|
Name |
Accession |
Description |
Interval |
E-value |
| hSH3 |
pfam14603 |
Helically-extended SH3 domain; This domain is the 70 C-terminal residues of ADAP - Adhesion ... |
576-655 |
1.11e-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: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 576 FRKKFKFEGEIVVHTKMMIDPNAKTRRGGGKHLGIRRGEILEVIEFTSNEEMLCRDPKGKYGYVPRTALLPLETEVYDDV 655
Cdd:pfam14603 1 FRKKFKYDGEIKVLYSMTVDPNLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNLLQNDGEIYDDI 80
|
|
| hSH3_ADAP |
cd11867 |
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ... |
570-646 |
2.33e-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: 77.18 E-value: 2.33e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530427551 570 EKAEREFRKKFKFEGEIVVHTKMMIDPNAKTRRGGGKHLGIRRGEILEVIEFTSNEEMLCRDPKGKYGYVPRTALLP 646
Cdd:cd11867 1 EKEEKEFRKKFKYNGEIKVLYSTTVLQTLTIKKFGSKDLQVKPGESLEVIQHTDDTKVLCRNEEGKYGYVLRSNLEP 77
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
56-412 |
4.81e-13 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 73.05 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 56 PKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTdlPKKPPPPEVTDLPKKPPPPEVTDLPKKPSKLELS-----DLSKK 130
Cdd:PHA03247 2589 PDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTH--APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPapgrvSRPRR 2666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 131 FPQLGATPFPRKPLQ--------PEVGEAPLKASLPEPGAPARKPLQPDELSHPARPPSEPKSGAFPRKLWQP-----EA 197
Cdd:PHA03247 2667 ARRLGRAAQASSPPQrprrraarPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPappavPA 2746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 198 GEATP----RSPQPELSTFPKKPAQPEFNVYPKKPPQPQVGGLP----KKSVPQPEFSEAAQTPLWKPQSSEPkrdSSAF 269
Cdd:PHA03247 2747 GPATPggpaRPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASlsesRESLPSPWDPADPPAAVLAPAAALP---PAAS 2823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 270 PKKASQPPLSDFPKKPPQPElgDLTRTSSEPEVSVLP-----KRPRPAEFKALSKKPPQPELGGLPRTSSEPEFNSLPRK 344
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPP--GPPPPSLPLGGSVAPggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALP 2901
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530427551 345 LLQPERRGPPRKFSQPEPSAVLKRHPQPEffgDLPRKPPLPSSASESSLPAAVAGFSSRHPLSPGFGA 412
Cdd:PHA03247 2902 PDQPERPPQPQAPPPPQPQPQPPPPPQPQ---PPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGA 2966
|
|
| ftsN |
TIGR02223 |
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ... |
71-252 |
1.80e-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: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 71 PPPPEVTDLPKKPPPPEVTDLPKKPPPPE-----VTDLPKkpPPPEVTDLPKKPSKLELSDLSKKFPQLGATPFPRKPLQ 145
Cdd:TIGR02223 52 KQANEPETLQPKNQTENGETAADLPPKPEerwsyIEELEA--REVLINDPEEPSNGGGVEESAQLTAEQRQLLEQMQADM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 146 pevgEAPLKASLPEPGAPARKPLQPDELSHPARPPSEPKsgafprklwqpeagEATPRSPQPELSTFPKKPAQPEFNVYP 225
Cdd:TIGR02223 130 ----RAAEKVLATAPSEQTVAVEARKQTAEKKPQKARTA--------------EAQKTPVETEKIASKVKEAKQKQKALP 191
|
170 180
....*....|....*....|....*..
gi 530427551 226 KKPPQPQVGGLPKKSVPQPEFSEAAQT 252
Cdd:TIGR02223 192 KQTAETQSNSKPIETAPKADKADKTKP 218
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
49-416 |
3.96e-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: 43.99 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 49 QPELSEHPKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPKKPPPPevtdlpkKPPPPEVTDLPKKPSKLELSDLS 128
Cdd:pfam03154 164 QQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPA-------TSQPPNQTQSTAAPHTLIQQTPT 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 129 KKFPQLgatPFPRKPLQPevgeaplkasLPEPGAPARKPLQ--PDELSHPARPPSEPKSGAFPRKLWQPEAGEATPRSPQ 206
Cdd:pfam03154 237 LHPQRL---PSPHPPLQP----------MTQPPPPSQVSPQplPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 207 PELSTFPkkpaqpefnvypkKPPQPQVGGLPKKSVPQPefseaaqTPLWKPQSSEPKRDSSAFPKKASQPPLSDfPKKPP 286
