|
Name |
Accession |
Description |
Interval |
E-value |
| CDC_Septin |
cd01850 |
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ... |
295-569 |
6.00e-175 |
|
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.
Pssm-ID: 206649 Cd Length: 275 Bit Score: 495.91 E-value: 6.00e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 295 QGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNEN 374
Cdd:cd01850 1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 375 CWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEER 454
Cdd:cd01850 81 CWKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 455 VHFKQRITADLLSNGIDVYPQKEFDEDSEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 534
Cdd:cd01850 161 TEFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240
|
250 260 270
....*....|....*....|....*....|....*
gi 164698494 535 YLRDLLIRTHMQNIKDITSSIHFEAYRVKRLNEGS 569
Cdd:cd01850 241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
|
|
| Septin |
pfam00735 |
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ... |
296-565 |
5.36e-139 |
|
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this family bind GTP. As regards the septins, these are polypeptides of 30-65kDa with three characteriztic GTPase motifs (G-1, G-3 and G-4) that are similar to those of the Ras family. The G-4 motif is strictly conserved with a unique septin consensus of AKAD. Most septins are thought to have at least one coiled-coil region, which in some cases is necessary for intermolecular interactions that allow septins to polymerize to form rod-shaped complexes. In turn, these are arranged into tandem arrays to form filaments. They are multifunctional proteins, with roles in cytokinesis, sporulation, germ cell development, exocytosis and apoptosis.
Pssm-ID: 395596 Cd Length: 272 Bit Score: 404.37 E-value: 5.36e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 296 GFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNENC 375
Cdd:pfam00735 1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 376 WQPIMKFINDQYEKYLQEEVNINRKKRIpDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEERV 455
Cdd:pfam00735 81 WRPIVEYIDEQYEQYLRDESGLNRKSIK-DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 456 HFKQRITADLLSNGIDVYPQKEFDEDS-EDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 534
Cdd:pfam00735 160 RFKKRIREEIERQNIPIYHFPDEESDEdEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
|
250 260 270
....*....|....*....|....*....|.
gi 164698494 535 YLRDLLIRTHMQNIKDITSSIHFEAYRVKRL 565
Cdd:pfam00735 240 KLRNMLIRTHLQDLKEVTHELHYETYRSEKL 270
|
|
| CDC3 |
COG5019 |
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ... |
277-583 |
2.16e-129 |
|
Septin family protein [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 227352 [Multi-domain] Cd Length: 373 Bit Score: 383.60 E-value: 2.16e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 277 GYVGIDSILEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISR-KSVQPTSEERIPKTIEIKSITHDIEEKGVR 355
Cdd:COG5019 2 GYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDeTEIDDIRAEGTSPTLEIKITKAELEEDGFH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 356 MKLTVIDTPGFGDHINNENCWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSK 435
Cdd:COG5019 82 LNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 436 VVNIVPVIAKADTLTLEERVHFKQRITADLLSNGIDVYPQKEFDEDSEDRL-VNEKFREMIPFAVVGSDHEYQVNGKRIL 514
Cdd:COG5019 162 RVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESLeENQDLRSLIPFAIIGSNTEIENGGEQVR 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164698494 515 GRKTKWGTIEVENTTHCEFAYLRDLLIRTHMQNIKDITSSIHFEAYRVKRLnEGSSAMANGMEEKEPEA 583
Cdd:COG5019 242 GRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKL-SGLKNSGEPSLKEIHEA 309
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
150-278 |
4.86e-08 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 55.89 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 150 TEITIVKPQESAHRRMEPPA-SKVPEVPTAPATDAAPKRVEIQMPKPAEAPTapspAQTLENSEPAPVSQLQSRLEPKPQ 228
Cdd:PHA03269 24 TNIPIPELHTSAATQKPDPApAPHQAASRAPDPAVAPTSAASRKPDLAQAPT----PAASEKFDPAPAPHQAASRAPDPA 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 164698494 229 --PPVAEA-TPRSQEATEAAPSCVGDMADTPRDAGLKQA-PASRNEKAPVDFGY 278
Cdd:PHA03269 100 vaPQLAAApKPDAAEAFTSAAQAHEAPADAGTSAASKKPdPAAHTQHSPPPFAY 153
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
298-365 |
1.31e-06 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 48.52 E-value: 1.31e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164698494 298 EFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIpktieiksITHDIEEKGVRMKLTVIDTPG 365
Cdd:TIGR00231 1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNY--------VTTVIEEDGKTYKFNLLDTAG 60
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
39-247 |
8.85e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.17 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 39 PNSTPPR-RVQTPLLRATVASSTQKFQDLgvkNSEPSArhvdslsqrsPKASLRRVELSGPKAAEPVSRR--TELSIDIS 115
Cdd:PHA03247 2767 PAPAPPAaPAAGPPRRLTRPAVASLSESR---ESLPSP----------WDPADPPAAVLAPAAALPPAASpaGPLPPPTS 2833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 116 SKQVENAGAIGPSRFGLKRAevlGHKTPE-PAPRR--TEITIVKPQESAHrrmePPASKVPEVPTAPATDAAPKRVEIQM 192
Cdd:PHA03247 2834 AQPTAPPPPPGPPPPSLPLG---GSVAPGgDVRRRppSRSPAAKPAAPAR----PPVRRLARPAVSRSTESFALPPDQPE 2906
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 164698494 193 PKPaeAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAeatPRSQEATEAAPS 247
Cdd:PHA03247 2907 RPP--QPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA---PTTDPAGAGEPS 2956
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
10-230 |
7.37e-05 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 45.76 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 10 RTSSGRLRRLGDSSGPALKRSFEVEEVETPNS-------TPPRRVQtpllratvasstqkfqdlgvknSEPSARHVDSLS 82
Cdd:TIGR00927 245 KTTPTPLKGMTDNTPTFLTREVETDLLTSPRSvvekntlTTPRRVE----------------------SNSSTNHWGLVG 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 83 QRSPKASLRRVELSGPKAAEpvsRRTELSIDISSKQVENAGAIGPSRFGlkraevlghktpEPAPrRTEITIVKPQESAH 162
Cdd:TIGR00927 303 KNNLTTPQGTVLEHTPATSE---GQVTISIMTGSSPAETKASTAAWKIR------------NPLS-RTSAPAVRIASATF 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164698494 163 RRMEPPASKVPEVPTAPATDAAP----KRVEIQMPKPAeAPTAPSPAQT--LENSEPAP-VSQL---QSRLEPKPQPP 230
Cdd:TIGR00927 367 RGLEKNPSTAPSTPATPRVRAVLttqvHHCVVVKPAPA-VPTTPSPSLTtaLFPEAPSPsPSALppgQPDLHPKAEYP 443
|
|
| PLN03118 |
PLN03118 |
Rab family protein; Provisional |
299-365 |
8.02e-04 |
|
Rab family protein; Provisional
Pssm-ID: 215587 [Multi-domain] Cd Length: 211 Bit Score: 41.19 E-value: 8.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164698494 299 FNIMVVGQSGLGKSTLINTLFKSKIsrKSVQPTseerIPKTIEIKSITHDieekGVRMKLTVIDTPG 365
Cdd:PLN03118 15 FKILLIGDSGVGKSSLLVSFISSSV--EDLAPT----IGVDFKIKQLTVG----GKRLKLTIWDTAG 71
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
156-238 |
1.91e-03 |
|
pneumococcal surface protein PspC, choline-binding 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 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.15 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 156 KPQESAHRRM--EPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPA--QTLEN------SEPAPVSQLQSrleP 225
Cdd:NF033838 397 KAEEEAKRKAaeEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEKPAdqQAEEDyarrseEEYNRLTQQQP---P 473
|
90
....*....|...
gi 164698494 226 KPQPPVAEATPRS 238
Cdd:NF033838 474 KTEKPAQPSTPKT 486
|
|
| DamX |
COG3266 |
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ... |
13-272 |
2.16e-03 |
|
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442497 [Multi-domain] Cd Length: 455 Bit Score: 40.99 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 13 SGRLRRLGDSSGPALKRSFEVEEVETPNSTPPRRVQTPLLRATVASSTQKFQDLGVKNSEPSARHVDSLSQRSPKASLRR 92
Cdd:COG3266 130 LVLLLLLALLLALLLDLPLLTLLIVLPLLEEQLLLLALQDIQGTLQALGAVAALLGLRKAEEALALRAGSAAADALALLL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 93 VELSGPKAAEPVSRRTELSIDISSKQVENAGAIGPSRFGLKRAEVLghKTPEPAPRRTEITIVKPQESAHRRMEPPASKV 172
Cdd:COG3266 210 LLLASALGEAVAAAAELAALALLAAGAAEVLTARLVLLLLIIGSAL--KAPSQASSASAPATTSLGEQQEVSLPPAVAAQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 173 P--EVPTAPATDAAPkrveiQMPKPAEAPTAPSPAQTLENSEPAPVS-QLQSRLEPKPQPPVAEATPRSQEATEAAPSCV 249
Cdd:COG3266 288 PaaAAAAQPSAVALP-----AAPAAAAAAAAPAEAAAPQPTAAKPVVtETAAPAAPAPEAAAAAAAPAAPAVAKKLAADE 362
|
250 260
....*....|....*....|...
gi 164698494 250 GDMADTPRDAGLKQAPASRNEKA 272
Cdd:COG3266 363 QWLASQPASHYTLQLLGASSEAA 385
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
143-274 |
3.97e-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: 39.75 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 143 PEPAPRRTEITIVKPQESAHRRmepPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSR 222
Cdd:NF040712 205 LAREPADARPEEVEPAPAAEGA---PATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPP 281
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 164698494 223 LEPKPQPPVAEATPRSQEATEAAPSCVGDMADTPRDAGLKQAPASRNEKAPV 274
Cdd:NF040712 282 APGAAETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPPPAPKPKRRRRRASV 333
|
|
| DedD |
COG3147 |
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ... |
168-236 |
4.32e-03 |
|
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442381 [Multi-domain] Cd Length: 140 Bit Score: 37.83 E-value: 4.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164698494 168 PASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQlqsrlePKPQPPVAEATP 236
Cdd:COG3147 1 PAEEAAAAPAAAAAPAAPAAAAAPAPAAAAAAAAPKPAAKPAAPKPAAAAA------AAPAAKAAAPAG 63
|
|
| DUF3729 |
pfam12526 |
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ... |
157-243 |
6.76e-03 |
|
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.
