|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
1-552 |
0e+00 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 863.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 1 MKIKRFVAPDMRTAFRMVREEHGPDAVILSNRRTAEGIEIVAASNYDEELVQRALETARSETSgrahnaVGPNQQAPAPQ 80
Cdd:PRK12727 1 MKIKRFVAPDMRTAFRMVREEHGPDAVILSNRRTAEGIEIVAASNYDEELVQRALETARSDTP------ATAAAPAPAPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 81 APTKPAAPVHAPLKLAANANVSQRQRVANAAEDMIAAMALRQPVNVPRQAPAAAPVRTASIPSPAAQALAHAVAVTTAPR 160
Cdd:PRK12727 75 APTKPAAPVHAPLKLSANANMSQRQRVASAAEDMIAAMALRQPVSVPRQAPAAAPVRAASIPSPAAQALAHAAAVRTAPR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 161 QEHALSAVPEQLFADFLTTAPMQAPVQAPvHAAPVQARTPIMAAALATHASYGQDDDEQDDDGFDMDDA----------- 229
Cdd:PRK12727 155 QEHALSAVPEQLFADFLTTAPVPRAPVQA-PVVAAPAPVPAIAAALAAHAAYAQDDDEQLDDDGFDLDDalpqilppaal 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 230 ---LPPIVVAPAAVAVAAAAPAPQNDEELKQLRGELALMRQMIEREMNRLTDERLRGSPARAQALELMDDYGFDAGLTRD 306
Cdd:PRK12727 234 ppiVVAPAAPAALAAVAAAAPAPQNDEELKQLRGELALMRQMIEREMNRLTDERLRGSPVRAQALELMDDYGFDAGLTRD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 307 VAMQIPADTELHRGRGLMLGLLSKRLPVAPVDPLERGGVIALVGPTGAGKTTTIAKLAQRFAAQHTPRDVALVTTDTQRV 386
Cdd:PRK12727 314 VAMQIPADTELHRGRGLMLGLLSKRLPVAPVDPLERGGVIALVGPTGAGKTTTIAKLAQRFAAQHAPRDVALVTTDTQRV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 387 GGREQLHSYGRQLGVAVHEADSAESLLDLFERLRDYKLVLIDTAGMGQRDRALAAQLNWLRAAQQVTSLLVLPANAHFSD 466
Cdd:PRK12727 394 GGREQLHSYGRQLGIAVHEADSAESLLDLLERLRDYKLVLIDTAGMGQRDRALAAQLNWLRAARQVTSLLVLPANAHFSD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 467 LDEVVRRFAHAKPQGVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVPDDLHRANAASLVLRLEDLRRAADKPCTPE 546
Cdd:PRK12727 474 LDEVVRRFAHAKPQGVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVPDDLHRANAASLVLRLEDLRRAADKPCTPE 553
|
....*.
gi 499727958 547 HNHAVA 552
Cdd:PRK12727 554 HNHAVA 559
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
1-532 |
8.65e-108 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 326.82 E-value: 8.65e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 1 MKIKRFVAPDMRTAFRMVREEHGPDAVILSNRRTAEG-----IEIVAASNYDEElvqraletarsetsgrahnavgpnqq 75
Cdd:COG1419 1 MKIKKFVAKDMREALRKVKEELGPDAVILSTRKVKKGgflkkVEVTAAVDEDEA-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 76 APAPQAPTKPAAPVHAPlklaananvsqrqrvanaaedmiaamalrqpvnvprqapaaapvrtasipspaaqalahavav 155
Cdd:COG1419 55 EKAPAAAAAPAAASAAA--------------------------------------------------------------- 71
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 156 ttaprqehalsavpeqlfadflttapmqapvqapvhaapvqartpimaaalathasygqdddeqdddgfdmddalppivv 235
Cdd:COG1419 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 236 apaavavaaaapapqNDEELKQLRGELALMRQMIEREMNRLTDERLRGSPARAQALELMDDYGFDAGLTRDVAMQIPADT 315
Cdd:COG1419 72 ---------------EEEELEELRRELAELKELLEEQLSGLAGESARLPPELAELLERLLEAGVSPELARELLEKLPEDL 136
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 316 ELHRGRGLMLGLLSKRLPVAPVDPLERGGVIALVGPTGAGKTTTIAKLAQRFAAQHtPRDVALVTTDTQRVGGREQLHSY 395
Cdd:COG1419 137 SAEEAWRALLEALARRLPVAEDPLLDEGGVIALVGPTGVGKTTTIAKLAARFVLRG-KKKVALITTDTYRIGAVEQLKTY 215
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 396 GRQLGVAVHEADSAESLLDLFERLRDYKLVLIDTAGMGQRDRALAAQL-NWLRAAQQVTSLLVLPANAHFSDLDEVVRRF 474
Cdd:COG1419 216 ARILGVPVEVAYDPEELKEALERLRDKDLVLIDTAGRSPRDPELIEELkALLDAGPPIEVYLVLSATTKYEDLKEIVEAF 295
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 499727958 475 AHAKPQGVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVPDDLHRANAASLVLRL 532
Cdd:COG1419 296 SSLGLDGLILTKLDETASLGSILNLLIRTGLPLSYITNGQRVPEDIEVADPERLARLL 353
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
1-534 |
1.01e-99 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 308.36 E-value: 1.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 1 MKIKRFVAPDMRTAFRMVREEHGPDAVILSNRRTAEG-------IEIVAASNYDEElvqraletarsetsgrahnAVGPN 73
Cdd:PRK05703 1 MKIKKFTAKDMREALKQIKEELGADAVILSNKKVRKGgflgkklVEVTAAVDEDET-------------------PKKNP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 74 QQAPAPQAPTKPAAPVHAPLKlAANANVSQRQRVANAAEDMIAAMALRQPVNVPRQAPAAAPvrtasipspaaqalahav 153
Cdd:PRK05703 62 VLREEKRKPAKSILSLQALLE-KRPSRTNSQDALLQAENALPEWKKELEKPSEPKEEEPKAA------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 154 avttaprqehalsavpeqlfadflttapmqapvqapvhaapvqartpimaaalathasygqdddeqdddgfdmddalppi 233
Cdd:PRK05703 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 234 vvapaavavaaaAPAPQNDEELKQLRGELALMRQMIEREMNRLTDErLRGSPARAQALELMDDYGFDAGLTRDVAMQIPA 313
Cdd:PRK05703 123 ------------AESKVVQKELDELRDELKELKNLLEDQLSGLRQV-ERIPPEFAELYKRLKRSGLSPEIAEKLLKLLLE 189
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 314 DTELHRGRGL--MLGLLSKRLPVAPVDPLERGGVIALVGPTGAGKTTTIAKLAQRFAAQHTPRDVALVTTDTQRVGGREQ 391
