTSAVTTPTPNAT 591

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037    411 RKTAVQDRKDGSSPP-LLEKQTVTKDVTDKPLDLSSKVV----DVDASKADHMKkMAPTVLVHSRAGSGLVLSGSEIPKE 485
Cdd:pfam05109  592 SPTVGETSPQANTTNhTLGGTSSTPVVTSPPKNATSAVTtgqhNITSSSTSSMS-LRPSSISETLSPSTSDNSTSHMPLL 670

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037    486 TLSPPGNGCAIYRSEIISTAPSSWVVPGPSPNEENNGKSMSLKNkaldwaipqqrSSSCPRMGGTDAvitnvsgsvsSAG 565
Cdd:pfam05109  671 TSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGN-----------SSTSTKPGEVNV----------TKG 729

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037    566 RPASASPAPNANAdGTKTSrssvetTPSVIQHVGQPPATPA-KHSSS---------TSSKGAKASNPEPSFKANENGLPP 635
Cdd:pfam05109  730 TPPKNATSPQAPS-GQKTA------VPTVTSTGGKANSTTGgKHTTGhgartstepTTDYGGDSTTPRTRYNATTYLPPS 802

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 21071037    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 ...
 1499-1524 9.12e-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: 9.12e-05
                            10        20
                    ....*....|....*....|....*.
gi 21071037    1499 PLHDAVENDHLEIVRLLLSYGADPTL 1524
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1429-1535 2.05e-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: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037 1429 GETLLQRAARLGYEEVVLYCLENKICDVNHRDN----AGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGT------- 1497
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpk 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 21071037 1498 -------RPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKM 1535
Cdd:cd22192  131 nliyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
503-720 4.00e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.79  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   503 STAPSSWVVPGPSPNEENNGKSMSLKNKALdwaiPQQRSSSCPRMGGTDAVITNVSGSVSSAGRPASASPAPNANADGTK 582
Cdd:PRK12323  404 AAPAAAPAAAAAARAVAAAPARRSPAPEAL----AAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAA 479

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   583 TSRSsvettpsviqhvgQPPATPAKHSSSTSS-KGAKASNPEPSFKANENGLPPSSIFLSPNEAFRSPPIPYPRsylPYP 661
Cdd:PRK12323  480 PARA-------------APAAAPAPADDDPPPwEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFET---LAP 543

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   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, ...
 1168-1380 1.40e-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: 1.40e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   1168 GLHPKKQRHLLHLRERWEQQVSAAD-GKPGRQSRKEVTQATQPEAI---PQGTNITEEKPGRKRAEAKGNRSWSEESLKP 1243
Cdd:pfam15808    1 GLRLKKQRHLQHLRELWEQQVSPAEpSKPGRQSRKEKAEAVQPEVTardRKVKDIAEEKPLRKRSEAKSNRSWSEESLKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   1244 SDNEQGLPVFSGSPPMKSLSSTSAGGKKQAQPSCAPASRPPAKQQKIKENQKTDVLCADEEEDCQAASLLQKYTDnSEKP 1323
Cdd:pfam15808   81 SDNEQGLPAFPPSPHMKSLSSANANGKKQTQPSCTPASRLSAKRQKLKESRKTDPSSPDEDEDCQAASLLQKHTD-SEKP 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   1324 SGKRLCKTKHLIPQESRRGLPLTGE--YYVENADGKVTV-RRFRKRPEPSSDYDLSPAKQ 1380
Cdd:pfam15808  160 KGKRQCKTKHLSLQERRRGLSLTGDsaYELENADGKVTVkRRFRKRPESSSDYDSSPVKP 219
PUFD pfam16553
BCORL-PCGF1-binding domain; PUFD is the minimal domain at the C-terminus of BCORL (BCL6 ...
 1600-1713 7.39e-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: 7.39e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   1600 SDVFEFEFSETPLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNVEIVTIAEAEFYRQVSASLLFSCSKDL 1679
Cdd:pfam16553    1 SDVFEFEFSDKPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRARFPHFEVVTIAEAEFYKQVSLSQLLSPPEDL 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 21071037   1680 EAFNPESKELLDLVEFTNEIQTLLGSSVEWLHPS 1713
Cdd:pfam16553   81 EAFNPDSKELVELVEFTPELQTLLGSSVEFLHPS 114
PUFD cd14261
PCGF Ub-like fold discriminator of BCOR; The PUFD domain binds the RAWUL (RING finger and ...
 1598-1712 1.50e-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: 225.88  E-value: 1.50e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037 1598 AYSDVFEFEFSETPLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNVEIVTIAEAEFYRQVSASLLFSCSK 1677
Cdd:cd14261    3 AYSDVFEFEFSDRPLLPCYNIQVSLSQGPRNWLLLSDVLKRLKMSSRIFRCNFPNVEVVTIAEAEFYRQVSLSQLFSCPK 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 21071037 1678 DLEAFNPESKELLDLVEFTNEIQTLLGSSVEWLHP 1712
Cdd:cd14261   83 DLEAFNPDSKELLDLVEFTNELQTLLGSSLEWLHP 117
PUFD_like cd14259
PCGF Ub-like fold discriminator and related domains; The PUFD domain binds the RAWUL (RING ...
 1601-1708 2.73e-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: 2.73e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037 1601 DVFEFEFSETPLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNVEIVTIAEAEFYRQVSASLLFSCSKDLe 1680
Cdd:cd14259    1 DDFEFEFSDEPLPPLYNLRISPNDGPRNWHLLSDVLTRLKLKSRDFLLKQICLELTSIPIEDFLEQASCLQLLCAGEKL- 79

