|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
235-799 |
0e+00 |
|
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441280 [Multi-domain] Cd Length: 611 Bit Score: 767.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 235 GGVSTPTALAPSVPSQAPFPLLPAPGLIQSNLPSDVHAPASPGSLPSVIPAQAPCVMALSPISAPSVAPAETLIPAQDDE 314
Cdd:COG1674 42 LLLLLGLLLLLLALLLLLLAGLLLLGLLLGLLLLLGLLLLLLLLLGLLGAALLALLALALALLLGALGLLALAAAALGAL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 315 QGPPRPIPASAAPLRHPcrgyqvPYDLLDQYSEDTYEGIDELTKNLALLLEETFSEFNIRVEITGIKKGPVVTMFELLPP 394
Cdd:COG1674 122 ALLLLAAAEALALAVLP------PLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 395 PGIKLSKITNLQDNVALKLAASSVRIVAPIPGKHAIGVEVPNKKRSLVTFKELLHTRTAGSNRMAIPVILGKDVTGEPQV 474
Cdd:COG1674 196 PGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 475 IDLAQTPHLLIAGATGSGKSVCVNALILSILYHKCPDETKLLLIDPKIVELKLYNDIAHLLTPVITEPKRALQALQYILC 554
Cdd:COG1674 276 ADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 555 EMERRYALLEQLECRDIKTYNKKIQEKSIAT------QPLPFIVIIIDEFADLMVASGKELETSVARLCAMSRAVGIHLV 628
Cdd:COG1674 356 EMERRYKLFAKAGVRNIAGYNEKVREAKAKGeeeeglEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 629 LATQRPSIDVITGLIKANIPSRIAFMVSSKMDSRIILDEMGAEKLLGRGDMLYMNPSQSFPTRIQGAYVSERELARVIAH 708
Cdd:COG1674 436 LATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDF 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 709 VRAWGTPEYLDEEIFFDDDDASISGNfvDESDPLYEQAVQVVQYAGKASTSYVQRKLKIGYNRAARLIEEMEARGVVGPP 788
Cdd:COG1674 516 LKSQGEPEYIEEILEEEEEEDEGGDD--DEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPA 593
|
570
....*....|.
gi 2030623205 789 NGSKPRDVLRS 799
Cdd:COG1674 594 EGSKPREVLVS 604
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
158-797 |
5.89e-150 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 473.42 E-value: 5.89e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 158 RDFIADGFQDPSFPPSTAdhpdTVSPPPAPSCATADVQTPEASAPPEGQFStevplqggefliseaevQPATQVAAcggv 237
Cdd:PRK10263 733 KALLDDGPHEPLFTPIVE----PVQQPQQPVAPQQQYQQPQQPVAPQPQYQ-----------------QPQQPVAP---- 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 238 stptalapsvPSQAPFPLLPAPGLIQSNLPSDVHAPASPGSLPSVIPAQAPCVMALSPISAPsvAPAETLIPAQDDEQGP 317
Cdd:PRK10263 788 ----------QPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAP--QPQDTLLHPLLMRNGD 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 318 PRPIPASAAPLRhpcrgyqvPYDLLDQYSEDTyEGIDELT-KNLALLLEETFSEFNIRVEITGIKKGPVVTMFELLPPPG 396
Cdd:PRK10263 856 SRPLHKPTTPLP--------SLDLLTPPPSEV-EPVDTFAlEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPG 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 397 IKLSKITNLQDNVALKLAASSVRIVAPIPGKHAIGVEVPNKKRSLVTFKELLHTRTAGSNRMAIPVILGKDVTGEPQVID 476
Cdd:PRK10263 927 VKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVAD 1006
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 477 LAQTPHLLIAGATGSGKSVCVNALILSILYHKCPDETKLLLIDPKIVELKLYNDIAHLLTPVITEPKRALQALQYILCEM 556
Cdd:PRK10263 1007 LAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEM 1086
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 557 ERRYALLEQLECRDIKTYNKKIQEKSIATQP---------------------LPFIVIIIDEFADLMVASGKELETSVAR 615
Cdd:PRK10263 1087 ERRYKLMSALGVRNLAGYNEKIAEADRMMRPipdpywkpgdsmdaqhpvlkkEPYIVVLVDEFADLMMTVGKKVEELIAR 1166
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 616 LCAMSRAVGIHLVLATQRPSIDVITGLIKANIPSRIAFMVSSKMDSRIILDEMGAEKLLGRGDMLYMNPSQSFPTRIQGA 695
Cdd:PRK10263 1167 LAQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGA 1246
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 696 YVSERELARVIAHVRAWGTPEYLDEEIFFDDDDASISG-NFVDESDPLYEQAVQVVQYAGKASTSYVQRKLKIGYNRAAR 774
Cdd:PRK10263 1247 FVRDQEVHAVVQDWKARGRPQYVDGITSDSESEGGAGGfDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAAR 1326
|
650 660
....*....|....*....|...
gi 2030623205 775 LIEEMEARGVVGPPNGSKPRDVL 797
Cdd:PRK10263 1327 IIEQMEAQGIVSEQGHNGNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
456-635 |
1.94e-56 |
|
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.
Pssm-ID: 279863 [Multi-domain] Cd Length: 219 Bit Score: 192.59 E-value: 1.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 456 NRMAIPVILGKDVTGEPQVIDLAQTP-HLLIAGATGSGKSVCVNALILSILYHKCPDETKLLLIDPKIVELKLYNDIAHL 534
Cdd:pfam01580 13 DYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGELSAYEDIPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 535 LT-PVITEPKRALQALQYILCEMERRYALLEQLECRDIKTYNKKIQE----------------KSIATQP-----LPFIV 592
Cdd:pfam01580 93 LSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEdpldgfgdvflviygvHVMCTAGrwleiLPYLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2030623205 593 IIIDEFADLMVASGKE----LETSVARLCAMSRAVGIHLVLATQRPS 635
Cdd:pfam01580 173 VIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
737-799 |
9.76e-33 |
|
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 197911 [Multi-domain] Cd Length: 63 Bit Score: 120.60 E-value: 9.76e-33
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2030623205 737 DESDPLYEQAVQVVQYAGKASTSYVQRKLKIGYNRAARLIEEMEARGVVGPPNGSKPRDVLRS 799
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
436-665 |
1.80e-28 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 123.17 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 436 NKKRSL---VTFKELLHTR-------------TAGSNRMAIPVIL-GKDvtgEPQVIDL---AQTPHLLIAGATGSGKSV 495
Cdd:TIGR03928 408 NLKNSIpesVTFLEMYGVKkveelniqerwakNETYKSLAVPIGLrGKD---DIVYLNLhekAHGPHGLVAGTTGSGKSE 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 496 CVNALILSILYHKCPDETKLLLIDPKIVEL-KLYNDIAHLLTpVIT-----EPKRALQAlqyILCEMERRYALLEQLECR 569
Cdd:TIGR03928 485 ILQTYILSLAVNFHPHEVAFLLIDYKGGGMaNLFKNLPHLLG-TITnldgaQSMRALAS---IKAELKKRQRLFGENNVN 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 570 DIKTYNKKIQEKsIATQPLPFIVIIIDEFADL-------MvasgKELeTSVARLcamSRAVGIHLVLATQRPSiDVITGL 642
Cdd:TIGR03928 561 HINQYQKLYKQG-KAKEPMPHLFLISDEFAELkseqpefM----KEL-VSTARI---GRSLGVHLILATQKPS-GVVDDQ 630
|
250 260
....*....|....*....|...