Cdd:PRK05703 190 HMPPRERTAWryLLELLANMIPVRVEDILKQGGVVALVGPTGVGKTTTLAKLAARYALLYGKKKVALITLDTYRIGAVEQ 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 392 LHSYGRQLGVAVHEADSAESLLDLFERLRDYKLVLIDTAGMGQRDRALAAQLNWL--RAAQQVTSLLVLPANAHFSDLDE 469
Cdd:PRK05703 270 LKTYAKIMGIPVEVVYDPKELAKALEQLRDCDVILIDTAGRSQRDKRLIEELKALieFSGEPIDVYLVLSATTKYEDLKD 349
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499727958 470 VVRRFAHAKPQGVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVPDDLHRANA---ASLVLRLED 534
Cdd:PRK05703 350 IYKHFSRLPLDGLIFTKLDETSSLGSILSLLIESGLPISYLTNGQRVPDDIKVANPeelVRLLLGGFN 417
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
1-531 |
1.32e-90 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 286.48 E-value: 1.32e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 1 MKIKRFVAPDMRTAFRMVREEHGPDAVILSNRRTAEGIEIVAASnyDEELVqraletarsetsgrahnavgpnqqAPAPQ 80
Cdd:PRK06995 1 MNIKKFFGKTSRDALRLVREALGADAVILSNRAVDGGVEIVALA--DSDLA------------------------ALAPP 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 81 APTKPAAPVHAPLKLAANANVSQRQRVANAAEDMIAAMALRQPVNVPRQAPAAAPVRTASIPSPAAQALAHAVAVTTAPR 160
Cdd:PRK06995 55 AAAAPAAAQPPPAAAPAAVSRPAAPAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAAENAARRLAR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 161 QEhalsavpeqlfadfltTAPMQAPVQAPVHAAPVQARTPIMAAALATHasygqdddeqdddgfdmddalppivvapaav 240
Cdd:PRK06995 135 AA----------------AAAPRPRVPADAAAAVADAVKARIERIVNDT------------------------------- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 241 avaaaapapqndeelkqLRGELALMRQMIEREMNRLT-DERLRGSPARAQALELMDDYGFDAGLTRDVAMQIPADTELHR 319
Cdd:PRK06995 168 -----------------VMQELRSLRGMLEEQLASLAwGERQRRDPVRAALLKHLLAAGFSAQLVRMLVDNLPEGDDAEA 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 320 GRGLMLGLLSKRLPVAPV--DPLERGGVIALVGPTGAGKTTTIAKLAQRFAAQHTPRDVALVTTDTQRVGGREQLHSYGR 397
Cdd:PRK06995 231 ALDWVQSALAKNLPVLDSedALLDRGGVFALMGPTGVGKTTTTAKLAARCVMRHGASKVALLTTDSYRIGGHEQLRIYGK 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 398 QLGVAVHEADSAESLLDLFERLRDYKLVLIDTAGMGQRDRALAAQLNWLRAA-QQVTSLLVLPANAHFSDLDEVVRRFAH 476
Cdd:PRK06995 311 ILGVPVHAVKDAADLRLALSELRNKHIVLIDTIGMSQRDRMVSEQIAMLHGAgAPVKRLLLLNATSHGDTLNEVVQAYRG 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 499727958 477 AKPQGVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVPDDLHRANAASLVLR 531
Cdd:PRK06995 391 PGLAGCILTKLDEAASLGGALDVVIRYKLPLHYVSNGQRVPEDLHLANKKFLLHR 445
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
344-532 |
2.83e-85 |
|
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP)-type GTPase that is essential for the placement and assembly of polar flagella. It is similar to the 54 kd subunit (SRP54) of the signal recognition particle (SRP) that mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR).
Pssm-ID: 349782 [Multi-domain] Cd Length: 189 Bit Score: 262.49 E-value: 2.83e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 344 GVIALVGPTGAGKTTTIAKLAQRFAAQHTPRdVALVTTDTQRVGGREQLHSYGRQLGVAVHEADSAESLLDLFERLRDYK 423
Cdd:cd17873 1 RVIALVGPTGVGKTTTLAKLAARYVLKKGKK-VALITTDTYRIGAVEQLKTYAEIMGIPVEVAEDPEDLADALERLSDRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 424 LVLIDTAGMGQRDRALAAQLNWL-RAAQQVTSLLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDETGRFGSALSVVVD 502
Cdd:cd17873 80 LILIDTAGRSPRDKEQLEELKELlGAGEDIEVHLVLSATTKAKDLKEIIERFSPLGYRGLILTKLDETTSLGSVLSVLAE 159
|
170 180 190
....*....|....*....|....*....|
gi 499727958 503 HQMPITWVTDGQRVPDDLHRANAASLVLRL 532
Cdd:cd17873 160 SQLPVSYVTTGQRVPEDIEVASPLRLARLL 189
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
1-431 |
3.04e-66 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 216.43 E-value: 3.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 1 MKIKRFVAPDMRTAFRMVREEHGPDAVILSNRRTAEG------IEIVAASNYDEelvqraletarsetsgrahnavgpnQ 74
Cdd:TIGR03499 1 MKIKKFTAPTMREALKKVKEELGPDAVILSTRKVRKGlfgkkfVEVTAAIDEEE-------------------------A 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 75 QAPAPQAPTKPAAPVHAPLKLAAnanvsqrqrvanaaedmiaamalrqpvnvprqapaaapvrtasipspaaqalahava 154
Cdd:TIGR03499 56 AAASAEEEASKALEQADPKPLSA--------------------------------------------------------- 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 155 vttaprqehalsavpeqlfadflTTAPMQAPVQAPVHAAPVQARTPIMAAAlathasygqdddeqdddgfdmddalppiv 234
Cdd:TIGR03499 79 -----------------------TAEPLELPAPQEEPAAPAAQAAEPLLPE----------------------------- 106
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 235 vapaavavaaaapapqndeelKQLRGELALMRQMIEREMNRLTDERLrgSPARAQALELMDDYGFDAGLTRDVAMQIPAD 314
Cdd:TIGR03499 107 ---------------------EELRKELEALRELLERLLAGLAWLQR--PPERAKLYERLLEAGVSEELARELLEKLPED 163
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 315 TELHRGRGLMLGLLSKRLPVAP--VDPLERGGVIALVGPTGAGKTTTIAKLAQRFAAQHTPRDVALVTTDTQRVGGREQL 392
Cdd:TIGR03499 164 ADAEDAWRWLREALEGMLPVKPeeDPILEQGGVIALVGPTGVGKTTTLAKLAARFALEHGKKKVALITTDTYRIGAVEQL 243
|
410 420 430
....*....|....*....|....*....|....*....