                         90       100
                 ....*....|....*....|....*...
gi 21071037 1681 aFNPESKELLDLVEFTNEIQTLLGSSVE 1708
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 ...
 1600-1708 1.43e-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: 134.21  E-value: 1.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037 1600 SDVFEFEFSETPLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNVEIVTIAEAEFYRQVSASLLFSCSKDL 1679
Cdd:cd14260    3 EDDFMFEFSDKPLLPCYNLQVSVSRGPCNWFLFSDVLKRLKLSSRIFQARFPHFEIATMPKAEFYRQVLSSQLLTPAERP 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 21071037 1680 EAFN----PESKELLDLVEFTNEIQTLLGSSVE 1708
Cdd:cd14260   83 GGLDdrspQGSSETVELVRYEPELLRLLGSAVE 115
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1427-1559 3.46e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.37  E-value: 3.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037 1427 NAGETLLQRAARLGYEEVVLYCLENKIcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN 1506
Cdd:COG0666  118 KDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 21071037 1507 DHLEIVRLLLSYGADPTLATYSGRT----IMKMTHSELMEKFLTDYLNDLQGRNDDD 1559
Cdd:COG0666  197 GHLEIVKLLLEAGADVNAKDNDGKTaldlAAENGNLEIVKLLLEAGADLNAKDKDGL 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1422-1531 2.55e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.98  E-value: 2.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037 1422 LIVNKNAGETLLQRAARLGYEEVVLYCLENKIcDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLH 1501
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158

                         90       100       110
                 ....*....|....*....|....*....|
gi 21071037 1502 DAVENDHLEIVRLLLSYGADPTLATYSGRT 1531
Cdd:COG0666  159 LAAANGNLEIVKLLLEAGADVNARDNDGET 188
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1417-1566 2.41e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.26  E-value: 2.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037 1417 PEARRLIVNKNA--------GETLLQRAARLGYEEVVLYCLENKiCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGAD 1488
Cdd:COG0666  133 LEIVKLLLEAGAdvnaqdndGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21071037 1489 VNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKMTHSELMEKFLTDYLNDLQGRNDDDASGTWDF 1566
Cdd:COG0666  212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1433-1524 2.79e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 2.79e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   1433 LQRAARLGYEEVVLYCLENKiCDVNHRDNAGYCALHEACARGWLNIVRHLLEYgADVNCSAQDGTrPLHDAVENDHLEIV 1512
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRT-ALHYAARSGHLEIV 77

                           90
                   ....*....|..
gi 21071037   1513 RLLLSYGADPTL 1524
Cdd:pfam12796   78 KLLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1422-1531 1.54e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.17  E-value: 1.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037 1422 LIVNKNAGETLLQRAARLGYEEVVLYCLENKICDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLH 1501
Cdd:COG0666   46 ALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLH 125

