|
Name |
Accession |
Description |
Interval |
E-value |
| hSH3 |
pfam14603 |
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ... |
578-657 |
1.12e-41 |
|
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown.
Pssm-ID: 464216 Cd Length: 89 Bit Score: 146.29 E-value: 1.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 578 FRKKFKFEGEIVVHTKMMIDPNAKTRRGGGKHLGIRRGEILEVIEFTSNEEMLCRDPKGKYGYVPRTALLPLETEVYDDV 657
Cdd:pfam14603 1 FRKKFKYDGEIKVLYSMTVDPNLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNLLQNDGEIYDDI 80
|
|
| hSH3_ADAP |
cd11867 |
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ... |
572-648 |
2.65e-17 |
|
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor Protein; ADAP, also called Fyn T-binding protein (FYB) or SLP-76-associated protein (SLAP), is expressed mainly in hematopoietic cells but not in B cells. It is required for the proliferation of mature T-cells and plays an important role in T-cell activation, TCR-induced integrin clustering, and T-cell adhesion. ADAP has been shown to bind many partners including SLP-76, Fyn, Src, SKAP1, SKAP2, dynein, Ena/VASP, Carma1, among others. It is connected to cytoskeleton via its binding to Ena and VASP, which impacts actin cytoskeletal remodeling upon TCR ligation. The SH3 domain of ADAP adopts an altered fold referred to as a helically extended SH3 (hSH3) domain characterized by clusters of positive charges. The hSH3 domain can no longer bind conventional proline-rich peptides, instead, it functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides.
Pssm-ID: 212801 Cd Length: 77 Bit Score: 76.79 E-value: 2.65e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768004344 572 EKAEREFRKKFKFEGEIVVHTKMMIDPNAKTRRGGGKHLGIRRGEILEVIEFTSNEEMLCRDPKGKYGYVPRTALLP 648
Cdd:cd11867 1 EKEEKEFRKKFKYNGEIKVLYSTTVLQTLTIKKFGSKDLQVKPGESLEVIQHTDDTKVLCRNEEGKYGYVLRSNLEP 77
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
58-414 |
3.27e-13 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 73.82 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 58 PKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTdlPKKPPPPEVTDLPKKPPPPEVTDLPKKPSKLELS-----DLSKK 132
Cdd:PHA03247 2589 PDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTH--APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPapgrvSRPRR 2666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 133 FPQLGATPFPRKPLQ--------PEVGEAPLKASLPEPGAPARKPLQPDELSHPARPPSEPKSGAFPRKLWQP-----EA 199
Cdd:PHA03247 2667 ARRLGRAAQASSPPQrprrraarPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPappavPA 2746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 200 GEATP----RSPQPELSTFPKKPAQPEFNVYPKKPPQPQVGGLP----KKSVPQPEFSEAAQTPLWKPQSSEPkrdSSAF 271
Cdd:PHA03247 2747 GPATPggpaRPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASlsesRESLPSPWDPADPPAAVLAPAAALP---PAAS 2823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 272 PKKASQPPLSDFPKKPPQPElgDLTRTSSEPEVSVLP-----KRPRPAEFKALSKKPPQPELGGLPRTSSEPEFNSLPRK 346
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPP--GPPPPSLPLGGSVAPggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALP 2901
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768004344 347 LLQPERRGPPRKFSQPEPSAVLKRHPQPEffgDLPRKPPLPSSASESSLPAAVAGFSSRHPLSPGFGA 414
Cdd:PHA03247 2902 PDQPERPPQPQAPPPPQPQPQPPPPPQPQ---PPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGA 2966
|
|
| ftsN |
TIGR02223 |
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ... |
73-254 |
1.51e-04 |
|
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis. [Cellular processes, Cell division]
Pssm-ID: 274041 [Multi-domain] Cd Length: 298 Bit Score: 44.30 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 73 PPPPEVTDLPKKPPPPEVTDLPKKPPPPE-----VTDLPKkpPPPEVTDLPKKPSKLELSDLSKKFPQLGATPFPRKPLQ 147
Cdd:TIGR02223 52 KQANEPETLQPKNQTENGETAADLPPKPEerwsyIEELEA--REVLINDPEEPSNGGGVEESAQLTAEQRQLLEQMQADM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 148 pevgEAPLKASLPEPGAPARKPLQPDELSHPARPPSEPKsgafprklwqpeagEATPRSPQPELSTFPKKPAQPEFNVYP 227
Cdd:TIGR02223 130 ----RAAEKVLATAPSEQTVAVEARKQTAEKKPQKARTA--------------EAQKTPVETEKIASKVKEAKQKQKALP 191
|
170 180
....*....|....*....|....*..