Cdd:pfam03154 304 SSQSQVP-------------PGPSPAAPGQSQQRIHTP-------PSQSQLQSQQPPREQPLPPAPLSMPHIKP-PPTTP 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 287 QPELGDLTRTSSEPEVSVlpkrprPAEFKALSKKPPQPELGGL-------PRTSSEPEFNSLPR-KLLQPERRGPPRKFS 358
Cdd:pfam03154 363 IPQLPNPQSHKHPPHLSG------PSPFQMNSNLPPPPALKPLsslsthhPPSAHPPPLQLMPQsQQLPPPPAQPPVLTQ 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 530427551 359 QPEPSAVLKRHPQPEFFGDLPRKPPLPSSASESSLPAAVAGFSSRHPLSPGFGAAGTP 416
Cdd:pfam03154 437 SQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQP 494
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
28-288 |
5.07e-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: 43.22 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 28 EPSDLPKKPPKPEFGKLKKFSQPELSEHPKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPKKP----PPPEVTDL 103
Cdd:NF033839 256 EIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPqlekPKPEVKPQ 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 104 PKKPPPpEVTDLPKKPSKLELSDLSKKFPQLGATPFPRKPLQPEVGEAPLKASLPEPGAParkplQPDELSHPARPPSEP 183
Cdd:NF033839 336 PEKPKP-EVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKP-----KPEVKPQPEKPKPEV 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 184 KsgafPRKLWQPEAGEATPRSPQPELSTFPKKPaQPEFNVYPKKpPQPQVGGLPKKSVPQPEFSEAAQTPLWKPQSSEPK 263
Cdd:NF033839 410 K----PQPEKPKPEVKPQPEKPKPEVKPQPEKP-KPEVKPQPEK-PKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPK 483
|
250 260
....*....|....*....|....*
gi 530427551 264 RDSSAFPKKASQPPLSDFPKKPPQP 288
Cdd:NF033839 484 PDNSKPQADDKKPSTPNNLSKDKQP 508
|
|
| BimA_second |
NF040983 |
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ... |
56-146 |
6.04e-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: 39.50 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 56 PKKAPLPefgavslkPPPPevtdlPKKPPPPEVTDLPKKPPPPEVTDLPKKPPPPEVTDLPKKPSklelSDLSKKFPQLG 135
Cdd:NF040983 86 PNKVPPP--------PPPP-----PPPPPPPPTPPPPPPPPPPPPPPSPPPPPPPSPPPSPPPPT----TTPPTRTTPST 148
|
90
....*....|..
gi 530427551 136 ATPFPR-KPLQP 146
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 ... |
576-655 |
1.11e-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: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 576 FRKKFKFEGEIVVHTKMMIDPNAKTRRGGGKHLGIRRGEILEVIEFTSNEEMLCRDPKGKYGYVPRTALLPLETEVYDDV 655
Cdd:pfam14603 1 FRKKFKYDGEIKVLYSMTVDPNLTIKKWGGKDLPVKPGEVLDVIQKTDDTKVLCRNEEGKYGYVLRSNLLQNDGEIYDDI 80
|
|
| hSH3_ADAP |
cd11867 |
Helically extended Src Homology 3 domain of Adhesion and Degranulation-promoting Adaptor ... |
570-646 |
2.33e-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: 77.18 E-value: 2.33e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530427551 570 EKAEREFRKKFKFEGEIVVHTKMMIDPNAKTRRGGGKHLGIRRGEILEVIEFTSNEEMLCRDPKGKYGYVPRTALLP 646
Cdd:cd11867 1 EKEEKEFRKKFKYNGEIKVLYSTTVLQTLTIKKFGSKDLQVKPGESLEVIQHTDDTKVLCRNEEGKYGYVLRSNLEP 77
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
56-412 |
4.81e-13 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 73.05 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 56 PKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTdlPKKPPPPEVTDLPKKPPPPEVTDLPKKPSKLELS-----DLSKK 130
Cdd:PHA03247 2589 PDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTH--APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPapgrvSRPRR 2666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 131 FPQLGATPFPRKPLQ--------PEVGEAPLKASLPEPGAPARKPLQPDELSHPARPPSEPKSGAFPRKLWQP-----EA 197
Cdd:PHA03247 2667 ARRLGRAAQASSPPQrprrraarPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPappavPA 2746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 198 GEATP----RSPQPELSTFPKKPAQPEFNVYPKKPPQPQVGGLP----KKSVPQPEFSEAAQTPLWKPQSSEPkrdSSAF 269
Cdd:PHA03247 2747 GPATPggpaRPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASlsesRESLPSPWDPADPPAAVLAPAAALP---PAAS 2823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 270 PKKASQPPLSDFPKKPPQPElgDLTRTSSEPEVSVLP-----KRPRPAEFKALSKKPPQPELGGLPRTSSEPEFNSLPRK 344
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPP--GPPPPSLPLGGSVAPggdvrRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALP 2901