                         90       100       110
                 ....*....|....*....|....*....|
gi 21071037 1502 DAVENDHLEIVRLLLSYGADPTLATYSGRT 1531
Cdd:COG0666  126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1467-1533 4.25e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 4.25e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21071037   1467 LHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGAdpTLATYSGRTIM 1533
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTAL 65
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1430-1551 2.16e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.15  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037  1430 ETLLQRAARLGYEEVVLYCLENKiCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHL 1509
Cdd:PHA03100  160 KLLIDKGVDINAKNRVNYLLSYG-VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21071037  1510 EIVRLLLSYGAD-----PTL-----ATYSGRTIMKMTHSELMEKFLTD---YLND 1551
Cdd:PHA03100  239 EIFKLLLNNGPSiktiiETLlyfkdKDLNTITKIKMLKKSIMYMFLLDpgfYKNR 293
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1424-1490 1.68e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 1.68e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21071037   1424 VNKNAGETLLQRAARLGYEEVVLYCLENkiCDVNHRDNaGYCALHEACARGWLNIVRHLLEYGADVN 1490
Cdd:pfam12796   25 LQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADIN 88
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1364-1518 3.45e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.92  E-value: 3.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037  1364 RKRPEPSSDYDLSPAKQEpkpFDRLQQLLPASQSTQLPCSSSPQETTQSRPMPPearrlIVNKNAGETLLQRAArlGYEE 1443
Cdd:PTZ00322   26 KRRAKPISFERMAAIQEE---IARIDTHLEALEATENKDATPDHNLTTEEVIDP-----VVAHMLTVELCQLAA--SGDA 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21071037  1444 VVLYCLENKICDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSY 1518
Cdd:PTZ00322   96 VGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1418-1531 2.08e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 2.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037 1418 EARRLIVNKNAGETLLQRAARLGYEEVVLYCLENKICDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGT 1497
Cdd:COG0666    9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 21071037 1498 RPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT 1531
Cdd:COG0666   89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGET 122
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1417-1531 2.71e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037  1417 PEARRLIVNKNA--------GETLLQRAA--RLGYEEVVLYcLENKICDVNHRDNAGYCALHEA--CARGWLNIVRHLLE 1484
Cdd:PHA03100   86 KEIVKLLLEYGAnvnapdnnGITPLLYAIskKSNSYSIVEY-LLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLID 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21071037  1485 YGADVNcsAQD------------------GTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT 1531
Cdd:PHA03100  165 KGVDIN--AKNrvnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1479-1535 5.24e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 5.24e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 21071037  1479 VRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKM 1535
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
Ank_4 pfam13637
Ankyrin repeats (many copies);
1466-1516 2.51e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 2.51e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 21071037   1466 ALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLL 1516
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1455-1531 5.01e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 5.01e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21071037  1455 DVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT 1531
Cdd:PHA02874  116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1433-1532 5.86e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.34  E-value: 5.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037  1433 LQRAARLGYEEVVLYCleNKICDVNHRDNAGYCALH-------EACARgwlnIVRHLLEYGADVNCSAQDGTRPLHDAVE 1505
Cdd:PHA03095   19 LLNASNVTVEEVRRLL--AAGADVNFRGEYGKTPLHlylhyssEKVKD----IVRLLLEAGADVNAPERCGFTPLHLYLY 92

                          90       100
                  ....*....|....*....|....*...
gi 21071037  1506 NDH-LEIVRLLLSYGADPTLATYSGRTI 1532
Cdd:PHA03095   93 NATtLDVIKLLIKAGADVNAKDKVGRTP 120
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 257-673 2.16e-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: 56.08  E-value: 2.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037    257 IPSSLASPMRLSTPSASPaipPLVHCADKSLPWKMGVSPG-NPVDSHAYPHiQNSKQPRVPSAKAVTSGLPGDTALLLPp 335
Cdd:pfam05109  448 LPSSTHVPTNLTAPASTG---PTVSTADVTSPTPAGTTSGaSPVTPSPSPR-DNGTESKAPDMTSPTSAVTTPTPNATS- 522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037    336 sprpsprvhlPTqPAADTYSEFHKHYARISTSPSVALSKPYMTVSSEFPAARLS--NGKYP---KAPEGGEGAQPVPGHA 410
Cdd:pfam05109  523 ----------PT-PAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPtpNATIPtlgKTSPTSAVTTPTPNAT 591