gi 2030623205 643 IKANIPSRIAFMVSSKMDSRIIL 665
Cdd:TIGR03928 631 IWSNSRFKLALKVQDASDSNEIL 653
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
482-655 |
5.75e-08 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 52.61 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 482 HLLIAGATGSGKSVCVNALILSIlyhkCPDETKLLLIDPK---IVELKLYNDIAHLLTPVITepkralQALQYILCEMER 558
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQ----AARGGSVIITDPKgelFLVIPDRDDSFAALRALFF------NQLFRALTELAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 559 RYALleqlecrdiktynkkiqeksiatQPLPFIVIIIDEFADLMVASGkeletsVARLCAMSRAVGIHLVLATQ------ 632
Cdd:cd01127 71 LSPG-----------------------RLPRRVWFILDEFANLGRIPN------LPNLLATGRKRGISVVLILQslaqle 121
|
170 180
....*....|....*....|...
gi 2030623205 633 RPSIDVITGLIKANIPSRIAFMV 655
Cdd:cd01127 122 AVYGKDGAQTILGNCNTKLYLGT 144
|
|
| DUF4813 |
pfam16072 |
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. ... |
168-288 |
8.56e-04 |
|
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between 345 and 672 amino acids in length.
Pssm-ID: 435117 [Multi-domain] Cd Length: 288 Bit Score: 42.05 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 168 PSFPPSTADHPDTVsPPPAPSCATADVQTPEAsappegqfstevPLQGGefliseaevqPATQVAACGGVSTPTALAPSV 247
Cdd:pfam16072 174 PAYPVAPAAYPAQA-PAAAPAPAPGAPQTPLA------------PLNPV----------AAAPAAAAGAAAAPVVAAAAP 230
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2030623205 248 PSQAPFPllPAPgliqsNLPSDVHAPASPGSLPSViPAQAP 288
Cdd:pfam16072 231 AAAAPPP--PAP-----AAPPADAAPPAPGGIICV-PVRVP 263
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
166-284 |
8.73e-04 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 42.16 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 166 QDPSFPPSTADHPDTVSPPPAPSCATADVQTPE-ASAPPEGQFSTEVPlqggefliSEAEVQPATQVAACGGVSTPTALA 244
Cdd:PHA02682 79 QSPLAPSPACAAPAPACPACAPAAPAPAVTCPApAPACPPATAPTCPP--------PAVCPAPARPAPACPPSTRQCPPA 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2030623205 245 PSVPSQAPFPL---------LPAPGLIQSNLPSDVHAPASPGSLPSVIP 284
Cdd:PHA02682 151 PPLPTPKPAPAakpiflhnqLPPPDYPAASCPTIETAPAASPVLEPRIP 199
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
235-799 |
0e+00 |
|
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441280 [Multi-domain] Cd Length: 611 Bit Score: 767.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 235 GGVSTPTALAPSVPSQAPFPLLPAPGLIQSNLPSDVHAPASPGSLPSVIPAQAPCVMALSPISAPSVAPAETLIPAQDDE 314
Cdd:COG1674 42 LLLLLGLLLLLLALLLLLLAGLLLLGLLLGLLLLLGLLLLLLLLLGLLGAALLALLALALALLLGALGLLALAAAALGAL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 315 QGPPRPIPASAAPLRHPcrgyqvPYDLLDQYSEDTYEGIDELTKNLALLLEETFSEFNIRVEITGIKKGPVVTMFELLPP 394
Cdd:COG1674 122 ALLLLAAAEALALAVLP------PLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 395 PGIKLSKITNLQDNVALKLAASSVRIVAPIPGKHAIGVEVPNKKRSLVTFKELLHTRTAGSNRMAIPVILGKDVTGEPQV 474
Cdd:COG1674 196 PGVKVSKITNLADDIALALAAKSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 475 IDLAQTPHLLIAGATGSGKSVCVNALILSILYHKCPDETKLLLIDPKIVELKLYNDIAHLLTPVITEPKRALQALQYILC 554
Cdd:COG1674 276 ADLAKMPHLLIAGATGSGKSVCINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 555 EMERRYALLEQLECRDIKTYNKKIQEKSIAT------QPLPFIVIIIDEFADLMVASGKELETSVARLCAMSRAVGIHLV 628
Cdd:COG1674 356 EMERRYKLFAKAGVRNIAGYNEKVREAKAKGeeeeglEPLPYIVVIIDELADLMMVAGKEVEEAIARLAQKARAAGIHLI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 629 LATQRPSIDVITGLIKANIPSRIAFMVSSKMDSRIILDEMGAEKLLGRGDMLYMNPSQSFPTRIQGAYVSERELARVIAH 708
Cdd:COG1674 436 LATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASKPIRVQGAFVSDEEVERVVDF 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 709 VRAWGTPEYLDEEIFFDDDDASISGNfvDESDPLYEQAVQVVQYAGKASTSYVQRKLKIGYNRAARLIEEMEARGVVGPP 788
Cdd:COG1674 516 LKSQGEPEYIEEILEEEEEEDEGGDD--DEDDELFDEAVELVVETQKASTSLLQRRLRIGYNRAARLIDQMEERGIVGPA 593
|
570
....*....|.