gi 499727958 393 HSYGRQLGVAVHEADSAESLLDLFERLRDYKLVLIDTAG 431
Cdd:TIGR03499 244 KTYAEILGIPVKVARDPKELREALDRLRDKDLILIDTAG 282
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
261-537 |
3.70e-58 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 199.79 E-value: 3.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 261 ELALMRQMIEREMNRL--TDERLRgSPARAQALELMDDYGFDAGLTRDVAMQIPADTELHRGRGLMLGLLSKRLPVAPVD 338
Cdd:PRK14721 107 EIRAMRQMLEEQLTTMgwSNFSQR-DPGGMKVLRTLLSAGFSPLLSRHLLEKLPADRDFEQSLKKTISLLTLNLRTIGGD 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 339 P-LERGGVIALVGPTGAGKTTTIAKLAQRFAAQHTPRDVALVTTDTQRVGGREQLHSYGRQLGVAVHEADSAESLLDLFE 417
Cdd:PRK14721 186 EiIEQGGVYALIGPTGVGKTTTTAKLAARAVIRHGADKVALLTTDSYRIGGHEQLRIYGKLLGVSVRSIKDIADLQLMLH 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 418 RLRDYKLVLIDTAGMGQRDRALAAQLNWL-RAAQQVTSLLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDETGRFGSA 496
Cdd:PRK14721 266 ELRGKHMVLIDTVGMSQRDQMLAEQIAMLsQCGTQVKHLLLLNATSSGDTLDEVISAYQGHGIHGCIITKVDEAASLGIA 345
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 499727958 497 LSVVVDHQMPITWVTDGQRVPDDLHRANAASLVLRLEDLRR 537
Cdd:PRK14721 346 LDAVIRRKLVLHYVTNGQKVPEDLHEANSRYLLHRIFKPSR 386
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
1-539 |
2.93e-57 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 204.26 E-value: 2.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 1 MKIKRFVAPDMRTAFRMVREEHGPDAVILSNRRTAEGIEIVAASNYDEElvqraletarsetsgrahnAVGPNQQAPAPQ 80
Cdd:PRK14723 1 MSVAKFVAASSREAMRQVREALGPDALVLSNRSVAEGVEIVAMLDEDLG-------------------AVAASAQAYAPP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 81 APTKPAAPVHAPlklaananvsqrqrvanaaedmiaamalrqpvnvprqAPAAAPvrtasipspaaqalahavavttapr 160
Cdd:PRK14723 62 APAPLPAALVAP-------------------------------------APAAAS------------------------- 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 161 qehalsavpeqlfadflttAPMQAPVQAPVHAApvqartpimaaalathasygqdddeqdddgfdmddalppivvapaav 240
Cdd:PRK14723 80 -------------------IAAPAAVPAPGAIG----------------------------------------------- 93
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 241 avaaaapapqndeelkQLRGELALMRQMIEREMNRL---TDERLRGSPARAQALELMDDYGFDAGLTRDVAMQIPADTEL 317
Cdd:PRK14723 94 ----------------DLRGELQSMRGMLERQLAGLlwaAGEVAGRDPLRASLFRWLLGAGFSGQLARALLERLPVGYDR 157
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 318 HRGRGLMLGLLSKRLPVA--PVDPLERGGVIALVGPTGAGKTTTIAKLAQRFAAQHTPRDVALVTTDTQRVGGREQLHSY 395
Cdd:PRK14723 158 PAAMAWIRNELATHLPVLrdEDALLAQGGVLALVGPTGVGKTTTTAKLAARCVAREGADQLALLTTDSFRIGALEQLRIY 237
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 396 GRQLGVAVHEADSAESLLDLFERLRDYKLVLIDTAGMGQRDRALAAQLNWLRAAQ-QVTSLLVLPANAHFSDLDEVVRRF 474
Cdd:PRK14723 238 GRILGVPVHAVKDAADLRFALAALGDKHLVLIDTVGMSQRDRNVSEQIAMLCGVGrPVRRLLLLNAASHGDTLNEVVHAY 317
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499727958 475 AHAKPQ---GVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVPDDLHRANAASLVLR-LEDLRRAA 539
Cdd:PRK14723 318 RHGAGEdvdGCIITKLDEATHLGPALDTVIRHRLPVHYVSTGQKVPEHLELAQADELVDRaFATPRRGA 386
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
343-532 |
3.11e-56 |
|
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.
Pssm-ID: 214940 Cd Length: 197 Bit Score: 187.23 E-value: 3.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 343 GGVIALVGPTGAGKTTTIAKLAQRFAAQHTPRdVALVTTDTQRVGGREQLHSYGRQLGVAV-------HEADSAESLLDL 415
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGGKK-VLLVAADTFRAAAVEQLKTYAEILGVVPvaggegaDPVAVAKDAVEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 416 FeRLRDYKLVLIDTAGMGQRDRALAAQLNWLRAAQQVTSLLVLPANAHFSDLDEVVRRFAHA-KPQGVVLTKLDETGRFG 494
Cdd:smart00962 80 A-KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIKPDEVLLVSDATTGQDAVEQAKAFNEAlGLTGIILTKLDGTAKGG 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 499727958 495 SALSVVVDHQMPITWVTDGQRVPdDLHRANAASLVLRL 532
Cdd:smart00962 159 AALSIAAETGLPIKFIGTGEKVP-DLEPFDPERFVSRL 195
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
261-529 |
2.60e-46 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 166.44 E-value: 2.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 261 ELALMRQMIEREMNRLT-DERLRGSPARAQALELMDDYGFDAGLTRDVAMQIPA----DTeLHRGRGLMLGLLSKRLPVA 335
Cdd:PRK14722 49 ELGSLRELMEEQFAGLMwNERQRRNPVHGALTKYLFAAGFSAQLVRMIVDNLPEgegyDT-LDAAADWAQSVLAANLPVL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 336 PVDP--LERGGVIALVGPTGAGKTTTIAKLAQRFAAQHTPRDVALVTTDTQRVGGREQLHSYGRQLGVAVHEADSAESLL 413
Cdd:PRK14722 128 DSEDalMERGGVFALMGPTGVGKTTTTAKLAARCVMRFGASKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDLQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 414 DLFERLRDYKLVLIDTAGMGQRDRALAAQLNWLRAAQQ-VTSLLVLPANAHFSDLDEVVRRFAHAKPQ---------GVV 483
Cdd:PRK14722 208 LALAELRNKHMVLIDTIGMSQRDRTVSDQIAMLHGADTpVQRLLLLNATSHGDTLNEVVQAYRSAAGQpkaalpdlaGCI 287
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499727958 484 LTKLDETGRFGSALSVVVDHQMPITWVTDGQRVPDDLHRANAASLV 529
Cdd:PRK14722 288 LTKLDEASNLGGVLDTVIRYKLPVHYVSTGQKVPENLYVATKKFLL 333
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
345-532 |
1.02e-39 |
|
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.
Pssm-ID: 459814 [Multi-domain] Cd Length: 193 Bit Score: 143.07 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 345 VIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGVAV----HEADSAESLLDLFE--R 418
Cdd:pfam00448 2 VILLVGLQGSGKTTTIAKLAAYLKKKG--KKVLLVAADTFRAAAIEQLKQLAEKLGVPVfgskTGADPAAVAFDAVEkaK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 419 LRDYKLVLIDTAGMGQRDRALAAQL-NWLRAAQQVTSLLVLPANAHFSDLdEVVRRFAHAKP-QGVVLTKLDETGRFGSA 496
Cdd:pfam00448 80 AENYDVVLVDTAGRLQNDKNLMDELkKIKRVVAPDEVLLVLDATTGQNAV-NQAKAFNEAVGiTGVILTKLDGDAKGGAA 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 499727958 497 LSVVVDHQMPITWVTDGQRVpDDLHRANAASLVLRL 532
Cdd:pfam00448 159 LSIVAETGKPIKFIGVGEKI-DDLEPFDPERFVSRL 193
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
345-532 |
9.18e-33 |
|
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349769 [Multi-domain] Cd Length: 193 Bit Score: 124.02 E-value: 9.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 345 VIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGVAVHEADSAESLLDLFE------R 418
Cdd:cd03115 2 VILLVGLQGSGKTTTLAKLARYYQEKG--KKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQeavekaK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 419 LRDYKLVLIDTAGMGQRDRALAAQLNWLRAAQQ-VTSLLVLPANAHFSDLDeVVRRFAHAKP-QGVVLTKLDETGRFGSA 496
Cdd:cd03115 80 LEGYDVLLVDTAGRLQKDEPLMEELKKVKEVESpDEVLLVLDATTGQEALS-QAKAFNEAVGlTGVILTKLDGTAKGGAA 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 499727958 497 LSVVVDHQMPITWVTDGQRvPDDLHRANAASLVLRL 532
Cdd:cd03115 159 LSIVAETKKPIKFIGVGEK-PEDLEPFDPERFVSAL 193
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
345-540 |
5.73e-30 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 121.55 E-value: 5.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 345 VIALVGPTGAGKTTTIAKLAQRFA--AQHTPRDVALVTTDTQRVGGREQLHSYGRQLGVAVHEADSAESLLDLFERLRDY 422
Cdd:PRK12723 176 VFILVGPTGVGKTTTIAKLAAIYGinSDDKSLNIKIITIDNYRIGAKKQIQTYGDIMGIPVKAIESFKDLKEEITQSKDF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 423 KLVLIDTAGMGQRDRALAAQLNWLRAA--QQVTSLLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDETGRFGSALSVV 500
Cdd:PRK12723 256 DLVLVDTIGKSPKDFMKLAEMKELLNAcgRDAEFHLAVSSTTKTSDVKEIFHQFSPFSYKTVIFTKLDETTCVGNLISLI 335
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499727958 501 VDHQMPITWVTDGQRVPDDLHRANAASLVLRLEDLRRAAD 540
Cdd:PRK12723 336 YEMRKEVSYVTDGQIVPHNISIAEPLTFIKKINGYRISDD 375
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
346-528 |
2.46e-26 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 111.70 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 346 IALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLG---VAVHEADSAESLLDLF-ERLR- 420
Cdd:PRK11889 244 IALIGPTGVGKTTTLAKMAWQFHGKK--KTVGFITTDHSRIGTVQQLQDYVKTIGfevIAVRDEAAMTRALTYFkEEARv 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 421 DYklVLIDTAGMGQRDRALAAQLnwLRAAQQVTS---LLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDETGRFGSAL 497
Cdd:PRK11889 322 DY--ILIDTAGKNYRASETVEEM--IETMGQVEPdyiCLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDETASSGELL 397
|
170 180 190
....*....|....*....|....*....|.