gi 768004344 228 KKPPQPQVGGLPKKSVPQPEFSEAAQT 254
Cdd:TIGR02223 192 KQTAETQSNSKPIETAPKADKADKTKP 218
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
51-418 |
1.89e-04 |
|
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: 44.76 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 51 QPELSEHPKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPKKPPPPevtdlpkKPPPPEVTDLPKKPSKLELSDLS 130
Cdd:pfam03154 164 QQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPA-------TSQPPNQTQSTAAPHTLIQQTPT 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 131 KKFPQLgatPFPRKPLQPevgeaplkasLPEPGAPARKPLQ--PDELSHPARPPSEPKSGAFPRKLWQPEAGEATPRSPQ 208
Cdd:pfam03154 237 LHPQRL---PSPHPPLQP----------MTQPPPPSQVSPQplPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 209 PELSTFPkkpaqpefnvypkKPPQPQVGGLPKKSVPQPefseaaqTPLWKPQSSEPKRDSSAFPKKASQPPLSDfPKKPP 288
Cdd:pfam03154 304 SSQSQVP-------------PGPSPAAPGQSQQRIHTP-------PSQSQLQSQQPPREQPLPPAPLSMPHIKP-PPTTP 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 289 QPELGDLTRTSSEPEVSvlpkrpRPAEFKALSKKPPQPELGGL-------PRTSSEPEFNSLPR-KLLQPERRGPPRKFS 360
Cdd:pfam03154 363 IPQLPNPQSHKHPPHLS------GPSPFQMNSNLPPPPALKPLsslsthhPPSAHPPPLQLMPQsQQLPPPPAQPPVLTQ 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 768004344 361 QPEPSAVLKRHPQPEFFGDLPRKPPLPSSASESSLPAAVAGFSSRHPLSPGFGAAGTP 418
Cdd:pfam03154 437 SQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQP 494
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
30-290 |
3.04e-04 |
|
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: 43.99 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 30 EPSDLPKKPPKPEFGKLKKFSQPELSEHPKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPKKP----PPPEVTDL 105
Cdd:NF033839 256 EIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPqlekPKPEVKPQ 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 106 PKKPPPpEVTDLPKKPSKLELSDLSKKFPQLGATPFPRKPLQPEVGEAPLKASLPEPGAParkplQPDELSHPARPPSEP 185
Cdd:NF033839 336 PEKPKP-EVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKP-----KPEVKPQPEKPKPEV 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 186 KsgafPRKLWQPEAGEATPRSPQPELSTFPKKPaQPEFNVYPKKpPQPQVGGLPKKSVPQPEFSEAAQTPLWKPQSSEPK 265
Cdd:NF033839 410 K----PQPEKPKPEVKPQPEKPKPEVKPQPEKP-KPEVKPQPEK-PKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPK 483
|
250 260
....*....|....*....|....*
gi 768004344 266 RDSSAFPKKASQPPLSDFPKKPPQP 290
Cdd:NF033839 484 PDNSKPQADDKKPSTPNNLSKDKQP 508
|
|
| BimA_second |
NF040983 |
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ... |
58-148 |
4.84e-03 |
|
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia intracellular motility A), WP_004266405.1-like proteins in Burkholderia mallei or B. pseudomallei. The term BimA has also been used for WP_011205626.1-like homologs that have a very different N-terminal half.
Pssm-ID: 468913 [Multi-domain] Cd Length: 382 Bit Score: 39.89 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 58 PKKAPLPefgavslkPPPPevtdlPKKPPPPEVTDLPKKPPPPEVTDLPKKPPPPEVTDLPKKPSklelSDLSKKFPQLG 137
Cdd:NF040983 86 PNKVPPP--------PPPP-----PPPPPPPPTPPPPPPPPPPPPPPSPPPPPPPSPPPSPPPPT----TTPPTRTTPST 148
|
90
....*....|..
gi 768004344 138 ATPFPR-KPLQP 148
Cdd:NF040983 149 TTPTPSmHPIQP 160
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| hSH3 |
pfam14603 |
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ... |
578-657 |
1.12e-41 |
|
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion and de-granulation promoting adapter protein. It shows homology to SH3 domains; however, conserved residues of the fold are absent. It thus represents an altered SH3 domain fold. An N-terminal, amphipathic, helix makes extensive contacts to residues of the regular SH3 domain fold thereby creating a composite surface with unusual surface properties. The domain can no longer bind conventional proline-rich peptides. There are key phosphorylation sites within the two hSH3 domains and it would appear that binding at these sites does not materially affect the folding of these regions although the equilibrium towards the unfolded state may be slightly altered. The binding partners of the hSH3 domains are still unknown.
Pssm-ID: 464216 Cd Length: 89 Bit Score: 146.29 E-value: 1.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 578 FRKKFKFEGEIVVHTKMMIDPNAKTRRGGGKHLGIRRGEILEVIEFTSNEEMLCRDPKGKYGYVPRTALLPLETEVYDDV 657
Cdd:pfam14603 1 FRKKFKYDGEIKVLYSMTVDPNLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNLLQNDGEIYDDI 80
|
|
| hSH3_ADAP |
cd11867 |
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ... |
572-648 |
2.65e-17 |
|
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor Protein; ADAP, also called Fyn T-binding protein (FYB) or SLP-76-associated protein (SLAP), is expressed mainly in hematopoietic cells but not in B cells. It is required for the proliferation of mature T-cells and plays an important role in T-cell activation, TCR-induced integrin clustering, and T-cell adhesion. ADAP has been shown to bind many partners including SLP-76, Fyn, Src, SKAP1, SKAP2, dynein, Ena/VASP, Carma1, among others. It is connected to cytoskeleton via its binding to Ena and VASP, which impacts actin cytoskeletal remodeling upon TCR ligation. The SH3 domain of ADAP adopts an altered fold referred to as a helically extended SH3 (hSH3) domain characterized by clusters of positive charges. The hSH3 domain can no longer bind conventional proline-rich peptides, instead, it functions as a novel lipid interaction domain and can bind acidic lipids such as phosphatidylserine, phosphatidylinositol, phosphatidic acid, and polyphosphoinositides.