gi 2030623205 789 NGSKPRDVLRS 799
Cdd:COG1674 594 EGSKPREVLVS 604
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
158-797 |
5.89e-150 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 473.42 E-value: 5.89e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 158 RDFIADGFQDPSFPPSTAdhpdTVSPPPAPSCATADVQTPEASAPPEGQFStevplqggefliseaevQPATQVAAcggv 237
Cdd:PRK10263 733 KALLDDGPHEPLFTPIVE----PVQQPQQPVAPQQQYQQPQQPVAPQPQYQ-----------------QPQQPVAP---- 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 238 stptalapsvPSQAPFPLLPAPGLIQSNLPSDVHAPASPGSLPSVIPAQAPCVMALSPISAPsvAPAETLIPAQDDEQGP 317
Cdd:PRK10263 788 ----------QPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAP--QPQDTLLHPLLMRNGD 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 318 PRPIPASAAPLRhpcrgyqvPYDLLDQYSEDTyEGIDELT-KNLALLLEETFSEFNIRVEITGIKKGPVVTMFELLPPPG 396
Cdd:PRK10263 856 SRPLHKPTTPLP--------SLDLLTPPPSEV-EPVDTFAlEQMARLVEARLADFRIKADVVNYSPGPVITRFELNLAPG 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 397 IKLSKITNLQDNVALKLAASSVRIVAPIPGKHAIGVEVPNKKRSLVTFKELLHTRTAGSNRMAIPVILGKDVTGEPQVID 476
Cdd:PRK10263 927 VKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNAKFRDNPSPLTVVLGKDIAGEPVVAD 1006
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 477 LAQTPHLLIAGATGSGKSVCVNALILSILYHKCPDETKLLLIDPKIVELKLYNDIAHLLTPVITEPKRALQALQYILCEM 556
Cdd:PRK10263 1007 LAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGIPHLLTEVVTDMKDAANALRWCVNEM 1086
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 557 ERRYALLEQLECRDIKTYNKKIQEKSIATQP---------------------LPFIVIIIDEFADLMVASGKELETSVAR 615
Cdd:PRK10263 1087 ERRYKLMSALGVRNLAGYNEKIAEADRMMRPipdpywkpgdsmdaqhpvlkkEPYIVVLVDEFADLMMTVGKKVEELIAR 1166
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 616 LCAMSRAVGIHLVLATQRPSIDVITGLIKANIPSRIAFMVSSKMDSRIILDEMGAEKLLGRGDMLYMNPSQSFPTRIQGA 695
Cdd:PRK10263 1167 LAQKARAAGIHLVLATQRPSVDVITGLIKANIPTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGPNSTLPVRVHGA 1246
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 696 YVSERELARVIAHVRAWGTPEYLDEEIFFDDDDASISG-NFVDESDPLYEQAVQVVQYAGKASTSYVQRKLKIGYNRAAR 774
Cdd:PRK10263 1247 FVRDQEVHAVVQDWKARGRPQYVDGITSDSESEGGAGGfDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAAR 1326
|
650 660
....*....|....*....|...
gi 2030623205 775 LIEEMEARGVVGPPNGSKPRDVL 797
Cdd:PRK10263 1327 IIEQMEAQGIVSEQGHNGNREVL 1349
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
456-635 |
1.94e-56 |
|
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.
Pssm-ID: 279863 [Multi-domain] Cd Length: 219 Bit Score: 192.59 E-value: 1.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 456 NRMAIPVILGKDVTGEPQVIDLAQTP-HLLIAGATGSGKSVCVNALILSILYHKCPDETKLLLIDPKIVELKLYNDIAHL 534
Cdd:pfam01580 13 DYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGELSAYEDIPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 535 LT-PVITEPKRALQALQYILCEMERRYALLEQLECRDIKTYNKKIQE----------------KSIATQP-----LPFIV 592
Cdd:pfam01580 93 LSvPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIAEdpldgfgdvflviygvHVMCTAGrwleiLPYLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2030623205 593 IIIDEFADLMVASGKE----LETSVARLCAMSRAVGIHLVLATQRPS 635
Cdd:pfam01580 173 VIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQRPS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
338-436 |
1.22e-35 |
|
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell division in bacteria. In addition to its role as activator of XerCD site-specific recombination, FtsK can translocate double-stranded DNA (dsDNA) rapidly and directionally and reverse direction. FtsK can be split into three domains called alpha (this entry), beta and gamma. The alpha and beta domains contain the core ATPase machinery of the DNA translocase.
Pssm-ID: 436096 [Multi-domain] Cd Length: 101 Bit Score: 129.96 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 338 PYDLLDQYSEDTYEGIDELTKNLALLLEETFSEFNIRVEITGIKKGPVVTMFELLPPPGIKLSKITNLQDNVALKLAASS 417
Cdd:pfam17854 3 PLDLLEPPPTSSQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSAPS 82
|
90
....*....|....*....
gi 2030623205 418 VRIVAPIPGKHAIGVEVPN 436
Cdd:pfam17854 83 IRIVAPIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
737-799 |
1.43e-34 |
|
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix structure. Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 462786 [Multi-domain] Cd Length: 63 Bit Score: 125.56 E-value: 1.43e-34
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2030623205 737 DESDPLYEQAVQVVQYAGKASTSYVQRKLKIGYNRAARLIEEMEARGVVGPPNGSKPRDVLRS 799
Cdd:pfam09397 1 EEEDELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
737-799 |
9.76e-33 |
|
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 197911 [Multi-domain] Cd Length: 63 Bit Score: 120.60 E-value: 9.76e-33
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2030623205 737 DESDPLYEQAVQVVQYAGKASTSYVQRKLKIGYNRAARLIEEMEARGVVGPPNGSKPRDVLRS 799
Cdd:smart00843 1 EEEDELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
436-665 |
1.80e-28 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 123.17 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 436 NKKRSL---VTFKELLHTR-------------TAGSNRMAIPVIL-GKDvtgEPQVIDL---AQTPHLLIAGATGSGKSV 495
Cdd:TIGR03928 408 NLKNSIpesVTFLEMYGVKkveelniqerwakNETYKSLAVPIGLrGKD---DIVYLNLhekAHGPHGLVAGTTGSGKSE 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 496 CVNALILSILYHKCPDETKLLLIDPKIVEL-KLYNDIAHLLTpVIT-----EPKRALQAlqyILCEMERRYALLEQLECR 569
Cdd:TIGR03928 485 ILQTYILSLAVNFHPHEVAFLLIDYKGGGMaNLFKNLPHLLG-TITnldgaQSMRALAS---IKAELKKRQRLFGENNVN 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 570 DIKTYNKKIQEKsIATQPLPFIVIIIDEFADL-------MvasgKELeTSVARLcamSRAVGIHLVLATQRPSiDVITGL 642
Cdd:TIGR03928 561 HINQYQKLYKQG-KAKEPMPHLFLISDEFAELkseqpefM----KEL-VSTARI---GRSLGVHLILATQKPS-GVVDDQ 630
|
250 260
....*....|....*....|...
