|
Name |
Accession |
Description |
Interval |
E-value |
| TTL |
pfam03133 |
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ... |
255-510 |
3.31e-45 |
|
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several post-translational modifications of which the reversible detyrosination/tyrosination of the carboxy-terminal end of most alpha-tubulins has been extensively analysed. This modification cycle involves a specific carboxypeptidase and the activity of the tubulin-tyrosine ligase (TTL). The true physiological function of TTL has so far not been established. Tubulin-tyrosine ligase (TTL) catalyzes the ATP-dependent post-translational addition of a tyrosine to the carboxy terminal end of detyrosinated alpha-tubulin. In normally cycling cells, the tyrosinated form of tubulin predominates. However, in breast cancer cells, the detyrosinated form frequently predominates, with a correlation to tumour aggressiveness. On the other hand, 3-nitrotyrosine has been shown to be incorporated, by TTL, into the carboxy terminal end of detyrosinated alpha-tubulin. This reaction is not reversible by the carboxypeptidase enzyme. Cells cultured in 3-nitrotyrosine rich medium showed evidence of altered microtubule structure and function, including altered cell morphology, epithelial barrier dysfunction, and apoptosis. Bacterial homologs of TTL are predicted to form peptide tags. Some of these are fused to a 2-oxoglutarate Fe(II)-dependent dioxygenase domain.
Pssm-ID: 397308 Cd Length: 291 Bit Score: 162.89 E-value: 3.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 255 EEFFPETYRLDLkhEREAFFTLF--DETQIWICKPTASNQGKGIFLlrkqeevaalqakTRSAEDDPIHHKSpfrgpQAR 332
Cdd:pfam03133 41 GDFLPRTFILPT--DLAEFVDYFedRERNTWIVKPSASARGRGIRV-------------TNKLSQIPKWSQS-----RPL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 333 VVQRYIQNPLLLDGRKFDVRSYLLIACTTPYMIF-FSHGYARLTLSLYDPHSSDLSG---HLTNQFMQKKSPL---YVLL 405
Cdd:pfam03133 101 VVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYvYREGLLRFASVKYSPSSSDLDDvemHLTNYSIQKKSSSlneDYNE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 406 KEDTVWSMERLNRYInttfwkaRGLPKDWVFTTLTK-RMQQIMAHCFLAAKSKLECKLGYFDLIGCDFLIDDNFKVWLLE 484
Cdd:pfam03133 181 PHGHKWSLQNFWKYL-------EEKDKDEIWLEIESiIIKTILAAEVEASRLNVQPLPNCFELYGFDFMIDENLKPWLLE 253
|
250 260
....*....|....*....|....*.
gi 1622824923 485 MNSNPALHTNCEVLKEVIPGVVIETL 510
Cdd:pfam03133 254 VNSSPSLHSTTKLDARLKEQLIDDVL 279
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
560-665 |
1.08e-06 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 51.91 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 560 PPPTRQAKSSGPPTPRAPDQPGTRRPVPPPLAPQRPQlPGPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQEPSP---GTA 636
Cdd:PRK07764 394 PAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQ-PAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPapaPAA 472
|
90 100
....*....|....*....|....*....
gi 1622824923 637 KEERKEPENARPWGGHPRPTPHAPATLPA 665
Cdd:PRK07764 473 APEPTAAPAPAPPAAPAPAAAPAAPAAPA 501
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
561-660 |
1.01e-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: 42.45 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 561 PPTRQAKSSGPPTPRAPDQPGTR--RPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQEPSPGTAKE 638
Cdd:pfam03154 171 PPVLQAQSGAASPPSPPPPGTTQaaTAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQ 250
|
90 100
....*....|....*....|....
gi 1622824923 639 ERKE--PENARPWGGHPRPTPHAP 660
Cdd:pfam03154 251 PMTQppPPSQVSPQPLPQPSLHGQ 274
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
560-668 |
1.10e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 41.68 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 560 PPPTRQAKSSGPPTPRAPDQPGTRRPV--PPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQEPSPGTAK 637
Cdd:NF040712 226 APATDSDPAEAGTPDDLASARRRRAGVeqPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPPAPAPAAPAAP 305
|
90 100 110
....*....|....*....|....*....|....
gi 1622824923 638 EERKEPENARPwGGHPRPTPHAP---ATLPAFRD 668
Cdd:NF040712 306 AAPEAEEPARP-EPPPAPKPKRRrrrASVPSWDD 338
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
563-664 |
3.88e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 40.52 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 563 TRQAKSSGPPTPRAPDQPGTRRPVP-------PPLAPQRPQLPGPSPDPDSahdgQPQAPGKEQSGTGDR-HPEQEPSPG 634
Cdd:NF033839 273 TKFKKGLTQDTPKEPGNKKPSAPKPgmqpspqPEKKEVKPEPETPKPEVKP----QLEKPKPEVKPQPEKpKPEVKPQLE 348
|
90 100 110
....*....|....*....|....*....|.
gi 1622824923 635 TAKEE-RKEPENARPwGGHPRPTPHAPATLP 664
Cdd:NF033839 349 TPKPEvKPQPEKPKP-EVKPQPEKPKPEVKP 378
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
556-666 |
4.02e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 40.14 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 556 RRRLPPPTRQAkssgpPTPRAPDQPGTRRPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQEPSPGT 635
Cdd:NF040712 196 LRPLATVPRLA-----REPADARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEP 270
|
90 100 110
....*....|....*....|....*....|.