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037    411 RKTAVQDRKDGSSPP-LLEKQTVTKDVTDKPLDLSSKVV----DVDASKADHMKkMAPTVLVHSRAGSGLVLSGSEIPKE 485
Cdd:pfam05109  592 SPTVGETSPQANTTNhTLGGTSSTPVVTSPPKNATSAVTtgqhNITSSSTSSMS-LRPSSISETLSPSTSDNSTSHMPLL 670

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037    486 TLSPPGNGCAIYRSEIISTAPSSWVVPGPSPNEENNGKSMSLKNkaldwaipqqrSSSCPRMGGTDAvitnvsgsvsSAG 565
Cdd:pfam05109  671 TSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGN-----------SSTSTKPGEVNV----------TKG 729

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037    566 RPASASPAPNANAdGTKTSrssvetTPSVIQHVGQPPATPA-KHSSS---------TSSKGAKASNPEPSFKANENGLPP 635
Cdd:pfam05109  730 TPPKNATSPQAPS-GQKTA------VPTVTSTGGKANSTTGgKHTTGhgartstepTTDYGGDSTTPRTRYNATTYLPPS 802

                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 21071037    636 SSIFLSPNEAFRSPPIPYPRSYLPYPAPEGIAVSPLSL 673
Cdd:pfam05109  803 TSSKLRPRWTFTSPPVTTAQATVPVPPTSQPRFSNLSM 840
Ank_5 pfam13857
Ankyrin repeats (many copies);
1482-1535 5.56e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 5.56e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 21071037   1482 LLEYG-ADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKM 1535
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1429-1542 9.29e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 9.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037  1429 GETLLQRAARLGYEEVVLYCLENKiCDVNHRDNAGYCALHEACA-------------------------------RGWLN 1477
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAISakhhkifrilyhfasisdphaagdllctaakRNDLT 636

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21071037  1478 IVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATysgrTIMKMTHSELME 1542
Cdd:PLN03192  637 AMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN----TDDDFSPTELRE 697
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1441-1535 7.45e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 7.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037  1441 YEEVVLYCLENKiCDVNHRDNAGYCALH-----EACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVEN--DHLEIVR 1513
Cdd:PHA03100   47 NIDVVKILLDNG-ADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVE 125

                          90       100
                  ....*....|....*....|..
gi 21071037  1514 LLLSYGADPTLATYSGRTIMKM 1535
Cdd:PHA03100  126 YLLDNGANVNIKNSDGENLLHL 147
Ank_4 pfam13637
Ankyrin repeats (many copies);
1431-1483 1.24e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 1.24e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 21071037   1431 TLLQRAARLGYEEVVLYCLENKIcDVNHRDNAGYCALHEACARGWLNIVRHLL 1483
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
1449-1501 2.08e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 2.08e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 21071037   1449 LENKICDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLH 1501
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1478-1522 3.53e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 3.53e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 21071037  1478 IVRHLLEYGADVNCSAQD-GTRPLHDAVENDHLEIVRLLLSYGADP 1522
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANV 194
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1477-1545 3.88e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.12  E-value: 3.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037  1477 NIVRHLLEYGADVNCSAQDGTRPLH-----DAVENDHLEIVRLLLSYGADPTLATYSGRTIM------KMTHSELMEKFL 1545
Cdd:PHA03100   49 DVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLlyaiskKSNSYSIVEYLL 128
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1401-1521 4.06e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037  1401 PCSSSPQETTQSRPMPPEARRLI-VN-KN-AGETLLQRAARLGYEEVVLYCLENKICDVNHRDNAGYCALHEACARG-WL 1476
Cdd:PHA02876  276 PLHHASQAPSLSRLVPKLLERGAdVNaKNiKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNK 355

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 21071037  1477 NIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGAD 1521
Cdd:PHA02876  356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1455-1532 4.59e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.10  E-value: 4.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037  1455 DVNHRDNAGYCALHeACARG-WLN--IVRHLLEYGADVNCSAQDGTRPLHDAVENDH--LEIVRLLLSYGADPTLATYSG 1529
Cdd:PHA03095  109 DVNAKDKVGRTPLH-VYLSGfNINpkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRF 187