Pssm-ID: 212801 Cd Length: 77 Bit Score: 76.79 E-value: 2.65e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768004344 572 EKAEREFRKKFKFEGEIVVHTKMMIDPNAKTRRGGGKHLGIRRGEILEVIEFTSNEEMLCRDPKGKYGYVPRTALLP 648
Cdd:cd11867 1 EKEEKEFRKKFKYNGEIKVLYSTTVLQTLTIKKFGSKDLQVKPGESLEVIQHTDDTKVLCRNEEGKYGYVLRSNLEP 77
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
58-414 |
3.27e-13 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 73.82 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 58 PKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTdlPKKPPPPEVTDLPKKPPPPEVTDLPKKPSKLELS-----DLSKK 132
Cdd:PHA03247 2589 PDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTH--APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPapgrvSRPRR 2666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 133 FPQLGATPFPRKPLQ--------PEVGEAPLKASLPEPGAPARKPLQPDELSHPARPPSEPKSGAFPRKLWQP-----EA 199
Cdd:PHA03247 2667 ARRLGRAAQASSPPQrprrraarPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPappavPA 2746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 200 GEATP----RSPQPELSTFPKKPAQPEFNVYPKKPPQPQVGGLP----KKSVPQPEFSEAAQTPLWKPQSSEPkrdSSAF 271
Cdd:PHA03247 2747 GPATPggpaRPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASlsesRESLPSPWDPADPPAAVLAPAAALP---PAAS 2823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 272 PKKASQPPLSDFPKKPPQPElgDLTRTSSEPEVSVLP-----KRPRPAEFKALSKKPPQPELGGLPRTSSEPEFNSLPRK 346
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPP--GPPPPSLPLGGSVAPggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALP 2901
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768004344 347 LLQPERRGPPRKFSQPEPSAVLKRHPQPEffgDLPRKPPLPSSASESSLPAAVAGFSSRHPLSPGFGA 414
Cdd:PHA03247 2902 PDQPERPPQPQAPPPPQPQPQPPPPPQPQ---PPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGA 2966
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
26-375 |
6.22e-13 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 72.41 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 26 ASQPEPSDLPKKPPKPEFgklkkfsqPELSEHPKKaplPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPKKPPPPEVTDL 105
Cdd:PTZ00449 564 AKEHKPSKIPTLSKKPEF--------PKDPKHPKD---PEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKS 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 106 PKKPPPPEVTDLPKKPSklelsdlSKKFPQLgatpfPRKPLQPEVgeaplkaslpePGAPARKPLQPDELSHPARPPSEP 185
Cdd:PTZ00449 633 PKRPPPPQRPSSPERPE-------GPKIIKS-----PKPPKSPKP-----------PFDPKFKEKFYDDYLDAAAKSKET 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 186 KSGAFPRKLWQPEAGEATPRSPQPELSTF----PKKPAQPEFNVYP-KKPPQPQVGGLPKKSVPQPEFSEAAQTPLWKP- 259
Cdd:PTZ00449 690 KTTVVLDESFESILKETLPETPGTPFTTPrplpPKLPRDEEFPFEPiGDPDAEQPDDIEFFTPPEEERTFFHETPADTPl 769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 260 ---------------QSSEP----KRDSSafPKKASQPPLSDFPKKPPQPELGD---LTRTSSEPEVSVLPKRP------ 311
Cdd:PTZ00449 770 pdilaeefkeedihaETGEPdeamKRPDS--PSEHEDKPPGDHPSLPKKRHRLDglaLSTTDLESDAGRIAKDAsgkivk 847
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768004344 312 --RPAEFKALSKKPPQPELGGLPR--------TSSEPEFNSLP--RKLLQPERRGPPRKFSQPEPSAVLKRHPQPE 375
Cdd:PTZ00449 848 lkRSKSFDDLTTVEEAEEMGAEARkivvdddgTEADDEDTHPPeeKHKSEVRRRRPPKKPSKPKKPSKPKKPKKPD 923
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
83-392 |
1.66e-09 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 61.24 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 83 KKPPPPEVTDLPKKPPPPEVTDL----PKKPPPPEVTDLPKKPSKLelSDLSKKFPQlgatpfPRKPLQPEVGEAPlkas 158
Cdd:PTZ00449 494 KKLAPIEEEDSDKHDEPPEGPEAsglpPKAPGDKEGEEGEHEDSKE--SDEPKEGGK------PGETKEGEVGKKP---- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 159 lpepgAPARKplqpdelSHPARPPSEPKSGAFPRKlwqpeageatPRSPQ-PELSTFPKKPAQPEFNVYPKKPPQPQVGG 237
Cdd:PTZ00449 562 -----GPAKE-------HKPSKIPTLSKKPEFPKD----------PKHPKdPEEPKKPKRPRSAQRPTRPKSPKLPELLD 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 238 LPkKSVPQPEFSEAAQTPLWKPQSSEPKRDSSAFPKKASQPPLSdfPKKPPQPEL-----GDLTRTSSEPEVSVLPKRPR 312
Cdd:PTZ00449 620 IP-KSPKRPESPKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKS--PKPPFDPKFkekfyDDYLDAAAKSKETKTTVVLD 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 313 PAEFKALskKPPQPELGGLPRTSSEPEFNSLPRKLLQPERrgPPRKFSQPEPSAVLKRHPQPE---FFGDLPRKPPLPSS 389
Cdd:PTZ00449 697 ESFESIL--KETLPETPGTPFTTPRPLPPKLPRDEEFPFE--PIGDPDAEQPDDIEFFTPPEEertFFHETPADTPLPDI 772
|
...
gi 768004344 390 ASE 392
Cdd:PTZ00449 773 LAE 775
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
27-276 |
4.17e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 60.34 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 27 SQPEPSDLPKKPPKPEFGKLKKFSQPELSEHPKKAPLPEFGAvslkpPPPEVTDLPKKPPPPEVTDLPKKPPPPEVTDL- 105
Cdd:PHA03247 2764 AGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPA-----DPPAAVLAPAAALPPAASPAGPLPPPTSAQPTa 2838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 106 PKKPPPPEVTDLPKKPSKLELSDLSKKFPQLGATPFPRKPLQPEVGEAPLKASLPEPGAPARKPLQPDELSHPArPPSEP 185
Cdd:PHA03247 2839 PPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ-APPPP 2917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 186 KSGAFPRKLWQPEAGEATPRSPQPELSTFPKKPAQPEFNvypKKPPQPQVGGLPKKSVPQPEFSEAAQTP-LWKPQSSEP 264
Cdd:PHA03247 2918 QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPS---GAVPQPWLGALVPGRVAVPRFRVPQPAPsREAPASSTP 2994
|
250
....*....|..