Pssm-ID: 372164 [Multi-domain] Cd Length: 115 Bit Score: 36.59 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 157 PQESAHRRMEPPaskvPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPvsqLQSRLEPKpqPPVAEATP 236
Cdd:pfam12526 31 PPESAHPDPPPP----VGDPRPPVVDTPPPVSAVWVLPPPSEPAAPEPDLVPPVTGPAG---PPSPLAPP--APAQKPPL 101
|
....*..
gi 164698494 237 RSQEATE 243
Cdd:pfam12526 102 PPPRPQR 108
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CDC_Septin |
cd01850 |
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ... |
295-569 |
6.00e-175 |
|
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.
Pssm-ID: 206649 Cd Length: 275 Bit Score: 495.91 E-value: 6.00e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 295 QGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNEN 374
Cdd:cd01850 1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 375 CWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEER 454
Cdd:cd01850 81 CWKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 455 VHFKQRITADLLSNGIDVYPQKEFDEDSEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 534
Cdd:cd01850 161 TEFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240
|
250 260 270
....*....|....*....|....*....|....*
gi 164698494 535 YLRDLLIRTHMQNIKDITSSIHFEAYRVKRLNEGS 569
Cdd:cd01850 241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
|
|
| Septin |
pfam00735 |
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ... |
296-565 |
5.36e-139 |
|
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this family bind GTP. As regards the septins, these are polypeptides of 30-65kDa with three characteriztic GTPase motifs (G-1, G-3 and G-4) that are similar to those of the Ras family. The G-4 motif is strictly conserved with a unique septin consensus of AKAD. Most septins are thought to have at least one coiled-coil region, which in some cases is necessary for intermolecular interactions that allow septins to polymerize to form rod-shaped complexes. In turn, these are arranged into tandem arrays to form filaments. They are multifunctional proteins, with roles in cytokinesis, sporulation, germ cell development, exocytosis and apoptosis.
Pssm-ID: 395596 Cd Length: 272 Bit Score: 404.37 E-value: 5.36e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 296 GFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNENC 375
Cdd:pfam00735 1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 376 WQPIMKFINDQYEKYLQEEVNINRKKRIpDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEERV 455
Cdd:pfam00735 81 WRPIVEYIDEQYEQYLRDESGLNRKSIK-DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 456 HFKQRITADLLSNGIDVYPQKEFDEDS-EDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 534
Cdd:pfam00735 160 RFKKRIREEIERQNIPIYHFPDEESDEdEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
|
250 260 270
....*....|....*....|....*....|.
gi 164698494 535 YLRDLLIRTHMQNIKDITSSIHFEAYRVKRL 565
Cdd:pfam00735 240 KLRNMLIRTHLQDLKEVTHELHYETYRSEKL 270
|
|
| CDC3 |
COG5019 |
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ... |
277-583 |
2.16e-129 |
|
Septin family protein [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 227352 [Multi-domain] Cd Length: 373 Bit Score: 383.60 E-value: 2.16e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 277 GYVGIDSILEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISR-KSVQPTSEERIPKTIEIKSITHDIEEKGVR 355
Cdd:COG5019 2 GYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDeTEIDDIRAEGTSPTLEIKITKAELEEDGFH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 356 MKLTVIDTPGFGDHINNENCWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSK 435
Cdd:COG5019 82 LNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 436 VVNIVPVIAKADTLTLEERVHFKQRITADLLSNGIDVYPQKEFDEDSEDRL-VNEKFREMIPFAVVGSDHEYQVNGKRIL 514
Cdd:COG5019 162 RVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESLeENQDLRSLIPFAIIGSNTEIENGGEQVR 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164698494 515 GRKTKWGTIEVENTTHCEFAYLRDLLIRTHMQNIKDITSSIHFEAYRVKRLnEGSSAMANGMEEKEPEA 583
Cdd:COG5019 242 GRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKL-SGLKNSGEPSLKEIHEA 309
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
249-368 |
2.84e-09 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 58.62 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 249 VGDMADTPRDAGLKQAPASRNEKapvdfgyvgIDSILEQMRRKAMkqgfEFNIMVVGQSGLGKSTLINTLFKSKISRKSV 328
Cdd:COG3596 3 TEVSSLTERLEALKRLPQVLREL---------LAEALERLLVELP----PPVIALVGKTGAGKSSLINALFGAEVAEVGV 69
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 164698494 329 qptseeRIPKTIEIKSITHDIEEKGVrmkLTVIDTPGFGD 368
Cdd:COG3596 70 ------GRPCTREIQRYRLESDGLPG---LVLLDTPGLGE 100
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
303-474 |
3.83e-09 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 55.93 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 303 VVGQSGLGKSTLINTLFKSKISrksvqPTSEERIPkTIEIKSITHDIEEKGVrmKLTVIDTPGFGDhinnencwqpimkf 382
Cdd:cd00882 2 VVGRGGVGKSSLLNALLGGEVG-----EVSDVPGT-TRDPDVYVKELDKGKV--KLVLVDTPGLDE-------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 383 indqyEKYLQEEvninRKKRIPDTRVHCCLYFIPATGH-SLRPLDIEFMKRLSKV-VNIVPVIAKADTLTLEERVHFKQR 460
Cdd:cd00882 60 -----FGGLGRE----ELARLLLRGADLILLVVDSTDReSEEDAKLLILRRLRKEgIPIILVGNKIDLLEEREVEELLRL 130
|
170
....*....|....
gi 164698494 461 ITAdLLSNGIDVYP 474
Cdd:cd00882 131 EEL-AKILGVPVFE 143
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
150-278 |
4.86e-08 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 55.89 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 150 TEITIVKPQESAHRRMEPPA-SKVPEVPTAPATDAAPKRVEIQMPKPAEAPTapspAQTLENSEPAPVSQLQSRLEPKPQ 228
Cdd:PHA03269 24 TNIPIPELHTSAATQKPDPApAPHQAASRAPDPAVAPTSAASRKPDLAQAPT----PAASEKFDPAPAPHQAASRAPDPA 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 164698494 229 --PPVAEA-TPRSQEATEAAPSCVGDMADTPRDAGLKQA-PASRNEKAPVDFGY 278
Cdd:PHA03269 100 vaPQLAAApKPDAAEAFTSAAQAHEAPADAGTSAASKKPdPAAHTQHSPPPFAY 153
|
|
| Toc34_like |
cd01853 |
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ... |
260-414 |
4.89e-08 |
|
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like (Translocon at the Outer-envelope membrane of Chloroplasts) family contains several Toc proteins, including Toc34, Toc33, Toc120, Toc159, Toc86, Toc125, and Toc90. The Toc complex at the outer envelope membrane of chloroplasts is a molecular machine of ~500 kDa that contains a single Toc159 protein, four Toc75 molecules, and four or five copies of Toc34. Toc64 and Toc12 are associated with the translocon, but do not appear to be part of the core complex. The Toc translocon initiates the import of nuclear-encoded preproteins from the cytosol into the organelle. Toc34 and Toc159 are both GTPases, while Toc75 is a beta-barrel integral membrane protein. Toc159 is equally distributed between a soluble cytoplasmic form and a membrane-inserted form, suggesting that assembly of the Toc complex is dynamic. Toc34 and Toc75 act sequentially to mediate docking and insertion of Toc159 resulting in assembly of the functional translocon.
