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Conserved domains on  [gi|30352010|ref|NP_775617|]
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protein IWS1 homolog [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TFIIS_I super family cl00146
N-terminal domain (domain I) of transcription elongation factor S-II (TFIIS); similar to a ...
475-739 3.25e-29

N-terminal domain (domain I) of transcription elongation factor S-II (TFIIS); similar to a domain found in elongin A and CRSP70; likely to be involved in transcription; domain I from TFIIS interacts with RNA polymerase II holoenzyme


The actual alignment was detected with superfamily member COG5139:

Pssm-ID: 469629  Cd Length: 397  Bit Score: 120.57  E-value: 3.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010 475 DFEMMLQRKKSMCGKRRRNRDGGTFISDADDVVSAMIVKMNEAAEEDRQLNNQKKPALKKLTLLPTVVMHLKKQDLKETF 554
Cdd:COG5139 126 ELGDTGDRQLKAPAASRARRKEDLLEQTVDEISLRLKKRMQDAAKKDNANNLEGRPATGKIKNLPEVSDVLMKKALQDTI 205
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010 555 IDSGVMSAIKEWLSPLPDRSLPALKIREELLKILQELPsVSQETLKHSGIGRAVMYLYKHPKESRSNKDMAGKLINEWSR 634
Cdd:COG5139 206 LDNNILDSVRGWLEPLPDKSLPNIKIQKSLLDVLKTLP-IHTEHLVESGVGRIVYFYTISKKEEKEVRRSAKALVQEWTR 284
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010 635 PIFGLTSNYKGmTREEREQRDLEQMPQRRRLSSTGGQTpRRDLEKVLTGEEKALRPGDPGFCARARV---PMPSNKDYVV 711
Cdd:COG5139 285 PIIKPSGNYRD-KRIMQLEFDSEKLRKKSVMDSAKNRK-KKSSGEDPTSRGSSVQTLYEQAAARRNRaaaPAQTTTDYKY 362
                       250       260       270
                ....*....|....*....|....*....|....*
gi 30352010 712 RP-------KWNVEMESSRFQASSKKGISRLDKQM 739
Cdd:COG5139 363 APvsnlsavPTNARAVGVGSTLNNSEMYKRLTSRL 397
MSCRAMM_ClfA super family cl41352
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
66-428 1.05e-11

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


The actual alignment was detected with superfamily member NF033609:

Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 68.78  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   66 GTDSENDEPSNANASDSESEElhrPKDSDSDSEEHAESpASDSENEPVNQHGSDSENeellnghASDSEKEEVSKHAASD 145
Cdd:NF033609 566 GSDSGSDSSNSDSGSDSGSDS---TSDSGSDSASDSDS-ASDSDSASDSDSASDSDS-------ASDSDSASDSDSASDS 634
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  146 SEAEDTLQPQVSESDSEDPPRPQASDSENEEPPKPRISDSESEELPKPRVSDSESEDPPRPQASDSESE-ELPKPRVSDS 224
Cdd:NF033609 635 DSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDS 714
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  225 ESE-DPPRPQASDSESEELPKPRVSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESDGHTDRKG 303
Cdd:NF033609 715 DSDsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 794
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  304 LHSSDSEEEEPKRQKIDSDDDEEKEGDEEKVAKRKAAVLSDSEDDAGNASAKKSRVVCDADDSDSDVVSDKSGKRETTVA 383
Cdd:NF033609 795 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVP 874
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 30352010  384 SDSEEEAGKEESSVKKKEDKDLFGSDSESGNEEENLIADIFGESG 428
Cdd:NF033609 875 PNSPKNGTNASNKNEAKDSKEPLPDTGSEDEANTSLIWGLLASLG 919
 
Name Accession Description Interval E-value
COG5139 COG5139
Uncharacterized conserved protein [Function unknown];
475-739 3.25e-29

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227468  Cd Length: 397  Bit Score: 120.57  E-value: 3.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010 475 DFEMMLQRKKSMCGKRRRNRDGGTFISDADDVVSAMIVKMNEAAEEDRQLNNQKKPALKKLTLLPTVVMHLKKQDLKETF 554
Cdd:COG5139 126 ELGDTGDRQLKAPAASRARRKEDLLEQTVDEISLRLKKRMQDAAKKDNANNLEGRPATGKIKNLPEVSDVLMKKALQDTI 205
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010 555 IDSGVMSAIKEWLSPLPDRSLPALKIREELLKILQELPsVSQETLKHSGIGRAVMYLYKHPKESRSNKDMAGKLINEWSR 634
Cdd:COG5139 206 LDNNILDSVRGWLEPLPDKSLPNIKIQKSLLDVLKTLP-IHTEHLVESGVGRIVYFYTISKKEEKEVRRSAKALVQEWTR 284
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010 635 PIFGLTSNYKGmTREEREQRDLEQMPQRRRLSSTGGQTpRRDLEKVLTGEEKALRPGDPGFCARARV---PMPSNKDYVV 711
Cdd:COG5139 285 PIIKPSGNYRD-KRIMQLEFDSEKLRKKSVMDSAKNRK-KKSSGEDPTSRGSSVQTLYEQAAARRNRaaaPAQTTTDYKY 362
                       250       260       270
                ....*....|....*....|....*....|....*
gi 30352010 712 RP-------KWNVEMESSRFQASSKKGISRLDKQM 739
Cdd:COG5139 363 APvsnlsavPTNARAVGVGSTLNNSEMYKRLTSRL 397
Med26 pfam08711
TFIIS helical bundle-like domain; Mediator is a large complex of up to 33 proteins that is ...
583-636 3.22e-12

TFIIS helical bundle-like domain; Mediator is a large complex of up to 33 proteins that is conserved from plants to fungi to humans - the number and representation of individual subunits varying with species {1-2]. It is arranged into four different sections, a core, a head, a tail and a kinase-activity part, and the number of subunits within each of these is what varies with species. Overall, Mediator regulates the transcriptional activity of RNA polymerase II but it would appear that each of the four different sections has a slightly different function. Mediator exists in two major forms in human cells: a smaller form that interacts strongly with pol II and activates transcription, and a large form that does not interact strongly with pol II and does not directly activate transcription. Notably, the 'small' and 'large' Mediator complexes differ in their subunit composition: the Med26 subunit preferentially associates with the small, active complex, whereas cdk8, cyclin C, Med12 and Med13 associate with the large Mediator complex. This family includesthe C terminal region of a number of eukaryotic hypothetical proteins which are homologous to the Saccharomyces cerevisiae protein IWS1. IWS1 is known to be an Pol II transcription elongation factor and interacts with Spt6 and Spt5.


Pssm-ID: 462573 [Multi-domain]  Cd Length: 52  Bit Score: 61.76  E-value: 3.22e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 30352010   583 ELLKILQELPsVSQETLKHSGIGRAVMYLYKHPkESRSNKDMAGKLINEWSRPI 636
Cdd:pfam08711   1 KLLKKLEKLP-VTLELLKSTGIGKVVNKLRKHK-ENPEIKKLAKELVKKWKRLV 52
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
66-428 1.05e-11

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 68.78  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   66 GTDSENDEPSNANASDSESEElhrPKDSDSDSEEHAESpASDSENEPVNQHGSDSENeellnghASDSEKEEVSKHAASD 145
Cdd:NF033609 566 GSDSGSDSSNSDSGSDSGSDS---TSDSGSDSASDSDS-ASDSDSASDSDSASDSDS-------ASDSDSASDSDSASDS 634
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  146 SEAEDTLQPQVSESDSEDPPRPQASDSENEEPPKPRISDSESEELPKPRVSDSESEDPPRPQASDSESE-ELPKPRVSDS 224
Cdd:NF033609 635 DSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDS 714
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  225 ESE-DPPRPQASDSESEELPKPRVSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESDGHTDRKG 303
Cdd:NF033609 715 DSDsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 794
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  304 LHSSDSEEEEPKRQKIDSDDDEEKEGDEEKVAKRKAAVLSDSEDDAGNASAKKSRVVCDADDSDSDVVSDKSGKRETTVA 383
Cdd:NF033609 795 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVP 874
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 30352010  384 SDSEEEAGKEESSVKKKEDKDLFGSDSESGNEEENLIADIFGESG 428
Cdd:NF033609 875 PNSPKNGTNASNKNEAKDSKEPLPDTGSEDEANTSLIWGLLASLG 919
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
3-312 6.25e-11