gi 768004344 265 KRDSSAFPKKAS 276
Cdd:PHA03247 2995 PLTGHSLSRVSS 3006
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
61-396 |
4.82e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.95 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 61 APLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLP-KKPPPPEV-----------TDLPKKPPPPEVTDLPKKPsklelSD 128
Cdd:PHA03247 2491 AAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPvGEPVHPRMltwirgleelaSDDAGDPPPPLPPAAPPAA-----PD 2565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 129 LSKKFPQLGATPF----------PRKPLQPEVGEAPLKASLPEPGAPARKPLQPDElSHPARPPSEPKSGAFPRKLWQPE 198
Cdd:PHA03247 2566 RSVPPPRPAPRPSepavtsrarrPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDT-HAPDPPPPSPSPAANEPDPHPPP 2644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 199 AGEATPR---SPQPELSTFPKKPAQPEFNVYPKKPPQ--------PQVGGLPKKSVPQPEFSEAAQTPlwKPQSSEPKRD 267
Cdd:PHA03247 2645 TVPPPERprdDPAPGRVSRPRRARRLGRAAQASSPPQrprrraarPTVGSLTSLADPPPPPPTPEPAP--HALVSATPLP 2722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 268 SSAFPKKASQPPLSDFPKKPPQPELGDLTRTSSEPEVSVLPKRPRPAEFKALSKKPPQPELGGLPRTSSEPEFNSLPRKL 347
Cdd:PHA03247 2723 PGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPW 2802
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 768004344 348 LQPERRGPPRKFSQPEPSAVLKRHPQPEFFGDLPRKPPLPSSASESSLP 396
Cdd:PHA03247 2803 DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
230-398 |
4.67e-06 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 50.07 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 230 PPQPQVGGLPKKSVPQPEFSEAAQTPLWKPQSSE----PKRDSSAFPKKASQPPLSDFPKKPP----QPELGDLTRTSSE 301
Cdd:PTZ00449 511 PEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKeggkPGETKEGEVGKKPGPAKEHKPSKIPtlskKPEFPKDPKHPKD 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 302 PEVSVLPKRPRPAEFKALSKKPPQPELGGLPRTSSEPEFNSLPRKLLQPERRGPPRKfsqPEPSAVLKRhPQPEFFGDLP 381
Cdd:PTZ00449 591 PEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPER---PEGPKIIKS-PKPPKSPKPP 666
|
170
....*....|....*..
gi 768004344 382 RKPPLPSSASESSLPAA 398
Cdd:PTZ00449 667 FDPKFKEKFYDDYLDAA 683
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
58-280 |
6.77e-06 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 49.49 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 58 PKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPKKPPPPEVTDLP-KKPPPPEVTDLPKKPSKLELSDLSKKFPQL 136
Cdd:PRK12323 375 ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPaRRSPAPEALAAARQASARGPGGAPAPAPAP 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 137 GATPFP--RKPLQPEVGEAPLKASLPEPGAPARKPLQPDElshpARPPSEPKSGAFPrklwQPEAGEATPRSPQPELSTF 214
Cdd:PRK12323 455 AAAPAAaaRPAAAGPRPVAAAAAAAPARAAPAAAPAPADD----DPPPWEELPPEFA----SPAPAQPDAAPAGWVAESI 526
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768004344 215 PKKPAQPEFNVYPKKPPQPQVGGLPKKSVPQPEFseAAQTPLWKPQSSEPKRDSSAFPKKASQPPL 280
Cdd:PRK12323 527 PDPATADPDDAFETLAPAPAAAPAPRAAAATEPV--VAPRPPRASASGLPDMFDGDWPALAARLPV 590
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
57-255 |
4.86e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.90 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 57 HPKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPKKPPPPEVTDLPKKPPPPEVTDLPKKPSKLELSDLSKKFPQL 136
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 137 GATPFPRKPLQPEVGEAPlkaslPEPGAPARKPLQPDELSHPARPPSEPKSGAFPRKLWQPEAGEATPRSPQPELSTFPK 216
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAP-----AAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPE 744
|
170 180 190
....*....|....*....|....*....|....*....
gi 768004344 217 KPAQPEFNVYPKKPPQPQVGGLPKKSVPQPEFSEAAQTP 255
Cdd:PRK07764 745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
29-435 |
6.60e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 46.32 E-value: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 29 PEPSDLPKKPPKPEFGKLKKFSQPELSEHPKKAPLPEFGAVSLKPPPPEVTDlPKKPPPPEVTDLPKK------------ 96
Cdd:PHA03307 71 PPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPP-PASPPPSPAPDLSEMlrpvgspgpppa 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 97 --PPPPEVtdlpkkPPPPEVTDLpkkPSKLELSDLSKKFPQLGATPFPRKPlqpevgEAPLKASLPEPGAPARKPLQPDE 174
Cdd:PHA03307 150 asPPAAGA------SPAAVASDA---ASSRQAALPLSSPEETARAPSSPPA------EPPPSTPPAAASPRPPRRSSPIS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 175 LSHPARPPSEPKSGAFPRklwqpeageatPRSPQPELSTFPKKPAQPEFNVYPKKPPQPQVGGLPKKSVPQPEfSEAAQT 254
Cdd:PHA03307 215 ASASSPAPAPGRSAADDA-----------GASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWN-GPSSRP 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 255 PLWKPQSSEPKRDSSAFPKKASQPPLSDFPKKP----PQPELGDLTRTSSEPEVSVLPKRPRPAEFKALSKKPPQPELGG 330
Cdd:PHA03307 283 GPASSSSSPRERSPSPSPSSPGSGPAPSSPRASssssSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 331 lPRTSSEPEFNSLPRKLLQPERRGPPRKFSQPEPSAVLKRHPQPEFFGDLPRKPPLPSSASESSLPAavagfssRHPL-- 408
Cdd:PHA03307 363 -SSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYA-------RYPLlt 434
|
410 420 430
....*....|....*....|....*....|..