Pssm-ID: 206652 Cd Length: 248 Bit Score: 54.25 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 260 GLKQAPASRNEKApvdfgyvgidsiLEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLF---KSKISRKSVQPTSEERI 336
Cdd:cd01853 5 GFQFFPDATQTKL------------HELEAKLKKELDFSLTILVLGKTGVGKSSTINSIFgerKVSVSAFQSETLRPREV 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164698494 337 PKTIeiksithdieeKGVrmKLTVIDTPGFgdhinNENCWQPIMKFINDQYEKYLqeevninrKKRIPDtrvhCCLYF 414
Cdd:cd01853 73 SRTV-----------DGF--KLNIIDTPGL-----LESQDQRVNRKILSIIKRFL--------KKKTID----VVLYV 120
|
|
| DLP_2 |
cd09912 |
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ... |
299-474 |
5.97e-07 |
|
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
Pssm-ID: 206739 [Multi-domain] Cd Length: 180 Bit Score: 49.85 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 299 FNIMVVGQSGLGKSTLINTLFkskisRKSVQPTSEerIPKTIEIKSITHDIeEKGVrmklTVIDTPGFGDHINNencwqp 378
Cdd:cd09912 1 FLLAVVGEFSAGKSTLLNALL-----GEEVLPTGV--TPTTAVITVLRYGL-LKGV----VLVDTPGLNSTIEH------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 379 imkfindqyekyLQEEVninrKKRIPdtRVHCCLYFIPAtGHSLRPLDIEFMKRLSKVV--NIVPVIAKADTLT---LEE 453
Cdd:cd09912 63 ------------HTEIT----ESFLP--RADAVIFVLSA-DQPLTESEREFLKEILKWSgkKIFFVLNKIDLLSeeeLEE 123
|
170 180
....*....|....*....|...
gi 164698494 454 RVHFKQRITA--DLLSNGIDVYP 474
Cdd:cd09912 124 VLEYSREELGvlELGGGEPRIFP 146
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
141-267 |
8.22e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.25 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 141 KTPEPAPRRTEITIVKPQESAHRRMEPPASKV----PEVPTAPATDAAPKRVeiqmPKPAEAPTAPSPAqtlenSEPAPV 216
Cdd:PHA03247 2706 PTPEPAPHALVSATPLPPGPAAARQASPALPAapapPAVPAGPATPGGPARP----ARPPTTAGPPAPA-----PPAAPA 2776
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 164698494 217 SQLQSRLEPKPQPPVAEATPRSQEATEAAPSCVGDMADTPRDAGlKQAPAS 267
Cdd:PHA03247 2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP-AASPAG 2826
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
300-443 |
9.51e-07 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 47.61 E-value: 9.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 300 NIMVVGQSGLGKSTLINTLF--KSKISRKSvqptseeriPKTIEIksITHDIEEKGVRMKLtvIDTPGFgdhinnencwq 377
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTgaKAIVSDYP---------GTTRDP--NEGRLELKGKQIIL--VDTPGL----------- 56
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164698494 378 pimkfindqYEKYLQEEVNINRKKRIpdTRVHCCLYFIPATgHSLRPLDIEFMKRLSKvvNIVPVI 443
Cdd:pfam01926 57 ---------IEGASEGEGLGRAFLAI--IEADLILFVVDSE-EGITPLDEELLELLRE--NKKPII 108
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
298-365 |
1.31e-06 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 48.52 E-value: 1.31e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164698494 298 EFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIpktieiksITHDIEEKGVRMKLTVIDTPG 365
Cdd:TIGR00231 1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNY--------VTTVIEEDGKTYKFNLLDTAG 60
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
141-251 |
3.40e-06 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 50.10 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 141 KTPEPAPRRTEITIVKPQESAHRRMEPPASKVPEVPTAPATDAAPKRV-----EIQMPKPAEAPTAPSPAQTLENSEPAP 215
Cdd:PRK14951 379 KTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVaapaaAAPAAAPAAAPAAVALAPAPPAQAAPE 458
|
90 100 110
....*....|....*....|....*....|....*..
gi 164698494 216 VSQLQSRLEPKPQPPVAEATPRSQEA-TEAAPSCVGD 251
Cdd:PRK14951 459 TVAIPVRVAPEPAVASAAPAPAAAPAaARLTPTEEGD 495
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
39-247 |
8.85e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.17 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 39 PNSTPPR-RVQTPLLRATVASSTQKFQDLgvkNSEPSArhvdslsqrsPKASLRRVELSGPKAAEPVSRR--TELSIDIS 115
Cdd:PHA03247 2767 PAPAPPAaPAAGPPRRLTRPAVASLSESR---ESLPSP----------WDPADPPAAVLAPAAALPPAASpaGPLPPPTS 2833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 116 SKQVENAGAIGPSRFGLKRAevlGHKTPE-PAPRR--TEITIVKPQESAHrrmePPASKVPEVPTAPATDAAPKRVEIQM 192
Cdd:PHA03247 2834 AQPTAPPPPPGPPPPSLPLG---GSVAPGgDVRRRppSRSPAAKPAAPAR----PPVRRLARPAVSRSTESFALPPDQPE 2906
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 164698494 193 PKPaeAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAeatPRSQEATEAAPS 247
Cdd:PHA03247 2907 RPP--QPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA---PTTDPAGAGEPS 2956
|
|
| GTPase_YqeH |
TIGR03597 |
ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of ... |
280-380 |
8.97e-06 |
|
ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of GTPases involved in ribosome biogenesis. Like YqlF, it shows a cyclical permutation relative to GTPases EngA (in which the GTPase domain is duplicated), Era, and others. Members of this protein family are found in a relatively small number of bacterial species, including Bacillus subtilis but not Escherichia coli. [Protein synthesis, Other]
Pssm-ID: 213834 [Multi-domain] Cd Length: 360 Bit Score: 48.00 E-value: 8.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 280 GIDSILEQMRRKAMKQgfefNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSeeRIPKTieiksiTHDIEEKGVRMKLT 359
Cdd:TIGR03597 140 GIDELLDKIKKARNKK----DVYVVGVTNVGKSSLINKLLKQNNGDKDVITTS--PFPGT------TLDLIEIPLDDGHS 207
|
90 100
....*....|....*....|....*.
gi 164698494 360 VIDTPGFGD-----HINNENCWQPIM 380
Cdd:TIGR03597 208 LYDTPGIINshqmaHYLDKKDLKYIT 233
|
|
| YqeH |
cd01855 |
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ... |
280-366 |
1.32e-05 |
|
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.
Pssm-ID: 206748 [Multi-domain] Cd Length: 191 Bit Score: 46.10 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 280 GIDSILEQMRRKAMKQGfefNIMVVGQSGLGKSTLINTLFKSKisRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLT 359
Cdd:cd01855 110 GVEELIEEIKKLAKYRG---DVYVVGATNVGKSTLINALLKSN--GGKVQAQALVQRLTVSPIPGTTLGLIKIPLGEGKK 184
|
....*..
gi 164698494 360 VIDTPGF 366
Cdd:cd01855 185 LYDTPGI 191
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
297-470 |
1.44e-05 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 45.74 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 297 FEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPtseeripkTIEIKSITHDIEEKGVRMKLTVIDTPGfgdhinnencw 376
Cdd:COG1100 2 GEKKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLS--------TNGVTIDKKELKLDGLDVDLVIWDTPG----------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 377 QPIMKFINDQYEKYLQEevninrkkripdtrVHCCLYFI----PATGHSLrPLDIEFMKRLSKVVNIVPVIAKADtLTLE 452
Cdd:COG1100 63 QDEFRETRQFYARQLTG--------------ASLYLFVVdgtrEETLQSL-YELLESLRRLGKKSPIILVLNKID-LYDE 126
|
170
....*....|....*...
gi 164698494 453 ERVHFKQRITADLLSNGI 470
Cdd:COG1100 127 EEIEDEERLKEALSEDNI 144
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
142-275 |
3.93e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 46.79 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 142 TPEPAPRRTEITivKPQESAHRRMEPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLEnSEPAPVSQLQS 221
Cdd:PRK12323 405 APAAAPAAAAAA--RAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPR-PVAAAAAAAPA 481
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 164698494 222 RLEPKPQP-PVAEATPRSQEATEAAPSCVGDMADtPRDAGLKQAPASRNEKAPVD 275
Cdd:PRK12323 482 RAAPAAAPaPADDDPPPWEELPPEFASPAPAQPD-AAPAGWVAESIPDPATADPD 535
|
|
| AIG1 |
pfam04548 |
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria. |
300-365 |
5.52e-05 |
|
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
Pssm-ID: 398307 [Multi-domain] Cd Length: 200 Bit Score: 44.52 E-value: 5.52e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164698494 300 NIMVVGQSGLGKSTLINTL-----FKSKISRKSVQPTSEE--RIPKTIEIKsithdieekgvrmkltVIDTPG 365
Cdd:pfam04548 2 RIVLVGKTGNGKSATGNSIlgrkaFESKLRAQGVTKTCQLvsRTWDGRIIN----------------VIDTPG 58
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
157-273 |
5.60e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 46.21 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 157 PQESAHRRMEPPASKVPEVpTAPATDAAPKRVEIQMPKPAEAPtapSPAQTLENSEPAPVsqlQSRLEPKPQPPVAEATP 236
Cdd:PRK14959 389 PASGGAATIPTPGTQGPQG-TAPAAGMTPSSAAPATPAPSAAP---SPRVPWDDAPPAPP---RSGIPPRPAPRMPEASP 461
|
90 100 110
....*....|....*....|....*....|....*..