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530427551 345 LLQPERRGPPRKFSQPEPSAVLKRHPQPEffgDLPRKPPLPSSASESSLPAAVAGFSSRHPLSPGFGA 412
Cdd:PHA03247 2902 PDQPERPPQPQAPPPPQPQPQPPPPPQPQ---PPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGA 2966
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
24-373 |
7.60e-13 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 72.03 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 24 ASQPEPSDLPKKPPKPEFgklkkfsqPELSEHPKKaplPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPKKPPPPEVTDL 103
Cdd:PTZ00449 564 AKEHKPSKIPTLSKKPEF--------PKDPKHPKD---PEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKS 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 104 PKKPPPPEVTDLPKKPSklelsdlSKKFPQLgatpfPRKPLQPEVgeaplkaslpePGAPARKPLQPDELSHPARPPSEP 183
Cdd:PTZ00449 633 PKRPPPPQRPSSPERPE-------GPKIIKS-----PKPPKSPKP-----------PFDPKFKEKFYDDYLDAAAKSKET 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 184 KSGAFPRKLWQPEAGEATPRSPQPELSTF----PKKPAQPEFNVYP-KKPPQPQVGGLPKKSVPQPEFSEAAQTPLWKP- 257
Cdd:PTZ00449 690 KTTVVLDESFESILKETLPETPGTPFTTPrplpPKLPRDEEFPFEPiGDPDAEQPDDIEFFTPPEEERTFFHETPADTPl 769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 258 ---------------QSSEP----KRDSSafPKKASQPPLSDFPKKPPQPELGD---LTRTSSEPEVSVLPKRP------ 309
Cdd:PTZ00449 770 pdilaeefkeedihaETGEPdeamKRPDS--PSEHEDKPPGDHPSLPKKRHRLDglaLSTTDLESDAGRIAKDAsgkivk 847
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530427551 310 --RPAEFKALSKKPPQPELGGLPR--------TSSEPEFNSLP--RKLLQPERRGPPRKFSQPEPSAVLKRHPQPE 373
Cdd:PTZ00449 848 lkRSKSFDDLTTVEEAEEMGAEARkivvdddgTEADDEDTHPPeeKHKSEVRRRRPPKKPSKPKKPSKPKKPKKPD 923
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
5-334 |
3.69e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 63.80 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 5 LPAAMESHQDFRSIKAKFQASQPEPSDLPKKPPKPEFGKLKKFSQPELSEHPKKAPLPEFGAVSLKPPPPEVTDLPKKPP 84
Cdd:PHA03247 2688 ARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPP 2767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 85 PPEVTDLPKKPPPPEVTDLPKKPPPPEVTDLPKKPSKLELSdlskkFPQLGATPFPRKPLQPEVGEAPLKASLPEPGAPA 164
Cdd:PHA03247 2768 APAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPP-----AAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPP 2842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 165 RKPLQPDELSHPARPPSEPKSGAFPRKlwQPEAGEATPrsPQPELSTFPKKPAQPEFNVYPKKPPQPQVGGLPKKSVPQP 244
Cdd:PHA03247 2843 PGPPPPSLPLGGSVAPGGDVRRRPPSR--SPAAKPAAP--ARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQ 2918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 245 EFSEAAQTPLWKPQSSEPKRDSSAFPKKASQPPLSDFPKKPPQPELGDLTRTSSEPEVSVLPKRPRPAEFKALSkkPPQP 324
Cdd:PHA03247 2919 PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASS--TPPL 2996
|
330
....*....|
gi 530427551 325 ELGGLPRTSS 334
Cdd:PHA03247 2997 TGHSLSRVSS 3006
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
81-390 |
1.96e-09 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 61.24 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 81 KKPPPPEVTDLPKKPPPPEVTDL----PKKPPPPEVTDLPKKPSKLelSDLSKKFPQlgatpfPRKPLQPEVGEAPlkas 156
Cdd:PTZ00449 494 KKLAPIEEEDSDKHDEPPEGPEAsglpPKAPGDKEGEEGEHEDSKE--SDEPKEGGK------PGETKEGEVGKKP---- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 157 lpepgAPARKplqpdelSHPARPPSEPKSGAFPRKlwqpeageatPRSPQ-PELSTFPKKPAQPEFNVYPKKPPQPQVGG 235
Cdd:PTZ00449 562 -----GPAKE-------HKPSKIPTLSKKPEFPKD----------PKHPKdPEEPKKPKRPRSAQRPTRPKSPKLPELLD 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 236 LPkKSVPQPEFSEAAQTPLWKPQSSEPKRDSSAFPKKASQPPLSdfPKKPPQPEL-----GDLTRTSSEPEVSVLPKRPR 310
Cdd:PTZ00449 620 IP-KSPKRPESPKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKS--PKPPFDPKFkekfyDDYLDAAAKSKETKTTVVLD 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 311 PAEFKALskKPPQPELGGLPRTSSEPEFNSLPRKLLQPERrgPPRKFSQPEPSAVLKRHPQPE---FFGDLPRKPPLPSS 387
Cdd:PTZ00449 697 ESFESIL--KETLPETPGTPFTTPRPLPPKLPRDEEFPFE--PIGDPDAEQPDDIEFFTPPEEertFFHETPADTPLPDI 772
|
...