gi 499727958 498 SVVVDHQMPITWVTDGQRVPDDLHRANAASL 528
Cdd:PRK11889 398 KIPAVSSAPIVLMTDGQDVKKNIHIATAEHL 428
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
345-532 |
2.47e-26 |
|
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and SRP54; both are GTPases. In E.coli, ftsY is an essential gene located in an operon with cell division genes ftsE and ftsX, but its apparent function is as the signal recognition particle docking protein. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 272883 [Multi-domain] Cd Length: 277 Bit Score: 108.50 E-value: 2.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 345 VIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGVAV----HEADSAESLLDLFE--R 418
Cdd:TIGR00064 79 VILFVGVNGVGKTTTIAKLANKLKKQG--KSVLLAAGDTFRAAAIEQLEEWAKRLGVDVikqkEGADPAAVAFDAIQkaK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 419 LRDYKLVLIDTAGMGQRDRALAAQLNWL-RAAQQVT------SLLVLPANAHFSDLdEVVRRFAHAKP-QGVVLTKLDET 490
Cdd:TIGR00064 157 ARNIDVVLIDTAGRLQNKVNLMDELKKIkRVIKKVDkdapdeVLLVLDATTGQNAL-EQAKVFNEAVGlTGIILTKLDGT 235
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499727958 491 GRFGSALSVVVDHQMPITWVTDGQRVpDDLHRANAASLVLRL 532
Cdd:TIGR00064 236 AKGGIILSIAYELKLPIKFIGVGEKI-DDLAPFDADWFVEAL 276
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
345-520 |
2.77e-24 |
|
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle (SRP) receptor (SR), is homologous to the SRP receptor alpha-subunit (SRalpha) of the eukaryotic SR. It interacts with the signal-recognition particle (SRP) and is required for the co-translational membrane targeting of proteins.
Pssm-ID: 349783 Cd Length: 199 Bit Score: 100.34 E-value: 2.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 345 VIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGVAV--HE--ADSAESLLD--LFER 418
Cdd:cd17874 2 VILFVGVNGVGKTTTIGKLAHYLKNQG--KKVVLAAGDTFRAAAVEQLEEWAERLGVPVisQNegADPAAVAFDaiQAAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 419 LRDYKLVLIDTAGMGQRDRALAAQLNWL-RAAQQVT------SLLVLPANAHfSDLDEVVRRFA-HAKPQGVVLTKLDET 490
Cdd:cd17874 80 ARGIDVVLIDTAGRLHTKKNLMEELKKIkRVIKKKDpeapheVLLVLDATTG-QNALEQAKEFNeAVGLTGIILTKLDGT 158
|
170 180 190
....*....|....*....|....*....|
gi 499727958 491 GRFGSALSVVVDHQMPITWVTDGQRVpDDL 520
Cdd:cd17874 159 AKGGIVLSIADELKIPVKFVGVGEGI-DDL 187
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
346-532 |
5.14e-24 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 101.75 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 346 IALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLG---VAVHEADSAESLLDLFERLRDY 422
Cdd:PRK06731 78 IALIGPTGVGKTTTLAKMAWQFHGKK--KTVGFITTDHSRIGTVQQLQDYVKTIGfevIAVRDEAAMTRALTYFKEEARV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 423 KLVLIDTAGMGQRDRALAAQLnwLRAAQQVTS---LLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDETGRFGSALSV 499
Cdd:PRK06731 156 DYILIDTAGKNYRASETVEEM--IETMGQVEPdyiCLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDETASSGELLKI 233
|
170 180 190
....*....|....*....|....*....|...
gi 499727958 500 VVDHQMPITWVTDGQRVPDDLHRANAASLVLRL 532
Cdd:PRK06731 234 PAVSSAPIVLMTDGQDVKKNIHIATAEHLAKQM 266
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
345-532 |
7.35e-22 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 96.97 E-value: 7.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 345 VIALVGPTGAGKTTTIAKLAQRFaaQHTPRDVALVTTDTQRVGGREQLHSYGRQLGVAV--HE--ADSAESLLDLFE--R 418
Cdd:PRK14974 142 VIVFVGVNGTGKTTTIAKLAYYL--KKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVikHKygADPAAVAYDAIEhaK 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 419 LRDYKLVLIDTAGMGQRDRALAAQlnwLRAAQQVT----SLLVLPANAHfSDLDEVVRRFAHA-KPQGVVLTKLDETGRF 493
Cdd:PRK14974 220 ARGIDVVLIDTAGRMHTDANLMDE---LKKIVRVTkpdlVIFVGDALAG-NDAVEQAREFNEAvGIDGVILTKVDADAKG 295
|
170 180 190
....*....|....*....|....*....|....*....
gi 499727958 494 GSALSVVVDHQMPITWVTDGQRVpDDLHRANAASLVLRL 532
Cdd:PRK14974 296 GAALSIAYVIGKPILFLGVGQGY-DDLIPFDPDWFVDKL 333
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
345-524 |
4.58e-21 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 95.80 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 345 VIALVGPTGAGKTTTIAKLAQRFAAqHTPRDVALVTTDTQRVGGREQLHSYGRQLGVAVHEADSAESLLDLFerLRD-YK 423
Cdd:PRK12724 225 VVFFVGPTGSGKTTSIAKLAAKYFL-HMGKSVSLYTTDNYRIAAIEQLKRYADTMGMPFYPVKDIKKFKETL--ARDgSE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 424 LVLIDTAGMGQRDRALAAQLNWLRAA----QQVTSLLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDETGRFGSALSV 499
Cdd:PRK12724 302 LILIDTAGYSHRNLEQLERMQSFYSCfgekDSVENLLVLSSTSSYHHTLTVLKAYESLNYRRILLTKLDEADFLGSFLEL 381
|
170 180
....*....|....*....|....*
gi 499727958 500 VVDHQMPITWVTDGQRVPDDLHRAN 524
Cdd:PRK12724 382 ADTYSKSFTYLSVGQEVPFDILNAT 406
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
345-518 |
2.01e-20 |
|
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349786 Cd Length: 193 Bit Score: 89.19 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 345 VIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGVAVHEADSAESLLDLFER------ 418
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKG--KKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRalekak 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 419 LRDYKLVLIDTAGMGQRDRALAAQLNWLRAAQQVTS-LLVLPAnAHFSDLDEVVRRFAHA-KPQGVVLTKLDETGRFGSA 496
Cdd:cd18539 80 EEGFDVVIVDTAGRLHIDEELMDELKEIKEVLNPDEvLLVVDA-MTGQDAVNVAKAFNERlGLTGVVLTKLDGDARGGAA 158
|
170 180
....*....|....*....|..