                  ...
gi 21071037  1530 RTI 1532
Cdd:PHA03095  188 RSL 190
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1499-1524 9.12e-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: 9.12e-05
                            10        20
                    ....*....|....*....|....*.
gi 21071037    1499 PLHDAVENDHLEIVRLLLSYGADPTL 1524
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1409-1531 9.20e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 9.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037  1409 TTQSRPMPPEARRLI-----VN--KNAGETLLQRAARLGYEEV--VLYCLENKICDVNHRDNAGYCALH-EACARGWLNI 1478
Cdd:PHA03095   20 LNASNVTVEEVRRLLaagadVNfrGEYGKTPLHLYLHYSSEKVkdIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDV 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21071037  1479 VRHLLEYGADVNCSAQDGTRPLHD--AVENDHLEIVRLLLSYGADPTLATYSGRT 1531
Cdd:PHA03095  100 IKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMT 154
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1463-1491 1.63e-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: 1.63e-04
                           10        20
                   ....*....|....*....|....*....
gi 21071037   1463 GYCALHEACARGWLNIVRHLLEYGADVNC 1491
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1429-1535 2.05e-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: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037 1429 GETLLQRAARLGYEEVVLYCLENKICDVNHRDN----AGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGT------- 1497
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpk 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 21071037 1498 -------RPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKM 1535
Cdd:cd22192  131 nliyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1422-1521 2.15e-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: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037 1422 LIVNKNAGETLLQRAARLGYEEVVLYCLENKICDVNHRDNAGYCALHEACARGWLNIVRHLLEYGAD-VN----CSAQDG 1496
Cdd:cd22192   10 LLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNepmtSDLYQG 89

                         90       100
                 ....*....|....*....|....*
gi 21071037 1497 TRPLHDAVENDHLEIVRLLLSYGAD 1521
Cdd:cd22192   90 ETALHIAVVNQNLNLVRELIARGAD 114
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1467-1526 2.46e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 2.46e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21071037  1467 LHEACARGWLNIVRHLLEYGADVN-CSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLAT 1526
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPN 132
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1433-1535 2.59e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.64  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037  1433 LQRAARLGYEEVVLYCLENKiCDVNHRDNAGYCALHEACARGW-LNIVRHLLEYGADVNC-SAQDGTRPLHDAVENDhlE 1510
Cdd:PHA02878  205 LHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCKdYDILKLLLEHGVDVNAkSYILGLTALHSSIKSE--R 281

                          90       100
                  ....*....|....*....|....*
gi 21071037  1511 IVRLLLSYGADPTLATYSGRTIMKM 1535
Cdd:PHA02878  282 KLKLLLEYGADINSLNSYKLTPLSS 306
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1449-1540 2.73e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037  1449 LENKICdVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDG-TRPLHDAVENDHLEIVRLLLSYGADPTLATy 1527
Cdd:PHA02875  155 IDHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF- 232

                          90
                  ....*....|...
gi 21071037  1528 sgrTIMKMTHSEL 1540
Cdd:PHA02875  233 ---MIEGEECTIL 242
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1495-1526 3.35e-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: 3.35e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 21071037   1495 DGTRPLHDAVE-NDHLEIVRLLLSYGADPTLAT 1526
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1454-1531 3.54e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037  1454 CDVNHRDNAGYCALHEA-----CARGwlnIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYS 1528
Cdd:PHA03095  213 CDPAATDMLGNTPLHSMatgssCKRS---LVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD 289


                  ...
gi 21071037  1529 GRT 1531
Cdd:PHA03095  290 GNT 292
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1430-1519 3.89e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037  1430 ETLLQRAARLGYEEVVLYCLENKiCDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHL 1509
Cdd:PHA02874  125 KTFLHYAIKKGDLESIKMLFEYG-ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDY 203