gi 2030623205 643 IKANIPSRIAFMVSSKMDSRIIL 665
Cdd:TIGR03928 631 IWSNSRFKLALKVQDASDSNEIL 653
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
454-698 |
3.07e-20 |
|
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274858 [Multi-domain] Cd Length: 658 Bit Score: 95.81 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 454 GSNRMAIPVilGKDVTGEPQVIDL---AQT---PHLLIAGATGSGKSVCVNALILSILYHKCPDETKLLLIDpkiveLKL 527
Cdd:TIGR03924 405 GRDRLRVPI--GVGDDGEPVELDLkesAEGgmgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVD-----FKG 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 528 ---YNDIAHLltP----VIT--EPKRALQALQY--ILCEMERRYALLEQL-ECRDIKTYNKKIQEKSiATQPLPFIVIII 595
Cdd:TIGR03924 478 gatFLGLEGL--PhvsaVITnlADEAPLVDRMQdaLAGEMNRRQELLRAAgNFANVAEYEKARAAGA-DLPPLPALFVVV 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 596 DEFADLMVASGK--ELETSVARLcamSRAVGIHLVLATQRPSIDVITGLiKANIPSRIAFMVSSKMDSRIILDEMGAEKL 673
Cdd:TIGR03924 555 DEFSELLSQHPDfaDLFVAIGRL---GRSLGVHLLLASQRLDEGRLRGL-ESHLSYRIGLKTFSASESRAVLGVPDAYHL 630
|
250 260
....*....|....*....|....*
gi 2030623205 674 LGRGDMLYMNPSQSFPTRIQGAYVS 698
Cdd:TIGR03924 631 PSTPGAGYLKVDTAEPVRFRAAYVS 655
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
471-684 |
5.26e-16 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 82.73 E-value: 5.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 471 EPQVIDLAQTPHLLIAGATGSGKSVCVNALILSILYHKCPDETKLLLIDPKIVELKLYNDIAHLLTPV-ITEPKRALQAL 549
Cdd:TIGR03928 801 EPLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPHVADYFtLDEEEKIEKLI 880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 550 QYILCEMERRYALLEQLECRDIKTYNKKIQEKsiatqpLPFIVIIIDEFADLMVASGKE-LETSVARLCAMSRAVGIHLV 628
Cdd:TIGR03928 881 RRIKKEIDRRKKLFSEYGVASISMYNKASGEK------LPQIVIIIDNYDAVKEEPFYEdFEELLIQLAREGASLGIYLV 954
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2030623205 629 L-ATQRPSIDVItglIKANIPSRIAFMVSSKMDSRIIL--DEMGAEKLLGRGDMLYMNP 684
Cdd:TIGR03928 955 MtAGRQNAVRMP---LMNNIKTKIALYLIDKSEYRSIVgrTKFTIEEIPGRGLIKKDEP 1010
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
471-664 |
9.11e-11 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 65.78 E-value: 9.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 471 EPQVIDLAQTPHLLIAGATGSGKSVCVNALILSILYHkcpDETKLLLIDPKIVELKLYNDIAHLLTpVITEPKRALQALQ 550
Cdd:TIGR03928 1087 EPVYIDLTENPHLLIVGESDDGKTNVLKSLLKTLAKQ---EKEKIGLIDSIDRGLLAYRDLKEVAT-YIEEKEDLKEILA 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 551 YILCEMERRYALLeqlecrdiktynKKIQEKSIATQPLPFIVIIIDEFADLMVASGKELETSVARLCAMSRAVGIHLVLA 630
Cdd:TIGR03928 1163 ELKEEIELREAAY------------KEALQNETGEPAFKPILLIIDDLEDFIQRTDLEIQDILALIMKNGKKLGIHFIVA 1230
|
170 180 190
....*....|....*....|....*....|....*...
gi 2030623205 631 TQRPSI----DVITGLIKAnipSRIAFMVSSKMDSRII 664
Cdd:TIGR03928 1231 GTHSELsksyDGVPKEIKQ---LRTGILGMRKSDQSFF 1265
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
482-655 |
5.75e-08 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 52.61 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 482 HLLIAGATGSGKSVCVNALILSIlyhkCPDETKLLLIDPK---IVELKLYNDIAHLLTPVITepkralQALQYILCEMER 558
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLLDQ----AARGGSVIITDPKgelFLVIPDRDDSFAALRALFF------NQLFRALTELAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 559 RYALleqlecrdiktynkkiqeksiatQPLPFIVIIIDEFADLMVASGkeletsVARLCAMSRAVGIHLVLATQ------ 632
Cdd:cd01127 71 LSPG-----------------------RLPRRVWFILDEFANLGRIPN------LPNLLATGRKRGISVVLILQslaqle 121
|
170 180
....*....|....*....|...
gi 2030623205 633 RPSIDVITGLIKANIPSRIAFMV 655
Cdd:cd01127 122 AVYGKDGAQTILGNCNTKLYLGT 144
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
166-347 |
1.07e-07 |
|
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: 55.54 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 166 QDPSFPPSTADHPDTVSPPPAPScaTADVQTPEASAPPEGQFSTEVP-LQGGEFLISEAevQPATQVAACGGVSTPTALA 244
Cdd:pfam03154 128 DEGSSDPKDIDQDNRSTSPSIPS--PQDNESDSDSSAQQQILQTQPPvLQAQSGAASPP--SPPPPGTTQAATAGPTPSA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 245 PSVPSQAPFPLLPAPGLIQSNLPSDVHAPASPGSLPSVIPAQAPCVMALSPISAPSVAPAETLIPAQDDEQGPPRPIPAS 324
Cdd:pfam03154 204 PSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQ 283
|
170 180
....*....|....*....|...
gi 2030623205 325 AAPLRHPCRGYQVPYDLLDQYSE 347
Cdd:pfam03154 284 TGPSHMQHPVPPQPFPLTPQSSQ 306
|
|
| PRK08691 |
PRK08691 |
DNA polymerase III subunits gamma and tau; Validated |
172-320 |
2.22e-06 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 51.25 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 172 PSTADHPdtvSPPPAPSCATADVQTPEASA-PPEGQFSTEVPLQggefliSEAEVQPATQVAACGGVSTPTALAPS-VPS 249
Cdd:PRK08691 388 ETAAKKP---QPRPEAETAQTPVQTASAAAmPSEGKTAGPVSNQ------ENNDVPPWEDAPDEAQTAAGTAQTSAkSIQ 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 250 QAPFPLLPAPGLIQSNLPSDVHAPASPGSLPSVIPAQA-PCVMALSPISAPSVAPAETLI---------PAQDDEQGPPR 319
Cdd:PRK08691 459 TASEAETPPENQVSKNKAADNETDAPLSEVPSENPIQAtPNDEAVETETFAHEAPAEPFYgygfpdndcPPEDGAEIPPP 538
|
.
gi 2030623205 320 P 320
Cdd:PRK08691 539 D 539
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
471-630 |
2.69e-06 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 50.76 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 471 EPQVIDLAQTPHLLIAGATGSGKSVCVNALILSILYHKCPDETKLLLIDpkivelklyndiahlltpvitePKRALqaLQ 550
Cdd:TIGR03925 354 APVYVDFAESPHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVD----------------------YRRTL--LG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 551 YILCEMERRYA--------LLEQLecrdIKTYNKKIQEKSIATQPL--------PFIVIIIDEFADLMVASGKELeTSVA 614
Cdd:TIGR03925 410 AVPEDYLAGYAatsaalteLIAAL----AALLERRLPGPDVTPQQLrarswwsgPEIYVVVDDYDLVATGSGNPL-APLV 484
|
170
....*....|....*.