gi 499727958 497 LSVVVDHQMPITWVTDGQRVPD 518
Cdd:cd18539 159 LSIRHVTGKPIKFIGVGEKIED 180
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
345-500 |
9.52e-20 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 91.62 E-value: 9.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 345 VIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGVAVHEADSAESLLDLFE------R 418
Cdd:COG0541 102 VIMMVGLQGSGKTTTAAKLAKYLKKKG--KKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPEEDGKDPVDIAKraleyaK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 419 LRDYKLVLIDTAGMGQRDRALAAQLNWLRAAQQVT-SLLVLPA-------NahfsdldeVVRRFAHAKP-QGVVLTKLDE 489
Cdd:COG0541 180 KNGYDVVIVDTAGRLHIDEELMDELKAIKAAVNPDeTLLVVDAmtgqdavN--------VAKAFNEALGlTGVILTKLDG 251
|
170
....*....|.
gi 499727958 490 TGRFGSALSVV 500
Cdd:COG0541 252 DARGGAALSIR 262
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
324-520 |
5.61e-19 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 87.85 E-value: 5.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 324 MLGLLSKRLPVAPVDPLerggVIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGVAV 403
Cdd:PRK10416 99 ILEPVEKPLNIEEKKPF----VILVVGVNGVGKTTTIGKLAHKYKAQG--KKVLLAAGDTFRAAAIEQLQVWGERVGVPV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 404 ----HEADSAeSLldLFE-----RLRDYKLVLIDTAGmgqRdraLAAQLNwL--------RAAQQV------TSLLVLPA 460
Cdd:PRK10416 173 iaqkEGADPA-SV--AFDaiqaaKARGIDVLIIDTAG---R---LHNKTN-LmeelkkikRVIKKAdpdaphEVLLVLDA 242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499727958 461 ----NAhFSDldevVRRFAHAKP-QGVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVpDDL 520
Cdd:PRK10416 243 ttgqNA-LSQ----AKAFHEAVGlTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGI-DDL 301
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
252-532 |
3.97e-18 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 86.71 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 252 DEELKQLRGELALMRQMI------EREMNRLTDERLRGspaRAQALELMDDYgFDAGltRDVAMQIPAdTELHRGRGLML 325
Cdd:PRK12726 116 EEELSAMRLELAALNRELavkmreEREQNSDFVKFLKG---RGISDTYVADF-MQAG--RKQFKQVET-AHLDDITDWFV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 326 GLLSKRLPVAPVDPLERGGVIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGVAVHE 405
Cdd:PRK12726 189 PYLSGKLAVEDSFDLSNHRIISLIGQTGVGKTTTLVKLGWQLLKQN--RTVGFITTDTFRSGAVEQFQGYADKLDVELIV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 406 ADSAESLLDLFERLRDYKLV---LIDTAGmgqRDRALAAQLNWLRAAQQVT----SLLVLPANAHFSDLDEVVRRFAHAK 478
Cdd:PRK12726 267 ATSPAELEEAVQYMTYVNCVdhiLIDTVG---RNYLAEESVSEISAYTDVVhpdlTCFTFSSGMKSADVMTILPKLAEIP 343
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 499727958 479 PQGVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVPDDLHRANAASLVLRL 532
Cdd:PRK12726 344 IDGFIITKMDETTRIGDLYTVMQETNLPVLYMTDGQNITENIFRPKSRWLAERF 397
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
324-532 |
5.28e-18 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 86.41 E-value: 5.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 324 MLGLLSKRLPVaPVDPLERGgVIALVGPTGAGKTTTIAKLAQRFaaQHTPRDVALVTTDTQRVGGREQLHSYGRQLGVAV 403
Cdd:PRK00771 78 LVKLLGEETEP-LVLPLKPQ-TIMLVGLQGSGKTTTAAKLARYF--KKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 404 H----EADSAESLLDLFERLRDYKLVLIDTAGmgqRDRALAAQLNWLRAAQQVTS----LLVLPA----NAHfsdldEVV 471
Cdd:PRK00771 154 YgdpdNKDAVEIAKEGLEKFKKADVIIVDTAG---RHALEEDLIEEMKEIKEAVKpdevLLVIDAtigqQAK-----NQA 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499727958 472 RRFAHAKP-QGVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVpDDLHRANAASLVLRL 532
Cdd:PRK00771 226 KAFHEAVGiGGIIITKLDGTAKGGGALSAVAETGAPIKFIGTGEKI-DDLERFDPDRFISRL 286
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
345-532 |
6.15e-18 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 84.69 E-value: 6.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 345 VIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGVAV---HE-ADSAeSLldLFE--- 417
Cdd:COG0552 102 VILVVGVNGVGKTTTIGKLAHRLKAEG--KSVLLAAGDTFRAAAIEQLEVWGERVGVPViaqKEgADPA-AV--AFDaiq 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 418 --RLRDYKLVLIDTAGMGQRDRALAAQL-------NWLRAAQQVTSLLVLPA----NAHfsdldEVVRRFAHA-KPQGVV 483
Cdd:COG0552 177 aaKARGADVVIIDTAGRLHNKKNLMEELkkikrviKKLDPDAPHEVLLVLDAttgqNAL-----SQAKVFNEAvGVTGIV 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499727958 484 LTKLDETGRFGSALSVVVDHQMPITWVTDGQRVpDDLHRANAASLVLRL 532
Cdd:COG0552 252 LTKLDGTAKGGVVLAIADELGIPIKFIGVGEGI-DDLRPFDAEEFVDAL 299
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
345-532 |
9.57e-18 |
|
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349784 Cd Length: 193 Bit Score: 81.47 E-value: 9.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 345 VIALVGPTGAGKTTTIAKLAQRFaaQHTPRDVALVTTDTQRVGGREQLHSYGRQLGVAVH----EADSAESLLDLFERLR 420
Cdd:cd17875 2 VIMFVGLQGSGKTTTAAKLAYYY--QKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYgsytEKDPVKIAKEGVEKFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 421 D--YKLVLIDTAGMGQRDRALAAQLNWLRAAQQVTS-LLVLPA----NAHfsdldEVVRRFAHAKPQG-VVLTKLDETGR 492
Cdd:cd17875 80 KekFDIIIVDTSGRHKQEEELFEEMKQISDAVKPDEvILVIDAsigqAAE-----DQAKAFKEAVDIGsVIITKLDGHAK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499727958 493 FGSALSVVVDHQMPITWVTDGQRVpDDLHRANAASLVLRL 532
Cdd:cd17875 155 GGGALSAVAATGAPIIFIGTGEHI-DDLEPFDPKRFVSRL 193
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
345-547 |
2.82e-13 |
|
signal recognition particle protein SRP54; This model represents examples from the eukaryotic cytosol of the signal recognition particle protein component, SRP54. This GTP-binding protein is a component of the eukaryotic signal recognition particle, along with several other protein subunits and a 7S RNA. Some species, including Arabidopsis, have several closely related forms. The extreme C-terminal region is glycine-rich and lower in complexity, poorly conserved between species, and excluded from this model.