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 66.09  E-value: 6.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    3 SEYYSGDQSDDGGATPVQDERDSGSDGEDGVTEQHSGSDTGSV-DHHSENETSDREDGLAKIHNGTDSENDEPSNANASD 81
Cdd:NF033609 571 SDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSAsDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDS 650
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   82 SESEELHRPKDSDSDSEEHAESpASDSENEPVNQHGSDSENEellnghaSDSEKEEVSKHAASDSEAEDTLQPQVSESDS 161
Cdd:NF033609 651 DSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSD-------SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 722
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  162 eDPPRPQASDSENEeppkpriSDSESEELPKPRVSDSESEDPPRPQASDSESEelpkprvSDSESE-DPPRPQASDSESE 240
Cdd:NF033609 723 -DSDSDSDSDSDSD-------SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD-------SDSDSDsDSDSDSDSDSDSD 787
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30352010  241 ELPKPRVSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESDGHTDRKGLHSSDSEEE 312
Cdd:NF033609 788 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESD 859
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
96-418 3.52e-09

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 60.31  E-value: 3.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   96 DSEEHAESPASDSENEPVNQHGSDSENEELLNGHASDSEKEEVSKHAASDSEAEDTLQPQVSESDSEDPPRPQASDSENE 175
Cdd:NF033609 549 DEPGEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDS 628
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  176 EPPKPRISDSESEELPKPRVSDSESEDPPRPQASDSESEelpkprvSDSESEdpprpqaSDSESEELPKPRVSDSESEDP 255
Cdd:NF033609 629 DSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSD-------SDSDSD-------SDSDSDSDSDSDSDSDSDSDS 694
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  256 QKGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESDGHTDRKGLHSSDSEEEEPKRQKIDSDDDEEKEGDEEKVA 335
Cdd:NF033609 695 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 774
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  336 KRKAAVLSDSEDDAGNASAKKSRVVCDADDSDSDVVSDKSGK-RETTVASDSEEEAGKEESSVKKKEDKDLFGSDSESGN 414
Cdd:NF033609 775 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 854

                 ....
gi 30352010  415 EEEN 418
Cdd:NF033609 855 DSES 858
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
2-300 7.16e-09

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 59.54  E-value: 7.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    2 DSEYYSGDQSDDGGATPVQDERDSGSDGE-----DGVTEQHSGSDTGSV-DHHSENETSDREDGLAKIHNGTDSENDEPS 75
Cdd:NF033609 589 DSGSDSASDSDSASDSDSASDSDSASDSDsasdsDSASDSDSASDSDSAsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 668
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   76 NANASDSESEELHRPKDSDSDSEEHAESpASDSENEPVNQHGSDSENEellNGHASDSEKEEVSKHAASDSEAEDTLQPQ 155
Cdd:NF033609 669 DSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSD---SDSDSDSDSDSDSDSDSDSDSDSDSDSDS 744
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  156 VSESDSEDPPRPQASDSENEEPPKPRISDSESEelpkprvSDSESE-DPPRPQASDSESEelpkprvSDSESEdpprpqa 234
Cdd:NF033609 745 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD-------SDSDSDsDSDSDSDSDSDSD-------SDSDSD------- 803
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30352010  235 SDSESEelpkprvSDSESE-DPQKGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESDGHTD 300
Cdd:NF033609 804 SDSDSD-------SDSDSDsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSD 863
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
95-317 1.14e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.48  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    95 SDSEEHAESPASD-SENEPVNQHGSDSENEELLNGHASDSEKEEVSKHAASDSEAEDTLQPQVSESDSEDPPRPQASDSE 173
Cdd:PHA03307  121 PPPASPPPSPAPDlSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPA 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   174 NEEPPKPRISDSESEELPKPRVSDSESEDPPRPQASDSESEELPKPRVSDSESEDP-PRP----------QASDSESEEL 242
Cdd:PHA03307  201 AASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPlPRPapitlptriwEASGWNGPSS 280
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30352010   243 PKPRVSdSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGENkREDSEVQNESDGHTDRK-GLHSSDSEEEEPKRQ 317
Cdd:PHA03307  281 RPGPAS-SSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSS-RESSSSSTSSSSESSRGaAVSPGPSPSRSPSPS 354
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
11-260 2.27e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 51.31  E-value: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    11 SDDGGATPV-QDERDSGSDGEDGVTEQHSGSDTGSVDHHSENETSDREDGLAKIHNGTD---SENDEPSNANASDSESEE 86
Cdd:pfam03154  27 SPDGRASPTnEDLRSSGRNSPSAASTSSNDSKAESMKKSSKKIKEEAPSPLKSAKRQREkgaSDTEEPERATAKKSKTQE 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    87 LHRPkdsDSDSEEHAESpasdSENEPVNQHG-SDSENEELLNGHASDSEKEEVSKHAASDSEAEDT-LQPQVSESDSEDP 164
Cdd:pfam03154 107 ISRP---NSPSEGEGES----SDGRSVNDEGsSDPKDIDQDNRSTSPSIPSPQDNESDSDSSAQQQiLQTQPPVLQAQSG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   165 PRPQASDSENEEPPKPRISDSESEELPKPRVSDSESEDPPRPQASDSeseelPKPRVSDSESEDPPRPQASDSESEELPK 244
Cdd:pfam03154 180 AASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAA-----PHTLIQQTPTLHPQRLPSPHPPLQPMTQ 254
                         250
                  ....*....|....*.
gi 30352010   245 PRVSDSESEDPQKGPA 260
Cdd:pfam03154 255 PPPPSQVSPQPLPQPS 270
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
2-288 1.20e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 49.14  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    2 DSEYYSGDQSDDGGATPVQDERDSGSDgEDGVTEQHSGSDTGSvDHHSENETSDREDGLAKIHNGTDSENDEPSNANASD 81
Cdd:NF033609 647 DSDSDSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 724
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   82 SESEELHRPKDSDSDSEEHAESPaSDSENEPVNQHGSDSENEEllnghASDSEKEEVSKHAASDSEAEDTLQPQVSESDS 161
Cdd:NF033609 725 DSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDS-----DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 798
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  162 EdpprpqaSDSENEeppkpriSDSESEELPKPRVSDSESEDPPRPQASDSESEELPKPRVSDSESEDPPRPQASDSESEe 241
Cdd:NF033609 799 D-------SDSDSD-------SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSD- 863
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 30352010  242 lpkprvSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGENKRED 288
Cdd:NF033609 864 ------SESGSNNNVVPPNSPKNGTNASNKNEAKDSKEPLPDTGSED 904
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
162-475 1.86e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 48.37  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  162 EDPPRPQASDSENEEPPKPRISDSESEElpkPRVSDSESEDPPRPQASDSESEELPKPRVSDSESEDPPRPQASDSESEE 241
Cdd:NF033609 540 DKPVVPEQPDEPGEIEPIPEDSDSDPGS---DSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDS 616
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  242 LPKPRVSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESDGHTDRKGLHSSDSEEEEPKRQKIDS 321
Cdd:NF033609 617 DSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 696
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  322 DDDEEKEGDEEKVAKRKAAVLSDSEDDAGNASAKKSRVVCDADDSDSDVVSDKS---GKRETTVASDSEEEAGKEESSVK 398
Cdd:NF033609 697 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsdSDSDSDSDSDSDSDSDSDSDSDS 776
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30352010  399 KKEDKDLFGSDSESGNEEENLIADIFGESGDEEEEEFTGFNQEDLEEEKNETQLKEAEDSDSDDNIKRGKHMDFLSD 475
Cdd:NF033609 777 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 853
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
205-462 2.04e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 44.99  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    205 RPQASDSESEELPKPRVSDSESEDPPRPQASDSESE-ELPKPRVSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGE 283
Cdd:TIGR00927  619 RPVAKVMALGDLSKGDVAEAEHTGERTGEEGERPTEaEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGE 698
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    284 NKREDSEVQNESDGHTDRKGLHSSDsEEEEPKRQKIDSDDDEEKEGDEEKVAKRKAAVLSDSEDDAGNASAKKSRVVCDA 363
Cdd:TIGR00927  699 IEAKEADHKGETEAEEVEHEGETEA-EGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKED 777
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    364 DDS----DSDVVSDKSGKRETTVASDSEEEAGKEESSVKKKEDKDLFGSDSESGNEEENLIADIFGESGDEEE-----EE 434
Cdd:TIGR00927  778 EDEgeiqAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKgvdggGG 857
                          250       260
                   ....*....|....*....|....*...
gi 30352010    435 FTGFNQEDLEEEKNETQLKEAEDSDSDD 462
Cdd:TIGR00927  858 SDGGDSEEEEEEEEEEEEEEEEEEEEEE 885
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
7-468 3.10e-03