gi 768004344 409 ---SPGFGAAGTP--RWRSGGLvhsGGARPGL 435
Cdd:PHA03307 435 psgEPWPGSPPPPpgRVRYGGL---GDSRPGL 463
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
153-423 |
6.75e-05 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 46.62 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 153 APLKASLPEPGAPARKPL--QPDELSHPARPPSEPKSGAFPR-KLWQPEAGEATPRSPQPELSTFPKKPAQPEFNVYPKK 229
Cdd:PRK10263 335 APVEPVTQTPPVASVDVPpaQPTVAWQPVPGPQTGEPVIAPApEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 230 PPQ-PQVGGLPKKSVPQPEFSEAAQTPLWKPQSSEPKRDSSAFPKKASQP------PLSDFPKKPPQPELGDLTRTSSEP 302
Cdd:PRK10263 415 PAQqPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTeqtyqqPAAQEPLYQQPQPVEQQPVVEPEP 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 303 EV-SVLPKRPRPAEFKALSKKppqpelgglpRTSSEPEFNSLPRKLLQPERRGPPRKFSQPEPSAvlkrhPQPEFFGDLP 381
Cdd:PRK10263 495 VVeETKPARPPLYYFEEVEEK----------RAREREQLAAWYQPIPEPVKEPEPIKSSLKAPSV-----AAVPPVEAAA 559
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 768004344 382 RKPPLPSSASESSLPAAVAGFSSRHPLSPGFGAAGTPRWRSG 423
Cdd:PRK10263 560 AVSPLASGVKKATLATGAAATVAAPVFSLANSGGPRPQVKEG 601
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
143-575 |
8.38e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 143 RKPLQPEVGEAPLKASLPEPGAPArkplQPDELShPARPPSEPKSGAFPRKLWQ-----PEAGEATPRSPQPELSTFPKk 217
Cdd:PHA03247 2487 RFPFAAGAAPDPGGGGPPDPDAPP----APSRLA-PAILPDEPVGEPVHPRMLTwirglEELASDDAGDPPPPLPPAAP- 2560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 218 PAQPEFNVYPKKP-PQPqvgglpkksvPQPEFSEAAQTPLWKPQSSEPK-----RDSSAFPKKASQPPLSDFPKKPPQPE 291
Cdd:PHA03247 2561 PAAPDRSVPPPRPaPRP----------SEPAVTSRARRPDAPPQSARPRapvddRGDPRGPAPPSPLPPDTHAPDPPPPS 2630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 292 LGDLTRTSSEPEVSVLPKRPRPAEFKALSKKPPQPELGGLPRTSSEPEFNSLPRKLLQPERRGPPRKFSQPEPSAVLKRH 371
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEP 2710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 372 PQPEFFGDLPrKPPLPSSASESSLPAAVAGFSSRHPLSPGFGAAGTPRWRSGGLVHSGGARPGLRPSHPPRRRPLPPASS 451
Cdd:PHA03247 2711 APHALVSATP-LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVA 2789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 452 LGHPPAKPPLPPGPVDMQSFRRPSAASIDLRRTRSAAGL----HFQDRQPEDIPQVPDEIYELYDDVEPRDDSSPSPKGR 527
Cdd:PHA03247 2790 SLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLppptSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSR 2869
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 768004344 528 DEAPSVQQAAR-------RPPQDPALRKEKDPQPQQLPPMDPKLLKQLRKAEKAE 575
Cdd:PHA03247 2870 SPAAKPAAPARppvrrlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPP 2924
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
151-356 |
1.35e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 45.25 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 151 GEAPLKASLPEPGAPARKPLQPDELSHPARPPSEPKSGAFPRKLWQPEAGEATPRSPQPELSTFPKKPAQPEFNVYPKKP 230
Cdd:PRK12323 370 GGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 231 PQPQVGGLPKKSVPQPEFSEAAQTPLWKPQSSEPKRDSSAFPKKASQPPLSDFPKKPPQPELGDLTRTSSEPEVSVLPKR 310
Cdd:PRK12323 450 PAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDP 529
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 768004344 311 PRPAEFKALSKKPPQPELGGLPRTSSEPEFNSLPRKLLQPERRGPP 356
Cdd:PRK12323 530 ATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPD 575
|
|
| ftsN |
TIGR02223 |
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ... |
73-254 |
1.51e-04 |
|
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis. [Cellular processes, Cell division]
Pssm-ID: 274041 [Multi-domain] Cd Length: 298 Bit Score: 44.30 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 73 PPPPEVTDLPKKPPPPEVTDLPKKPPPPE-----VTDLPKkpPPPEVTDLPKKPSKLELSDLSKKFPQLGATPFPRKPLQ 147
Cdd:TIGR02223 52 KQANEPETLQPKNQTENGETAADLPPKPEerwsyIEELEA--REVLINDPEEPSNGGGVEESAQLTAEQRQLLEQMQADM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 148 pevgEAPLKASLPEPGAPARKPLQPDELSHPARPPSEPKsgafprklwqpeagEATPRSPQPELSTFPKKPAQPEFNVYP 227
Cdd:TIGR02223 130 ----RAAEKVLATAPSEQTVAVEARKQTAEKKPQKARTA--------------EAQKTPVETEKIASKVKEAKQKQKALP 191
|
170 180
....*....|....*....|....*..