gi 530427551 388 ASE 390
Cdd:PTZ00449 773 LAE 775
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
59-394 |
7.78e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.57 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 59 APLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLP-KKPPPPEV-----------TDLPKKPPPPEVTDLPKKPsklelSD 126
Cdd:PHA03247 2491 AAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPvGEPVHPRMltwirgleelaSDDAGDPPPPLPPAAPPAA-----PD 2565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 127 LSKKFPQLGATPF----------PRKPLQPEVGEAPLKASLPEPGAPARKPLQPDElSHPARPPSEPKSGAFPRKLWQPE 196
Cdd:PHA03247 2566 RSVPPPRPAPRPSepavtsrarrPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDT-HAPDPPPPSPSPAANEPDPHPPP 2644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 197 AGEATPR---SPQPELSTFPKKPAQPEFNVYPKKPPQ--------PQVGGLPKKSVPQPEFSEAAQTPlwKPQSSEPKRD 265
Cdd:PHA03247 2645 TVPPPERprdDPAPGRVSRPRRARRLGRAAQASSPPQrprrraarPTVGSLTSLADPPPPPPTPEPAP--HALVSATPLP 2722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 266 SSAFPKKASQPPLSDFPKKPPQPELGDLTRTSSEPEVSVLPKRPRPAEFKALSKKPPQPELGGLPRTSSEPEFNSLPRKL 345
Cdd:PHA03247 2723 PGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPW 2802
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 530427551 346 LQPERRGPPRKFSQPEPSAVLKRHPQPEFFGDLPRKPPLPSSASESSLP 394
Cdd:PHA03247 2803 DPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
228-396 |
4.86e-06 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 50.07 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 228 PPQPQVGGLPKKSVPQPEFSEAAQTPLWKPQSSE----PKRDSSAFPKKASQPPLSDFPKKPP----QPELGDLTRTSSE 299
Cdd:PTZ00449 511 PEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKeggkPGETKEGEVGKKPGPAKEHKPSKIPtlskKPEFPKDPKHPKD 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 300 PEVSVLPKRPRPAEFKALSKKPPQPELGGLPRTSSEPEFNSLPRKLLQPERRGPPRKfsqPEPSAVLKRhPQPEFFGDLP 379
Cdd:PTZ00449 591 PEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPSSPER---PEGPKIIKS-PKPPKSPKPP 666
|
170
....*....|....*..
gi 530427551 380 RKPPLPSSASESSLPAA 396
Cdd:PTZ00449 667 FDPKFKEKFYDDYLDAA 683
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
56-278 |
9.34e-06 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 49.10 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 56 PKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPKKPPPPEVTDLP-KKPPPPEVTDLPKKPSKLELSDLSKKFPQL 134
Cdd:PRK12323 375 ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPaRRSPAPEALAAARQASARGPGGAPAPAPAP 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 135 GATPFP--RKPLQPEVGEAPLKASLPEPGAPARKPLQPDElshpARPPSEPKSGAFPrklwQPEAGEATPRSPQPELSTF 212
Cdd:PRK12323 455 AAAPAAaaRPAAAGPRPVAAAAAAAPARAAPAAAPAPADD----DPPPWEELPPEFA----SPAPAQPDAAPAGWVAESI 526
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530427551 213 PKKPAQPEFNVYPKKPPQPQVGGLPKKSVPQPEFseAAQTPLWKPQSSEPKRDSSAFPKKASQPPL 278
Cdd:PRK12323 527 PDPATADPDDAFETLAPAPAAAPAPRAAAATEPV--VAPRPPRASASGLPDMFDGDWPALAARLPV 590
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
55-253 |
5.23e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.52 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 55 HPKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPKKPPPPEVTDLPKKPPPPEVTDLPKKPSKLELSDLSKKFPQL 134
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 135 GATPFPRKPLQPEVGEAPlkaslPEPGAPARKPLQPDELSHPARPPSEPKSGAFPRKLWQPEAGEATPRSPQPELSTFPK 214
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAP-----AAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPE 744
|
170 180 190
....*....|....*....|....*....|....*....
gi 530427551 215 KPAQPEFNVYPKKPPQPQVGGLPKKSVPQPEFSEAAQTP 253
Cdd:PRK07764 745 PDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
151-421 |
7.64e-05 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 46.23 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 151 APLKASLPEPGAPARKPL--QPDELSHPARPPSEPKSGAFPR-KLWQPEAGEATPRSPQPELSTFPKKPAQPEFNVYPKK 227
Cdd:PRK10263 335 APVEPVTQTPPVASVDVPpaQPTVAWQPVPGPQTGEPVIAPApEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 228 PPQ-PQVGGLPKKSVPQPEFSEAAQTPLWKPQSSEPKRDSSAFPKKASQP------PLSDFPKKPPQPELGDLTRTSSEP 300
Cdd:PRK10263 415 PAQqPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTeqtyqqPAAQEPLYQQPQPVEQQPVVEPEP 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 301 EV-SVLPKRPRPAEFKALSKKppqpelgglpRTSSEPEFNSLPRKLLQPERRGPPRKFSQPEPSAvlkrhPQPEFFGDLP 379
Cdd:PRK10263 495 VVeETKPARPPLYYFEEVEEK----------RAREREQLAAWYQPIPEPVKEPEPIKSSLKAPSV-----AAVPPVEAAA 559
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 530427551 380 RKPPLPSSASESSLPAAVAGFSSRHPLSPGFGAAGTPRWRSG 421
Cdd:PRK10263 560 AVSPLASGVKKATLATGAAATVAAPVFSLANSGGPRPQVKEG 601
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
27-433 |
8.06e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 46.32 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 27 PEPSDLPKKPPKPEFGKLKKFSQPELSEHPKKAPLPEFGAVSLKPPPPEVTDlPKKPPPPEVTDLPKK------------ 94
Cdd:PHA03307 71 PPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPP-PASPPPSPAPDLSEMlrpvgspgpppa 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 95 --PPPPEVtdlpkkPPPPEVTDLpkkPSKLELSDLSKKFPQLGATPFPRKPlqpevgEAPLKASLPEPGAPARKPLQPDE 172
Cdd:PHA03307 150 asPPAAGA------SPAAVASDA---ASSRQAALPLSSPEETARAPSSPPA------EPPPSTPPAAASPRPPRRSSPIS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 173 LSHPARPPSEPKSGAFPRklwqpeageatPRSPQPELSTFPKKPAQPEFNVYPKKPPQPQVGGLPKKSVPQPEfSEAAQT 252
Cdd:PHA03307 215 ASASSPAPAPGRSAADDA-----------GASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWN-GPSSRP 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 253 PLWKPQSSEPKRDSSAFPKKASQPPLSDFPKKP----PQPELGDLTRTSSEPEVSVLPKRPRPAEFKALSKKPPQPELGG 328
Cdd:PHA03307 283 GPASSSSSPRERSPSPSPSSPGSGPAPSSPRASssssSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 329 lPRTSSEPEFNSLPRKLLQPERRGPPRKFSQPEPSAVLKRHPQPEFFGDLPRKPPLPSSASESSLPAavagfssRHPL-- 406
Cdd:PHA03307 363 -SSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYA-------RYPLlt 434
|
410 420 430
....*....|....*....|....*....|..