gi 164698494 237 rsqeaTEAAPSCVGDMADTPRDAGLKQAPASRNEKAP 273
Cdd:PRK14959 462 -----VPGAPDSVASASDAPPTLGDPSDTAEHTPSGP 493
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
304-367 |
5.82e-05 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 43.10 E-value: 5.82e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164698494 304 VGQSGLGKSTLINTLFKSKISRKSVqptseeRIPKTIEIKSITHDIEEKGvrmkLTVIDTPGFG 367
Cdd:cd11383 3 MGKTGAGKSSLCNALFGTEVAAVGD------RRPTTRAAQAYVWQTGGDG----LVLLDLPGVG 56
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
118-273 |
5.94e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 46.00 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 118 QVENAGAIGPSRFGLKRAEVLGHKTPEPAPRRTEITIVKPQESAHRRMEPPASKVPEVPTAPATDAAPKRVEIQMPKPAE 197
Cdd:PRK07003 373 PARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAK 452
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164698494 198 APTAPSPAQTLENSEPAPVSQLQSRLEP---KPQPPVAEATPRSQEATEAAPSCVGDmADTPRDAGLKQAPASRNEKAP 273
Cdd:PRK07003 453 ANARASADSRCDERDAQPPADSGSASAPasdAPPDAAFEPAPRAAAPSAATPAAVPD-ARAPAAASREDAPAAAAPPAP 530
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
143-259 |
6.19e-05 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.13 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 143 PEPAPRRteitiVKPQESAHRRMEPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSR 222
Cdd:PRK07764 406 PAAAPAP-----AAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAP 480
|
90 100 110
....*....|....*....|....*....|....*..
gi 164698494 223 LEPKPQPPVAEATPRSQEATEAAPScvGDMADTPRDA 259
Cdd:PRK07764 481 APAPPAAPAPAAAPAAPAAPAAPAG--ADDAATLRER 515
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
7-236 |
6.27e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.47 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 7 GGTRTSSGRLRRLGDSSGPALKRSFEVEEVETPN--STPPRRVQTPLLRATVASSTQkFQDLGVKNSEPSAR-HVDSLSQ 83
Cdd:PHA03247 2641 HPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAqaSSPPQRPRRRAARPTVGSLTS-LADPPPPPPTPEPApHALVSAT 2719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 84 RSPKASLRRVELSGPKAAEPVSRRTElsidisskqvenAGAIGPSRFGLKRAEVLGHKTPEPAPRRTeitivkPQESAHR 163
Cdd:PHA03247 2720 PLPPGPAAARQASPALPAAPAPPAVP------------AGPATPGGPARPARPPTTAGPPAPAPPAA------PAAGPPR 2781
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164698494 164 RMEPP--ASKVPEVPTAPA-TDAAPKRVEIQMPKPAEaPTAPSPAQTLensePAPVSQLQSRlEPKPQPPVAEATP 236
Cdd:PHA03247 2782 RLTRPavASLSESRESLPSpWDPADPPAAVLAPAAAL-PPAASPAGPL----PPPTSAQPTA-PPPPPGPPPPSLP 2851
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
103-269 |
6.51e-05 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 45.69 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 103 PVSRRTELSIDISSKQV---ENAGAIGPSRFGLKRAEVLGHKTP-EPAPRRTEITIVKPQE--SAHRRMEPPASKVPEVP 176
Cdd:PLN03209 312 PLTPMEELLAKIPSQRVppkESDAADGPKPVPTKPVTPEAPSPPiEEEPPQPKAVVPRPLSpyTAYEDLKPPTSPIPTPP 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 177 TAPAtdAAPKRVE-IQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSR----------LEPKPQP-PVAEATPRSQEATEA 244
Cdd:PLN03209 392 SSSP--ASSKSVDaVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRplspyaryedLKPPTSPsPTAPTGVSPSVSSTS 469
|
170 180
....*....|....*....|....*
gi 164698494 245 APSCVGDMAdTPRDAGLKQAPASRN 269
Cdd:PLN03209 470 SVPAVPDTA-PATAATDAAAPPPAN 493
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
10-230 |
7.37e-05 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 45.76 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 10 RTSSGRLRRLGDSSGPALKRSFEVEEVETPNS-------TPPRRVQtpllratvasstqkfqdlgvknSEPSARHVDSLS 82
Cdd:TIGR00927 245 KTTPTPLKGMTDNTPTFLTREVETDLLTSPRSvvekntlTTPRRVE----------------------SNSSTNHWGLVG 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 83 QRSPKASLRRVELSGPKAAEpvsRRTELSIDISSKQVENAGAIGPSRFGlkraevlghktpEPAPrRTEITIVKPQESAH 162
Cdd:TIGR00927 303 KNNLTTPQGTVLEHTPATSE---GQVTISIMTGSSPAETKASTAAWKIR------------NPLS-RTSAPAVRIASATF 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164698494 163 RRMEPPASKVPEVPTAPATDAAP----KRVEIQMPKPAeAPTAPSPAQT--LENSEPAP-VSQL---QSRLEPKPQPP 230
Cdd:TIGR00927 367 RGLEKNPSTAPSTPATPRVRAVLttqvHHCVVVKPAPA-VPTTPSPSLTtaLFPEAPSPsPSALppgQPDLHPKAEYP 443
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
139-284 |
8.38e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 45.64 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 139 GHKTPEPAPRRTEITIVKPQESAHRRMEPPASKVPEVPTAPATDAAPKRVEIQMP-KPAEAPTAPSPAQTLENSEPAPVS 217
Cdd:PRK12323 369 GGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPaRRSPAPEALAAARQASARGPGGAP 448
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164698494 218 QLQSRLEPKPQP--PVAEATPRSQEATEAAPSCVGDMADTPRDAGLKQAPAsrnEKAPVDFGYVGIDSI 284
Cdd:PRK12323 449 APAPAPAAAPAAaaRPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPW---EELPPEFASPAPAQP 514
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
280-366 |
1.11e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 43.54 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 280 GIDSILEQMRRKamkqgfefNIMVVGQSGLGKSTLINTLFKskisrKSVQPTSEERipktieiKSI-------TH----D 348
Cdd:cd01854 75 GLDELRELLKGK--------TSVLVGQSGVGKSTLLNALLP-----ELVLATGEIS-------EKLgrgrhttTHrelfP 134
|
90
....*....|....*...
gi 164698494 349 IEEKGVrmkltVIDTPGF 366
Cdd:cd01854 135 LPGGGL-----IIDTPGF 147
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
146-274 |
1.33e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.16 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 146 APRRTEITIVKPQESAHRRMEPPASKVPEVPTAPATDAAPKRVeiQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEP 225
Cdd:PHA03307 61 ACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPARE--GSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEML 138
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 164698494 226 KPQPPVAEATPRSQEATEAAPSCVGDMADTPRDAGLKQAPASRNEKAPV 274
Cdd:PHA03307 139 RPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPS 187
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
40-253 |
1.43e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.87 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 40 NSTPPRRVQTPLLRATVASStqkfqdlgvknSEPSARHVDSLSQRSPKASLRRVELSGPKAAEPVSRRTELSIDISSKQV 119
Cdd:PRK12323 371 GAGPATAAAAPVAQPAPAAA-----------APAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQA 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 120 ENAGAIGPSRFGLKRAEVlghktPEPAPRRTeitIVKPQESAHRRMEPPASKVPEVPTAPATDAAPKRVEI--QMPKPAE 197
Cdd:PRK12323 440 SARGPGGAPAPAPAPAAA-----PAAAARPA---AAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELppEFASPAP 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 164698494 198 APTAPSPAQTLENSEPAPVSQLQS--RLEPKPQPPVAEATPRSQEATEAAPSCVGDMA 253
Cdd:PRK12323 512 AQPDAAPAGWVAESIPDPATADPDdaFETLAPAPAAAPAPRAAAATEPVVAPRPPRAS 569
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
303-368 |
1.46e-04 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 42.62 E-value: 1.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164698494 303 VVGQSGLGKSTLINTLFKSKISRKSVQP-TSEERIPKTIEIKSIThdieekgvrmKLTVIDTPGFGD 368
Cdd:cd00880 2 IFGRPNVGKSSLLNALLGQNVGIVSPIPgTTRDPVRKEWELLPLG----------PVVLIDTPGLDE 58
|
|
| 3a0901s04IAP86 |
TIGR00993 |
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ... |
297-383 |
1.54e-04 |
|
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K protein originally described is proposed to have three domains. The N-terminal A-domain is acidic, repetitive, weakly conserved, readily removed by proteolysis during chloroplast isolation, and not required for protein translocation. The other domains are designated G (GTPase) and M (membrane anchor); this family includes most of the G domain and all of M. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 273381 [Multi-domain] Cd Length: 763 Bit Score: 44.94 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 297 FEFNIMVVGQSGLGKSTLINTLF-KSKISRKSVQPTSeeripktieiKSIThDIEEKGVRMKLTVIDTPGF----GDHIN 371
Cdd:TIGR00993 117 FSLNILVLGKSGVGKSATINSIFgEVKFSTDAFGMGT----------TSVQ-EIEGLVQGVKIRVIDTPGLkssaSDQSK 185
|
90
....*....|..
gi 164698494 372 NENCWQPIMKFI 383
Cdd:TIGR00993 186 NEKILSSVKKFI 197
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
167-252 |
1.74e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 44.42 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 167 PPASKVPEVPTAPATDAA-PKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAEATPRSQEATEAA 245
Cdd:PRK14950 362 PVPAPQPAKPTAAAPSPVrPTPAPSTRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVDEK 441
|
....*..
gi 164698494 246 PSCVGDM 252
Cdd:PRK14950 442 PKYTPPA 448
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
141-232 |
1.83e-04 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 44.33 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 141 KTPEPAPRRTEITIVKPQ------ESAHRRMEPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTapSPAQTLENSEPA 214
Cdd:PHA03269 52 RAPDPAVAPTSAASRKPDlaqaptPAASEKFDPAPAPHQAASRAPDPAVAPQLAAAPKPDAAEAFT--SAAQAHEAPADA 129
|
90 100
....*....|....*....|...
gi 164698494 215 PVSQLQSRLEP-----KPQPPVA 232
Cdd:PHA03269 130 GTSAASKKPDPaahtqHSPPPFA 152
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
142-268 |
1.88e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 142 TPEPAPRRTEITIvkpQESAHRRMEPPASKVPEVP---------TAPATDAAPKRVEIQMPKPAEAP---------TAPS 203
Cdd:PHA03247 2570 PPRPAPRPSEPAV---TSRARRPDAPPQSARPRAPvddrgdprgPAPPSPLPPDTHAPDPPPPSPSPaanepdphpPPTV 2646
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164698494 204 PAQTLENSEPAPVS-QLQSRLEPKPQPPVAEATPRSQEaTEAAPSCVGDMADTPRDAGLKQAPASR 268
Cdd:PHA03247 2647 PPPERPRDDPAPGRvSRPRRARRLGRAAQASSPPQRPR-RRAARPTVGSLTSLADPPPPPPTPEPA 2711
|
|
| YlqF |
cd01856 |
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ... |
281-365 |
1.97e-04 |
|
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga).