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 41.15  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    7 SGDQSDDGGATPVQDERDSGSDGEDGVTEQHSgSDTGSVDHHSENETSDREDGLAKIHNGTDSENDEPSNANASDSESEE 86
Cdd:COG5271  552 DADETDEPEATAEEDEPDEAEAETEDATENAD-ADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEE 630
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   87 LHRPKDSDSDSEEHAESPASDSENEPVNQHGSDSENEELLNGHASDSEKEEVSKHAASDSEAEDTLQpqVSESDSEDPPR 166
Cdd:COG5271  631 EAAEDEAAEPETDASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAAAAEASDDEEE--TEEADEDAETA 708
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  167 PQASDSENEEPPKPRISDSESEelPKPRVSDSESEDPPRPQASDSESEELPKPRVSDSESedpprpQASDSESEELPKPR 246
Cdd:COG5271  709 SEEADAEEADTEADGTAEEAEE--AAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDA------DGLEEALEEEKADA 780
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  247 VSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESDGHTDRKGLHSSDSEEEEPKRQKIDSDDDEE 326
Cdd:COG5271  781 EEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDA 860
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  327 KEGDEEKVAK-RKAAVLSDSEDDAGNASAKKSRVVCDADDSDSDVVSDKSGKRETTVASDSEEEAGKEESSVKKKEDKDL 405
Cdd:COG5271  861 DLDLDADLAAdEHEAEEAQEAETDADADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDEL 940
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30352010  406 FGSDSESGNEEENLIADIFGESGDEEEEEFTGFNQEDLEEEKNETQLKEAEDSDSDDNIKRGK 468
Cdd:COG5271  941 GAAEDDLDALALDEAGDEESDDAAADDAGDDSLADDDEALADAADDAEADDSELDASESTGEA 1003
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
152-280 6.09e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 40.14  E-value: 6.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  152 LQPQVSESDSEDPPRPQASDSE-NEEPPKPRISDSESEELPKPRVsdseSEDPPRPQASDSESEELPKPRVSDSesedPP 230
Cdd:NF033839 365 VKPQPEKPKPEVKPQPETPKPEvKPQPEKPKPEVKPQPEKPKPEV----KPQPEKPKPEVKPQPEKPKPEVKPQ----PE 436
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30352010  231 RPQASDSESEELPKPRV-SDSESEDPQKGPASDSEAEDASRHKEKPDSDDS 280
Cdd:NF033839 437 KPKPEVKPQPEKPKPEVkPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNS 487
 
Name Accession Description Interval E-value
COG5139 COG5139
Uncharacterized conserved protein [Function unknown];
475-739 3.25e-29

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227468  Cd Length: 397  Bit Score: 120.57  E-value: 3.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010 475 DFEMMLQRKKSMCGKRRRNRDGGTFISDADDVVSAMIVKMNEAAEEDRQLNNQKKPALKKLTLLPTVVMHLKKQDLKETF 554
Cdd:COG5139 126 ELGDTGDRQLKAPAASRARRKEDLLEQTVDEISLRLKKRMQDAAKKDNANNLEGRPATGKIKNLPEVSDVLMKKALQDTI 205
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010 555 IDSGVMSAIKEWLSPLPDRSLPALKIREELLKILQELPsVSQETLKHSGIGRAVMYLYKHPKESRSNKDMAGKLINEWSR 634
Cdd:COG5139 206 LDNNILDSVRGWLEPLPDKSLPNIKIQKSLLDVLKTLP-IHTEHLVESGVGRIVYFYTISKKEEKEVRRSAKALVQEWTR 284
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010 635 PIFGLTSNYKGmTREEREQRDLEQMPQRRRLSSTGGQTpRRDLEKVLTGEEKALRPGDPGFCARARV---PMPSNKDYVV 711
Cdd:COG5139 285 PIIKPSGNYRD-KRIMQLEFDSEKLRKKSVMDSAKNRK-KKSSGEDPTSRGSSVQTLYEQAAARRNRaaaPAQTTTDYKY 362
                       250       260       270
                ....*....|....*....|....*....|....*
gi 30352010 712 RP-------KWNVEMESSRFQASSKKGISRLDKQM 739
Cdd:COG5139 363 APvsnlsavPTNARAVGVGSTLNNSEMYKRLTSRL 397
Med26 pfam08711
TFIIS helical bundle-like domain; Mediator is a large complex of up to 33 proteins that is ...
583-636 3.22e-12

TFIIS helical bundle-like domain; Mediator is a large complex of up to 33 proteins that is conserved from plants to fungi to humans - the number and representation of individual subunits varying with species {1-2]. It is arranged into four different sections, a core, a head, a tail and a kinase-activity part, and the number of subunits within each of these is what varies with species. Overall, Mediator regulates the transcriptional activity of RNA polymerase II but it would appear that each of the four different sections has a slightly different function. Mediator exists in two major forms in human cells: a smaller form that interacts strongly with pol II and activates transcription, and a large form that does not interact strongly with pol II and does not directly activate transcription. Notably, the 'small' and 'large' Mediator complexes differ in their subunit composition: the Med26 subunit preferentially associates with the small, active complex, whereas cdk8, cyclin C, Med12 and Med13 associate with the large Mediator complex. This family includesthe C terminal region of a number of eukaryotic hypothetical proteins which are homologous to the Saccharomyces cerevisiae protein IWS1. IWS1 is known to be an Pol II transcription elongation factor and interacts with Spt6 and Spt5.


Pssm-ID: 462573 [Multi-domain]  Cd Length: 52  Bit Score: 61.76  E-value: 3.22e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 30352010   583 ELLKILQELPsVSQETLKHSGIGRAVMYLYKHPkESRSNKDMAGKLINEWSRPI 636
Cdd:pfam08711   1 KLLKKLEKLP-VTLELLKSTGIGKVVNKLRKHK-ENPEIKKLAKELVKKWKRLV 52
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
66-428 1.05e-11

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 68.78  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   66 GTDSENDEPSNANASDSESEElhrPKDSDSDSEEHAESpASDSENEPVNQHGSDSENeellnghASDSEKEEVSKHAASD 145
Cdd:NF033609 566 GSDSGSDSSNSDSGSDSGSDS---TSDSGSDSASDSDS-ASDSDSASDSDSASDSDS-------ASDSDSASDSDSASDS 634
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  146 SEAEDTLQPQVSESDSEDPPRPQASDSENEEPPKPRISDSESEELPKPRVSDSESEDPPRPQASDSESE-ELPKPRVSDS 224
Cdd:NF033609 635 DSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDS 714
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  225 ESE-DPPRPQASDSESEELPKPRVSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESDGHTDRKG 303
Cdd:NF033609 715 DSDsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 794
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  304 LHSSDSEEEEPKRQKIDSDDDEEKEGDEEKVAKRKAAVLSDSEDDAGNASAKKSRVVCDADDSDSDVVSDKSGKRETTVA 383
Cdd:NF033609 795 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVP 874
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 30352010  384 SDSEEEAGKEESSVKKKEDKDLFGSDSESGNEEENLIADIFGESG 428
Cdd:NF033609 875 PNSPKNGTNASNKNEAKDSKEPLPDTGSEDEANTSLIWGLLASLG 919
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
3-312 6.25e-11

