|
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
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90 100 110
....*....|....*....|....*....|....*..
gi 30352010 219 prVSDSESEDpprpQASDSESEElpKPRVSDSESEDP 255
Cdd:pfam05110 474 --ESDSESES----SSSDSEANE--PPRSATPEPEPP 502
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|
| 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
|
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