gi 2030623205 615 RLCAMSRAVGIHLVLA 630
Cdd:TIGR03925 485 ELLPHARDIGLHVVVA 500
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
461-712 |
2.85e-06 |
|
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];
Pssm-ID: 440202 [Multi-domain] Cd Length: 388 Bit Score: 50.38 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 461 PVILGKDV-TGEPQVIDLAQ--TPHLLIAGATGSGKSVCVNALILSILYHKCPdetkLLLIDPK------------IVEL 525
Cdd:COG0433 25 GILIGKLLsPGVPVYLDLDKllNRHILILGATGSGKSNTLQVLLEELSRAGVP----VLVFDPHgeysglaepgaeRADV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 526 KLYN-------------------DIAHLLTPVITEPKRALQALQYILCEMERRYA-------LLEQL-ECRDIKTYNKKI 578
Cdd:COG0433 101 GVFDpgagrplpinpwdlfatasELGPLLLSRLDLNDTQRGVLREALRLADDKGLllldlkdLIALLeEGEELGEEYGNV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 579 QEKSIAT--------------------------------------------------------------------QPLPf 590
Cdd:COG0433 181 SAASAGAllrrleslesadglfgepgldledllrtdgrvtvidlsglpeelqstfvlwllrelfearpevgdaddRKLP- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 591 IVIIIDEFADLMVASGKELETSVARLCAMSRAVGIHLVLATQRPSiDVITGlIKANIPSRIAFMVSSKMDSRIILDEMGA 670
Cdd:COG0433 260 LVLVIDEAHLLAPAAPSALLEILERIAREGRKFGVGLILATQRPS-DIDED-VLSQLGTQIILRLFNPRDQKAVKAAAET 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2030623205 671 EKL--------LGRGDMLYMNPSQSFPTRIQGAYVSERELARVIAHVRAW 712
Cdd:COG0433 338 LSEdllerlpsLGTGEALVLGEGIPLPVLVKIRLPESRPGGESPDLVREW 387
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
168-331 |
3.74e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.09 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 168 PSFPPSTADhPDTVSPPPAPSCATADVQTPEASAP----PEGQFSTEVPLQGGEFLISEAEVQPATQVAAcGGVSTPTAL 243
Cdd:PHA03247 2757 PARPPTTAG-PPAPAPPAAPAAGPPRRLTRPAVASlsesRESLPSPWDPADPPAAVLAPAAALPPAASPA-GPLPPPTSA 2834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 244 APSVPSQAPFPLLPAPGLIQSNLPSDVHAPASPGSLPSVIPAqAPCVMALSPISAPSVAPAETLIPAQDDEQGPPRPIPA 323
Cdd:PHA03247 2835 QPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPA-APARPPVRRLARPAVSRSTESFALPPDQPERPPQPQA 2913
|
....*...
gi 2030623205 324 SAAPLRHP 331
Cdd:PHA03247 2914 PPPPQPQP 2921
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
171-330 |
4.51e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.71 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 171 PPSTADHPDTVSPP---------PAPSCATADVQTPEASAPPEGQFSTEVPLQG-----GEFLISEAEVQPATQVAACG- 235
Cdd:PHA03247 2801 PWDPADPPAAVLAPaaalppaasPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGsvapgGDVRRRPPSRSPAAKPAAPAr 2880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 236 ---------GVSTPT---ALAPSVPSQAPFPLLPAPGLIQSNLPSDvHAPASPGSLPSVIPAQAPCVMALSPISAPS--- 300
Cdd:PHA03247 2881 ppvrrlarpAVSRSTesfALPPDQPERPPQPQAPPPPQPQPQPPPP-PQPQPPPPPPPRPQPPLAPTTDPAGAGEPSgav 2959
|
170 180 190
....*....|....*....|....*....|....*...
gi 2030623205 301 -------VAPAETLIP-AQDDEQGPPRPIPASAAPLRH 330
Cdd:PHA03247 2960 pqpwlgaLVPGRVAVPrFRVPQPAPSREAPASSTPPLT 2997
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
157-338 |
1.37e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.17 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 157 PRDFIADGFQDPSFPPSTADHPDTVS---PPPAPSCATADVQTPEASAPPEGQFSTEVPLQGGEFLISEAEVQP-ATQVA 232
Cdd:PHA03247 2598 PRAPVDDRGDPRGPAPPSPLPPDTHApdpPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGrAAQAS 2677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 233 ACGGVSTPTALAPSVPSQAPFPLLPAPGLIQSNLP----SDVHAPASPGSLPSVIPAQAPCVMALSPISAPSVAPAETLI 308
Cdd:PHA03247 2678 SPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPhalvSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARP 2757
|
170 180 190
....*....|....*....|....*....|
gi 2030623205 309 PAQDDEQGPPRPIPAsAAPLRHPCRGYQVP 338
Cdd:PHA03247 2758 ARPPTTAGPPAPAPP-AAPAAGPPRRLTRP 2786
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
167-332 |
1.37e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.17 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 167 DPSFPPSTADHPDTVSPPPAPSCATADVQTPEASAPPEGQFSTEVPLQGGefliseAEVQPATQVAACGgvsTPTALAPS 246
Cdd:PHA03247 2703 PPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPG------GPARPARPPTTAG---PPAPAPPA 2773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 247 VPSQAPFPLLPAPGlIQSNLPSDVHAPASPGSLPSVIPAQAPcvmalSPISAPSVAPAETLIPAQDDEQGPPRPIPASAA 326
Cdd:PHA03247 2774 APAAGPPRRLTRPA-VASLSESRESLPSPWDPADPPAAVLAP-----AAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP 2847
|
....*.
gi 2030623205 327 PLRHPC 332
Cdd:PHA03247 2848 PSLPLG 2853
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
471-663 |
3.42e-05 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 47.29 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 471 EPQVIDLAQTP-HLLIAGATGSGKSVCVNALILSI-LYHKcPDETKLLLIDPKIVELKLYNDIAHlLTPVIT--EPKRAL 546
Cdd:TIGR03925 69 DPLVVDLSGAAgHVAIVGAPQSGKSTALRTLILALaLTHT-PEEVQFYCLDFGGGGLASLADLPH-VGGVAGrlDPERVR 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 547 QALQYILCEMERRYALLEQLECRDIKTYNKKIQEKSIATQPLPFIVIIIDEFADLmVASGKELETSVARLCAMSRAVGIH 626
Cdd:TIGR03925 147 RTVAEVEGLLRRRERLFRTHGIDSMAQYRARRAAGRLPEDPFGDVFLVIDGWGTL-RQDFEDLEDKVTDLAARGLAYGVH 225
|
170 180 190
....*....|....*....|....*....|....*..