Pssm-ID: 206749 [Multi-domain] Cd Length: 171 Bit Score: 42.52 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 281 IDSILEQMRRKAMKQGF--EFNIMVVGQSGLGKSTLINTLFKSKISRKSVQP--TseeripKTIEIKSITHDIEekgvrm 356
Cdd:cd01856 96 AKKLLKENEKLKAKGLLprPLRAMVVGIPNVGKSTLINRLRGKKVAKVGNKPgvT------RGQQWIRIGPNIE------ 163
|
....*....
gi 164698494 357 kltVIDTPG 365
Cdd:cd01856 164 ---LLDTPG 169
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
143-272 |
2.11e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 44.29 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 143 PEPAPR-RTEITIVKPQESAHRRMEPPAS---KVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTlenSEPAPVSQ 218
Cdd:PHA03378 711 PGRAQRpAAATGRARPPAAAPGRARPPAAapgRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPP---PQAPPAPQ 787
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 164698494 219 LQSRLEPKPQPPVAEATPRSQEATEAAPSCVGDMADTPRD---AGLKQA-PASRNEKA 272
Cdd:PHA03378 788 QRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQlltGGVKRGrPSLKKPAA 845
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
165-251 |
2.24e-04 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 44.50 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 165 MEPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSqlqsrlePKPQPPVAEATPRSQEATEA 244
Cdd:PRK12270 36 YGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAA-------AAAAAAAPAAPPAAAAAAAP 108
|
....*..
gi 164698494 245 APSCVGD 251
Cdd:PRK12270 109 AAAAVED 115
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
96-273 |
2.52e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.10 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 96 SGPKAAEPVSRRTELSIDISSKQVENAGAIGPSRFGLKRAEVLGHKTPEPAPrrtEITIVKPQESAHRrmepPASKVPEV 175
Cdd:PRK12323 379 AAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAP---EALAAARQASARG----PGGAPAPA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 176 PTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPqPPVAEATPRSQEATEAApscvGDMADT 255
Cdd:PRK12323 452 PAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELP-PEFASPAPAQPDAAPAG----WVAESI 526
|
170
....*....|....*...
gi 164698494 256 PRDaGLKQAPASRNEKAP 273
Cdd:PRK12323 527 PDP-ATADPDDAFETLAP 543
|
|
| YihA_EngB |
cd01876 |
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ... |
301-454 |
2.71e-04 |
|
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.
Pssm-ID: 206665 [Multi-domain] Cd Length: 170 Bit Score: 41.73 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 301 IMVVGQSGLGKSTLINTLFKskisRKSVQPTSeeRIP-KTIEIksITHDIEEkgvrmKLTVIDTPGFG----DHINNENc 375
Cdd:cd01876 2 VAFAGRSNVGKSSLINALTN----RKKLARTS--KTPgRTQLI--NFFNVGD-----KFRLVDLPGYGyakvSKEVREK- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 376 WQPIMkfindqyEKYLQEEVNINRkkripdtrvhccLYFIPATGHSLRPLDIEFMKRLSKV-VNIVPVIAKADTLTLEER 454
Cdd:cd01876 68 WGKLI-------EEYLENRENLKG------------VVLLIDARHGPTPIDLEMLEFLEELgIPFLIVLTKADKLKKSEL 128
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
70-268 |
3.12e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 43.71 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 70 NSEPSARHVDSLSQRSPKASLRRVELSGPKAAEPVSRRTELSIDISSKQVENAGAIGPSRFGLKRAEVLGHKTPEPAPRR 149
Cdd:PRK12323 371 GAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAP 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 150 TEITIVKPQESAHRRM---EPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPsPAQTLENSEPAPVsqlQSRLEPK 226
Cdd:PRK12323 451 APAPAAAPAAAARPAAagpRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEF-ASPAPAQPDAAPA---GWVAESI 526
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 164698494 227 PQPPVAEATPRSQEATEAAPSCVgdmADTPRDAGLKQAPASR 268
Cdd:PRK12323 527 PDPATADPDDAFETLAPAPAAAP---APRAAAATEPVVAPRP 565
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
156-274 |
3.15e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 43.55 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 156 KPQeSAHRRMEPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTA--PSPAQTLENSEPAPVSQLQSRLEPKPQPPVAE 233
Cdd:PRK14951 365 KPA-AAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAaaSAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPA 443
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 164698494 234 ATPRSQEATEAAPSCVGDMADT--PRDAGLKQAPASRNEKAPV 274
Cdd:PRK14951 444 AVALAPAPPAQAAPETVAIPVRvaPEPAVASAAPAPAAAPAAA 486
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
293-474 |
3.17e-04 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 41.68 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 293 MKQGFefnIMVVGQSGLGKSTLINTLFKSKISrksvqPTSeeRIPKTieiksiT-HDIeeKGVRMK----LTVIDTPGfg 367
Cdd:cd04163 1 FKSGF---VAIIGRPNVGKSTLLNALVGQKIS-----IVS--PKPQT------TrNRI--RGIYTDddaqIIFVDTPG-- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 368 dhinnencwqpIMKfindqYEKYLQEEVNINRKKRIPDtrVHCCLYFIPATgHSLRPLDIEFMKRLSKV-VNIVPVIAKA 446
Cdd:cd04163 61 -----------IHK-----PKKKLGERMVKAAWSALKD--VDLVLFVVDAS-EWIGEGDEFILELLKKSkTPVILVLNKI 121
|
170 180
....*....|....*....|....*...
gi 164698494 447 DTLTLEERVhFKQRITADLLSNGIDVYP 474
Cdd:cd04163 122 DLVKDKEDL-LPLLEKLKELHPFAEIFP 148
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
157-259 |
4.60e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.05 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 157 PQESAHRRMEPPASKVPEvPTAPATDAAPKRVEIQMPKPAEAP-TAPSPAQTLENSEPAPVSQLQSRLEPKPQP-PVAEA 234
Cdd:PRK07764 394 PAAAAPSAAAAAPAAAPA-PAAAAPAAAAAPAPAAAPQPAPAPaPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPaPAPAA 472
|
90 100
....*....|....*....|....*
gi 164698494 235 TPRSQEATEAAPSCVGDMADTPRDA 259
Cdd:PRK07764 473 APEPTAAPAPAPPAAPAPAAAPAAP 497
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
41-262 |
5.06e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 43.30 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 41 STPPRRVQTPLLRATVASSTQKFQDLGVKNSEPSARhvdslsQRSPKASLRRVELSGPKAAEPVSRRTELSIDISSKQVE 120
Cdd:PRK07003 374 ARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAA------LAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 121 NAGAIGPSRFGLKRAEVLGHKTPEPAPRrteitivkPQESAHRRMEPPASKVPEVPTAPATDAAPKRVeiqmpKPAEAPT 200
Cdd:PRK07003 448 PVPAKANARASADSRCDERDAQPPADSG--------SASAPASDAPPDAAFEPAPRAAAPSAATPAAV-----PDARAPA 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164698494 201 APSpaqtlENSEPAPVSQLQSRLEPkPQPpvAEATPRSQEATEAAPscvgdmADTPRDAGLK 262
Cdd:PRK07003 515 AAS-----REDAPAAAAPPAPEARP-PTP--AAAAPAARAGGAAAA------LDVLRNAGMR 562
|
|
| PRK08691 |
PRK08691 |
DNA polymerase III subunits gamma and tau; Validated |
144-278 |
5.35e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 43.16 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 144 EPAPRRTEITIVKPQESAHRRMEPPASKVPEvptaPATDAAPKRVeiqmpKPAEAptAPSPAQTLENSEPAPVSQLQSRL 223
Cdd:PRK08691 393 KPQPRPEAETAQTPVQTASAAAMPSEGKTAG----PVSNQENNDV-----PPWED--APDEAQTAAGTAQTSAKSIQTAS 461
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 164698494 224 EP-KPQPPVAEATPRSQEATEAAPSCVGDMAD---TPRDAGLKQAPASRNEKAPVDFGY 278
Cdd:PRK08691 462 EAeTPPENQVSKNKAADNETDAPLSEVPSENPiqaTPNDEAVETETFAHEAPAEPFYGY 520
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
143-249 |
5.68e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 143 PEPAPRRTeitiVKPQESAHRRMEPPASKVPEVPTAPATDAAPkRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSR 222
Cdd:PHA03247 2560 PPAAPDRS----VPPPRPAPRPSEPAVTSRARRPDAPPQSARP-RAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPA 2634
|
90 100
....*....|....*....|....*..