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 66.09  E-value: 6.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    3 SEYYSGDQSDDGGATPVQDERDSGSDGEDGVTEQHSGSDTGSV-DHHSENETSDREDGLAKIHNGTDSENDEPSNANASD 81
Cdd:NF033609 571 SDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSAsDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDS 650
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   82 SESEELHRPKDSDSDSEEHAESpASDSENEPVNQHGSDSENEellnghaSDSEKEEVSKHAASDSEAEDTLQPQVSESDS 161
Cdd:NF033609 651 DSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSD-------SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 722
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  162 eDPPRPQASDSENEeppkpriSDSESEELPKPRVSDSESEDPPRPQASDSESEelpkprvSDSESE-DPPRPQASDSESE 240
Cdd:NF033609 723 -DSDSDSDSDSDSD-------SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD-------SDSDSDsDSDSDSDSDSDSD 787
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30352010  241 ELPKPRVSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESDGHTDRKGLHSSDSEEE 312
Cdd:NF033609 788 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESD 859
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
96-418 3.52e-09

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 60.31  E-value: 3.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   96 DSEEHAESPASDSENEPVNQHGSDSENEELLNGHASDSEKEEVSKHAASDSEAEDTLQPQVSESDSEDPPRPQASDSENE 175
Cdd:NF033609 549 DEPGEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDS 628
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  176 EPPKPRISDSESEELPKPRVSDSESEDPPRPQASDSESEelpkprvSDSESEdpprpqaSDSESEELPKPRVSDSESEDP 255
Cdd:NF033609 629 DSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSD-------SDSDSD-------SDSDSDSDSDSDSDSDSDSDS 694
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  256 QKGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESDGHTDRKGLHSSDSEEEEPKRQKIDSDDDEEKEGDEEKVA 335
Cdd:NF033609 695 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 774
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  336 KRKAAVLSDSEDDAGNASAKKSRVVCDADDSDSDVVSDKSGK-RETTVASDSEEEAGKEESSVKKKEDKDLFGSDSESGN 414
Cdd:NF033609 775 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 854

                 ....
gi 30352010  415 EEEN 418
Cdd:NF033609 855 DSES 858
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
2-300 7.16e-09

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 59.54  E-value: 7.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    2 DSEYYSGDQSDDGGATPVQDERDSGSDGE-----DGVTEQHSGSDTGSV-DHHSENETSDREDGLAKIHNGTDSENDEPS 75
Cdd:NF033609 589 DSGSDSASDSDSASDSDSASDSDSASDSDsasdsDSASDSDSASDSDSAsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 668
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   76 NANASDSESEELHRPKDSDSDSEEHAESpASDSENEPVNQHGSDSENEellNGHASDSEKEEVSKHAASDSEAEDTLQPQ 155
Cdd:NF033609 669 DSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSD---SDSDSDSDSDSDSDSDSDSDSDSDSDSDS 744
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  156 VSESDSEDPPRPQASDSENEEPPKPRISDSESEelpkprvSDSESE-DPPRPQASDSESEelpkprvSDSESEdpprpqa 234
Cdd:NF033609 745 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD-------SDSDSDsDSDSDSDSDSDSD-------SDSDSD------- 803
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30352010  235 SDSESEelpkprvSDSESE-DPQKGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESDGHTD 300
Cdd:NF033609 804 SDSDSD-------SDSDSDsDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSD 863
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
95-317 1.14e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.48  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    95 SDSEEHAESPASD-SENEPVNQHGSDSENEELLNGHASDSEKEEVSKHAASDSEAEDTLQPQVSESDSEDPPRPQASDSE 173
Cdd:PHA03307  121 PPPASPPPSPAPDlSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPA 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   174 NEEPPKPRISDSESEELPKPRVSDSESEDPPRPQASDSESEELPKPRVSDSESEDP-PRP----------QASDSESEEL 242
Cdd:PHA03307  201 AASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPlPRPapitlptriwEASGWNGPSS 280
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30352010   243 PKPRVSdSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGENkREDSEVQNESDGHTDRK-GLHSSDSEEEEPKRQ 317
Cdd:PHA03307  281 RPGPAS-SSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSS-RESSSSSTSSSSESSRGaAVSPGPSPSRSPSPS 354
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
11-260 2.27e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 51.31  E-value: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    11 SDDGGATPV-QDERDSGSDGEDGVTEQHSGSDTGSVDHHSENETSDREDGLAKIHNGTD---SENDEPSNANASDSESEE 86
Cdd:pfam03154  27 SPDGRASPTnEDLRSSGRNSPSAASTSSNDSKAESMKKSSKKIKEEAPSPLKSAKRQREkgaSDTEEPERATAKKSKTQE 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    87 LHRPkdsDSDSEEHAESpasdSENEPVNQHG-SDSENEELLNGHASDSEKEEVSKHAASDSEAEDT-LQPQVSESDSEDP 164
Cdd:pfam03154 107 ISRP---NSPSEGEGES----SDGRSVNDEGsSDPKDIDQDNRSTSPSIPSPQDNESDSDSSAQQQiLQTQPPVLQAQSG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   165 PRPQASDSENEEPPKPRISDSESEELPKPRVSDSESEDPPRPQASDSeseelPKPRVSDSESEDPPRPQASDSESEELPK 244
Cdd:pfam03154 180 AASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAA-----PHTLIQQTPTLHPQRLPSPHPPLQPMTQ 254
                         250
                  ....*....|....*.
gi 30352010   245 PRVSDSESEDPQKGPA 260
Cdd:pfam03154 255 PPPPSQVSPQPLPQPS 270
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
64-270 4.28e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.55  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    64 HNGTDSENDEPSNANASDSESEELHRPKDSD--SDSEEHAESPASDSENEPVNQHGSDSEneellnghASDSEKEEVSKH 141
Cdd:PHA03307  144 PGPPPAASPPAAGASPAAVASDAASSRQAALplSSPEETARAPSSPPAEPPPSTPPAAAS--------PRPPRRSSPISA 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   142 AASDSEAedtlqpqVSESDSEDPPRPQASDSENEEPPkpRISDSESEELPKPRVSDSESEDPPRPQASDSESEELP---K 218
Cdd:PHA03307  216 SASSPAP-------APGRSAADDAGASSSDSSSSESS--GCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPgpaS 286
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30352010   219 PRVSDSESEDPPRPQASDSESEElPKPRVSDSESEDPQKGPASDSEAEDASR 270
Cdd:PHA03307  287 SSSSPRERSPSPSPSSPGSGPAP-SSPRASSSSSSSRESSSSSTSSSSESSR 337
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
90-297 5.51e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 50.07  E-value: 5.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   90 PKDSDSDSEEHAESPASDSENEPVNQHGSDSENEELLNGHASDSEKEEVSKHAASDSEAEDTLQP-QVSESDSEDPPRPQ 168
Cdd:PTZ00449 497 APIEEEDSDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPgPAKEHKPSKIPTLS 576
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  169 ASDSENEEPPKPRisDSESEELPKPRVSDSESEDPP---RPQASD-------SESEELPKPRVSDSESEDPPRPQAsdSE 238
Cdd:PTZ00449 577 KKPEFPKDPKHPK--DPEEPKKPKRPRSAQRPTRPKspkLPELLDipkspkrPESPKSPKRPPPPQRPSSPERPEG--PK 652
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  239 SEELPKPRVSDSESEDPQ-KGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESDG 297
Cdd:PTZ00449 653 IIKSPKPPKSPKPPFDPKfKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPG 712
PHA03321 PHA03321
tegument protein VP11/12; Provisional
161-319 8.62e-06

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 49.19  E-value: 8.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  161 SEDPPRPQASDSENEEPPKPRISDSESEElpKPRVSDSESEDPPRPQASDSESE--ELPKPRVSDSESEDPPRPQA---S 235
Cdd:PHA03321 427 SRQPPGAPAPRRDNDPPPPPRARPGSTPA--CARRARAQRARDAGPEYVDPLGAlrRLPAGAAPPPEPAAAPSPATyytR 504
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  236 DSESEELPKPRVSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESD-GHTDRKGLHSSDSEEEEP 314
Cdd:PHA03321 505 MGGGPPRLPPRNRATETLRPDWGPPAAAPPEQMEDPYLEPDDDRFDRRDGAAAAATSHPREaPAPDDDPIYEGVSDSEEP 584

                 ....*
gi 30352010  315 KRQKI 319
Cdd:PHA03321 585 VYEEI 589
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
48-281 9.74e-06