gi 768004344 228 KKPPQPQVGGLPKKSVPQPEFSEAAQT 254
Cdd:TIGR02223 192 KQTAETQSNSKPIETAPKADKADKTKP 218
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
51-418 |
1.89e-04 |
|
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: 44.76 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 51 QPELSEHPKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPKKPPPPevtdlpkKPPPPEVTDLPKKPSKLELSDLS 130
Cdd:pfam03154 164 QQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPA-------TSQPPNQTQSTAAPHTLIQQTPT 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 131 KKFPQLgatPFPRKPLQPevgeaplkasLPEPGAPARKPLQ--PDELSHPARPPSEPKSGAFPRKLWQPEAGEATPRSPQ 208
Cdd:pfam03154 237 LHPQRL---PSPHPPLQP----------MTQPPPPSQVSPQplPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 209 PELSTFPkkpaqpefnvypkKPPQPQVGGLPKKSVPQPefseaaqTPLWKPQSSEPKRDSSAFPKKASQPPLSDfPKKPP 288
Cdd:pfam03154 304 SSQSQVP-------------PGPSPAAPGQSQQRIHTP-------PSQSQLQSQQPPREQPLPPAPLSMPHIKP-PPTTP 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 289 QPELGDLTRTSSEPEVSvlpkrpRPAEFKALSKKPPQPELGGL-------PRTSSEPEFNSLPR-KLLQPERRGPPRKFS 360
Cdd:pfam03154 363 IPQLPNPQSHKHPPHLS------GPSPFQMNSNLPPPPALKPLsslsthhPPSAHPPPLQLMPQsQQLPPPPAQPPVLTQ 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 768004344 361 QPEPSAVLKRHPQPEFFGDLPRKPPLPSSASESSLPAAVAGFSSRHPLSPGFGAAGTP 418
Cdd:pfam03154 437 SQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQP 494
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
30-290 |
3.04e-04 |
|
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: 43.99 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 30 EPSDLPKKPPKPEFGKLKKFSQPELSEHPKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPKKP----PPPEVTDL 105
Cdd:NF033839 256 EIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPqlekPKPEVKPQ 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 106 PKKPPPpEVTDLPKKPSKLELSDLSKKFPQLGATPFPRKPLQPEVGEAPLKASLPEPGAParkplQPDELSHPARPPSEP 185
Cdd:NF033839 336 PEKPKP-EVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKP-----KPEVKPQPEKPKPEV 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 186 KsgafPRKLWQPEAGEATPRSPQPELSTFPKKPaQPEFNVYPKKpPQPQVGGLPKKSVPQPEFSEAAQTPLWKPQSSEPK 265
Cdd:NF033839 410 K----PQPEKPKPEVKPQPEKPKPEVKPQPEKP-KPEVKPQPEK-PKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPK 483
|
250 260
....*....|....*....|....*
gi 768004344 266 RDSSAFPKKASQPPLSDFPKKPPQP 290
Cdd:NF033839 484 PDNSKPQADDKKPSTPNNLSKDKQP 508
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
26-162 |
3.69e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 26 ASQPEPSDLPKKPPKPEFGKLKKFSQPELSEHPKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPKKPPPPevtdL 105
Cdd:PHA03247 2863 RRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP----R 2938
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 768004344 106 PKKPPPPEVTDLPKKPSKLELSDLSKKFPQLGATPFPRKPLQPEVGEAPLKASLPEP 162
Cdd:PHA03247 2939 PQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPP 2995
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
75-315 |
5.29e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 43.33 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 75 PPEVTDLPKKPPPPEVTDLPKKPPPPEVTDLPKKPPPPEVTDLPKKPSklelsdlskkfPQLGATPFPRK--PLQPEVGE 152
Cdd:PRK12323 380 APVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRS-----------PAPEALAAARQasARGPGGAP 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 153 APLKASLPEPGAPARKPLQPdelshpARPPsepksgafprklwqPEAGEATPRSPQPELSTFPKKPAQPEFNVYPKKPPq 232
Cdd:PRK12323 449 APAPAPAAAPAAAARPAAAG------PRPV--------------AAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFA- 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 233 pqvgglpkksVPQPEFSEAAQTPLwkpqssepkrDSSAFPKKASQPPLSDFPKKPPQPELGDLTRTSSEPEVSVLPKRPR 312
Cdd:PRK12323 508 ----------SPAPAQPDAAPAGW----------VAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPR 567
|
...
gi 768004344 313 PAE 315
Cdd:PRK12323 568 ASA 570
|
|
| PRK14954 |
PRK14954 |
DNA polymerase III subunits gamma and tau; Provisional |
42-149 |
6.34e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184918 [Multi-domain] Cd Length: 620 Bit Score: 43.01 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 42 EFGKLKKFSQPELSEHP---KKAPLPEFGAVSLKPPP--PEVTDL-PKKPPPPEVTDLPKK-PPPPEVTDLPKKPPPPEV 114
Cdd:PRK14954 372 ELVRNDGGVAPSPAGSPdvkKKAPEPDLPQPDRHPGPakPEAPGArPAELPSPASAPTPEQqPPVARSAPLPPSPQASAP 451
|
90 100 110
....*....|....*....|....*....|....*
gi 768004344 115 TDLPKKPSKLELSDLSKKFPQLGATPFPRKPLQPE 149
Cdd:PRK14954 452 RNVASGKPGVDLGSWQGKFMNFTRNGSRKQPVQAS 486
|
|
| PRK14948 |
PRK14948 |
DNA polymerase III subunit gamma/tau; |
18-133 |
1.01e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237862 [Multi-domain] Cd Length: 620 Bit Score: 42.26 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 18 RSIKAKFQASQPEPSDLPKKPPKPefgklkkfsQPELSEHPKKAPLPEFGAVSLKPPPPEvtdlpkkPPPPEVTDLPKKP 97
Cdd:PRK14948 504 RSIKLNLESQSGSASNTAKTPPPP---------QKSPPPPAPTPPLPQPTATAPPPTPPP-------PPPTATQASSNAP 567
|
90 100 110
....*....|....*....|....*....|....*..
gi 768004344 98 PPPEVTDLPKKPPPPEVTDLPKKPSKLE-LSDLSKKF 133
Cdd:PRK14948 568 AQIPADSSPPPPIPEEPTPSPTKDSSPEeIDKAAKNL 604
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
22-185 |
1.47e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.79 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 22 AKFQASQPEPSDLPKKPPKPEfgklkkfSQPELSEHPKKAPLPEFGAVSLKPPPPEvtdlpkkPPPPEVTDLPKKPPPPE 101
Cdd:PRK12323 435 AARQASARGPGGAPAPAPAPA-------AAPAAAARPAAAGPRPVAAAAAAAPARA-------APAAAPAPADDDPPPWE 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 102 vtDLPKKPPPPEVTDLPKKPSKLELSDLSKKFPQLGATPFPRKPLQPEVGEAPLKASLPEPGAPARKPLQPDELSHPARP 181
Cdd:PRK12323 501 --ELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFD 578
|
....