gi 1622824923 636 AKEERKEPENARPWGGHPRPTPHAPATLPAF 666
Cdd:NF040712 271 DEATRDAGEPPAPGAAETPEAAEPPAPAPAA 301
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
572-662 |
6.66e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 39.75 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 572 PTPRAPDQPGTRRP-VPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKE---QSGTGDrhPEQEPSPGTAKEERK-EPENA 646
Cdd:NF033839 405 PKPEVKPQPEKPKPeVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEvkpQPETPK--PEVKPQPEKPKPEVKpQPEKP 482
|
90
....*....|....*.
gi 1622824923 647 RPWGGHPRPTPHAPAT 662
Cdd:NF033839 483 KPDNSKPQADDKKPST 498
|
|
| BimA_second |
NF040983 |
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ... |
560-629 |
7.07e-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: 39.12 E-value: 7.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 560 PPPTRQAKSSGPPTPRAPDQPGTRRPVPPPLAPQRPQLPGPSPDPDSahdgqpQAPGKEQSGTGDRHPEQ 629
Cdd:NF040983 96 PPPPPPPPPTPPPPPPPPPPPPPPSPPPPPPPSPPPSPPPPTTTPPT------RTTPSTTTPTPSMHPIQ 159
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
572-664 |
7.91e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 39.37 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 572 PTPRAPDQPGTRRPV--PPPLAPQ---RPQLPGPSPD-------PDSAHDGQPQAPgkeqsgtgdrHPEQEPSPGTAKEE 639
Cdd:NF033839 339 PKPEVKPQLETPKPEvkPQPEKPKpevKPQPEKPKPEvkpqpetPKPEVKPQPEKP----------KPEVKPQPEKPKPE 408
|
90 100
....*....|....*....|....*.
gi 1622824923 640 RK-EPENARPwGGHPRPTPHAPATLP 664
Cdd:NF033839 409 VKpQPEKPKP-EVKPQPEKPKPEVKP 433
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| TTL |
pfam03133 |
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ... |
255-510 |
3.31e-45 |
|
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several post-translational modifications of which the reversible detyrosination/tyrosination of the carboxy-terminal end of most alpha-tubulins has been extensively analysed. This modification cycle involves a specific carboxypeptidase and the activity of the tubulin-tyrosine ligase (TTL). The true physiological function of TTL has so far not been established. Tubulin-tyrosine ligase (TTL) catalyzes the ATP-dependent post-translational addition of a tyrosine to the carboxy terminal end of detyrosinated alpha-tubulin. In normally cycling cells, the tyrosinated form of tubulin predominates. However, in breast cancer cells, the detyrosinated form frequently predominates, with a correlation to tumour aggressiveness. On the other hand, 3-nitrotyrosine has been shown to be incorporated, by TTL, into the carboxy terminal end of detyrosinated alpha-tubulin. This reaction is not reversible by the carboxypeptidase enzyme. Cells cultured in 3-nitrotyrosine rich medium showed evidence of altered microtubule structure and function, including altered cell morphology, epithelial barrier dysfunction, and apoptosis. Bacterial homologs of TTL are predicted to form peptide tags. Some of these are fused to a 2-oxoglutarate Fe(II)-dependent dioxygenase domain.
Pssm-ID: 397308 Cd Length: 291 Bit Score: 162.89 E-value: 3.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 255 EEFFPETYRLDLkhEREAFFTLF--DETQIWICKPTASNQGKGIFLlrkqeevaalqakTRSAEDDPIHHKSpfrgpQAR 332
Cdd:pfam03133 41 GDFLPRTFILPT--DLAEFVDYFedRERNTWIVKPSASARGRGIRV-------------TNKLSQIPKWSQS-----RPL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 333 VVQRYIQNPLLLDGRKFDVRSYLLIACTTPYMIF-FSHGYARLTLSLYDPHSSDLSG---HLTNQFMQKKSPL---YVLL 405
Cdd:pfam03133 101 VVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYvYREGLLRFASVKYSPSSSDLDDvemHLTNYSIQKKSSSlneDYNE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 406 KEDTVWSMERLNRYInttfwkaRGLPKDWVFTTLTK-RMQQIMAHCFLAAKSKLECKLGYFDLIGCDFLIDDNFKVWLLE 484
Cdd:pfam03133 181 PHGHKWSLQNFWKYL-------EEKDKDEIWLEIESiIIKTILAAEVEASRLNVQPLPNCFELYGFDFMIDENLKPWLLE 253
|
250 260
....*....|....*....|....*.
gi 1622824923 485 MNSNPALHTNCEVLKEVIPGVVIETL 510
Cdd:pfam03133 254 VNSSPSLHSTTKLDARLKEQLIDDVL 279
|
|
| ATPgrasp_YheCD |
pfam14398 |
YheC/D like ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the ... |
237-489 |
3.92e-07 |
|
YheC/D like ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the modification/biosynthesis of spore-wall and capsular proteins.