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 49.27  E-value: 9.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    48 HSENETSDREDGLAKIHNGTDSENDEPSNANASDSESEELHRPKDSDSDSEEHAESPASDSENepvNQHGSDSENEELLN 127
Cdd:PTZ00108 1157 RLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSN---SSGSDQEDDEEQKT 1233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   128 GHASDSEKEEVSKHAASDSEAEDTLQPQVSESDSEDPPR--PQASDSENEEPPKP-RISDSESEELPKPRVSDSESEDPP 204
Cdd:PTZ00108 1234 KPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKnaPKRVSAVQYSPPPPsKRPDGESNGGSKPSSPTKKKVKKR 1313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   205 -RPQASDSESEELPKPRVSDSESEDPPRPQASDSESEEL---PKPRVSDSESEDpqkgpaSDSEAEDASRHKEKPDSDDS 280
Cdd:PTZ00108 1314 lEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLlrrPRKKKSDSSSED------DDDSEVDDSEDEDDEDDEDD 1387

                  .
gi 30352010   281 D 281
Cdd:PTZ00108 1388 D 1388
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
2-288 1.20e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 49.14  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    2 DSEYYSGDQSDDGGATPVQDERDSGSDgEDGVTEQHSGSDTGSvDHHSENETSDREDGLAKIHNGTDSENDEPSNANASD 81
Cdd:NF033609 647 DSDSDSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 724
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   82 SESEELHRPKDSDSDSEEHAESPaSDSENEPVNQHGSDSENEEllnghASDSEKEEVSKHAASDSEAEDTLQPQVSESDS 161
Cdd:NF033609 725 DSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDSDSDSDS-----DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 798
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  162 EdpprpqaSDSENEeppkpriSDSESEELPKPRVSDSESEDPPRPQASDSESEELPKPRVSDSESEDPPRPQASDSESEe 241
Cdd:NF033609 799 D-------SDSDSD-------SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSD- 863
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 30352010  242 lpkprvSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGENKRED 288
Cdd:NF033609 864 ------SESGSNNNVVPPNSPKNGTNASNKNEAKDSKEPLPDTGSED 904
PRK08581 PRK08581
amidase domain-containing protein;
57-302 1.84e-05

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 48.25  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   57 EDGLAKIHNGTDSENDEPSNANaSDSESEELHRPKDSDSDSEEHAESPASDSENEPVNQHGSDSENEELLNGHASDSEKE 136
Cdd:PRK08581  28 DDPQKDSTAKTTSHDSKKSNDD-ETSKDTSSKDTDKADNNNTSNQDNNDKKFSTIDSSTSDSNNIIDFIYKNLPQTNINQ 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  137 EVSKHAASDSEAEDTLQPQVSESDSEDPPRPQASDSENEEPPKPRISDSESEElpkprVSDSESEDPPRPQASDSESEEL 216
Cdd:PRK08581 107 LLTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPRNSEKSTNDSNKNSDSSIKN-----DTDTQSSKQDKADNQKAPSSNN 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  217 PKPRVSDSESEDPPRPQASDSESEelpkprvSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESD 296
Cdd:PRK08581 182 TKPSTSNKQPNSPKPTQPNQSNSQ-------PASDDTANQKSSSKDNQSMSDSALDSILDQYSEDAKKTQKDYASQSKKD 254

                 ....*.
gi 30352010  297 GHTDRK 302
Cdd:PRK08581 255 KTETSN 260
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
162-475 1.86e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 48.37  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  162 EDPPRPQASDSENEEPPKPRISDSESEElpkPRVSDSESEDPPRPQASDSESEELPKPRVSDSESEDPPRPQASDSESEE 241
Cdd:NF033609 540 DKPVVPEQPDEPGEIEPIPEDSDSDPGS---DSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDS 616
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  242 LPKPRVSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESDGHTDRKGLHSSDSEEEEPKRQKIDS 321
Cdd:NF033609 617 DSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 696
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  322 DDDEEKEGDEEKVAKRKAAVLSDSEDDAGNASAKKSRVVCDADDSDSDVVSDKS---GKRETTVASDSEEEAGKEESSVK 398
Cdd:NF033609 697 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdsdSDSDSDSDSDSDSDSDSDSDSDS 776
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30352010  399 KKEDKDLFGSDSESGNEEENLIADIFGESGDEEEEEFTGFNQEDLEEEKNETQLKEAEDSDSDDNIKRGKHMDFLSD 475
Cdd:NF033609 777 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 853
PHA03169 PHA03169
hypothetical protein; Provisional
74-297 1.03e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.35  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   74 PSNANASDSESEELHRpkdSDSDSEEHAESPASDSENEPVNQHGSDSENEEllnGHASDSEKEEVSKHAASDSEAEDTLQ 153
Cdd:PHA03169  42 RAAKPAPPAPTTSGPQ---VRAVAEQGHRQTESDTETAEESRHGEKEERGQ---GGPSGSGSESVGSPTPSPSGSAEELA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  154 PQVSESDSEDppRPQASDSENEEPPKPRISDSESEElpkprvSDSESEDPPRPQASDSESEElpkprvSDSESEDPPRPQ 233
Cdd:PHA03169 116 SGLSPENTSG--SSPESPASHSPPPSPPSHPGPHEP------APPESHNPSPNQQPSSFLQP------SHEDSPEEPEPP 181
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30352010  234 ASDSEsEELPKPRVSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESDG 297
Cdd:PHA03169 182 TSEPE-PDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREG 244
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
84-294 1.13e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.93  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    84 SEELHRPKDSDSDSEEHAESPASDSENEPVNQHGSDSENEELLNGHASDSEKEEVSKHAASDSEAEDTLQPqvsESDSED 163
Cdd:PHA03307   39 SQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPP---GPSSPD 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   164 PPRPQASDSENEEPPKPRIS---DSESEELPKPRVSDSESEDPPRPQASDSESE---ELPKPRVSDSE-------SEDPP 230
Cdd:PHA03307  116 PPPPTPPPASPPPSPAPDLSemlRPVGSPGPPPAASPPAAGASPAAVASDAASSrqaALPLSSPEETArapssppAEPPP 195
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30352010   231 RPQASDSEseelPKPRVSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDgENKREDSEVQNE 294
Cdd:PHA03307  196 STPPAAAS----PRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSS-ESSGCGWGPENE 254
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
205-462 2.04e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 44.99  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    205 RPQASDSESEELPKPRVSDSESEDPPRPQASDSESE-ELPKPRVSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGE 283
Cdd:TIGR00927  619 RPVAKVMALGDLSKGDVAEAEHTGERTGEEGERPTEaEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGE 698
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    284 NKREDSEVQNESDGHTDRKGLHSSDsEEEEPKRQKIDSDDDEEKEGDEEKVAKRKAAVLSDSEDDAGNASAKKSRVVCDA 363
Cdd:TIGR00927  699 IEAKEADHKGETEAEEVEHEGETEA-EGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKED 777
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    364 DDS----DSDVVSDKSGKRETTVASDSEEEAGKEESSVKKKEDKDLFGSDSESGNEEENLIADIFGESGDEEE-----EE 434
Cdd:TIGR00927  778 EDEgeiqAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKgvdggGG 857
                          250       260
                   ....*....|....*....|....*...
gi 30352010    435 FTGFNQEDLEEEKNETQLKEAEDSDSDD 462
Cdd:TIGR00927  858 SDGGDSEEEEEEEEEEEEEEEEEEEEEE 885
ECM1 pfam05782
Extracellular matrix protein 1 (ECM1); This family consists of several eukaryotic ...
164-275 2.10e-04

Extracellular matrix protein 1 (ECM1); This family consists of several eukaryotic extracellular matrix protein 1 (ECM1) sequences. ECM1 has been shown to regulate endochondral bone formation, stimulate the proliferation of endothelial cells and induce angiogenesis. Mutations in the ECM1 gene can cause lipoid proteinosis, a disorder which causes generalized thickening of skin, mucosae and certain viscera. Classical features include beaded eyelid papules and laryngeal infiltration leading to hoarseness.