Pssm-ID: 273615 [Multi-domain] Cd Length: 428 Bit Score: 71.79 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 345 VIALVGPTGAGKTTTIAKLAQRFaaQHTPRDVALVTTDTQRVGGREQLHSYGRQLGVAVH----EADSAESLLDLFERLR 420
Cdd:TIGR01425 102 VIMFVGLQGAGKTTTCTKLAYYY--KRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYgsyeESDPVKIASEGVEKFR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 421 DYK--LVLIDTAGMGQRDRALAAQLNWLRAAQQVTSLLVLPANAHFSDLDEVVRRFAHAKPQG-VVLTKLDETGRFGSAL 497
Cdd:TIGR01425 180 KEKfdIIIVDTSGRHKQEKELFEEMQQVREAIKPDSIIFVMDGSIGQAAFGQAKAFKDSVEVGsVIITKLDGHAKGGGAL 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499727958 498 SVVVDHQMPITWVTDGQRVpDDLHRANAASLVLRL-------------EDLRRAADKPCTPEH 547
Cdd:TIGR01425 260 SAVAATKSPIIFIGTGEHV-DEFEIFDAEPFVSKLlgmgdlkglidkvQDLALNDEEKTLIEH 321
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
345-529 |
2.12e-11 |
|
C-terminal domain of signal recognition particle receptor alpha subunit; The signal-recognition particle (SRP) receptor (SR) alpha-subunit (SRalpha) of the eukaryotic SR interacts with the signal-recognition particle (SRP) and is essential for the co-translational membrane targeting of proteins.
Pssm-ID: 349785 Cd Length: 204 Bit Score: 63.40 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 345 VIALVGPTGAGKTTTIAKLAQRFAaQHTPRdVALVTTDTQRVGGREQLHSYGRQLGVAVHEA----DSAESLLDLFERLR 420
Cdd:cd17876 2 VIVFCGVNGVGKSTNLAKIAYWLL-SNGFR-VLIAACDTFRSGAVEQLRTHARRLGVELYEKgygkDPAAVAKEAIKYAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 421 D--YKLVLIDTAGMGQRDRALAAQLNWL-RAAQQVTSLLV---LPANAHFSDLDEVVRRFAHAKPQ-------GVVLTKL 487
Cdd:cd17876 80 DqgFDVVLIDTAGRMQNNEPLMRALAKLiKENNPDLVLFVgeaLVGNDAVDQLKKFNQALADYSPSdnprlidGIVLTKF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499727958 488 DETG-RFGSALSVVVDHQMPITWVTDGQRVPdDLHRANAASLV 529
Cdd:cd17876 160 DTIDdKVGAALSMVYATGQPIVFVGTGQTYT-DLKKLNVKAVV 201
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
342-440 |
1.80e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.61 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 342 RGGVIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHsyGRQLGVAVHEADSAESLLDLFERLR- 420
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPG--GGVIYIDGEDILEEVLDQLL--LIIVGGKKASGSGELRLRLALALARk 76
|
90 100
....*....|....*....|.
gi 499727958 421 -DYKLVLIDTAGMGQRDRALA 440
Cdd:smart00382 77 lKPDVLILDEITSLLDAEQEA 97
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
341-447 |
6.96e-08 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 51.19 E-value: 6.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 341 ERGGVIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTdTQRVGGREQLHSYGRQLGVAVHEADSAESLLDLFER-- 418
Cdd:pfam13401 3 FGAGILVLTGESGTGKTTLLRRLLEQLPEVR--DSVVFVDL-PSGTSPKDLLRALLRALGLPLSGRLSKEELLAALQQll 79
|
90 100 110
....*....|....*....|....*....|.
gi 499727958 419 --LRDYKLVLIDTAgmgqrDRALAAQLNWLR 447
Cdd:pfam13401 80 laLAVAVVLIIDEA-----QHLSLEALEELR 105
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
340-507 |
1.65e-07 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 52.23 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 340 LERGGVIALVGPTGAGKTTtiakLAQRFAAQ--HTPRDVALVTTDTqrvgGREQLHSYGRQLG-----------VAVHEA 406
Cdd:COG0467 17 LPRGSSTLLSGPPGTGKTT----LALQFLAEglRRGEKGLYVSFEE----SPEQLLRRAESLGldleeyiesglLRIIDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 407 DSAESLLD---LFERLRDY------KLVLID--------TAGMGQRDRALAAQLNWLRaAQQVTSLLVLPANA-HFSDLD 468
Cdd:COG0467 89 SPEELGLDleeLLARLREAveefgaKRVVIDslsglllaLPDPERLREFLHRLLRYLK-KRGVTTLLTSETGGlEDEATE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499727958 469 EVVRRFAHakpqGVVLTKLDET-GRFGSALSVV----VDHQMPI 507
Cdd:COG0467 168 GGLSYLAD----GVILLRYVELgGELRRALSVLkmrgSAHDRTI 207
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
341-430 |
4.54e-06 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 48.25 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 341 ERGGVIALVGPTGAGKTTTIAKLAQRFaaqhtPRDVALVTTDTQRVGGREQLHSYGRQLGVAVHEADSAESLLDLFERLR 420
Cdd:COG3267 41 QGGGFVVLTGEVGTGKTTLLRRLLERL-----PDDVKVAYIPNPQLSPAELLRAIADELGLEPKGASKADLLRQLQEFLL 115
|
90
....*....|....*.
gi 499727958 421 DYK------LVLIDTA 430
Cdd:COG3267 116 ELAaagrrvVLIIDEA 131
|
|
| MobB |
COG1763 |
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ... |
345-427 |
6.49e-06 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 441369 [Multi-domain] Cd Length: 162 Bit Score: 46.33 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 345 VIALVGPTGAGKTTTIAKLAQRFAAQ--------HTPRDVALVT--TDTQRvggreqlHsygRQLG---VAV-------- 403
Cdd:COG1763 3 VLGIVGYSGSGKTTLLEKLIPELKARglrvgtikHAHHDFDIDTpgKDSYR-------H---REAGadeVLVasperwal 72
|
90 100
....*....|....*....|....*
gi 499727958 404 -HEADSAESLLDLFERLRDYKLVLI 427
Cdd:COG1763 73 mTELPEEPSLDELLARLDDVDLVLV 97
|
|
| CoaA |
COG1072 |
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ... |
259-382 |
8.43e-06 |
|
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 440690 Cd Length: 309 Bit Score: 47.98 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 259 RGELALMRQMIEREMNRLTDERLRGSPARAQALELMDDYgfdAGLTRDVAMQIPADTELHRGRGLMLGLLSKRLPVapvd 338
Cdd:COG1072 15 REEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIY---LPLSRLLNLYVAATQRLHRATSAFLGQADKKTPF---- 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 499727958 339 plerggVIALVGPTGAGKTTTIAKLAQRFAAQHTPRDVALVTTD 382
Cdd:COG1072 88 ------IIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTD 125
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
346-486 |
4.57e-05 |
|
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: 42.99 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 346 IALVGPTGAGKTTTIAKLAQRFAAQHtprDVALVTTDtqrvggreqlhsygRQLGVAvheadsaeslldlfeRLRDYKLV 425
Cdd:pfam01926 2 VALVGRPNVGKSTLINALTGAKAIVS---DYPGTTRD--------------PNEGRL---------------ELKGKQII 49
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499727958 426 LIDTAGM---GQRDRALAAQLNWLRAAQQVtsLLVLPANAHFSDLDEVVRRFAHA--KPQGVVLTK 486
Cdd:pfam01926 50 LVDTPGLiegASEGEGLGRAFLAIIEADLI--LFVVDSEEGITPLDEELLELLREnkKPIILVLNK 113
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
250-438 |
4.83e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 250 QNDEELKQLRGELALMRQMIEREMNRLTD----ERLRGSPARAQALELMDDYGFDAGLT------RDVAMQIPADTElhr 319
Cdd:TIGR00956 698 QKGEILVFRRGSLKRAKKAGETSASNKNDieagEVLGSTDLTDESDDVNDEKDMEKESGedifhwRNLTYEVKIKKE--- 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 320 grglmlgllsKRLPVAPVDPLERGGVI-ALVGPTGAGKTTTIAKLAQRfaaqhtpRDVALVTTDTQRVGGREQLHSYGRQ 398
Cdd:TIGR00956 775 ----------KRVILNNVDGWVKPGTLtALMGASGAGKTTLLNVLAER-------VTTGVITGGDRLVNGRPLDSSFQRS 837
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499727958 399 LG-----------VAVHEA-------------------DSAESLLDLFErLRDYKLVLIDTAGMG----QRDRA 438
Cdd:TIGR00956 838 IGyvqqqdlhlptSTVRESlrfsaylrqpksvsksekmEYVEEVIKLLE-MESYADAVVGVPGEGlnveQRKRL 910
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
340-367 |
8.76e-05 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 43.14 E-value: 8.76e-05
10 20
....*....|....*....|....*...