Pssm-ID: 405146 [Multi-domain] Cd Length: 256 Bit Score: 51.80 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 237 DLPWTSPG---------HLRPQRVLRmeEFFPETYRLDlkhEREAFFTLFDETQIWICKPTASNQGKGIFLLRKQEEVAA 307
Cdd:pfam14398 1 GIPFFNPGffnkwevyeLLSKDPELR--PYLPETELLQ---SPEDLERMLEKYGSVYLKPVNGSLGKGILRIEKDGGGYY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 308 LQAKTR--------SAEDDPIHHKSPFRGPQARVVQRYIqNPLLLDGRKFDVRsyLLI--------ACTTpymiffshGY 371
Cdd:pfam14398 76 LYGRYGknsktnrfLDFSELESFLRRLLGKKRYIIQQGI-DLATIDGRPFDFR--VLVqkngkgkwVVTG--------IA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 372 ARLTlslyDPHS--SDLSGHLTnqfmqkksplyvllkedtvwsMERLNRYINTTFWKARGLPkdwvfttLTKRMQQImah 449
Cdd:pfam14398 145 ARIA----GPGSitTNLSGGGT---------------------AIPLEEALRRAFGEERAEK-------ILEKLEEL--- 189
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1622824923 450 CFLAAKSkLECKLGYFDLIGCDFLIDDNFKVWLLEMNSNP 489
Cdd:pfam14398 190 ALELARA-LEESFGGLGELGLDLGIDKNGRVWLLEVNSKP 228
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
560-665 |
1.08e-06 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 51.91 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 560 PPPTRQAKSSGPPTPRAPDQPGTRRPVPPPLAPQRPQlPGPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQEPSP---GTA 636
Cdd:PRK07764 394 PAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQ-PAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPapaPAA 472
|
90 100
....*....|....*....|....*....
gi 1622824923 637 KEERKEPENARPWGGHPRPTPHAPATLPA 665
Cdd:PRK07764 473 APEPTAAPAPAPPAAPAPAAAPAAPAAPA 501
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
557-667 |
3.35e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.71 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 557 RRL--PPPTRQAKS--------SGPPTPRAPDQPGTRRPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGkEQSGTGDRH 626
Cdd:PHA03247 2884 RRLarPAVSRSTESfalppdqpERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAG-EPSGAVPQP 2962
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1622824923 627 PEQEPSPGTAKEERKEPENARPWGGHPRPTPHAPATLPAFR 667
Cdd:PHA03247 2963 WLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSR 3003
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
555-655 |
1.18e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.78 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 555 LRRRLP---PPTRQAKSSGPPTPRAPDQPGTRRPVPPPLAPQRPQlPGPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQ-- 629
Cdd:PHA03247 2862 VRRRPPsrsPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPE-RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRpq 2940
|
90 100
....*....|....*....|....*....
gi 1622824923 630 ---EPSPGTAKEERKEPENARPWGGHPRP 655
Cdd:PHA03247 2941 pplAPTTDPAGAGEPSGAVPQPWLGALVP 2969
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
556-662 |
1.41e-05 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 48.52 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 556 RRRLPP--PTRQAKSSGPPTPRAPDQPGTRRPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTGD-RHPEQEPS 632
Cdd:PHA03378 693 TMQPPPraPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRaRPPAAAPG 772
|
90 100 110
....*....|....*....|....*....|...
gi 1622824923 633 PGTAKEERKEPENA--RPWGG-HPRPTPHAPAT 662
Cdd:PHA03378 773 APTPQPPPQAPPAPqqRPRGApTPQPPPQAGPT 805
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
557-665 |
1.61e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.40 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 557 RRLPPPTRQAKSSGPPTPRAPDQPGTRRPVPPPLAP----QRPQLPGPSPD--PDSAHDGQPQAPGKEQSGTGDRHPEQE 630
Cdd:PHA03247 2659 GRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSltslADPPPPPPTPEpaPHALVSATPLPPGPAAARQASPALPAA 2738
|
90 100 110
....*....|....*....|....*....|....*
gi 1622824923 631 PSPGTAKEerkepENARPWGGHPRPTPHAPATLPA 665
Cdd:PHA03247 2739 PAPPAVPA-----GPATPGGPARPARPPTTAGPPA 2768
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
562-668 |
2.66e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 47.38 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 562 PTRQAKSSGPPTPRAPDQPGTRRPVPPPLAPQRPQLPgPSPDPDSAHDgQPQAPGKEQSGTGDRHP--EQEPSPGTAKEE 639
Cdd:PTZ00449 573 PTLSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRP-KSPKLPELLD-IPKSPKRPESPKSPKRPppPQRPSSPERPEG 650
|
90 100
....*....|....*....|....*....
gi 1622824923 640 RKEPENARPwgghprPTPHAPATLPAFRD 668
Cdd:PTZ00449 651 PKIIKSPKP------PKSPKPPFDPKFKE 673
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
557-669 |
3.83e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.24 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 557 RRLPPP------------TRQAKSSGPP---TPRAP-----DQPGTRRPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPG 616
Cdd:PHA03247 2566 RSVPPPrpaprpsepavtSRARRPDAPPqsaRPRAPvddrgDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPT 2645
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622824923 617 KEQSgtgdRHPEQEPSPGTAKEERKEPENARPWGGH-----PRPtPHAPATLPAFRDL 669
Cdd:PHA03247 2646 VPPP----ERPRDDPAPGRVSRPRRARRLGRAAQASsppqrPRR-RAARPTVGSLTSL 2698
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
547-664 |
5.58e-05 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 46.60 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 547 PRLGGSCSLRRRLPPPTRQAKSSGPPTPRAPdqpgtrrPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPgkeqSGTGDRH 626
Cdd:PHA03378 676 PSPTGANTMLPIQWAPGTMQPPPRAPTPMRP-------PAAPPGRAQRPAAATGRARPPAAAPGRARPP----AAAPGRA 744
|
90 100 110
....*....|....*....|....*....|....*....