Pssm-ID: 461739  Cd Length: 518  Bit Score: 44.45  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   164 PPRPqasdsenEEPPKPRISDSESEELPKPRVSDSESEDPPRPQASDSESEELPKPRVSDSESEDPPRPQASDSESEELP 243
Cdd:pfam05782   6 PPSP-------PQTRGLPVDHPDTSQHDPPFEGQSEVQPPPSQEAIPVQEEELPPPQLPVEKKVDPPLPQEAIPLQEELP 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 30352010   244 KPRVSDSESE-DPQKGPasDSEAEDASRHKEKP 275
Cdd:pfam05782  79 PPQLPIEQKEiDPPFPQ--QEEITPSKQREEKP 109
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
74-270 2.48e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    74 PSNANASDSESEELHRPKDSDSDSEEHAESPASDSENEPVNQHGSDSENEELLNGHASDSEKEEVSKHAASDSEAEDTLQ 153
Cdd:PHA03307  218 SSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPS 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   154 PQVS-ESDSEDPPRPQASDSEneeppkpriSDSESEELPKPrvsdSESEDPPRPQASDSESEELPKPR-VSDSESEDPPR 231
Cdd:PHA03307  298 PSPSsPGSGPAPSSPRASSSS---------SSSRESSSSST----SSSSESSRGAAVSPGPSPSRSPSpSRPPPPADPSS 364
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 30352010   232 PQASDSESEELPKPRVSDSESEDPQKGPASDSEAEDASR 270
Cdd:PHA03307  365 PRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDA 403
PRK10263 PRK10263
DNA translocase FtsK; Provisional
66-235 3.51e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 44.31  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    66 GTDSENDEPSNANASDSESE-ELHRPKDSDSDSEEHAESPA-------SDSENEPVNQHGSDSENEELLNGhasdsekee 137
Cdd:PRK10263  677 GEQYQHDVPVNAEDADAAAEaELARQFAQTQQQRYSGEQPAganpfslDDFEFSPMKALLDDGPHEPLFTP--------- 747
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   138 vSKHAASDSEAEDTLQPQVSESDSEDPPRPQASDSENEEPPKPRISDSESEELPKPRVSDSESEDPPRPQASDSESEELP 217
Cdd:PRK10263  748 -IVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAP 826
                         170
                  ....*....|....*...
gi 30352010   218 KPRVSDSESEDPPRPQAS 235
Cdd:PRK10263  827 QPQYQQPQQPVAPQPQDT 844
PTZ00121 PTZ00121
MAEBL; Provisional
46-468 6.45e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 6.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    46 DHHSENETSDREDGLAKIHNGTDSENDEPSNANASDSESEELHRPKDSDSDSEEHAESPASDSENEPVNQHGSDSENEEL 125
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADE 1448
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   126 LNGHASDSEKEEVSKHAASDSEAEDTLQPQVSESDSEDPPRPQASDSEN--EEPPKPRISDSESEELPKprVSDSESEDP 203
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKkaDEAKKAAEAKKKADEAKK--AEEAKKADE 1526
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   204 PRPQASDSESEELPKprVSDSESEDPPRPQASDSESEELPKPRVSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGE 283
Cdd:PTZ00121 1527 AKKAEEAKKADEAKK--AEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   284 NKREDSEVQNESDGHTDRKGLHssdSEEEEPKRQKIDSDDDEEKegdeekvaKRKAAVLSDSEDDAGNASAKKSRVVCDA 363
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELK---KAEEEKKKVEQLKKKEAEE--------KKKAEELKKAEEENKIKAAEEAKKAEED 1673
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   364 DDSDSDVVSDKSGKRETTVASDSEEEAGKEESSVKKKEDKDLFGSDSESGNEEENLI-ADIFGESGDEEEEEFTGFNQEd 442
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIkAEEAKKEAEEDKKKAEEAKKD- 1752
                         410       420
                  ....*....|....*....|....*.
gi 30352010   443 lEEEKNETQLKEAEDSDSDDNIKRGK 468
Cdd:PTZ00121 1753 -EEEKKKIAHLKKEEEKKAEEIRKEK 1777
PRK08581 PRK08581
amidase domain-containing protein;
2-203 7.72e-04

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 42.85  E-value: 7.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    2 DSEYYSGDQSDDGGATPVQDERDSGSDGEDGVTEQHSGSDTGSVDHHSENETSDREDGLAKIHNGTDSEND-EPSNANAS 80
Cdd:PRK08581 104 INQLLTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPRNSEKSTNDSNKNSDSSIKNDTDTQSSKQDKADNQkAPSSNNTK 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   81 DSESEELHRPK------DSDSDSEEHAESPASDSENEpvNQHGSDSENEELLNGHASDSEKEEVSKHAASDSEAEDTLQ- 153
Cdd:PRK08581 184 PSTSNKQPNSPkptqpnQSNSQPASDDTANQKSSSKD--NQSMSDSALDSILDQYSEDAKKTQKDYASQSKKDKTETSNt 261
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30352010  154 --PQVSESDSEDPPRPQASDSENEEPPKPRISDSESEELPKprVSDSESEDP 203
Cdd:PRK08581 262 knPQLPTQDELKHKSKPAQSFENDVNQSNTRSTSLFETGPS--LSNNDDSGS 311
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
93-236 8.47e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 42.66  E-value: 8.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   93 SDSDSEEHAESPASDSEnepvnQHGSDSENEELLNGHASDSEKEEVSKHAASDSEAEDTlQPQVSESDSEDPPRPQASDS 172
Cdd:PRK13108 306 AAVASAASAVGPVGPGE-----PNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGES-TPAVEETSEADIEREQPGDL 379
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30352010  173 ENEEPPKPRISDSESEELP-KPRVSDSESEDPPRPQASDSESEELPKPRVSDSESEDP-PRPQASD 236
Cdd:PRK13108 380 AGQAPAAHQVDAEAASAAPeEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPgDDPAEPD 445
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
128-314 1.06e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  128 GHASDSEKEEVSKHAASDSEAEDTLQPQVSESDSEDP-PRPQASDSENEEPPKPRISDSESEELPKPRVSDSESEDPPRP 206
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAaPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDG 668
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  207 QASD------SESEELPKPRVSDSESEDPPRPQASDSESEElPKPRVSDSESEDPQK----GPASDSEAEDASRHKEKPD 276
Cdd:PRK07764 669 WPAKaggaapAAPPPAPAPAAPAAPAGAAPAQPAPAPAATP-PAGQADDPAAQPPQAaqgaSAPSPAADDPVPLPPEPDD 747
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 30352010  277 SDDSDGENKREDSEVQNESDGHTDRKGLHSSDSEEEEP 314
Cdd:PRK07764 748 PPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEM 785
PHA03247 PHA03247
large tegument protein UL36; Provisional
153-261 1.57e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   153 QPQVSEsdsedPPRPQASDSENEEPPKPRISDSESEELPKPRVSDSESEDPPRPQASDSESEELPKPRVSDSESEDPPRP 232
Cdd:PHA03247 2888 RPAVSR-----STESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962
                          90       100
                  ....*....|....*....|....*....
gi 30352010   233 QASDSESEELPKPRVSDSESEDPQKGPAS 261
Cdd:PHA03247 2963 WLGALVPGRVAVPRFRVPQPAPSREAPAS 2991
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
57-210 2.45e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 41.12  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   57 EDGLAKIHNGTDSENDEPSNANAS-DSESEELHRPKDSDSD-SEEHAESPASDSENEPVNQHGSDSENeellNGHASDSE 134
Cdd:PRK13108 292 VDEALEREPAELAAAAVASAASAVgPVGPGEPNQPDDVAEAvKAEVAEVTDEVAAESVVQVADRDGES----TPAVEETS 367
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30352010  135 KEEVSKHAASDSEAEDTLQPQVSES-DSEDPPRPQASDSENEEPPKPRISDSESEELPKPRVSDSESEDP-PRPQASD 210
Cdd:PRK13108 368 EADIEREQPGDLAGQAPAAHQVDAEaASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPDELAVAGPgDDPAEPD 445
AF-4 pfam05110
AF-4 proto-oncoprotein N-terminal region; This family consists of AF4 (Proto-oncogene AF4) and ...
144-238 2.65e-03

AF-4 proto-oncoprotein N-terminal region; This family consists of AF4 (Proto-oncogene AF4) and FMR2 (Fragile X E mental retardation syndrome) nuclear proteins. These proteins have been linked to human diseases such as acute lymphoblastic leukaemia and mental retardation. The family also contains a Drosophila AF4 protein homolog Lilliputian which contains an AT-hook domain. Lilliputian represents a novel pair-rule gene that acts in cytoskeleton regulation, segmentation and morphogenesis in Drosophila.