gi 164698494 223 LEPKPQPPVAEATPRSQEATEAAPSCV 249
Cdd:PHA03247 2635 ANEPDPHPPPTVPPPERPRDDPAPGRV 2661
|
|
| era |
TIGR00436 |
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ... |
301-495 |
6.32e-04 |
|
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other bacteria. It plays a role in ribosome biogenesis. Few bacteria lack this protein. [Protein synthesis, Other]
Pssm-ID: 129528 [Multi-domain] Cd Length: 270 Bit Score: 41.99 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 301 IMVVGQSGLGKSTLINTLFKSKISRKSvqptseeRIPKTIEIKSITHDIEEKGvrmKLTVIDTPGFGD--HINNENCWQP 378
Cdd:TIGR00436 3 VAILGRPNVGKSTLLNQLHGQKISITS-------PKAQTTRNRISGIHTTGAS---QIIFIDTPGFHEkkHSLNRLMMKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 379 IMK---------FINDQYEKYLQEE--VNINRKKRIPdtrVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPViakaD 447
Cdd:TIGR00436 73 ARSaiggvdlilFVVDSDQWNGDGEfvLTKLQNLKRP---VVLTRNKLDNKFKDKLLPLIDKYAILEDFKDIVPI----S 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 164698494 448 TLTLEERVHFKQRITADlLSNGIDVYPQKEFDEDSEDRLVNEKFREMI 495
Cdd:TIGR00436 146 ALTGDNTSFLAAFIEVH-LPEGPFRYPEDYVTDQPDRFKISEIIREKI 192
|
|
| PLN03118 |
PLN03118 |
Rab family protein; Provisional |
299-365 |
8.02e-04 |
|
Rab family protein; Provisional
Pssm-ID: 215587 [Multi-domain] Cd Length: 211 Bit Score: 41.19 E-value: 8.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164698494 299 FNIMVVGQSGLGKSTLINTLFKSKIsrKSVQPTseerIPKTIEIKSITHDieekGVRMKLTVIDTPG 365
Cdd:PLN03118 15 FKILLIGDSGVGKSSLLVSFISSSV--EDLAPT----IGVDFKIKQLTVG----GKRLKLTIWDTAG 71
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
163-273 |
8.45e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.28 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 163 RRMEPPASKVPEVPTAPATDAAPkrveiqmPKPAEAPtAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAEATPRSQEAT 242
Cdd:PRK07764 383 RRLGVAGGAGAPAAAAPSAAAAA-------PAAAPAP-AAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAP 454
|
90 100 110
....*....|....*....|....*....|.
gi 164698494 243 EAAPSCVGDMADTPRDAGLKQAPASRNEKAP 273
Cdd:PRK07764 455 SPPPAAAPSAQPAPAPAAAPEPTAAPAPAPP 485
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
142-273 |
8.68e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 42.16 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 142 TPEPAPRRTEITIVKPQESAHRRMEPPASKVPEVPTAPATDAAPK-----RVEIQMPKPAEAPTAPSPAQTlenSEPAPV 216
Cdd:PRK07994 376 APAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSqllaaRQQLQRAQGATKAKKSEPAAA---SRARPV 452
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 164698494 217 SQLQSRLEPK-PQPPVAEATPRSQEATEAAPSCVGDMADTPRDAGLKQAPASRNEKAP 273
Cdd:PRK07994 453 NSALERLASVrPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKALEHEKTP 510
|
|
| MJ1464 |
cd01859 |
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ... |
280-365 |
9.04e-04 |
|
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.
Pssm-ID: 206752 [Multi-domain] Cd Length: 157 Bit Score: 39.99 E-value: 9.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 280 GIDSILEQMRRKAMKqGFEFNIMVVGQSGLGKSTLINTLfkskiSRKSVQPTSeeRIPKtieIKSITHDIEEKGVRMKLT 359
Cdd:cd01859 82 GTRILRRTIKELAID-GKPVIVGVVGYPKVGKSSIINAL-----KGRHSASTS--PIPG---SPGYTKGIQLVRIDSKIY 150
|
....*.
gi 164698494 360 VIDTPG 365
Cdd:cd01859 151 LIDTPG 156
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
142-264 |
1.05e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.90 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 142 TPEPAPRRTEITIVKPQESAHRRMEPPASKVPEVPTAPATDAA-----PKRVEIQMPKPAEAPTAPSPAQTLENSEPAPV 216
Cdd:PRK07764 684 APAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQgasapSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPA 763
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 164698494 217 SQlqSRLEPKPQPPVAEATPRSQEATEAAPScvgdMADTPRDAGLKQA 264
Cdd:PRK07764 764 PA--PAAAPAAAPPPSPPSEEEEMAEDDAPS----MDDEDRRDAEEVA 805
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
300-368 |
1.05e-03 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 41.04 E-value: 1.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164698494 300 NIMVVGQSGLGKSTLINT-LFKSK-ISRK-------SVQPTSEERIPKTIEIKSITHDIEEKGVrmKLTVIDTPGFGD 368
Cdd:cd04170 1 NIALVGHSGSGKTTLAEAlLYATGaIDRLgrvedgnTVSDYDPEEKKRKMSIETSVAPLEWNGH--KINLIDTPGYAD 76
|
|
| PHA03291 |
PHA03291 |
envelope glycoprotein I; Provisional |
123-245 |
1.36e-03 |
|
envelope glycoprotein I; Provisional
Pssm-ID: 223033 [Multi-domain] Cd Length: 401 Bit Score: 41.48 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 123 GAIGPSRFGLKRAEVLGHKTPEPAPR--RTEITIVKPQ-ESAHRRMEPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAP 199
Cdd:PHA03291 152 GATNASLFPLGLAAFPAEGTLAAPPLgeGSADGSCDPAlPLSAPRLGPADVFVPATPRPTPRTTASPETTPTPSTTTSPP 231
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 164698494 200 TAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVA--EATPRSQEATEAA 245
Cdd:PHA03291 232 STTIPAPSTTIAAPQAGTTPEAEGTPAPPTPGGgeAPPANATPAPEAS 279
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
121-283 |
1.39e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.70 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 121 NAGAIGPSRFGLKRAEVLGHKTPEPAPRR------TEITIVKPQESAHRRMEPPASKVPE------VPTAPATDAAPKRV 188
Cdd:PHA03307 56 VAGAAACDRFEPPTGPPPGPGTEAPANESrstptwSLSTLAPASPAREGSPTPPGPSSPDpppptpPPASPPPSPAPDLS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 189 EI------------QMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAEATPRSQeATEAAPSC------VG 250
Cdd:PHA03307 136 EMlrpvgspgpppaASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTP-PAAASPRPprrsspIS 214
|
170 180 190
....*....|....*....|....*....|...
gi 164698494 251 DMADTPRDAGLKQAPASRNEKAPVDFGYVGIDS 283
Cdd:PHA03307 215 ASASSPAPAPGRSAADDAGASSSDSSSSESSGC 247
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
280-366 |
1.40e-03 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 40.87 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 280 GIDSILEQMRRKamkqgfefNIMVVGQSGLGKSTLINTLFKskisrKSVQPTSE--ERIPK----TieiksiTH----DI 349
Cdd:COG1162 156 GLDELRELLKGK--------TSVLVGQSGVGKSTLINALLP-----DADLATGEisEKLGRgrhtT------THaelyPL 216
|
90
....*....|....*..
gi 164698494 350 EEKGVrmkltVIDTPGF 366
Cdd:COG1162 217 PGGGW-----LIDTPGF 228
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
303-366 |
1.61e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.83 E-value: 1.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164698494 303 VVGQSGLGKSTLINTLfkskisrksvQPTSEERipktieiksiTHDIEEKGVRMKLT--------------VIDTPGF 366
Cdd:pfam03193 111 LAGQSGVGKSTLLNAL----------LPELDLR----------TGEISEKLGRGRHTtthvelfplpggglLIDTPGF 168
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
154-263 |
1.64e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 41.11 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 154 IVKPQESAHRRMEPPASKVP---EVPTAPATDAAPKRVEiqMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPP 230
Cdd:PRK06995 51 LAPPAAAAPAAAQPPPAAAPaavSRPAAPAAEPAPWLVE--HAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAAENA 128
|
90 100 110
....*....|....*....|....*....|...
gi 164698494 231 VAEATPRSQEATEAAPScvGDMADTPRDAGLKQ 263
Cdd:PRK06995 129 ARRLARAAAAAPRPRVP--ADAAAAVADAVKAR 159
|
|
| PHA03369 |
PHA03369 |
capsid maturational protease; Provisional |
155-254 |
1.65e-03 |
|
capsid maturational protease; Provisional
Pssm-ID: 223061 [Multi-domain] Cd Length: 663 Bit Score: 41.52 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 155 VKPQESAHRRMEPPASKVPEVPTAPATDAAPKRVE-IQMPKPAEAPTAPSPAQTLENSEPAPVSQLQsrlepkPQPPVAE 233
Cdd:PHA03369 354 TAPSRVLAAAAKVAVIAAPQTHTGPADRQRPQRPDgIPYSVPARSPMTAYPPVPQFCGDPGLVSPYN------PQSPGTS 427
|
90 100
....*....|....*....|.
gi 164698494 234 ATPRSQEATEAAPSCVGDMAD 254
Cdd:PHA03369 428 YGPEPVGPVPPQPTNPYVMPI 448
|
|
| AIG1 |
cd01852 |
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ... |
300-368 |
1.68e-03 |
|
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins).