gi 1622824923 627 PEQEPSPGTAKEERKEPENARPWGGHP-RPTPHAPATLP 664
Cdd:PHA03378 745 RPPAAAPGRARPPAAAPGRARPPAAAPgAPTPQPPPQAP 783
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
550-667 |
1.34e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 550 GGSCSLRRRLPPPTRQAKSSGPP---TPRA--------------PDQPGTRRPVPPPLAPQRPQLPGP-----SPDPDSA 607
Cdd:PHA03247 2658 PGRVSRPRRARRLGRAAQASSPPqrpRRRAarptvgsltsladpPPPPPTPEPAPHALVSATPLPPGPaaarqASPALPA 2737
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 608 HDGQPQAPGKEQSGTGDRHPEQEPSPGTAkeERKEPENARPWGGHPRPTPHAPATLPAFR 667
Cdd:PHA03247 2738 APAPPAVPAGPATPGGPARPARPPTTAGP--PAPAPPAAPAAGPPRRLTRPAVASLSESR 2795
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
567-665 |
1.39e-04 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 45.07 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 567 KSSGPPTPRAPDQpgTRRPVPP--PLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQEPSPGTAKEERKEP- 643
Cdd:PTZ00449 704 KETLPETPGTPFT--TPRPLPPklPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHETPADTPLPDILAEEFKEEd 781
|
90 100 110
....*....|....*....|....*....|.
gi 1622824923 644 ---ENARPWGGHPRP------TPHAPATLPA 665
Cdd:PTZ00449 782 ihaETGEPDEAMKRPdspsehEDKPPGDHPS 812
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
552-665 |
1.58e-04 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 44.82 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 552 SCSLRRRLPPPTRQA----KSSGPPTPrapdqpgtrrPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTGDRHP 627
Cdd:PRK14086 71 SETLSRELGRPIRIAitvdPSAGEPAP----------PPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQDQLP 140
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622824923 628 EQEPSpGTAKEERKEP------ENARPW----GGHPRPTPHAPATLPA 665
Cdd:PRK14086 141 TARPA-YPAYQQRPEPgawpraADDYGWqqqrLGFPPRAPYASPASYA 187
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
542-661 |
1.61e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.98 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 542 EADVWPRLGGSCSLRRRLPPPTRQAKSSGPPTPRAPDQPGTRRPVPPPlapqrpqlPGPSPDPDSAHDGQPQAPGKEQSG 621
Cdd:PRK07764 663 SDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPP--------AGQADDPAAQPPQAAQGASAPSPA 734
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622824923 622 TGD---RHPEQEPSPGTAKEERKE-----PENARPWGGHPRPTPHAPA 661
Cdd:PRK07764 735 ADDpvpLPPEPDDPPDPAGAPAQPppppaPAPAAAPAAAPPPSPPSEE 782
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
566-665 |
2.92e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.21 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 566 AKSSGPPTPRAPDQPGtrrpvpPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTGdrHPEQEPSPGTAKEERKEPEN 645
Cdd:PRK07764 592 PGAAGGEGPPAPASSG------PPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAP--APGVAAPEHHPKHVAVPDAS 663
|
90 100
....*....|....*....|
gi 1622824923 646 ARPWGGHPRPTPHAPATLPA 665
Cdd:PRK07764 664 DGGDGWPAKAGGAAPAAPPP 683
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
559-665 |
3.19e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 559 LPPPTRQAKSSgPPTPRAPDQPG------------------TRRPVPPPLAPQRP---QLPGPSPDPDSAHDGQPQAPGK 617
Cdd:PHA03247 2828 LPPPTSAQPTA-PPPPPGPPPPSlplggsvapggdvrrrppSRSPAAKPAAPARPpvrRLARPAVSRSTESFALPPDQPE 2906
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1622824923 618 EQsgtgdRHPEQEPSPGTAKEERKEPENARPWGGHPRP-TPHAPATLPA 665
Cdd:PHA03247 2907 RP-----PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPqPPLAPTTDPA 2950
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
561-668 |
3.20e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 43.93 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 561 PPTRQAKSSGPPTPRAPDQPGTRRP---VPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQEPSPGTAK 637
Cdd:PRK14951 383 RPEAAAPAAAPVAQAAAAPAPAAAPaaaASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAI 462
|
90 100 110
....*....|....*....|....*....|.
gi 1622824923 638 EERKEPENARPWGGHPRPTPHAPATLPAFRD 668
Cdd:PRK14951 463 PVRVAPEPAVASAAPAPAAAPAAARLTPTEE 493
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
572-667 |
3.87e-04 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 43.56 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 572 PTPRAPDQPGTRRPVPPPLAPQRP-QLPGPSPDPDSAHDGQPQaPGKEQSGTGDRHPEQEPSPGTAKEERKEPENARPWG 650
Cdd:PHA03269 27 PIPELHTSAATQKPDPAPAPHQAAsRAPDPAVAPTSAASRKPD-LAQAPTPAASEKFDPAPAPHQAASRAPDPAVAPQLA 105
|
90
....*....|....*..