gi 2030623205 627 LVLATQRPSidVITGLIKANIPSRIAFMVSSKMDSRI 663
Cdd:TIGR03925 226 VVLTASRWS--EIRPALRDLIGTRIELRLGDPMDSEI 260
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
448-520 |
3.81e-05 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 47.25 E-value: 3.81e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2030623205 448 LHTRTAGSNRmaiPVILGKDVTGEPQVIDLAQT---PHLLIAGATGSGKSVCVNALILSILYHKcpdeTKLLLIDP 520
Cdd:COG3451 172 FHSFELGDPW---GIYLLNTRSGTPVFFDFHDGldnGNTLILGPSGSGKSFLLKLLLLQLLRYG----ARIVIFDP 240
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
164-331 |
4.14e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.63 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 164 GFQDPSFPPSTADHPDTVSPPPAPscatadvQTPEaSAPPEGQFSTEVPL--QGGEFLISEAEVQPATQVAACGGVSTPT 241
Cdd:PHA03247 2682 RPRRRAARPTVGSLTSLADPPPPP-------PTPE-PAPHALVSATPLPPgpAAARQASPALPAAPAPPAVPAGPATPGG 2753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 242 ALAPSVPSQAPFPLLPAPGLIQSNLPSDVhAPASPGSLPSVIPAQAPCVMALSPISAPSVAPAETLIPAQddEQGPPRPI 321
Cdd:PHA03247 2754 PARPARPPTTAGPPAPAPPAAPAAGPPRR-LTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAA--SPAGPLPP 2830
|
170
....*....|
gi 2030623205 322 PASAAPLRHP 331
Cdd:PHA03247 2831 PTSAQPTAPP 2840
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
189-361 |
4.62e-05 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 46.01 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 189 CATADVQTPEASAPPEGQFStevPL------QGGEFLISEAEVQPATQVAACGgvSTPTALAPSVPSQAPFPLLPAPGLI 262
Cdd:PHA02682 29 CPQATIPAPAAPCPPDADVD---PLdkysvkEAGRYYQSRLKANSACMQRPSG--QSPLAPSPACAAPAPACPACAPAAP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 263 QSNLPSDVHAPASPGSLPSVIPAQAPCVMALSPISA--------------PSVAPAETLIPAQDDEQGPPRPIPASA--- 325
Cdd:PHA02682 104 APAVTCPAPAPACPPATAPTCPPPAVCPAPARPAPAcppstrqcppapplPTPKPAPAAKPIFLHNQLPPPDYPAAScpt 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 2030623205 326 ---APLRHPCRGYQVPYDLLDQYSEDTyegiDELTKNLA 361
Cdd:PHA02682 184 ietAPAASPVLEPRIPDKIIDADNDDK----DLIKKELA 218
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
154-328 |
5.01e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 46.77 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 154 ARIPRDFIADGFQDPSFPPSTADHPDTVSPPPAPSCATADVQTPEASAPPEGQFSTEVPLQGGEFLISEAEVQPATQVAA 233
Cdd:PRK07003 374 ARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 234 CGGVSTPTALAP--------SVPSQAPFPLLPAPGLIQSNLPSDvhaPASPGSLPSVIPAQAPCVMALSPISAPSVAPAE 305
Cdd:PRK07003 454 NARASADSRCDErdaqppadSGSASAPASDAPPDAAFEPAPRAA---APSAATPAAVPDARAPAAASREDAPAAAAPPAP 530
|
170 180
....*....|....*....|...
gi 2030623205 306 TLIPAQDDEQGPPRPIPASAAPL 328
Cdd:PRK07003 531 EARPPTPAAAAPAARAGGAAAAL 553
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
168-338 |
6.46e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.52 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 168 PSFPPSTADHPDTVSPPPAPScatADVQTPEASAPPEGQFSTEVPLQGGEFLISEAEVQPATQVAACGGVSTPTAlAPSV 247
Cdd:PRK07764 605 SSGPPEEAARPAAPAAPAAPA---APAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGA-APAA 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 248 PSQAPFPLLPAPGLIQSNLPSDVHAPASPGSLPSVIPAQAPCVMALSPISAPSVAPAETLIPAQDDEQGPPRPIPASAAP 327
Cdd:PRK07764 681 PPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPP 760
|
170
....*....|.
gi 2030623205 328 LRHPCRGYQVP 338
Cdd:PRK07764 761 PPAPAPAAAPA 771
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
154-325 |
1.46e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 154 ARIPRDFIADGFQDPSFPPSTADHPDTVSPPPAPSCATADVQTPE------------ASAPPEGQFSTEVPLQGGeflis 221
Cdd:PHA03247 2781 RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAgplppptsaqptAPPPPPGPPPPSLPLGGS----- 2855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 222 eaeVQPATQVAAcGGVSTPTALAPSVPSQAPFPLLPAPGLIQSNLPSDVhAPASPGSLPSVIPAQAPCVMALSPISAPSV 301
Cdd:PHA03247 2856 ---VAPGGDVRR-RPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFAL-PPDQPERPPQPQAPPPPQPQPQPPPPPQPQ 2930
|
170 180
....*....|....*....|....
gi 2030623205 302 APAETliPAQDDEQGPPRPIPASA 325
Cdd:PHA03247 2931 PPPPP--PPRPQPPLAPTTDPAGA 2952
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
171-329 |
2.35e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.87 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 171 PPSTADHPDTVSPPP--APSCATADVQTPEASAPPEGQFSTEVPLQGGefliSEAEVQPA---------TQVAACGGVST 239
Cdd:PRK12323 374 PATAAAAPVAQPAPAaaAPAAAAPAPAAPPAAPAAAPAAAAAARAVAA----APARRSPApealaaarqASARGPGGAPA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 240 PTALAPSVPSQAPFPLLPAPgliQSNLPSDVHAPAS--------------------PGSLPSVIPAQ---APCVMALSPI 296
Cdd:PRK12323 450 PAPAPAAAPAAAARPAAAGP---RPVAAAAAAAPARaapaaapapadddpppweelPPEFASPAPAQpdaAPAGWVAESI 526
|
170 180 190
....*....|....*....|....*....|...
gi 2030623205 297 SAPSVAPAETLIPAQdDEQGPPRPIPASAAPLR 329
Cdd:PRK12323 527 PDPATADPDDAFETL-APAPAAAPAPRAAAATE 558
|
|
| PHA03377 |
PHA03377 |
EBNA-3C; Provisional |
165-331 |
2.96e-04 |
|
EBNA-3C; Provisional
Pssm-ID: 177614 [Multi-domain] Cd Length: 1000 Bit Score: 44.66 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 165 FQDPSFPPSTADHPDTVSPPP--APSCATADVQTPEASAPP-EGQFSTEVPLQGgeflISEAEVQpATQVAACGGVSTPT 241
Cdd:PHA03377 723 YEDPDDPLDLSLHPDQAPPPShqAPYSGHEEPQAQQAPYPGyWEPRPPQAPYLG----YQEPQAQ-GVQVSSYPGYAGPW 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 242 ALAPSVP----SQAPFPLLPAPGLIQSnlPSDVHAPaspgslpsvipaqapcvmALSPISAPSVAPAETLI---PAQDDE 314
Cdd:PHA03377 798 GLRAQHPryrhSWAYWSQYPGHGHPQG--PWAPRPP------------------HLPPQWDGSAGHGQDQVsqfPHLQSE 857
|
170
....*....|....*..