gi 530427551 407 ---SPGFGAAGTP--RWRSGGLvhsGGARPGL 433
Cdd:PHA03307 435 psgEPWPGSPPPPpgRVRYGGL---GDSRPGL 463
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
141-573 |
1.07e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 141 RKPLQPEVGEAPLKASLPEPGAPArkplQPDELShPARPPSEPKSGAFPRKLWQ-----PEAGEATPRSPQPELSTFPKk 215
Cdd:PHA03247 2487 RFPFAAGAAPDPGGGGPPDPDAPP----APSRLA-PAILPDEPVGEPVHPRMLTwirglEELASDDAGDPPPPLPPAAP- 2560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 216 PAQPEFNVYPKKP-PQPqvgglpkksvPQPEFSEAAQTPLWKPQSSEPK-----RDSSAFPKKASQPPLSDFPKKPPQPE 289
Cdd:PHA03247 2561 PAAPDRSVPPPRPaPRP----------SEPAVTSRARRPDAPPQSARPRapvddRGDPRGPAPPSPLPPDTHAPDPPPPS 2630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 290 LGDLTRTSSEPEVSVLPKRPRPAEFKALSKKPPQPELGGLPRTSSEPEFNSLPRKLLQPERRGPPRKFSQPEPSAVLKRH 369
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEP 2710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 370 PQPEFFGDLPrKPPLPSSASESSLPAAVAGFSSRHPLSPGFGAAGTPRWRSGGLVHSGGARPGLRPSHPPRRRPLPPASS 449
Cdd:PHA03247 2711 APHALVSATP-LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVA 2789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 450 LGHPPAKPPLPPGPVDMQSFRRPSAASIDLRRTRSAAGL----HFQDRQPEDIPQVPDEIYELYDDVEPRDDSSPSPKGR 525
Cdd:PHA03247 2790 SLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLppptSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSR 2869
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 530427551 526 DEAPSVQQAAR-------RPPQDPALRKEKDPQPQQLPPMDPKLLKQLRKAEKAE 573
Cdd:PHA03247 2870 SPAAKPAAPARppvrrlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPP 2924
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
149-354 |
1.60e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.87 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 149 GEAPLKASLPEPGAPARKPLQPDELSHPARPPSEPKSGAFPRKLWQPEAGEATPRSPQPELSTFPKKPAQPEFNVYPKKP 228
Cdd:PRK12323 370 GGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 229 PQPQVGGLPKKSVPQPEFSEAAQTPLWKPQSSEPKRDSSAFPKKASQPPLSDFPKKPPQPELGDLTRTSSEPEVSVLPKR 308
Cdd:PRK12323 450 PAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDP 529
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 530427551 309 PRPAEFKALSKKPPQPELGGLPRTSSEPEFNSLPRKLLQPERRGPP 354
Cdd:PRK12323 530 ATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPD 575
|
|
| ftsN |
TIGR02223 |
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ... |
71-252 |
1.80e-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: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 71 PPPPEVTDLPKKPPPPEVTDLPKKPPPPE-----VTDLPKkpPPPEVTDLPKKPSKLELSDLSKKFPQLGATPFPRKPLQ 145
Cdd:TIGR02223 52 KQANEPETLQPKNQTENGETAADLPPKPEerwsyIEELEA--REVLINDPEEPSNGGGVEESAQLTAEQRQLLEQMQADM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 146 pevgEAPLKASLPEPGAPARKPLQPDELSHPARPPSEPKsgafprklwqpeagEATPRSPQPELSTFPKKPAQPEFNVYP 225
Cdd:TIGR02223 130 ----RAAEKVLATAPSEQTVAVEARKQTAEKKPQKARTA--------------EAQKTPVETEKIASKVKEAKQKQKALP 191
|
170 180
....*....|....*....|....*..