Pssm-ID: 461550 [Multi-domain]  Cd Length: 514  Bit Score: 40.88  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   144 SDSEAEDTLQPQVSESDSEDPPRPQASDSENEEPPKPRISDSESEelpkprvSDSESEdpprpQASDSESEElpkpRVSD 223
Cdd:pfam05110 422 SSSEDSDDDQAPEKPPPSSAPPSAPQSQPNSVASAHSSSGESGSS-------SDSESS-----SESDSESES----SSSD 485
                          90
                  ....*....|....*
gi 30352010   224 SESEDPPRPQASDSE 238
Cdd:pfam05110 486 SEANEPPRSATPEPE 500
PRK08581 PRK08581
amidase domain-containing protein;
9-257 2.79e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 40.93  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    9 DQSDDGGATPVQDERDSGSDGEDGVTEQHSGSDTgsvdhhSENETSDREDGLAKIHNGTDSEND-EPSNANASDSESEEL 87
Cdd:PRK08581  50 ETSKDTSSKDTDKADNNNTSNQDNNDKKFSTIDS------STSDSNNIIDFIYKNLPQTNINQLlTKNKYDDNYSLTTLI 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   88 HRPKDSDSDSEEHaESPASDSenepvnqHGSDSENEELLNGHASDSEKEEVSKHAASDSEAEDTLQPQVSESDSEDPPRP 167
Cdd:PRK08581 124 QNLFNLNSDISDY-EQPRNSE-------KSTNDSNKNSDSSIKNDTDTQSSKQDKADNQKAPSSNNTKPSTSNKQPNSPK 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  168 QASDSENEEPP-----KPRISDSESEELPKPRVSDS---ESEDPPRPQASDSESEElPKPRVSDSESEDPPRPQASDSES 239
Cdd:PRK08581 196 PTQPNQSNSQPasddtANQKSSSKDNQSMSDSALDSildQYSEDAKKTQKDYASQS-KKDKTETSNTKNPQLPTQDELKH 274
                        250
                 ....*....|....*...
gi 30352010  240 EELPKPrvsDSESEDPQK 257
Cdd:PRK08581 275 KSKPAQ---SFENDVNQS 289
rad2 TIGR00600
DNA excision repair protein (rad2); All proteins in this family for which functions are known ...
17-296 2.89e-03

DNA excision repair protein (rad2); All proteins in this family for which functions are known are flap endonucleases that generate the 3' incision next to DNA damage as part of nucleotide excision repair. This family is related to many other flap endonuclease families including the fen1 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273166 [Multi-domain]  Cd Length: 1034  Bit Score: 41.04  E-value: 2.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010     17 TPVQDERDSGSDGEDGVTEQHSGsDTGSVDHHSE--NETSDREDGLAKIHNGTDSENDEP----SNANASDSESEELHRP 90
Cdd:TIGR00600  433 IEVEDDDLDYLDQGEGIPLMAAL-QLSSVNSKPEavASTKIAREVTSSGHEAVPKAVQSLllgaTNDSPIPSEFTILDRK 511
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010     91 K------------DSDSDSEEHAESPASDSENEPVNQHGSDSENEELLNGHASDSEKEEVSKHAASDSEAEDTLQPQVSE 158
Cdd:TIGR00600  512 SelsiertvkpvsSEFGLPSQREDKLAIPTEGTQNLQGISDHPEQFEFQNELSPLETKNNESNLSSDAETEGSPNPEMPS 591
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    159 SDSEDPPRPQASDSENEEPpkprisdSESEELPKPrvSDSESEDPPRPQASDSESEELPK---PRVSDSE-SEDPPRPQA 234
Cdd:TIGR00600  592 WSSVTVPSEALDNYETTNP-------SNAKEVRNF--AETGIQTTNVGESADLLLISNPMevePMESEKEeSESDGSFIE 662
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30352010    235 SDSESEELPKPRVSDSESEDPQKGPASD---SEAEDASRHKEKPDSDDSDGENKREDSEVQNESD 296
Cdd:TIGR00600  663 VDSVSSTLELQVPSKSQPTDESEENAENkvaSIEGEHRKEIEDLLFDESEEDNIVGMIEEEKDAD 727
MDN1 COG5271
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ...
7-468 3.10e-03

Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444083 [Multi-domain]  Cd Length: 1028  Bit Score: 41.15  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    7 SGDQSDDGGATPVQDERDSGSDGEDGVTEQHSgSDTGSVDHHSENETSDREDGLAKIHNGTDSENDEPSNANASDSESEE 86
Cdd:COG5271  552 DADETDEPEATAEEDEPDEAEAETEDATENAD-ADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEE 630
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   87 LHRPKDSDSDSEEHAESPASDSENEPVNQHGSDSENEELLNGHASDSEKEEVSKHAASDSEAEDTLQpqVSESDSEDPPR 166
Cdd:COG5271  631 EAAEDEAAEPETDASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAAAAEASDDEEE--TEEADEDAETA 708
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  167 PQASDSENEEPPKPRISDSESEelPKPRVSDSESEDPPRPQASDSESEELPKPRVSDSESedpprpQASDSESEELPKPR 246
Cdd:COG5271  709 SEEADAEEADTEADGTAEEAEE--AAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDA------DGLEEALEEEKADA 780
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  247 VSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESDGHTDRKGLHSSDSEEEEPKRQKIDSDDDEE 326
Cdd:COG5271  781 EEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDA 860
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  327 KEGDEEKVAK-RKAAVLSDSEDDAGNASAKKSRVVCDADDSDSDVVSDKSGKRETTVASDSEEEAGKEESSVKKKEDKDL 405
Cdd:COG5271  861 DLDLDADLAAdEHEAEEAQEAETDADADADAGEADSSGESSAAAEDDDAAEDADSDDGANDEDDDDDAEEERKDAEEDEL 940
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30352010  406 FGSDSESGNEEENLIADIFGESGDEEEEEFTGFNQEDLEEEKNETQLKEAEDSDSDDNIKRGK 468
Cdd:COG5271  941 GAAEDDLDALALDEAGDEESDDAAADDAGDDSLADDDEALADAADDAEADDSELDASESTGEA 1003
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
30-317 3.74e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 40.75  E-value: 3.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010     30 EDGVTEQHSGSDTGSvdhhsENETSDREDGLAKIHNGTDSENDEPSNANASDSESEELHRPKDSDSDSEEHAESPASDse 109
Cdd:TIGR00927  633 GDVAEAEHTGERTGE-----EGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERKGEQEGEGEIEAKEAD-- 705
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    110 nepvnqHGSDSENEELLNGHASDSEKEEVSKHAASDSEAEDTLQPQVSESDSEDPPRPQASDSENEEPPKPRISDSESEE 189
Cdd:TIGR00927  706 ------HKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDED 779
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    190 lpkprVSDSESEDPPRPQASDSESEELPKPRVSDSESEDPPRPQASDSESEELPKPRVSDSE-SEDPQKGPASDSEAEDA 268
Cdd:TIGR00927  780 -----EGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQElNAENQGEAKQDEKGVDG 854
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 30352010    269 SRHKEKPDSDDSDGENKREDSEVQNESDghtdrkglhssDSEEEEPKRQ 317
Cdd:TIGR00927  855 GGGSDGGDSEEEEEEEEEEEEEEEEEEE-----------EEEEEEENEE 892
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
102-281 3.77e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 40.35  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  102 ESPASDSENEPVNQHGSDSENEEL----LNGHASDSEKEEVSKHAASDSEAEDTLQPQVSESDSEDPPRPQASDSENEEP 177
Cdd:PRK13108 280 EAPGALRGSEYVVDEALEREPAELaaaaVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGES 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  178 PkPRISDSESEELPKPRVSDSESEDPPRPQASDSESEELPKPRVS----DSESEDPPRPQASDSESEelpkprvSDSESE 253
Cdd:PRK13108 360 T-PAVEETSEADIEREQPGDLAGQAPAAHQVDAEAASAAPEEPAAlaseAHDETEPEVPEKAAPIPD-------PAKPDE 431
                        170       180
                 ....*....|....*....|....*...
gi 30352010  254 DPQKGPASDSEAEDASRHKEKPDSDDSD 281
Cdd:PRK13108 432 LAVAGPGDDPAEPDGIRRQDDFSSRRRR 459
PHA02664 PHA02664
hypothetical protein; Provisional
206-317 4.69e-03