gi 2030623205 315 QGPPRPIPASAAPLRHP 331
Cdd:PHA03377 858 TGPPRLQLSQVPQLPYS 874
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
172-344 |
4.25e-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: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 172 PSTADHPDTVSPPPAPSCATADVQTP-EASAPPEGQfstevPLQGGEFLISE-AEVQP---ATQVAACGGVSTPTALAPS 246
Cdd:pfam03154 245 PHPPLQPMTQPPPPSQVSPQPLPQPSlHGQMPPMPH-----SLQTGPSHMQHpVPPQPfplTPQSSQSQVPPGPSPAAPG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 247 VPSQAPFPLLPAPGLIQSNLPSDVHAPASPGSLPSVIPaqaPCVMALSPISAPSVA--PAETLIPA--QDDEQGPPRPI- 321
Cdd:pfam03154 320 QSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKP---PPTTPIPQLPNPQSHkhPPHLSGPSpfQMNSNLPPPPAl 396
|
170 180
....*....|....*....|....
gi 2030623205 322 -PASAAPLRHPCRGYQVPYDLLDQ 344
Cdd:pfam03154 397 kPLSSLSTHHPPSAHPPPLQLMPQ 420
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
171-331 |
4.59e-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: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 171 PPSTADHPDTVSPPPAPSCATADVQTPeasAPPEGqfSTEVPLQGgefliSEAEVQPATQVAACGG-----VSTPTALAP 245
Cdd:pfam03154 171 PPVLQAQSGAASPPSPPPPGTTQAATA---GPTPS--APSVPPQG-----SPATSQPPNQTQSTAAphtliQQTPTLHPQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 246 SVPS------QAPFPLLPAPGLIQSNLPSDVHAPASPGS---------LPSVIPAQ--------APCVMALSPISAPSVA 302
Cdd:pfam03154 241 RLPSphpplqPMTQPPPPSQVSPQPLPQPSLHGQMPPMPhslqtgpshMQHPVPPQpfpltpqsSQSQVPPGPSPAAPGQ 320
|
170 180 190
....*....|....*....|....*....|...
gi 2030623205 303 PAET--LIPAQD--DEQGPPRPIPASAAPLRHP 331
Cdd:pfam03154 321 SQQRihTPPSQSqlQSQQPPREQPLPPAPLSMP 353
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
170-327 |
5.98e-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: 43.60 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 170 FPPSTADHPDTVSPPPAPSCATADVQT----PEASAPPEGQFSTEVPLQGGEFLISEAEVQPAT---QVAACGGVSTPTA 242
Cdd:pfam03154 298 FPLTPQSSQSQVPPGPSPAAPGQSQQRihtpPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTpipQLPNPQSHKHPPH 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 243 LAPSVPSQAPFPLLPAPGL-----IQSNLPSDVHAPA-----------SPGSLPSVIP---------AQAPCVMALSPIS 297
Cdd:pfam03154 378 LSGPSPFQMNSNLPPPPALkplssLSTHHPPSAHPPPlqlmpqsqqlpPPPAQPPVLTqsqslpppaASHPPTSGLHQVP 457
|
170 180 190
....*....|....*....|....*....|
gi 2030623205 298 APSVAPAETLIPAQDDEQGPPRPIPASAAP 327
Cdd:pfam03154 458 SQSPFPQHPFVPGGPPPITPPSGPPTSTSS 487
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
187-376 |
6.67e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 43.16 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 187 PSCATADVQTPEASAPPEGQFSTEVPLQggefliseaevQPATQVAAcgGVSTPTALAPSVPSQAPFPLLPApgliqsnl 266
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPAAAP-----------VAQAAAAP--APAAAPAAAASAPAAPPAAAPPA-------- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 267 PSDVHAPASPGSLPSVIPAQAPCVMALSPISAP-SVAPAETLIPAQDDEQGPPRPIPASAAPLRHPCRGYQVPYDLLDQY 345
Cdd:PRK14951 425 PVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPeTVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEGDVWHATVQQL 504
|
170 180 190
....*....|....*....|....*....|....
gi 2030623205 346 SEDtyEGIDELTKNLAL---LLEETFSEFNIRVE 376
Cdd:PRK14951 505 AAA--EAITALARELALqseLVARDGDQWLLRVE 536
|
|
| Not5 |
COG5665 |
CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription]; |
157-326 |
6.99e-04 |
|
CCR4-NOT transcriptional regulation complex, NOT5 subunit [Transcription];
Pssm-ID: 444384 [Multi-domain] Cd Length: 874 Bit Score: 43.11 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 157 PRDFIADGFQDPSFPPSTADHPDT----VSPPPAPSCATADVQTPEASAPPEGQFSTEvplqgGEFLISEAEVQPATqva 232
Cdd:COG5665 337 PTTEETTAFTTPSSVPSTPAEKDTpatdLATPVSPTPPETSVDKKVSPDSATSSTKSE-----KEGGTASSPMPPNI--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 233 ACGGVSTPTALAPSVPSQAPFPLLPAPGLIQSNLPSDVHAPASPGS----LPSVIPAQAPCVMALSPISAPSVAPAETLI 308
Cdd:COG5665 409 AIGAKDDVDATDPSQEAKEYTKNAPMTPEADSAPESSVRTEASPSAgsdlEPENTTLRDPAPNAIPPPEDPSTIGRLSSG 488
|
170
....*....|....*...
gi 2030623205 309 PAQDDEQGPPRPIPASAA 326
Cdd:COG5665 489 DKLANETGPPVIRRDSTP 506
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
150-334 |
7.97e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.24 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 150 VWFHARIPRDFIADGFQDPSFPPSTADHPDTVSPPPAPSCATADVQTPEASAPPEGQFSTEVPlqggefliSEAEVQPAT 229
Cdd:PHA03307 93 STLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAA--------GASPAAVAS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 230 QVAACGGVSTPTALAPS-----VPSQAPFPLLPAPGLiqsnLPSDVHAPASPGSLPSVIPAQAPCVMALSPI--SAPSVA 302
Cdd:PHA03307 165 DAASSRQAALPLSSPEEtarapSSPPAEPPPSTPPAA----ASPRPPRRSSPISASASSPAPAPGRSAADDAgaSSSDSS 240
|
170 180 190
....*....|....*....|....*....|..
gi 2030623205 303 PAETLIPAQDDEQGPPRPIPASAAPLRHPCRG 334
Cdd:PHA03307 241 SSESSGCGWGPENECPLPRPAPITLPTRIWEA 272
|
|
| DUF4813 |
pfam16072 |
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. ... |
168-288 |
8.56e-04 |
|
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between 345 and 672 amino acids in length.