gi 768004344 182 PSEP 185
Cdd:PRK12323 579 GDWP 582
|
|
| SH3_Eps8 |
cd11764 |
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar ... |
608-649 |
1.91e-03 |
|
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar proteins; This group is composed of Eps8 and Eps8-like proteins including Eps8-like 1-3, among others. These proteins contain N-terminal Phosphotyrosine-binding (PTB), central SH3, and C-terminal effector domains. Eps8 binds either Abi1 (also called E3b1) or Rab5 GTPase activating protein RN-tre through its SH3 domain. With Abi1 and Sos1, it becomes part of a trimeric complex that is required to activate Rac. Together with RN-tre, it inhibits the internalization of EGFR. The SH3 domains of Eps8 and similar proteins recognize peptides containing a PxxDY motif, instead of the classical PxxP motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212698 [Multi-domain] Cd Length: 54 Bit Score: 36.86 E-value: 1.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 768004344 608 KHLGIRRGEILEVIEfTSNEEMLCRDPKGKYGYVPRTALLPL 649
Cdd:cd11764 14 KELSVLKGEYLEVLD-DSRQWWKVRNSRGQVGYVPHNILEPY 54
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
25-191 |
2.23e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.40 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 25 QASQPEPSDLPKKPPKPEFGKLKKFSQPELSEHPKKAPLPE--------FGAVSLKPPPPEVTDLP---------KKPPP 87
Cdd:PRK12323 393 AAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALaaarqasaRGPGGAPAPAPAPAAAPaaaarpaaaGPRPV 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 88 PEVTDLPKKPPPPEVTDLPKKPPPPEVTDLPKKPSKLELSDLSKKFPQLGATPFPRKPLQPEVGEAPLKASLPePGAPAR 167
Cdd:PRK12323 473 AAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAP-AAAPAP 551
|
170 180
....*....|....*....|....
gi 768004344 168 KPLQPDELSHPARPPSEPKSGAFP 191
Cdd:PRK12323 552 RAAAATEPVVAPRPPRASASGLPD 575
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
26-367 |
3.26e-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: 40.91 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 26 ASQPEPSDLPKKPPK--PEFGKLKKFSQPELSEHPKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPkKPPPPEVT 103
Cdd:pfam03154 195 ATAGPTPSAPSVPPQgsPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQP-LPQPSLHG 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 104 DLPKKP------PPPEVTDLPKKPSKLELSDLSKKFPQLGATPFPrKPLQPEVGEAPLKASLPEPGAPARKPLQPDELSH 177
Cdd:pfam03154 274 QMPPMPhslqtgPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAP-GQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSM 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 178 P-ARPPSEPKSGAFPRKLWQPEAGEATPRSPQPELSTFPKKPA-QPEFNVYPKKPPQPQVGGLPKKSVPQPEFSEAAQTP 255
Cdd:pfam03154 353 PhIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPPAlKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPP 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 256 LWKPQSSEPKRDSSAFPKKASQ--PPLSDFPKKPPQPELGDLTRTSSEPEVSVLPKRP--RPAEFKALSKKPPQPELGGL 331
Cdd:pfam03154 433 VLTQSQSLPPPAASHPPTSGLHqvPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPgiQPPSSASVSSSGPVPAAVSC 512
|
330 340 350
....*....|....*....|....*....|....*.
gi 768004344 332 PRTSSEPEfNSLPRKLLQPERRGPPRKFSQPEPSAV 367
Cdd:pfam03154 513 PLPPVQIK-EEALDEAEEPESPPPPPRSPSPEPTVV 547
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
162-567 |
3.34e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 162 PGAPARKPLQPDELSHPARPPSEPKSGAFPRKLWQPEAGEATPR-------------------------------SPQPE 210
Cdd:PHA03247 2475 PGAPVYRRPAEARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAPAilpdepvgepvhprmltwirgleelasddagDPPPP 2554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 211 LSTFPkKPAQPEFNVYPKKP-PQPqvgglpkksvPQPEFSEAAQTPLWKPQSSEPK-----RDSSAFPKKASQPPLSDFP 284
Cdd:PHA03247 2555 LPPAA-PPAAPDRSVPPPRPaPRP----------SEPAVTSRARRPDAPPQSARPRapvddRGDPRGPAPPSPLPPDTHA 2623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 285 KKPPQPELGDLTRTSSEPEVSVLPKRPRPAEFKALSKKPPQPELGGLPRTSSEPEFNSLPRKLLQPERRGPPRKFSQPEP 364
Cdd:PHA03247 2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPP 2703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 365 SAVLKRHPQPEFFGDLPrKPPLPSSASESSLPAAVAGFSSRHPLSPGFGAAGTPRWRSGGLVHSGGARPGLRPSHPPRRR 444
Cdd:PHA03247 2704 PPPTPEPAPHALVSATP-LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 445 PLPPASSLGHPPAKPPLPPGPVDMQSFRRPSAASIDLRRTRSAAGL----HFQDRQPEDIPQVPDEIYELYDDVEPRDDS 520
Cdd:PHA03247 2783 LTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLppptSAQPTAPPPPPGPPPPSLPLGGSVAPGGDV 2862
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 768004344 521 SPSPKGRdEAPSVQQAARRPP--QDPALRKEKDPQPQQLPPMDPKLLKQ 567
Cdd:PHA03247 2863 RRRPPSR-SPAAKPAAPARPPvrRLARPAVSRSTESFALPPDQPERPPQ 2910
|
|
| BimA_second |
NF040983 |
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ... |
58-148 |
4.84e-03 |
|
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia intracellular motility A), WP_004266405.1-like proteins in Burkholderia mallei or B. pseudomallei. The term BimA has also been used for WP_011205626.1-like homologs that have a very different N-terminal half.