gi 1622824923 651 GHPRPTPHAPATLPAFR 667
Cdd:PHA03269 106 AAPKPDAAEAFTSAAQA 122
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
560-665 |
3.94e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.82 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 560 PPPTRQAKSSGPPTPRAPDQPGTRRPVPPPLAPQRPqlPGPSPDPDSahdGQPQAPGKEQSGTGDRHPEQEPSPGTAKEE 639
Cdd:PRK07764 406 PAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAP--PSPAGNAPA---GGAPSPPPAAAPSAQPAPAPAAAPEPTAAP 480
|
90 100
....*....|....*....|....*.
gi 1622824923 640 RKEPENARPWGGHPRPTPHAPATLPA 665
Cdd:PRK07764 481 APAPPAAPAPAAAPAAPAAPAAPAGA 506
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
571-668 |
6.68e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.39 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 571 PPTPRAPDQPGTRRPVPPPLAPQRPqlPGPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQEPSPGTAKEERKEPENARPWG 650
Cdd:PHA03247 2553 PPLPPAAPPAAPDRSVPPPRPAPRP--SEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPS 2630
|
90 100
....*....|....*....|..
gi 1622824923 651 GHPRPT----PHAPATLPAFRD 668
Cdd:PHA03247 2631 PSPAANepdpHPPPTVPPPERP 2652
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
561-660 |
1.01e-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: 42.45 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 561 PPTRQAKSSGPPTPRAPDQPGTR--RPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQEPSPGTAKE 638
Cdd:pfam03154 171 PPVLQAQSGAASPPSPPPPGTTQaaTAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQ 250
|
90 100
....*....|....*....|....
gi 1622824923 639 ERKE--PENARPWGGHPRPTPHAP 660
Cdd:pfam03154 251 PMTQppPPSQVSPQPLPQPSLHGQ 274
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
560-652 |
1.06e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 42.39 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 560 PPPTRQAKSSGPPTPRAP---DQPGTRRPVPPPLAPQRPQLPGPSPDPDSAHDGQpQAPGKEQSGTGDRHPEQEPSPGTA 636
Cdd:PRK14951 406 APAAAASAPAAPPAAAPPapvAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETV-AIPVRVAPEPAVASAAPAPAAAPA 484
|
90
....*....|....*.
gi 1622824923 637 KEERKEPENARPWGGH 652
Cdd:PRK14951 485 AARLTPTEEGDVWHAT 500
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
560-668 |
1.10e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 41.68 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 560 PPPTRQAKSSGPPTPRAPDQPGTRRPV--PPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQEPSPGTAK 637
Cdd:NF040712 226 APATDSDPAEAGTPDDLASARRRRAGVeqPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPPAPAPAAPAAP 305
|
90 100 110
....*....|....*....|....*....|....
gi 1622824923 638 EERKEPENARPwGGHPRPTPHAP---ATLPAFRD 668
Cdd:NF040712 306 AAPEAEEPARP-EPPPAPKPKRRrrrASVPSWDD 338
|
|
| PRK14954 |
PRK14954 |
DNA polymerase III subunits gamma and tau; Provisional |
503-637 |
1.12e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184918 [Multi-domain] Cd Length: 620 Bit Score: 42.24 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 503 PGVVIETLDLALETfQKSLRGQKMLPL---LSQRRFVLLHNGEADVWPRLGGSCSLRRRLPPPTRQAKSSGPPtPRAPDQ 579
Cdd:PRK14954 336 PAAVMQMTDFLMKT-QGELKFQFEYQFrfeLALLRLIELVRNDGGVAPSPAGSPDVKKKAPEPDLPQPDRHPG-PAKPEA 413
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622824923 580 PGtRRPVPpplapqrpqlpGPSPDPDSAHDGQPQAPgkeQSGTGDRHPEQEPSPGTAK 637
Cdd:PRK14954 414 PG-ARPAE-----------LPSPASAPTPEQQPPVA---RSAPLPPSPQASAPRNVAS 456
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
550-665 |
1.19e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.28 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 550 GGSCSLRRRLPPPTRQAKSSGPPTPRAPDQPGTRR-PVPPPLAPQRPQLPGPSPDPDSAHDGQPQA--PGKEQSGTGDRH 626
Cdd:PRK07764 638 EASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKaGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPapAATPPAGQADDP 717
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622824923 627 PEQEPSPGTAKEERK-----------EPENARPWGGHPRPTPHAPATLPA 665
Cdd:PRK07764 718 AAQPPQAAQGASAPSpaaddpvplppEPDDPPDPAGAPAQPPPPPAPAPA 767
|
|
| PHA03264 |
PHA03264 |
envelope glycoprotein D; Provisional |
539-661 |
1.27e-03 |
|
envelope glycoprotein D; Provisional
Pssm-ID: 223029 [Multi-domain] Cd Length: 416 Bit Score: 41.53 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 539 HNGEADVWPRLGGscslrRRLPPPTRQAKSSGPPTprAPDQpGTRRPVPPPLAPQRPQlPGPSPDPDSAHDGQPQAPGKE 618
Cdd:PHA03264 239 HKAIVDYWFMRHG-----GVVPPYFEESKGYEPPP--APSG-GSPAPPGDDRPEAKPE-PGPVEDGAPGRETGGEGEGPE 309
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622824923 619 QSGTgDRHPEQEPSPGTAkeeRKEPENARPWG-------GHPRPTPHAPA 661
Cdd:PHA03264 310 PAGR-DGAAGGEPKPGPP---RPAPDADRPEGwpsleaiTFPPPTPATPA 355
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
561-665 |
1.96e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.40 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 561 PPTRQAKSSGPPTPRAPdqpgTRRPVPPPLAPQRPQLPGPSPDPDSAHDGQP-QAPGKEQSGTGDRHPEQEPSPGTAKEE 639
Cdd:PRK12323 434 AAARQASARGPGGAPAP----APAPAAAPAAAARPAAAGPRPVAAAAAAAPArAAPAAAPAPADDDPPPWEELPPEFASP 509
|
90 100
....*....|....*....|....*.