                          90
                  ....*....|
gi 21071037  1510 EIVRLLLSYG 1519
Cdd:PHA02874  204 ACIKLLIDHG 213
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1455-1517 4.54e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 4.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21071037  1455 DVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLS 1517
Cdd:PHA03095  249 SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1476-1534 4.77e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 4.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 21071037  1476 LNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMK 1534
Cdd:PHA02876  158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLE 216
Ank_4 pfam13637
Ankyrin repeats (many copies);
1496-1545 5.17e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 5.17e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 21071037   1496 GTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIM----KMTHSELMEKFL 1545
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALhfaaSNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1463-1491 7.07e-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: 7.07e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 21071037   1463 GYCALHEACAR-GWLNIVRHLLEYGADVNC 1491
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNA 31
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1455-1531 8.59e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 8.59e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21071037  1455 DVNHRD-NAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT 1531
Cdd:PHA02878  159 DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1423-1558 9.04e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.72  E-value: 9.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037  1423 IVNKNAGETLLQRAARLGYEEVVLYCLeNKICDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHD 1502
Cdd:PHA02878  162 MKDRHKGNTALHYATENKDQRLTELLL-SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHI 240

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 21071037  1503 AVEN-DHLEIVRLLLSYGADPTLATY-SGRTIMKMT-HSELMEKFLTDYLNDLQGRNDD 1558
Cdd:PHA02878  241 SVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSiKSERKLKLLLEYGADINSLNSY 299
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 1463-1522 1.65e-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: 1.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21071037 1463 GYCALHEACARGWLNIVRHLLEYGADVNCSAQD-------------GTRPLHDAVENDHLEIVRLLLSYGADP 1522
Cdd:cd21882   73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQP 145
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
503-720 4.00e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.79  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   503 STAPSSWVVPGPSPNEENNGKSMSLKNKALdwaiPQQRSSSCPRMGGTDAVITNVSGSVSSAGRPASASPAPNANADGTK 582
Cdd:PRK12323  404 AAPAAAPAAAAAARAVAAAPARRSPAPEAL----AAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAA 479

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   583 TSRSsvettpsviqhvgQPPATPAKHSSSTSS-KGAKASNPEPSFKANENGLPPSSIFLSPNEAFRSPPIPYPRsylPYP 661
Cdd:PRK12323  480 PARA-------------APAAAPAPADDDPPPwEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFET---LAP 543

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   662 APEGIAVSPLSLHGKGPVYPHPVLLPNGSLFPGHLAPKPGLPYGLP-TGRPEFVTYQDAL 720
Cdd:PRK12323  544 APAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPALAARLPvRGLAQQLARQSEL 603
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1455-1516 5.85e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 5.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21071037  1455 DVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLL 1516
Cdd:PHA02876  170 DVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
PHA02946 PHA02946
ankyin-like protein; Provisional
 1461-1562 7.32e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 7.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037  1461 NAGYCALHEACARGWLN--IVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRT---IMKM 1535
Cdd:PHA02946   35 SGNYHILHAYCGIKGLDerFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTplyYLSG 114

                          90       100
                  ....*....|....*....|....*....
gi 21071037  1536 THSELMEK--FLTDYLNDLQGRNDDDASG 1562
Cdd:PHA02946  115 TDDEVIERinLLVQYGAKINNSVDEEGCG 143
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 482-700 9.64e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 40.68  E-value: 9.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   482 IPKETLSPPGNGCAiyrsEIISTAPSSWVVPGP--SPNEENNGKSMSLKNKALD------------WAIPQQRSSSCPRM 547
Cdd:PLN03209  323 IPSQRVPPKESDAA----DGPKPVPTKPVTPEApsPPIEEEPPQPKAVVPRPLSpytayedlkpptSPIPTPPSSSPASS 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   548 GGTDAVITNVSGSVSSAGRPASASPAPNANADGTKTSRSsveTTPSVIQHVGQPPATPakhsSSTSSKGAKASNPEPSFK 627
Cdd:PLN03209  399 KSVDAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRP---LSPYARYEDLKPPTSP----SPTAPTGVSPSVSSTSSV 471

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071037   628 ANENGLPPSSIFLS---PNEAFRSPPIPYPRSYLPYPAPegiAVSPLSLHGKGPVYPHPVLLPNGSLFPG--------HL 696
Cdd:PLN03209  472 PAVPDTAPATAATDaaaPPPANMRPLSPYAVYDDLKPPT---SPSPAAPVGKVAPSSTNEVVKVGNSAPPtaladeqhHA 548


                  ....
gi 21071037   697 APKP 700
Cdd:PLN03209  549 QPKP 552
 
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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