Pssm-ID: 206651 [Multi-domain] Cd Length: 201 Bit Score: 39.83 E-value: 1.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164698494 300 NIMVVGQSGLGKSTLINTL-----FKSKISRKSVqptseeripkTIEIKSITHDIEEKgvrmKLTVIDTPGFGD 368
Cdd:cd01852 2 RLVLVGKTGNGKSATGNTIlgrkvFESKLSASGV----------TKTCQKESAVWDGR----RVNVIDTPGLFD 61
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
142-273 |
1.69e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.51 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 142 TPEPAPRRTEITIVKPQESAHRRMEPPASKVPEVPTAPATDAAPkrveiqmPKPAEAPTAPSPAQTLENSEPAPVSQLQS 221
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAA-------AAPAEASAAPAPGVAAPEHHPKHVAVPDA 662
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 164698494 222 RLEPKPQP-PVAEATPRSQEATEAAPSCVGDMADTPRDAGLKQAPASRNEKAP 273
Cdd:PRK07764 663 SDGGDGWPaKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQAD 715
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
140-327 |
1.79e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.21 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 140 HKTPEPAPRRTEITIVKPQESAHRRMEPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQL 219
Cdd:PHA03378 652 HQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAP 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 220 QSRLEPKPQP---PVAEATPRSQEATEAAPSCVGDMADTPRDAGLKQAPAS--------RNEKAPVDFGYVGIDSILEQM 288
Cdd:PHA03378 732 GRARPPAAAPgraRPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAppapqqrpRGAPTPQPPPQAGPTSMQLMP 811
|
170 180 190
....*....|....*....|....*....|....*....
gi 164698494 289 RRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISRKS 327
Cdd:PHA03378 812 RAAPGQQGPTKQILRQLLTGGVKRGRPSLKKPAALERQA 850
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
156-238 |
1.91e-03 |
|
pneumococcal surface protein PspC, choline-binding 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 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.15 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 156 KPQESAHRRM--EPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPA--QTLEN------SEPAPVSQLQSrleP 225
Cdd:NF033838 397 KAEEEAKRKAaeEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEKPAdqQAEEDyarrseEEYNRLTQQQP---P 473
|
90
....*....|...
gi 164698494 226 KPQPPVAEATPRS 238
Cdd:NF033838 474 KTEKPAQPSTPKT 486
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
283-373 |
2.06e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 40.57 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 283 SILEQMRRKAMKQGFEFNI-MVVGQSGLGKSTLINTLfkskisrksvqptseerIPKtIEIKsiTHDIEEKGVRMKLT-- 359
Cdd:PRK00098 148 SAKEGEGLDELKPLLAGKVtVLAGQSGVGKSTLLNAL-----------------APD-LELK--TGEISEALGRGKHTtt 207
|
90 100 110
....*....|....*....|....*....|
gi 164698494 360 ------------VIDTPGFG----DHINNE 373
Cdd:PRK00098 208 hvelydlpggglLIDTPGFSsfglHDLEAE 237
|
|
| DamX |
COG3266 |
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ... |
13-272 |
2.16e-03 |
|
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442497 [Multi-domain] Cd Length: 455 Bit Score: 40.99 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 13 SGRLRRLGDSSGPALKRSFEVEEVETPNSTPPRRVQTPLLRATVASSTQKFQDLGVKNSEPSARHVDSLSQRSPKASLRR 92
Cdd:COG3266 130 LVLLLLLALLLALLLDLPLLTLLIVLPLLEEQLLLLALQDIQGTLQALGAVAALLGLRKAEEALALRAGSAAADALALLL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 93 VELSGPKAAEPVSRRTELSIDISSKQVENAGAIGPSRFGLKRAEVLghKTPEPAPRRTEITIVKPQESAHRRMEPPASKV 172
Cdd:COG3266 210 LLLASALGEAVAAAAELAALALLAAGAAEVLTARLVLLLLIIGSAL--KAPSQASSASAPATTSLGEQQEVSLPPAVAAQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 173 P--EVPTAPATDAAPkrveiQMPKPAEAPTAPSPAQTLENSEPAPVS-QLQSRLEPKPQPPVAEATPRSQEATEAAPSCV 249
Cdd:COG3266 288 PaaAAAAQPSAVALP-----AAPAAAAAAAAPAEAAAPQPTAAKPVVtETAAPAAPAPEAAAAAAAPAAPAVAKKLAADE 362
|
250 260
....*....|....*....|...
gi 164698494 250 GDMADTPRDAGLKQAPASRNEKA 272
Cdd:COG3266 363 QWLASQPASHYTLQLLGASSEAA 385
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
156-279 |
2.48e-03 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 39.60 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 156 KPQESAHRRMEPPASkvPEVPTAPATDAAPkrvEIQMPKPAEAPTAPSPAQTlENSEPAPVSQLQSRLEPKPQPPVAEAt 235
Cdd:PRK11633 46 KPGDRDEPDMMPAAT--QALPTQPPEGAAE---AVRAGDAAAPSLDPATVAP-PNTPVEPEPAPVEPPKPKPVEKPKPK- 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 164698494 236 PRSQEATEAAPscvgdmadTPRDAglkQAPASRNEKAPVDFGYV 279
Cdd:PRK11633 119 PKPQQKVEAPP--------APKPE---PKPVVEEKAAPTGKAYV 151
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
167-266 |
2.51e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.74 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 167 PPASKVPEVPTAPATDAAPkrveiQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQ-PPVAEATPRSQEATEAA 245
Cdd:PRK07764 399 PSAAAAAPAAAPAPAAAAP-----AAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSpPPAAAPSAQPAPAPAAA 473
|
90 100
....*....|....*....|.
gi 164698494 246 PSCVGDMADTPRDAGLKQAPA 266
Cdd:PRK07764 474 PEPTAAPAPAPPAAPAPAAAP 494
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
166-276 |
3.14e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 40.47 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 166 EPPASKVPEVPTAPATDAAPKRVeiqMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAEAtpRSQEATEAA 245
Cdd:PRK14951 388 APAAAPVAQAAAAPAPAAAPAAA---ASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPA--QAAPETVAI 462
|
90 100 110
....*....|....*....|....*....|....
gi 164698494 246 PSCVG---DMADTPRDAGLKQAPASRNEKAPVDF 276
Cdd:PRK14951 463 PVRVApepAVASAAPAPAAAPAAARLTPTEEGDV 496
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
141-275 |
3.20e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 40.23 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 141 KTPEPAPrrteitiVKPQESAHRRMEPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQLQ 220
Cdd:PRK07994 362 AAPLPEP-------EVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQG 434
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 164698494 221 SRLEPKPQPPVAEATPRSQEATEAAPScVGDMADTPRDAGLKQAPASRNEKAPVD 275
Cdd:PRK07994 435 ATKAKKSEPAAASRARPVNSALERLAS-VRPAPSALEKAPAKKEAYRWKATNPVE 488
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
141-236 |
3.47e-03 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 141 KTPEPA----PRRTEITIVKPQ-----ESAHRRMEPPASKVPEVPTAPATDAAPKRVE-IQMPKPAEAPTAP-SPAQTLE 209
Cdd:PTZ00449 559 KKPGPAkehkPSKIPTLSKKPEfpkdpKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPElLDIPKSPKRPESPkSPKRPPP 638
|
90 100
....*....|....*....|....*...