gi 1622824923 640 RKEPENARPWGGHPRPTPHaPATLPA 665
Cdd:PRK12323 510 APAQPDAAPAGWVAESIPD-PATADP 534
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
547-666 |
2.12e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.46 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 547 PRLGGSCSLRRRLPP----PTRQAKSSGPPTPRAPDQPGTRRPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGT 622
Cdd:PHA03247 2720 PLPPGPAAARQASPAlpaaPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLP 2799
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1622824923 623 GDRHPEQEPSPGTAKEErKEPENARPWGGHPRPT---PHAPATLPAF 666
Cdd:PHA03247 2800 SPWDPADPPAAVLAPAA-ALPPAASPAGPLPPPTsaqPTAPPPPPGP 2845
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
558-665 |
2.13e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.46 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 558 RLPPPTRQAKSSGPPTPRAPDQPGTRRPvPPPLAPQRPQLP-GPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQEPSPGTA 636
Cdd:PHA03247 2706 PTPEPAPHALVSATPLPPGPAAARQASP-ALPAAPAPPAVPaGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLT 2784
|
90 100
....*....|....*....|....*....
gi 1622824923 637 KEERKEPENARPWGGHPRPTPHAPATLPA 665
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVLA 2813
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
555-648 |
2.29e-03 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 555 LRRRLPPPTRQAKSSGPPTPRAPDQPGT-RRPVPPPlAPQRPQ---LPGPSPDPDSAHdgQPQAPGKEQSGTGDRHPEQE 630
Cdd:PTZ00449 575 LSKKPEFPKDPKHPKDPEEPKKPKRPRSaQRPTRPK-SPKLPElldIPKSPKRPESPK--SPKRPPPPQRPSSPERPEGP 651
|
90
....*....|....*...
gi 1622824923 631 PSPGTAkeerKEPENARP 648
Cdd:PTZ00449 652 KIIKSP----KPPKSPKP 665
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
556-665 |
2.71e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 556 RRRLPPPTRQAKSSGPPT-PRAPDQPGTRRPVPPPLAPQRPQLPGPS--PDPDSAHDGQPQAPGKEQSGTGDRHPEQEPS 632
Cdd:PHA03247 2756 RPARPPTTAGPPAPAPPAaPAAGPPRRLTRPAVASLSESRESLPSPWdpADPPAAVLAPAAALPPAASPAGPLPPPTSAQ 2835
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1622824923 633 PGTAKEERKEPENARPWGG--------HPRPTPHAPATLPA 665
Cdd:PHA03247 2836 PTAPPPPPGPPPPSLPLGGsvapggdvRRRPPSRSPAAKPA 2876
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
558-655 |
2.88e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 40.96 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 558 RLPPPTRQAKS-SGPPTPRAPDQP----GTRRPVP-PPLAPQRPQLPGPSPD-PDsahDGQPQAPGKEQSGTGDRHPEQE 630
Cdd:PRK14086 94 EPAPPPPHARRtSEPELPRPGRRPyegyGGPRADDrPPGLPRQDQLPTARPAyPA---YQQRPEPGAWPRAADDYGWQQQ 170
|
90 100 110
....*....|....*....|....*....|..
gi 1622824923 631 PS-------PGTAKEERKEPENARPWGGHPRP 655
Cdd:PRK14086 171 RLgfpprapYASPASYAPEQERDREPYDAGRP 202
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
560-669 |
2.94e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.74 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 560 PPPTRQAKSSGPPTPRAPDQPGTRRPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQEPSPGTAKEE 639
Cdd:PRK07764 703 PAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
|
90 100 110
....*....|....*....|....*....|
gi 1622824923 640 RKEPENARPwggHPRPTPHAPATLPAFRDL 669
Cdd:PRK07764 783 EEMAEDDAP---SMDDEDRRDAEEVAMELL 809
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
569-661 |
3.35e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 40.84 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 569 SGPPTPRAPDQPGTRR--PVPPPLAPQRPQLPGPsPDPDSAHDGQPQAPGKEQsgtgdRHPEQEPSPGTAKEERKEPENA 646
Cdd:PRK10263 753 QQPQQPVAPQQQYQQPqqPVAPQPQYQQPQQPVA-PQPQYQQPQQPVAPQPQY-----QQPQQPVAPQPQYQQPQQPVAP 826
|
90
....*....|....*
gi 1622824923 647 RPWGGHPRPtPHAPA 661
Cdd:PRK10263 827 QPQYQQPQQ-PVAPQ 840
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
557-665 |
3.47e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 40.92 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 557 RRLPPPTRQAKSSGPPTPRAPDQPGTRRPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTG---------DRHP 627
Cdd:PHA03307 101 AREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAAssrqaalplSSPE 180
|
90 100 110
....*....|....*....|....*....|....*...