gi 499727958 340 LERGGVIALVGPTGAGKtTTIAKLAQRF 367
Cdd:cd03228 25 IKPGEKVAIVGPSGSGK-STLLKLLLRL 51
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
340-367 |
1.19e-04 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 44.77 E-value: 1.19e-04
10 20
....*....|....*....|....*...
gi 499727958 340 LERGGVIALVGPTGAGKtTTIAKLAQRF 367
Cdd:COG1132 363 IPPGETVALVGPSGSGK-STLVNLLLRF 389
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
340-443 |
1.29e-04 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 43.69 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 340 LERGGVIALVGPTGAGKTTTIAKLA------------QRFAAQHTP----RDVALVTTDT---QRVGGREQLHSYGRQLG 400
Cdd:COG4555 24 AKDGEITGLLGPNGAGKTTLLRMLAgllkpdsgsiliDGEDVRKEPrearRQIGVLPDERglyDRLTVRENIRYFAELYG 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 499727958 401 VAVHEADS-AESLLDLFErLRDYKLVLIDTAGMGQRDR-ALAAQL 443
Cdd:COG4555 104 LFDEELKKrIEELIELLG-LEEFLDRRVGELSTGMKKKvALARAL 147
|
|
| mobB |
TIGR00176 |
molybdopterin-guanine dinucleotide biosynthesis protein MobB; This molybdenum cofactor ... |
345-427 |
2.72e-04 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobB; This molybdenum cofactor biosynthesis enzyme is similar to the urease accessory protein UreG and to the hydrogenase accessory protein HypB, both GTP hydrolases involved in loading nickel into the metallocenters of their respective target enzymes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]
Pssm-ID: 272943 [Multi-domain] Cd Length: 155 Bit Score: 41.59 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 345 VIALVGPTGAGKTTTIAKLAQRFAAQ----------HTPRDVALVTTDTQRV--GGREQLHSYGRQLGVAVHEADSAESL 412
Cdd:TIGR00176 1 VLQIVGPKNSGKTTLIERLVKALKARgyrvatikhdHHDFDIDKNGKDSYRHreAGADQVIVASSRRYAFMHETQEERDL 80
|
90
....*....|....*
gi 499727958 413 LDLFERLRDYKLVLI 427
Cdd:TIGR00176 81 EALLDRLPDLDIILV 95
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
346-488 |
3.23e-04 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 41.89 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 346 IALVGPTGAGKTTtiakLAQRFAAQHTPRDVALVTtdtqrvggreqlhsygrqLGVAVHEADsaeslLDLFErlRDYKLV 425
Cdd:COG1100 6 IVVVGTGGVGKTS----LVNRLVGDIFSLEKYLST------------------NGVTIDKKE-----LKLDG--LDVDLV 56
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499727958 426 LIDTAgmGQRDRALAAQL--NWLRAAqqvtSLLVL-------PANAHFSDLDEVVRRFAHAKPQGVVLTKLD 488
Cdd:COG1100 57 IWDTP--GQDEFRETRQFyaRQLTGA----SLYLFvvdgtreETLQSLYELLESLRRLGKKSPIILVLNKID 122
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
47-211 |
4.26e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 43.49 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 47 DEELVQRALETARSETSGRAHNAVGPNQQAPAPQAPTKPAAPVHAPLKLAANANVSQRQRVANAAEDMIAAMALRQPvNV 126
Cdd:PRK10811 852 DVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQP-QV 930
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 127 PRQAPAAAPVRTASIPSPAAQALAHAVAVTTAPRQEHALSAVPEQLFADFL--TTAPMQAPVQAPVHAAPVQARTPIMAA 204
Cdd:PRK10811 931 ITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPAApvVAEVAAEVETVTAVEPEVAPAQVPEAT 1010
|
....*..
gi 499727958 205 ALATHAS 211
Cdd:PRK10811 1011 VEHNHAT 1017
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
340-360 |
4.45e-04 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 41.23 E-value: 4.45e-04
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
345-382 |
5.18e-04 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 41.36 E-value: 5.18e-04
10 20 30
....*....|....*....|....*....|....*...
gi 499727958 345 VIALVGPTGAGKTTTIAKLAQRFAAQHtprdVALVTTD 382
Cdd:COG0572 9 IIGIAGPSGSGKTTFARRLAEQLGADK----VVVISLD 42
|
|
| ComEC |
COG2333 |
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ... |
425-534 |
5.47e-04 |
|
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 441904 [Multi-domain] Cd Length: 253 Bit Score: 41.77 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 425 VLIDTAGMGQRDRALAAQLNWLRAaQQVTSL--LVL--PANAHFSDLDEVVRRFahakPQGVVLT--KLDETGRFGSALS 498
Cdd:COG2333 24 ILIDTGPRPSFDAGERVVLPYLRA-LGIRRLdlLVLthPDADHIGGLAAVLEAF----PVGRVLVsgPPDTSETYERLLE 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 499727958 499 VVVDHQMPITWVTDGQRVPDD------LH---------RANAASLVLRLED 534
Cdd:COG2333 99 ALKEKGIPVRPCRAGDTWQLGgvrfevLWppedllegsDENNNSLVLRLTY 149
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
347-488 |
6.83e-04 |
|
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: 40.52 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 347 ALVGPTGAGKTTTIAKLAQRFAAQhtPRDVALVTTDTQRvgGREQLHSYGrqlgvavheadsaeslldlferlrdYKLVL 426
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGE--VSDVPGTTRDPDV--YVKELDKGK-------------------------VKLVL 51
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499727958 427 IDTAGMGQRDRALAAQLNWlRAAQQVTS-LLVLPANAHFSDLDE----VVRRFAHAKPQGVVLTKLD 488
Cdd:cd00882 52 VDTPGLDEFGGLGREELAR-LLLRGADLiLLVVDSTDRESEEDAklliLRRLRKEGIPIILVGNKID 117
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
340-367 |
9.07e-04 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 41.06 E-value: 9.07e-04
10 20
....*....|....*....|....*...