gi 164698494 210 NSEPAPVSQLQSRLEPK-PQPPVAEATP 236
Cdd:PTZ00449 639 PQRPSSPERPEGPKIIKsPKPPKSPKPP 666
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
37-263 |
3.59e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.69 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 37 ETPNSTPPRRVQTPLLRATVASSTQkfqdlgvknSEPSARHVDSLSQRSPKASLRRVELSGPKAAEPVSRRTELSIDISS 116
Cdd:PHA03247 2818 LPPAASPAGPLPPPTSAQPTAPPPP---------PGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLAR 2888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 117 KQVEnagaigpsrfglKRAEVLGHKTPEPAPRRTEITIVKPQESAHRRMEPPASKVPEVPTAPATDAAPKRVEIQMPKPA 196
Cdd:PHA03247 2889 PAVS------------RSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPS 2956
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 197 EAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAEATPRSQEA---TEAAPSCVGDMADTPRDAGLKQ 263
Cdd:PHA03247 2957 GAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLsrvSSWASSLALHEETDPPPVSLKQ 3026
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
143-274 |
3.97e-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: 39.75 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 143 PEPAPRRTEITIVKPQESAHRRmepPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSR 222
Cdd:NF040712 205 LAREPADARPEEVEPAPAAEGA---PATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPP 281
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 164698494 223 LEPKPQPPVAEATPRSQEATEAAPSCVGDMADTPRDAGLKQAPASRNEKAPV 274
Cdd:NF040712 282 APGAAETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPPPAPKPKRRRRRASV 333
|
|
| DedD |
COG3147 |
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ... |
168-236 |
4.32e-03 |
|
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442381 [Multi-domain] Cd Length: 140 Bit Score: 37.83 E-value: 4.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164698494 168 PASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQlqsrlePKPQPPVAEATP 236
Cdd:COG3147 1 PAEEAAAAPAAAAAPAAPAAAAAPAPAAAAAAAAPKPAAKPAAPKPAAAAA------AAPAAKAAAPAG 63
|
|
| COG5373 |
COG5373 |
Uncharacterized membrane protein [Function unknown]; |
148-215 |
4.48e-03 |
|
Uncharacterized membrane protein [Function unknown];
Pssm-ID: 444140 [Multi-domain] Cd Length: 854 Bit Score: 39.98 E-value: 4.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164698494 148 RRTEITIVKPQESAHRRMEP-PASKVPEVPTAPATDAAPkrVEIQMPKPAEAPTAPSPAQTLENSEPAP 215
Cdd:COG5373 31 EELEAELAEAAEAASAPAEPePEAAAAATAAAPEAAPAP--VPEAPAAPPAAAEAPAPAAAAPPAEAEP 97
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
39-230 |
4.75e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.31 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 39 PNSTPPRRvqtpLLRATVASSTQKFQDL-GVKNSEPSARHVDSLSQRSPKASLRRVELSGPKAAEPVSRRTELSIDISSK 117
Cdd:PHA03247 2775 PAAGPPRR----LTRPAVASLSESRESLpSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSL 2850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 118 QVEnaGAIGP----SRFGLKRAEVLGHKTPEPAPRRTeitIVKPQESahRRMEPPASKVPEVPTAPATDAAPKRVEIQMP 193
Cdd:PHA03247 2851 PLG--GSVAPggdvRRRPPSRSPAAKPAAPARPPVRR---LARPAVS--RSTESFALPPDQPERPPQPQAPPPPQPQPQP 2923
|
170 180 190
....*....|....*....|....*....|....*..
gi 164698494 194 KPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPP 230
Cdd:PHA03247 2924 PPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVP 2960
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
150-267 |
5.40e-03 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 39.15 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 150 TEITIVKPQESAHRRMEPPASKVPEvpTAPATDAAPKRVEIQMPKPAEAPTAP--SPAQTLENSEPA------PVSQLQS 221
Cdd:PRK10905 125 TEPATVAPVRNGNASRQTAKTQTAE--RPATTRPARKQAVIEPKKPQATAKTEpkPVAQTPKRTEPAapvastKAPAATS 202
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 164698494 222 RLEPKPQPPVAEATPRSQEATEAAPSCVGDMADtprDAG-LKQAPAS 267
Cdd:PRK10905 203 TPAPKETATTAPVQTASPAQTTATPAAGGKTAG---NVGsLKSAPSS 246
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
147-273 |
5.40e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 39.92 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 147 PRRTEITIVKPQESAH-RRMEPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEP 225
Cdd:PHA03247 2664 PRRARRLGRAAQASSPpQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPA 2743
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 164698494 226 KPQPPVAEATPRSQE-----ATEAAPSCVGDMADTPRDAGLKQAPASRNEKAP 273
Cdd:PHA03247 2744 VPAGPATPGGPARPArppttAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRE 2796
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
162-278 |
5.41e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 39.85 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 162 HRRMEPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQ--LQSRLEPKPQPPVAEATPRSQ 239
Cdd:PRK07994 360 HPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPetTSQLLAARQQLQRAQGATKAK 439
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 164698494 240 EATEAAPSCVGDMAD-TPRDAGLKQAPASRNEKAPVDFGY 278
Cdd:PRK07994 440 KSEPAAASRARPVNSaLERLASVRPAPSALEKAPAKKEAY 479
|
|
| GTPase_YsxC |
TIGR03598 |
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ... |
304-475 |
5.78e-03 |
|
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]
Pssm-ID: 274670 [Multi-domain] Cd Length: 179 Bit Score: 38.22 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 304 VGQSGLGKSTLINTLFKSK-ISRKSVQPTseeripKTIEIksITHDIEEkgvrmKLTVIDTPGFG-------DHINnenc 375
Cdd:TIGR03598 24 AGRSNVGKSSLINALTNRKkLARTSKTPG------RTQLI--NFFEVND-----GFRLVDLPGYGyakvskeEKEK---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 376 WQPIMkfindqyEKYLQEEVNInrkkripdtrvhCCLYFIPATGHSLRPLDIEFMKRL-SKVVNIVPVIAKADTLTLEER 454
Cdd:TIGR03598 87 WQKLI-------EEYLEKRENL------------KGVVLLMDIRHPLKELDLEMIEWLrERGIPVLIVLTKADKLKKSEL 147
|
170 180
....*....|....*....|.
gi 164698494 455 VHFKQRITADLLSNGIDVYPQ 475
Cdd:TIGR03598 148 NKQLKKIKKALKKDADDPSVQ 168
|
|
| DUF3729 |
pfam12526 |
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ... |
157-243 |
6.76e-03 |
|
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.
Pssm-ID: 372164 [Multi-domain] Cd Length: 115 Bit Score: 36.59 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 157 PQESAHRRMEPPaskvPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPvsqLQSRLEPKpqPPVAEATP 236
Cdd:pfam12526 31 PPESAHPDPPPP----VGDPRPPVVDTPPPVSAVWVLPPPSEPAAPEPDLVPPVTGPAG---PPSPLAPP--APAQKPPL 101
|
....*..
gi 164698494 237 RSQEATE 243
Cdd:pfam12526 102 PPPRPQR 108
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
142-221 |
7.74e-03 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 38.77 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 142 TPEPAPRRTEITIVKPQESAHRRMEPPASKV----PEVPTAPA------TDAAPKRVEIQMPKPAEAPTAPSPAQTLENS 211
Cdd:PRK10905 153 TTRPARKQAVIEPKKPQATAKTEPKPVAQTPkrtePAAPVASTkapaatSTPAPKETATTAPVQTASPAQTTATPAAGGK 232
|
90
....*....|
gi 164698494 212 EPAPVSQLQS 221
Cdd:PRK10905 233 TAGNVGSLKS 242
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
166-266 |
8.39e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 39.20 E-value: 8.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 166 EPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSePAPVSQLQSRLEPKPQPPVAEATPRSQEATEAA 245
Cdd:PRK07764 410 PAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPS-PPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAP 488
|
90 100
....*....|....*....|.
gi 164698494 246 PScvGDMADTPRDAGLKQAPA 266
Cdd:PRK07764 489 AP--AAAPAAPAAPAAPAGAD 507
|
|
| PRK11901 |
PRK11901 |
hypothetical protein; Reviewed |
176-268 |
9.05e-03 |
|
hypothetical protein; Reviewed
Pssm-ID: 237015 [Multi-domain] Cd Length: 327 Bit Score: 38.51 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 176 PTAPATDAAPKrveiQMPKPAEAPTAPSPAQTLENSEPAPVsqlqsrlePKPQPPVA-EATPRSQEATEAAPScvgdmad 254
Cdd:PRK11901 175 PTAPATVAPSK----GAKVPATAETHPTPPQKPATKKPAVN--------HHKTATVAvPPATSGKPKSGAASA------- 235
|
90
....*....|....
gi 164698494 255 tprdAGLKQAPASR 268
Cdd:PRK11901 236 ----RALSSAPASH 245
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
175-290 |
9.51e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 38.79 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 175 VPTAPATDAAPkrveiqMPKPAEAPTAPS-PAQTLENSEPAPVSQLQSRLEPKPQPPVAEATPRSQEATEAAPSCVGDMA 253
Cdd:PRK06995 52 APPAAAAPAAA------QPPPAAAPAAVSrPAAPAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAA 125
|
90 100 110
....*....|....*....|....*....|....*..
gi 164698494 254 DTPRDAGLKQAPASRNEKAPVDFGYVGIDSILEQMRR 290
Cdd:PRK06995 126 ENAARRLARAAAAAPRPRVPADAAAAVADAVKARIER 162
|
|
| PRK12373 |
PRK12373 |
NADH-quinone oxidoreductase subunit E; |
100-260 |
9.94e-03 |
|
NADH-quinone oxidoreductase subunit E;
Pssm-ID: 237082 [Multi-domain] Cd Length: 400 Bit Score: 38.63 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 100 AAEPVSRRTELSIDISSKQVeNAGAigpsrfglKRAEVLGHKTPEPAPRRTEITIVKPQESAHRrmePPASKVPEVPTAP 179
Cdd:PRK12373 187 ASEPAGGLTSLTEEAGKARY-NASK--------ALAEDIGDTVKRIDGTEVPLLAPWQGDAAPV---PPSEAARPKSADA 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698494 180 ATDAAPKrveiqmpKPAEAPTApsPAQTLENSEPAPVSQLqSRLEPKPQPPVAEATPRSQEATEAAPScvgdMADTPRDA 259
Cdd:PRK12373 255 ETNAALK-------TPATAPKA--AAKNAKAPEAQPVSGT-AAAEPAPKEAAKAAAAAAKPALEDKPR----PLGIARPG 320
|
.
gi 164698494 260 G 260
Cdd:PRK12373 321 G 321
|
|
| |