gi 1622824923 628 EQEPSPGTAKEERKePENARPWGGHPRPTPHAPATLPA 665
Cdd:PHA03307 181 ETARAPSSPPAEPP-PSTPPAAASPRPPRRSSPISASA 217
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
561-648 |
3.64e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 40.84 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 561 PPTRQAKSSGPPTPRAPDQP--GTRRPVPPPLAPQRPQLPgPSPDPDSAHDGQPQAPGKEQsgtgdRHPEQEPSPGTAKE 638
Cdd:PRK10263 758 PVAPQQQYQQPQQPVAPQPQyqQPQQPVAPQPQYQQPQQP-VAPQPQYQQPQQPVAPQPQY-----QQPQQPVAPQPQYQ 831
|
90
....*....|
gi 1622824923 639 ERKEPENARP 648
Cdd:PRK10263 832 QPQQPVAPQP 841
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
563-664 |
3.88e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 40.52 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 563 TRQAKSSGPPTPRAPDQPGTRRPVP-------PPLAPQRPQLPGPSPDPDSahdgQPQAPGKEQSGTGDR-HPEQEPSPG 634
Cdd:NF033839 273 TKFKKGLTQDTPKEPGNKKPSAPKPgmqpspqPEKKEVKPEPETPKPEVKP----QLEKPKPEVKPQPEKpKPEVKPQLE 348
|
90 100 110
....*....|....*....|....*....|.
gi 1622824923 635 TAKEE-RKEPENARPwGGHPRPTPHAPATLP 664
Cdd:NF033839 349 TPKPEvKPQPEKPKP-EVKPQPEKPKPEVKP 378
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
556-666 |
4.02e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 40.14 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 556 RRRLPPPTRQAkssgpPTPRAPDQPGTRRPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQEPSPGT 635
Cdd:NF040712 196 LRPLATVPRLA-----REPADARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEP 270
|
90 100 110
....*....|....*....|....*....|.
gi 1622824923 636 AKEERKEPENARPWGGHPRPTPHAPATLPAF 666
Cdd:NF040712 271 DEATRDAGEPPAPGAAETPEAAEPPAPAPAA 301
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
557-644 |
4.07e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.69 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 557 RRLPPPTRQAKSS--------------GPPTPRAPDQPGTRRPVPPPLAPQRPQLP-GPSPDPDSAHDGQPQAPGKEQSG 621
Cdd:PHA03247 376 KRASLPTRKRRSArhaatpfargpggdDQTRPAAPVPASVPTPAPTPVPASAPPPPaTPLPSAEPGSDDGPAPPPERQPP 455
|
90 100 110
....*....|....*....|....*....|
gi 1622824923 622 TgDRHPEQEPSPGTAKE-------ERKEPE 644
Cdd:PHA03247 456 A-PATEPAPDDPDDATRkaldalrERRPPE 484
|
|
| PRK11901 |
PRK11901 |
hypothetical protein; Reviewed |
569-665 |
4.26e-03 |
|
hypothetical protein; Reviewed
Pssm-ID: 237015 [Multi-domain] Cd Length: 327 Bit Score: 39.67 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 569 SGPPTPRAPDQPgtrRPVPPPLAPQRPQLPGPSPDPDSAHDGQ---------------PQAPGKEQSGTGDRHPEQEPSP 633
Cdd:PRK11901 120 SAPPISPTPTQA---APPQTPNGQQRIELPGNISDALSQQQGQvnaasqnaqgntstlPTAPATVAPSKGAKVPATAETH 196
|
90 100 110
....*....|....*....|....*....|....
gi 1622824923 634 GTAKEerkEPENARPWGGHPR--PTPHAPATLPA 665
Cdd:PRK11901 197 PTPPQ---KPATKKPAVNHHKtaTVAVPPATSGK 227
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
541-665 |
4.66e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 40.19 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 541 GEADVWPRLGGSCSLRR-RLPPPTRQakssgPPTPRAPDQPGTRRPVPPPlAPQRPQLPGPSPDPDSahdgqpQAPGKEQ 619
Cdd:PRK14086 153 PEPGAWPRAADDYGWQQqRLGFPPRA-----PYASPASYAPEQERDREPY-DAGRPEYDQRRRDYDH------PRPDWDR 220
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1622824923 620 SGtGDRHPEQEPSPGTAKEERKEP-ENARPWGGHPRPTPHAPATLPA 665
Cdd:PRK14086 221 PR-RDRTDRPEPPPGAGHVHRGGPgPPERDDAPVVPIRPSAPGPLAA 266
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
560-668 |
5.68e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 39.86 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 560 PPPTRQAKSSGPPTPRAPDQPGTRRPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQEPSPGTAKEE 639
Cdd:PRK12323 385 PAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARP 464
|
90 100
....*....|....*....|....*....