gi 530427551 226 KKPPQPQVGGLPKKSVPQPEFSEAAQT 252
Cdd:TIGR02223 192 KQTAETQSNSKPIETAPKADKADKTKP 218
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
49-416 |
3.96e-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: 43.99 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 49 QPELSEHPKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPKKPPPPevtdlpkKPPPPEVTDLPKKPSKLELSDLS 128
Cdd:pfam03154 164 QQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPA-------TSQPPNQTQSTAAPHTLIQQTPT 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 129 KKFPQLgatPFPRKPLQPevgeaplkasLPEPGAPARKPLQ--PDELSHPARPPSEPKSGAFPRKLWQPEAGEATPRSPQ 206
Cdd:pfam03154 237 LHPQRL---PSPHPPLQP----------MTQPPPPSQVSPQplPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 207 PELSTFPkkpaqpefnvypkKPPQPQVGGLPKKSVPQPefseaaqTPLWKPQSSEPKRDSSAFPKKASQPPLSDfPKKPP 286
Cdd:pfam03154 304 SSQSQVP-------------PGPSPAAPGQSQQRIHTP-------PSQSQLQSQQPPREQPLPPAPLSMPHIKP-PPTTP 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 287 QPELGDLTRTSSEPEVSVlpkrprPAEFKALSKKPPQPELGGL-------PRTSSEPEFNSLPR-KLLQPERRGPPRKFS 358
Cdd:pfam03154 363 IPQLPNPQSHKHPPHLSG------PSPFQMNSNLPPPPALKPLsslsthhPPSAHPPPLQLMPQsQQLPPPPAQPPVLTQ 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 530427551 359 QPEPSAVLKRHPQPEFFGDLPRKPPLPSSASESSLPAAVAGFSSRHPLSPGFGAAGTP 416
Cdd:pfam03154 437 SQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQP 494
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
28-288 |
5.07e-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: 43.22 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 28 EPSDLPKKPPKPEFGKLKKFSQPELSEHPKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPKKP----PPPEVTDL 103
Cdd:NF033839 256 EIENTVHKIFADMDAVVTKFKKGLTQDTPKEPGNKKPSAPKPGMQPSPQPEKKEVKPEPETPKPEVKPqlekPKPEVKPQ 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 104 PKKPPPpEVTDLPKKPSKLELSDLSKKFPQLGATPFPRKPLQPEVGEAPLKASLPEPGAParkplQPDELSHPARPPSEP 183
Cdd:NF033839 336 PEKPKP-EVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKPQPEKP-----KPEVKPQPEKPKPEV 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 184 KsgafPRKLWQPEAGEATPRSPQPELSTFPKKPaQPEFNVYPKKpPQPQVGGLPKKSVPQPEFSEAAQTPLWKPQSSEPK 263
Cdd:NF033839 410 K----PQPEKPKPEVKPQPEKPKPEVKPQPEKP-KPEVKPQPEK-PKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPK 483
|
250 260
....*....|....*....|....*
gi 530427551 264 RDSSAFPKKASQPPLSDFPKKPPQP 288
Cdd:NF033839 484 PDNSKPQADDKKPSTPNNLSKDKQP 508
|
|
| PRK14954 |
PRK14954 |
DNA polymerase III subunits gamma and tau; Provisional |
40-147 |
6.48e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184918 [Multi-domain] Cd Length: 620 Bit Score: 43.01 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 40 EFGKLKKFSQPELSEHP---KKAPLPEFGAVSLKPPP--PEVTDL-PKKPPPPEVTDLPKK-PPPPEVTDLPKKPPPPEV 112
Cdd:PRK14954 372 ELVRNDGGVAPSPAGSPdvkKKAPEPDLPQPDRHPGPakPEAPGArPAELPSPASAPTPEQqPPVARSAPLPPSPQASAP 451
|
90 100 110
....*....|....*....|....*....|....*
gi 530427551 113 TDLPKKPSKLELSDLSKKFPQLGATPFPRKPLQPE 147
Cdd:PRK14954 452 RNVASGKPGVDLGSWQGKFMNFTRNGSRKQPVQAS 486
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
73-313 |
7.62e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.94 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 73 PPEVTDLPKKPPPPEVTDLPKKPPPPEVTDLPKKPPPPEVTDLPKKPSklelsdlskkfPQLGATPFPRK--PLQPEVGE 150
Cdd:PRK12323 380 APVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRS-----------PAPEALAAARQasARGPGGAP 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 151 APLKASLPEPGAPARKPLQPdelshpARPPsepksgafprklwqPEAGEATPRSPQPELSTFPKKPAQPEFNVYPKKPPq 230
Cdd:PRK12323 449 APAPAPAAAPAAAARPAAAG------PRPV--------------AAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFA- 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 231 pqvgglpkksVPQPEFSEAAQTPLwkpqssepkrDSSAFPKKASQPPLSDFPKKPPQPELGDLTRTSSEPEVSVLPKRPR 310
Cdd:PRK12323 508 ----------SPAPAQPDAAPAGW----------VAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPR 567
|
...
gi 530427551 311 PAE 313
Cdd:PRK12323 568 ASA 570
|
|
| PRK14948 |
PRK14948 |
DNA polymerase III subunit gamma/tau; |
16-131 |
1.18e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237862 [Multi-domain] Cd Length: 620 Bit Score: 42.26 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 16 RSIKAKFQASQPEPSDLPKKPPKPefgklkkfsQPELSEHPKKAPLPEFGAVSLKPPPPEvtdlpkkPPPPEVTDLPKKP 95
Cdd:PRK14948 504 RSIKLNLESQSGSASNTAKTPPPP---------QKSPPPPAPTPPLPQPTATAPPPTPPP-------PPPTATQASSNAP 567
|
90 100 110
....*....|....*....|....*....|....*..