Pssm-ID: 468913 [Multi-domain] Cd Length: 382 Bit Score: 39.89 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 58 PKKAPLPefgavslkPPPPevtdlPKKPPPPEVTDLPKKPPPPEVTDLPKKPPPPEVTDLPKKPSklelSDLSKKFPQLG 137
Cdd:NF040983 86 PNKVPPP--------PPPP-----PPPPPPPPTPPPPPPPPPPPPPPSPPPPPPPSPPPSPPPPT----TTPPTRTTPST 148
|
90
....*....|..
gi 768004344 138 ATPFPR-KPLQP 148
Cdd:NF040983 149 TTPTPSmHPIQP 160
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
55-416 |
5.12e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 40.44 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 55 SEHPKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPKKP-PPPEVTDLPKKPPPPEVTDLPKKPSKLELSDLSKKF 133
Cdd:PHA03378 438 TEQPRATPHSQAPTVVLHRPPTQPLEGPTGPLSVQAPLEPWQPlPHPQVTPVILHQPPAQGVQAHGSMLDLLEKDDEDME 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 134 PQLGATPFPRKPLQPEVGEAP-------LKASLPEPGAPARKPLQPDELSHPARPPSEPKSGAFPRKLWQPEAGEATPRS 206
Cdd:PHA03378 518 QRVMATLLPPSPPQPRAGRRApcvytedLDIESDEPASTEPVHDQLLPAPGLGPLQIQPLTSPTTSQLASSAPSYAQTPW 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 207 PQPELSTFPKKP---AQPEFNVYPKKPPQP--QVGGLPKKSVPQPEFSEAAQTPLWKPQSSEPKRDS------------- 268
Cdd:PHA03378 598 PVPHPSQTPEPPttqSHIPETSAPRQWPMPlrPIPMRPLRMQPITFNVLVFPTPHQPPQVEITPYKPtwtqighipyqps 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 269 ----------SAFPKKASQPPLSDFPKKPPQPELGDLTR----TSSEPEVSVLPKRPRPAEFKALSKKPPQPELGGLPRT 334
Cdd:PHA03378 678 ptgantmlpiQWAPGTMQPPPRAPTPMRPPAAPPGRAQRpaaaTGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPP 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 335 SSEPEFNSLP-----RKLLQPERRGPPRKFSQPEPSAVLKRHPQ--PEFFGDLPRKPPLPSSASESSLPAAVAGFSSRHP 407
Cdd:PHA03378 758 AAAPGRARPPaaapgAPTPQPPPQAPPAPQQRPRGAPTPQPPPQagPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRGR 837
|
....*....
gi 768004344 408 LSPGFGAAG 416
Cdd:PHA03378 838 PSLKKPAAL 846
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
58-175 |
6.95e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 39.70 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 58 PKKAPL-PEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPkkPPPPEVTDLPKKPPPPEVTDLPKKPSKLELSDLSKKFPQL 136
Cdd:PRK14951 377 EKKTPArPEAAAPAAAPVAQAAAAPAPAAAPAAAASAP--AAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQ 454
|
90 100 110
....*....|....*....|....*....|....*....
gi 768004344 137 GATPFPRKPLQPEVGEAPLKASLPEPGAPARKPLQPDEL 175
Cdd:PRK14951 455 AAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEE 493
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
137-262 |
7.43e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 39.68 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 137 GATPF--------PRKPLQPEVGEAPLKASLPEPGAPARKPLQPDELSHPARPPSEPksgafPRKLWQPEageaTPRSPQ 208
Cdd:PRK10263 718 GANPFslddfefsPMKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAP-----QPQYQQPQ----QPVAPQ 788
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 768004344 209 PELSTFPKKPAQPEFNVYPKKP--PQPQVGGLPKKSVPQPEFSEAAQTPLWKPQSS 262
Cdd:PRK10263 789 PQYQQPQQPVAPQPQYQQPQQPvaPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDT 844
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
12-387 |
8.32e-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: 39.75 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 12 ESHQDFRSIKAKFQASQPEPSDLPKKPPKPEFGKLKKFSQPELSEHPKKAPLPEFGAVSLKPPP--PEVTDLPKKPPPPE 89
Cdd:pfam03154 155 ESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPnqTQSTAAPHTLIQQT 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 90 VTDLPKKPPPPE--VTDLPKKPPPPEVTDLPKKPSKLELSDLSKKFPQLGATPFPRKPLQPEVGEAPLKASLPE--PGAP 165
Cdd:pfam03154 235 PTLHPQRLPSPHppLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQvpPGPS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 166 ARKPLQPDELSHPARPPSEPKSGAFPRKLWQPEAGEATPRSPQPELSTFPKKPAqPEFNVYPKKPPQPQVGGLPKKSVPQ 245
Cdd:pfam03154 315 PAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPN-PQSHKHPPHLSGPSPFQMNSNLPPP 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 246 PEFSEAAQTPLWKPQSSEPK-----RDSSAFPKKASQPPLSDFPKKPPQPELGDLTRTSSEPevsVLPKRPRPAEFKALS 320
Cdd:pfam03154 394 PALKPLSSLSTHHPPSAHPPplqlmPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQ---VPSQSPFPQHPFVPG 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768004344 321 KKPPQPELGGLPRTSSEPEFNSLPRKLLQPERRGP-PRKFSQPEPSAVLKRHPQPEffGDLPRKPPLP 387
Cdd:pfam03154 471 GPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPvPAAVSCPLPPVQIKEEALDE--AEEPESPPPP 536
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
70-288 |
9.82e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 39.14 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 70 SLKPPPPE--VTDLPKKPPPPEVTDLPKKPP----PPEVTDLPKKPPPPEVT--DL--PKKPSKLELSDLSKKFPQLGAT 139
Cdd:PLN03209 325 SQRVPPKEsdAADGPKPVPTKPVTPEAPSPPieeePPQPKAVVPRPLSPYTAyeDLkpPTSPIPTPPSSSPASSKSVDAV 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 140 PFPRKP-LQPEVGEAPLKASLPEPGAPARK--PLQP----DELSHPARPPSEPKSGAFPRKLwQPEAGEATPRSPQPELS 212
Cdd:PLN03209 405 AKPAEPdVVPSPGSASNVPEVEPAQVEAKKtrPLSPyaryEDLKPPTSPSPTAPTGVSPSVS-STSSVPAVPDTAPATAA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004344 213 TFPKKPAQP------EFNVYPK-KPPQPQVGGLPKKSVPQPEFSEAAQTPLWKPQSSEPKRDSSAFPKkasQPPLSDFPK 285
Cdd:PLN03209 484 TDAAAPPPAnmrplsPYAVYDDlKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQPK---PRPLSPYTM 560
|
....*..
gi 768004344 286 ----KPP 288
Cdd:PLN03209 561 yedlKPP 567
|
|
| |