hypothetical protein; Provisional


Pssm-ID: 177447  Cd Length: 534  Bit Score: 40.37  E-value: 4.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  206 PQASDSESEELPKPrvsDSESEDPPRPQASDSESEELpkprvSDSESEDPQKGPASDSEAEDASRHKEKPDSDDS--DGE 283
Cdd:PHA02664 424 PADQDVEAEAHDEF---DQDPGAPAHADRADSDEDDM-----DEQESGDERADGEDDSDSSYSYSTTSSEDESDSadDSW 495
                         90       100       110
                 ....*....|....*....|....*....|....
gi 30352010  284 NKREDSEVQNESDghtdrkGLHSSDSEEEEPKRQ 317
Cdd:PHA02664 496 GDESDSGIEHDDG------GVGQAIEEEEEEERA 523
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
2-203 5.34e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 40.36  E-value: 5.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010      2 DSEYYSGDQSDDGGATPVQDERDSGSDGEDGVTEQHSGSDTGSVDHHSENETSDREDGLAKIHNGTDSENDEPSNANASD 81
Cdd:TIGR00927  698 EIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKED 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010     82 SESEELHRPKDSDSDSEEHAESPAsdsENEPVNQHGSDSENEELLNGHASDSEKEEVSKHAasDSEAEDTLQPQVSESDS 161
Cdd:TIGR00927  778 EDEGEIQAGEDGEMKGDEGAEGKV---EHEGETEAGEKDEHEGQSETQADDTEVKDETGEQ--ELNAENQGEAKQDEKGV 852
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 30352010    162 EDPPRPQASDSENEEPPKPRISDSESEELPKPRvSDSESEDP 203
Cdd:TIGR00927  853 DGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEE-EEEENEEP 893
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
152-280 6.09e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 40.14  E-value: 6.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  152 LQPQVSESDSEDPPRPQASDSE-NEEPPKPRISDSESEELPKPRVsdseSEDPPRPQASDSESEELPKPRVSDSesedPP 230
Cdd:NF033839 365 VKPQPEKPKPEVKPQPETPKPEvKPQPEKPKPEVKPQPEKPKPEV----KPQPEKPKPEVKPQPEKPKPEVKPQ----PE 436
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30352010  231 RPQASDSESEELPKPRV-SDSESEDPQKGPASDSEAEDASRHKEKPDSDDS 280
Cdd:NF033839 437 KPKPEVKPQPEKPKPEVkPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNS 487
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
82-327 6.18e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 40.03  E-value: 6.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    82 SESEELHRPKDSDSDSEEHAESPASDSENEPVNQHGSDSENEELLNGHASDSEKEEVSKHAASDSEAEDTLQPQvSESDS 161
Cdd:PTZ00108 1150 KEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGS-DQEDD 1228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   162 EDPPRPQASDSENEEPPKPRISDSESEELPKPRVSDSESEDPPRpqasdseseELPKPRVSDSESEDPPRPQASDSESee 241
Cdd:PTZ00108 1229 EEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPK---------NAPKRVSAVQYSPPPPSKRPDGESN-- 1297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   242 lPKPRVSDSESEDPQKGPASDSEAEDASRHKEKPDSDDsDGENKREDSEVQNESD--GHTDRKGLHSSDSEEEEPKRQKI 319
Cdd:PTZ00108 1298 -GGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARK-KKSKTRVKQASASQSSrlLRRPRKKKSDSSSEDDDDSEVDD 1375

                  ....*...
gi 30352010   320 DSDDDEEK 327
Cdd:PTZ00108 1376 SEDEDDED 1383
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
102-265 6.97e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.14  E-value: 6.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   102 ESPAS-DSENEPVNQ--HGSDSENEELLNGHASDSEKEEVSKHAAS-DSEAEDTL-----QPQVSESDSEDPPRPQASDS 172
Cdd:pfam03154  23 KQTASpDGRASPTNEdlRSSGRNSPSAASTSSNDSKAESMKKSSKKiKEEAPSPLksakrQREKGASDTEEPERATAKKS 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   173 ENEEPPKPRI-SDSESEELPKPRVSDSESEDPPR-PQASDSESEELPKPRVSDSESEDPPRPQASDSESEELPKPRVSDS 250
Cdd:pfam03154 103 KTQEISRPNSpSEGEGESSDGRSVNDEGSSDPKDiDQDNRSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAAS 182
                         170
                  ....*....|....*
gi 30352010   251 ESEDPQKGPASDSEA 265
Cdd:pfam03154 183 PPSPPPPGTTQAATA 197
AF-4 pfam05110
AF-4 proto-oncoprotein N-terminal region; This family consists of AF4 (Proto-oncogene AF4) and ...
139-255 7.24e-03

AF-4 proto-oncoprotein N-terminal region; This family consists of AF4 (Proto-oncogene AF4) and FMR2 (Fragile X E mental retardation syndrome) nuclear proteins. These proteins have been linked to human diseases such as acute lymphoblastic leukaemia and mental retardation. The family also contains a Drosophila AF4 protein homolog Lilliputian which contains an AT-hook domain. Lilliputian represents a novel pair-rule gene that acts in cytoskeleton regulation, segmentation and morphogenesis in Drosophila.


Pssm-ID: 461550 [Multi-domain]  Cd Length: 514  Bit Score: 39.72  E-value: 7.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   139 SKHAASDSEAEDTLQPQVSESDSEDPPRPQASdseneEPPKPRISDSESEELPKPRVSDSESEDPPRPQASDSESEElpk 218
Cdd:pfam05110 402 SKTLPTSQQGTSMLEDDLKLSSSEDSDDDQAP-----EKPPPSSAPPSAPQSQPNSVASAHSSSGESGSSSDSESSS--- 473
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 30352010   219 prVSDSESEDpprpQASDSESEElpKPRVSDSESEDP 255
Cdd:pfam05110 474 --ESDSESES----SSSDSEANE--PPRSATPEPEPP 502
PTZ00121 PTZ00121
MAEBL; Provisional
72-466 8.33e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 8.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010    72 DEPSNANASDSESEELHRPKDSDSDSEEhAESPASDSENEPVNQHGSDSENEELLNGHASDSEKEEVSKHAASDSEAEDT 151
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKKADEAKKKAEE-AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   152 LQPQVSESDSEDPPRPQASDSENEEPPKprisdsESEELPKPRVSDSESEDPPRPQASDSESEELPKPRVSDSESEDPPR 231
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKKAEEDKK------KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   232 PQASDSESEELPKPRVSDSESEDPQKGPASDSEAEDASRHKEKPDSDDSDGENKREDSEVQNESdghtdRKGLHSSDSEE 311
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA-----KKAEEAKKADE 1526
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   312 EEPKRQKIDSDDDEEKEGDEEKVAKRKAAVLSDSEDDAGNASAKKSRVVCDADDSDSDVVSDKSGKRETTVASDSEEEAG 391
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30352010   392 KEESSVKKKEDKDLFGSDSESGNEEENLIADIFGESGDEEEEEftgfnqEDLEEEKNETQLKEAEDSDSDDNIKR 466
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA------EELKKAEEENKIKAAEEAKKAEEDKK 1675
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
73-268 8.46e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 8.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010   73 EPSNANASDSESEELHRPKDSDS---DSEEHAESPASDSENEPVNQHGSDSENEELLNGHASDSEKEEVSKHAASDSEAE 149
Cdd:PRK07764 598 EGPPAPASSGPPEEAARPAAPAApaaPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAA 677
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30352010  150 DTLQPQVSESDSEDPPRPQASDSENEEPPKPRISDSESEELPKPR--------VSDSESEDPPRPQASDSESEELPKPRV 221
Cdd:PRK07764 678 PAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPqaaqgasaPSPAADDPVPLPPEPDDPPDPAGAPAQ 757
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 30352010  222 SDSESEDPPRPQASDSESeelPKPRVSDSESEDPQKGPASDSEAEDA 268
Cdd:PRK07764 758 PPPPPAPAPAAAPAAAPP---PSPPSEEEEMAEDDAPSMDDEDRRDA 801
 
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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