gi 530427551 96 PPPEVTDLPKKPPPPEVTDLPKKPSKLE-LSDLSKKF 131
Cdd:PRK14948 568 AQIPADSSPPPPIPEEPTPSPTKDSSPEeIDKAAKNL 604
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
72-286 |
1.67e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.79 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 72 PPPEVTDLPKKPPPPEVTDLPKKPPPPevtdlPKKPPPPEVTDLPKKPSKLELSDLSKKFPQLGATPFPRK--PLQPEVG 149
Cdd:PRK12323 373 GPATAAAAPVAQPAPAAAAPAAAAPAP-----AAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQasARGPGGA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 150 EAPLKASLPEPGAPARKPLQpdelshPARPPSEPKSGAFPRKlwQPEAGEATPRSPQPELSTFPKKPAQPEFNVYPKKPP 229
Cdd:PRK12323 448 PAPAPAPAAAPAAAARPAAA------GPRPVAAAAAAAPARA--APAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPA 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530427551 230 QPQVGGLPKKSVPQPEFSEAAQTPLwKPQSSEPKRDSSAFPKKASQPPLSDFPKKPP 286
Cdd:PRK12323 520 GWVAESIPDPATADPDDAFETLAPA-PAAAPAPRAAAATEPVVAPRPPRASASGLPD 575
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
20-183 |
1.84e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.40 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 20 AKFQASQPEPSDLPKKPPKPEfgklkkfSQPELSEHPKKAPLPEFGAVSLKPPPPEvtdlpkkPPPPEVTDLPKKPPPPE 99
Cdd:PRK12323 435 AARQASARGPGGAPAPAPAPA-------AAPAAAARPAAAGPRPVAAAAAAAPARA-------APAAAPAPADDDPPPWE 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 100 vtDLPKKPPPPEVTDLPKKPSKLELSDLSKKFPQLGATPFPRKPLQPEVGEAPLKASLPEPGAPARKPLQPDELSHPARP 179
Cdd:PRK12323 501 --ELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFD 578
|
....
gi 530427551 180 PSEP 183
Cdd:PRK12323 579 GDWP 582
|
|
| SH3_Eps8 |
cd11764 |
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar ... |
606-647 |
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 530427551 606 KHLGIRRGEILEVIEfTSNEEMLCRDPKGKYGYVPRTALLPL 647
Cdd:cd11764 14 KELSVLKGEYLEVLD-DSRQWWKVRNSRGQVGYVPHNILEPY 54
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
23-189 |
2.97e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.01 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 23 QASQPEPSDLPKKPPKPEFGKLKKFSQPELSEHPKKAPLPE--------FGAVSLKPPPPEVTDLP---------KKPPP 85
Cdd:PRK12323 393 AAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALaaarqasaRGPGGAPAPAPAPAAAPaaaarpaaaGPRPV 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 86 PEVTDLPKKPPPPEVTDLPKKPPPPEVTDLPKKPSKLELSDLSKKFPQLGATPFPRKPLQPEVGEAPLKASLPePGAPAR 165
Cdd:PRK12323 473 AAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAP-AAAPAP 551
|
170 180
....*....|....*....|....
gi 530427551 166 KPLQPDELSHPARPPSEPKSGAFP 189
Cdd:PRK12323 552 RAAAATEPVVAPRPPRASASGLPD 575
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
160-565 |
4.29e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.69 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 160 PGAPARKPLQPDELSHPARPPSEPKSGAFPRKLWQPEAGEATPR-------------------------------SPQPE 208
Cdd:PHA03247 2475 PGAPVYRRPAEARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAPAilpdepvgepvhprmltwirgleelasddagDPPPP 2554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 209 LSTFPkKPAQPEFNVYPKKP-PQPqvgglpkksvPQPEFSEAAQTPLWKPQSSEPK-----RDSSAFPKKASQPPLSDFP 282
Cdd:PHA03247 2555 LPPAA-PPAAPDRSVPPPRPaPRP----------SEPAVTSRARRPDAPPQSARPRapvddRGDPRGPAPPSPLPPDTHA 2623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 283 KKPPQPELGDLTRTSSEPEVSVLPKRPRPAEFKALSKKPPQPELGGLPRTSSEPEFNSLPRKLLQPERRGPPRKFSQPEP 362
Cdd:PHA03247 2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPP 2703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 363 SAVLKRHPQPEFFGDLPrKPPLPSSASESSLPAAVAGFSSRHPLSPGFGAAGTPRWRSGGLVHSGGARPGLRPSHPPRRR 442
Cdd:PHA03247 2704 PPPTPEPAPHALVSATP-LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 443 PLPPASSLGHPPAKPPLPPGPVDMQSFRRPSAASIDLRRTRSAAGL----HFQDRQPEDIPQVPDEIYELYDDVEPRDDS 518
Cdd:PHA03247 2783 LTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLppptSAQPTAPPPPPGPPPPSLPLGGSVAPGGDV 2862
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 530427551 519 SPSPKGRdEAPSVQQAARRPP--QDPALRKEKDPQPQQLPPMDPKLLKQ 565
Cdd:PHA03247 2863 RRRPPSR-SPAAKPAAPARPPvrRLARPAVSRSTESFALPPDQPERPPQ 2910
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
24-365 |
5.85e-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: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 24 ASQPEPSDLPKKPPK--PEFGKLKKFSQPELSEHPKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPkKPPPPEVT 101
Cdd:pfam03154 195 ATAGPTPSAPSVPPQgsPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQP-LPQPSLHG 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 102 DLPKKP------PPPEVTDLPKKPSKLELSDLSKKFPQLGATPFPrKPLQPEVGEAPLKASLPEPGAPARKPLQPDELSH 175
Cdd:pfam03154 274 QMPPMPhslqtgPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAP-GQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSM 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 176 P-ARPPSEPKSGAFPRKLWQPEAGEATPRSPQPELSTFPKKPA-QPEFNVYPKKPPQPQVGGLPKKSVPQPEFSEAAQTP 253
Cdd:pfam03154 353 PhIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPPAlKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPP 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 254 LWKPQSSEPKRDSSAFPKKASQ--PPLSDFPKKPPQPELGDLTRTSSEPEVSVLPKRP--RPAEFKALSKKPPQPELGGL 329
Cdd:pfam03154 433 VLTQSQSLPPPAASHPPTSGLHqvPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPgiQPPSSASVSSSGPVPAAVSC 512
|
330 340 350
....*....|....*....|....*....|....*.