gi 1622824923 640 RKEPENARPWGGHPRPTPHAPATLPAFRD 668
Cdd:PRK12323 465 AAAGPRPVAAAAAAAPARAAPAAAPAPAD 493
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
572-662 |
6.66e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 39.75 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 572 PTPRAPDQPGTRRP-VPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKE---QSGTGDrhPEQEPSPGTAKEERK-EPENA 646
Cdd:NF033839 405 PKPEVKPQPEKPKPeVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEvkpQPETPK--PEVKPQPEKPKPEVKpQPEKP 482
|
90
....*....|....*.
gi 1622824923 647 RPWGGHPRPTPHAPAT 662
Cdd:NF033839 483 KPDNSKPQADDKKPST 498
|
|
| BimA_second |
NF040983 |
trimeric autotransporter actin-nucleating factor BimA; This HMM describes BimA (Burkholderia ... |
560-629 |
7.07e-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: 39.12 E-value: 7.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 560 PPPTRQAKSSGPPTPRAPDQPGTRRPVPPPLAPQRPQLPGPSPDPDSahdgqpQAPGKEQSGTGDRHPEQ 629
Cdd:NF040983 96 PPPPPPPPPTPPPPPPPPPPPPPPSPPPPPPPSPPPSPPPPTTTPPT------RTTPSTTTPTPSMHPIQ 159
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
572-664 |
7.91e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 39.37 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 572 PTPRAPDQPGTRRPV--PPPLAPQ---RPQLPGPSPD-------PDSAHDGQPQAPgkeqsgtgdrHPEQEPSPGTAKEE 639
Cdd:NF033839 339 PKPEVKPQLETPKPEvkPQPEKPKpevKPQPEKPKPEvkpqpetPKPEVKPQPEKP----------KPEVKPQPEKPKPE 408
|
90 100
....*....|....*....|....*.
gi 1622824923 640 RK-EPENARPwGGHPRPTPHAPATLP 664
Cdd:NF033839 409 VKpQPEKPKP-EVKPQPEKPKPEVKP 433
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
560-637 |
8.30e-03 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 39.49 E-value: 8.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622824923 560 PPPTRQAKSSGPPTPRAPDQPGTRRPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQEPSPGTAK 637
Cdd:PRK12270 48 AAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAAAAAAPAAAAVEDEVTPLRGAAA 125
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
560-661 |
8.62e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 39.20 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 560 PPPTRQAKSSGPPTPRAPDQPgtRRPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQEPSPGTAKEE 639
Cdd:PRK07764 624 PAAPAPAGAAAAPAEASAAPA--PGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQP 701
|
90 100
....*....|....*....|..
gi 1622824923 640 RKEPENARPWGGHPRPTPHAPA 661
Cdd:PRK07764 702 APAPAATPPAGQADDPAAQPPQ 723
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
562-665 |
9.02e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 39.09 E-value: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 562 PTRQAKSSGPPTPRApdqpGTRRPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTGDRhpeqEPSPGTAKEERK 641
Cdd:PRK12323 365 PGQSGGGAGPATAAA----APVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPA----RRSPAPEALAAA 436
|
90 100
....*....|....*....|....
gi 1622824923 642 EPENARPWGGHPRPTPhAPATLPA 665
Cdd:PRK12323 437 RQASARGPGGAPAPAP-APAAAPA 459
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
560-665 |
9.08e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 39.38 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 560 PPPTRQAKSSGPPTPRAPDQPGTRRPVPPPLAPQrPQLPGPSPDPDSAHDGQPQAPgkeqsgtgDRHPEQEPSPGTAKEE 639
Cdd:PHA03307 89 TWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPP-PASPPPSPAPDLSEMLRPVGS--------PGPPPAASPPAAGASP 159
|
90 100
....*....|....*....|....*.
gi 1622824923 640 RKEPENARPWGGHPRPTPHAPATLPA 665
Cdd:PHA03307 160 AAVASDAASSRQAALPLSSPEETARA 185
|
|
| PRK14965 |
PRK14965 |
DNA polymerase III subunits gamma and tau; Provisional |
560-607 |
9.52e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237871 [Multi-domain] Cd Length: 576 Bit Score: 38.95 E-value: 9.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1622824923 560 PPPTRQAkssgPPTPRAPDQPGTRRPVPPPLAPQRPQLPGPSPDPDSA 607
Cdd:PRK14965 400 PPPAAAP----PVPPAAPARPAAARPAPAPAPPAAAAPPARSADPAAA 443
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
560-665 |
9.71e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 39.20 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824923 560 PPPTRQAKSSGPPTPRAPDQPGTR---RPVPPPLAPQRPQLPGPSPDPDSAHDGQPQAPGKEQSGTGDRHPEQEPSPGTA 636
Cdd:PRK07764 615 PAAPAAPAAPAAPAPAGAAAAPAEasaAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA 694
|
90 100
....*....|....*....|....*....
gi 1622824923 637 KEERKEPENARPWGGHPRPTPHAPATLPA 665
Cdd:PRK07764 695 GAAPAQPAPAPAATPPAGQADDPAAQPPQ 723
|
|
|