Pssm-ID: 435117 [Multi-domain] Cd Length: 288 Bit Score: 42.05 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 168 PSFPPSTADHPDTVsPPPAPSCATADVQTPEAsappegqfstevPLQGGefliseaevqPATQVAACGGVSTPTALAPSV 247
Cdd:pfam16072 174 PAYPVAPAAYPAQA-PAAAPAPAPGAPQTPLA------------PLNPV----------AAAPAAAAGAAAAPVVAAAAP 230
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2030623205 248 PSQAPFPllPAPgliqsNLPSDVHAPASPGSLPSViPAQAP 288
Cdd:pfam16072 231 AAAAPPP--PAP-----AAPPADAAPPAPGGIICV-PVRVP 263
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
166-284 |
8.73e-04 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 42.16 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 166 QDPSFPPSTADHPDTVSPPPAPSCATADVQTPE-ASAPPEGQFSTEVPlqggefliSEAEVQPATQVAACGGVSTPTALA 244
Cdd:PHA02682 79 QSPLAPSPACAAPAPACPACAPAAPAPAVTCPApAPACPPATAPTCPP--------PAVCPAPARPAPACPPSTRQCPPA 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2030623205 245 PSVPSQAPFPL---------LPAPGLIQSNLPSDVHAPASPGSLPSVIP 284
Cdd:PHA02682 151 PPLPTPKPAPAakpiflhnqLPPPDYPAASCPTIETAPAASPVLEPRIP 199
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
166-324 |
1.06e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.85 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 166 QDPSFPPSTADHPDTVSPPPAPSCATADVQ----TPEASAPPEGQFSTEVPLQGGEFLISEAEVQPATQVAACGGVSTPT 241
Cdd:PHA03307 82 NESRSTPTWSLSTLAPASPAREGSPTPPGPsspdPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 242 ALAPSVPSQAPFPLLPAPgliqsnlPSDVHAPASPGSLPSVIPAQAPCVMALSPISAPSVAPAETLIPAQDDEQGPPRPI 321
Cdd:PHA03307 162 VASDAASSRQAALPLSSP-------EETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGA 234
|
...
gi 2030623205 322 PAS 324
Cdd:PHA03307 235 SSS 237
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
177-327 |
1.30e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 42.16 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 177 HPDTVSPPPApscatadvQTPEASAPPEGQFSTEVPlqggefliSEAEVQPATQVAACGGVSTPTALAPSVPSQAPFPLL 256
Cdd:PRK07994 360 HPAAPLPEPE--------VPPQSAAPAASAQATAAP--------TAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLL 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2030623205 257 PAPGLIQSNLPSDVHAPASPGSLPSVIPAQApcvmALSPISAPSVAPAETLIPAQDDEQGPPRPIPASAAP 327
Cdd:PRK07994 424 AARQQLQRAQGATKAKKSEPAAASRARPVNS----ALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVK 490
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
224-327 |
1.42e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.17 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 224 EVQPATQVAACGGVSTPTALAPSVPSQAPFPLLPAPGLIQSNLPSDVHAPASPGSLPSVIPAQAPCVMALS----PISAP 299
Cdd:PRK12323 371 GAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASArgpgGAPAP 450
|
90 100
....*....|....*....|....*...
gi 2030623205 300 SVAPAETLIPAQDDEQGPPRPIPASAAP 327
Cdd:PRK12323 451 APAPAAAPAAAARPAAAGPRPVAAAAAA 478
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
184-327 |
2.63e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.40 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 184 PPAPSCATADVQTPEASAPPEGQFSTEVPlqggefliSEAEVQPATQVAAcggVSTPTALAPSVPSQAPFPLLPAPGLIQ 263
Cdd:PRK12323 373 GPATAAAAPVAQPAPAAAAPAAAAPAPAA--------PPAAPAAAPAAAA---AARAVAAAPARRSPAPEALAAARQASA 441
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2030623205 264 SNLPSDVHAPASPGSLPsvIPAQAPCVMALSPISAPSVAPAETLIPAQDDEQGPPRPIPASAAP 327
Cdd:PRK12323 442 RGPGGAPAPAPAPAAAP--AAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELP 503
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
172-333 |
2.83e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.21 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 172 PSTADHPDTVSPPPAPSCATADVQTPEASAPPEGQFSTEVPLQGGEfliseaevQPATQVAACGGVSTPTALAPS--VPS 249
Cdd:PHA03378 676 PSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAAT--------GRARPPAAAPGRARPPAAAPGraRPP 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 250 QAPFPLLPAPGLIQSNLPSDVHAPASPGSLPsviPAQAPCVMALSPISAPSVAPAETLIPAQddEQGPPRPIPASAAPLR 329
Cdd:PHA03378 748 AAAPGRARPPAAAPGRARPPAAAPGAPTPQP---PPQAPPAPQQRPRGAPTPQPPPQAGPTS--MQLMPRAAPGQQGPTK 822
|
....
gi 2030623205 330 HPCR 333
Cdd:PHA03378 823 QILR 826
|
|
| MISS |
pfam15822 |
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ... |
168-338 |
3.17e-03 |
|
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.
Pssm-ID: 318115 [Multi-domain] Cd Length: 238 Bit Score: 39.97 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 168 PSFPPSTADHPDTVSPPPAPscaTADVQTPEASAPPEGQFSTEVPLQGGefliseAEVQPATQVAACGGVSTPT-ALAPS 246
Cdd:pfam15822 82 APFPPSGPSCPPPGGPYPAP---TVPGPGPIGPYPTPNMPFPELPRPYG------APTDPAAAAPSGPWGSMSSgPWAPG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 247 VPSQAPFPLLPAPgliqsnlpsdvhapaSPGSLPSVIPAQapcvmalSPISAPSVaPAETLIPAQddeQGPPRPIPAS-- 324
Cdd:pfam15822 153 MGGQYPAPNMPYP---------------SPGPYPAVPPPQ-------SPGAAPPV-PWGTVPPGP---WGPPAPYPDPtg 206
|
170
....*....|....*...
gi 2030623205 325 --AAPLRHPC--RGYQVP 338
Cdd:pfam15822 207 syPMPGLYPTpnNPFQVP 224
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
171-315 |
6.02e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.35 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2030623205 171 PPSTADHPDTVSPPPAPSCATADVQTPEASAPpegqfstevplqggefliseAEVQPATQVAACGGVSTPTALAPSVPSQ 250
Cdd:PRK07764 386 GVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAP--------------------AAAAAPAPAAAPQPAPAPAPAPAPPSPA 445
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2030623205 251 APFPLLPAPGLIQSNLPSDVHAPAS-PGSLPSVIPAQAPCVMALSPISAPSVAPAETLIPAQDDEQ 315
Cdd:PRK07764 446 GNAPAGGAPSPPPAAAPSAQPAPAPaAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAAT 511
|
|
| |