gi 530427551 330 PRTSSEPEfNSLPRKLLQPERRGPPRKFSQPEPSAV 365
Cdd:pfam03154 513 PLPPVQIK-EEALDEAEEPESPPPPPRSPSPEPTVV 547
|
|
| BimA_second |
NF040983 |
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ... |
56-146 |
6.04e-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: 39.50 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 56 PKKAPLPefgavslkPPPPevtdlPKKPPPPEVTDLPKKPPPPEVTDLPKKPPPPEVTDLPKKPSklelSDLSKKFPQLG 135
Cdd:NF040983 86 PNKVPPP--------PPPP-----PPPPPPPPTPPPPPPPPPPPPPPSPPPPPPPSPPPSPPPPT----TTPPTRTTPST 148
|
90
....*....|..
gi 530427551 136 ATPFPR-KPLQP 146
Cdd:NF040983 149 TTPTPSmHPIQP 160
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
53-414 |
6.47e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 40.05 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 53 SEHPKKAPLPEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPKKP-PPPEVTDLPKKPPPPEVTDLPKKPSKLELSDLSKKF 131
Cdd:PHA03378 438 TEQPRATPHSQAPTVVLHRPPTQPLEGPTGPLSVQAPLEPWQPlPHPQVTPVILHQPPAQGVQAHGSMLDLLEKDDEDME 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 132 PQLGATPFPRKPLQPEVGEAP-------LKASLPEPGAPARKPLQPDELSHPARPPSEPKSGAFPRKLWQPEAGEATPRS 204
Cdd:PHA03378 518 QRVMATLLPPSPPQPRAGRRApcvytedLDIESDEPASTEPVHDQLLPAPGLGPLQIQPLTSPTTSQLASSAPSYAQTPW 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 205 PQPELSTFPKKP---AQPEFNVYPKKPPQP--QVGGLPKKSVPQPEFSEAAQTPLWKPQSSEPKRDS------------- 266
Cdd:PHA03378 598 PVPHPSQTPEPPttqSHIPETSAPRQWPMPlrPIPMRPLRMQPITFNVLVFPTPHQPPQVEITPYKPtwtqighipyqps 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 267 ----------SAFPKKASQPPLSDFPKKPPQPELGDLTR----TSSEPEVSVLPKRPRPAEFKALSKKPPQPELGGLPRT 332
Cdd:PHA03378 678 ptgantmlpiQWAPGTMQPPPRAPTPMRPPAAPPGRAQRpaaaTGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPP 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 333 SSEPEFNSLP-----RKLLQPERRGPPRKFSQPEPSAVLKRHPQ--PEFFGDLPRKPPLPSSASESSLPAAVAGFSSRHP 405
Cdd:PHA03378 758 AAAPGRARPPaaapgAPTPQPPPQAPPAPQQRPRGAPTPQPPPQagPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRGR 837
|
....*....
gi 530427551 406 LSPGFGAAG 414
Cdd:PHA03378 838 PSLKKPAAL 846
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
56-173 |
8.01e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 39.31 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 56 PKKAPL-PEFGAVSLKPPPPEVTDLPKKPPPPEVTDLPkkPPPPEVTDLPKKPPPPEVTDLPKKPSKLELSDLSKKFPQL 134
Cdd:PRK14951 377 EKKTPArPEAAAPAAAPVAQAAAAPAPAAAPAAAASAP--AAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQ 454
|
90 100 110
....*....|....*....|....*....|....*....
gi 530427551 135 GATPFPRKPLQPEVGEAPLKASLPEPGAPARKPLQPDEL 173
Cdd:PRK14951 455 AAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEE 493
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
135-260 |
8.19e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 39.68 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530427551 135 GATPF--------PRKPLQPEVGEAPLKASLPEPGAPARKPLQPDELSHPARPPSEPksgafPRKLWQPEageaTPRSPQ 206
Cdd:PRK10263 718 GANPFslddfefsPMKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAP-----QPQYQQPQ----QPVAPQ 788
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 530427551 207 PELSTFPKKPAQPEFNVYPKKP--PQPQVGGLPKKSVPQPEFSEAAQTPLWKPQSS 260
Cdd:PRK10263 789 PQYQQPQQPVAPQPQYQQPQQPvaPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDT 844
|
|
|