gi 499727958 340 LERGGVIALVGPTGAGKtTTIAKLAQRF 367
Cdd:cd03254 26 IKPGETVAIVGPTGAGK-TTLINLLMRF 52
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
330-442 |
1.30e-03 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 40.43 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 330 KRLPVAPVDPL----ERGGVIALVGPTGAGKTTTIAKLA------------QRFAAQHTPRDV----ALVTTDT---QRV 386
Cdd:cd03266 14 VKKTVQAVDGVsftvKPGEVTGLLGPNGAGKTTTLRMLAgllepdagfatvDGFDVVKEPAEArrrlGFVSDSTglyDRL 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 499727958 387 GGREQLHSYGRQLGVAVHEADSAesLLDLFERLRDYKLVLIDTAGM--GQRDRALAAQ 442
Cdd:cd03266 94 TARENLEYFAGLYGLKGDELTAR--LEELADRLGMEELLDRRVGGFstGMRQKVAIAR 149
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
345-486 |
1.52e-03 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 38.18 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 345 VIALVGPT-GAGKTTTIAKLAQRFAAQHtpRDVALVTTDtqrvggreqlhsygrqlgvavheadsaeslldlferlrdyK 423
Cdd:cd01983 2 VIAVTGGKgGVGKTTLAAALAVALAAKG--YKVLLIDLD----------------------------------------D 39
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 424 LVLIDTAGMGQRDRALAAQLNWLRAaqQVTSLLVLPANAHFSDLDEVVRRFAHA-------KPQGVVLTK 486
Cdd:cd01983 40 YVLIDGGGGLETGLLLGTIVALLAL--KKADEVIVVVDPELGSLLEAVKLLLALlllgigiRPDGIVLNK 107
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
340-447 |
1.57e-03 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 39.17 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 340 LERGGVIALVGPTGAGKTTtiakLAQRFAAQHTPrDVALVTTDTQRVGGREqLHSYGRQLGVaVHEADSAESLLDLFERL 419
Cdd:pfam00005 8 LNPGEILALVGPNGAGKST----LLKLIAGLLSP-TEGTILLDGQDLTDDE-RKSLRKEIGY-VFQDPQLFPRLTVRENL 80
|
90 100
....*....|....*....|....*...
gi 499727958 420 RdYKLVLIDTAGMGQRDRALAAqLNWLR 447
Cdd:pfam00005 81 R-LGLLLKGLSKREKDARAEEA-LEKLG 106
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
340-435 |
1.83e-03 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 40.05 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 340 LERGGVIALVGPTGAGKTTTI-------------AKLAQRFAAQHTP---RDVALVttdTQRVG------GREQLHSYGR 397
Cdd:COG1131 23 VEPGEIFGLLGPNGAGKTTTIrmllgllrptsgeVRVLGEDVARDPAevrRRIGYV---PQEPAlypdltVRENLRFFAR 99
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 499727958 398 QLGVAVHEADS-AESLLDLFErLRDYKLVLIDT--AGMGQR 435
Cdd:COG1131 100 LYGLPRKEARErIDELLELFG-LTDAADRKVGTlsGGMKQR 139
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
340-476 |
2.37e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 38.77 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 340 LERGGVIALVGPTGAGKTT---TIAKLAQRFA--AQHTPRDVALVTTDTQR--VGGREQLhSYG-RQLgVAVheadsAES 411
Cdd:cd00267 22 LKAGEIVALVGPNGSGKSTllrAIAGLLKPTSgeILIDGKDIAKLPLEELRrrIGYVPQL-SGGqRQR-VAL-----ARA 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499727958 412 LldlferLRDYKLVLID--TAGMGQRDRA-LAAQLNWLrAAQQVTSLLVLPanaHFSDLDEVVRRFAH 476
Cdd:cd00267 95 L------LLNPDLLLLDepTSGLDPASRErLLELLREL-AEEGRTVIIVTH---DPELAELAADRVIV 152
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
343-367 |
4.06e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 39.94 E-value: 4.06e-03
10 20
....*....|....*....|....*
gi 499727958 343 GGVIALVGPTGAGKTTTIAkLAQRF 367
Cdd:PRK13657 361 GQTVAIVGPTGAGKSTLIN-LLQRV 384
|
|
| MobB |
cd03116 |
molybdopterin-guanine dinucleotide biosynthesis protein B; Molybdenum is an essential trace ... |
345-427 |
4.35e-03 |
|
molybdopterin-guanine dinucleotide biosynthesis protein B; Molybdenum is an essential trace element in the form of molybdenum cofactor (Moco) which is associated with the metabolism of nitrogen, carbon and sulfur by redox active enzymes. In Escherichia coli, the synthesis of Moco involves genes from several loci: moa, mob, mod, moe and mog. The mob locus contains mobA and mobB genes. MobB catalyzes the attachment of the guanine dinucleotide to molybdopterin.
Pssm-ID: 349770 [Multi-domain] Cd Length: 157 Bit Score: 38.00 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 345 VIALVGPTGAGKTTTIAKLAQRFAAQ--------HTPRDVALVT--TDT---QRVGGREQLHSYGRQLGVAVHEADSAES 411
Cdd:cd03116 2 IVGVVGKSGSGKTTLIEKLIPELKARglrvavikHTHHGFDIDTpgKDSyrhRQAGADAVLVSSPNRLALIHERPEWELT 81
|
90
....*....|....*.
gi 499727958 412 LLDLFERLRDYKLVLI 427
Cdd:cd03116 82 LLELLARFSDVDLVLV 97
|
|
| Kti12 |
COG4088 |
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ... |
340-382 |
4.40e-03 |
|
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];
Pssm-ID: 443264 [Multi-domain] Cd Length: 179 Bit Score: 38.55 E-value: 4.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 499727958 340 LERGGVIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTD 382
Cdd:COG4088 1 MDSPMLLILTGPPGSGKTTFAKALAQRLYAEG--IAVALLHSD 41
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
341-367 |
4.64e-03 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 38.75 E-value: 4.64e-03
10 20
....*....|....*....|....*..
gi 499727958 341 ERGGVIALVGPTGAGKtTTIAKLAQRF 367
Cdd:cd03251 26 PAGETVALVGPSGSGK-STLVNLIPRF 51
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
69-210 |
5.76e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 39.47 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 69 AVGPNQQAPAPQAPTKPAAPVHAPLKLAANANVSQRQRVANAAEDMIAAMALRQPVNVPRQAPAAAPVRTASIPSPAAQA 148
Cdd:PRK12323 402 PPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPA 481
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499727958 149 LAHAVAVTTAprqehALSAVP--EQLFADFLTTAPMQapvQAPVHAAPVQARTPIMAAALATHA 210
Cdd:PRK12323 482 RAAPAAAPAP-----ADDDPPpwEELPPEFASPAPAQ---PDAAPAGWVAESIPDPATADPDDA 537
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
342-435 |
6.19e-03 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 38.50 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 342 RGGVIALVGPTGAGKTTTIAKLA--------QRFAAQHT----PRDV----ALVTTDT---QRVGGREQLHSYGRQLGVA 402
Cdd:cd03265 25 RGEIFGLLGPNGAGKTTTIKMLTtllkptsgRATVAGHDvvrePREVrrriGIVFQDLsvdDELTGWENLYIHARLYGVP 104
|
90 100 110
....*....|....*....|....*....|....*.
gi 499727958 403 VHEADS-AESLLDLFERL--RDyKLVLIDTAGMGQR 435
Cdd:cd03265 105 GAERRErIDELLDFVGLLeaAD-RLVKTYSGGMRRR 139
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
303-509 |
6.71e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 39.16 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 303 LTRDVAMQIP-ADTELHRGRGLMLGLLSKRLPVApVDPLERGGV--IALVGPTGAGKTTTIAKLAQRFAAQHTprDVALV 379
Cdd:COG3451 162 TTSNLAALFPfHSFELGDPWGIYLLNTRSGTPVF-FDFHDGLDNgnTLILGPSGSGKSFLLKLLLLQLLRYGA--RIVIF 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 380 TTD------TQRVGGREQLHSYGRQLGVA----VHEADSAESLLDLFERlrdykLVLIDTAGMGQRDRALaaqlnWLRAA 449
Cdd:COG3451 239 DPGgsyeilVRALGGTYIDLSPGSPTGLNpfdlEDTEEKRDFLLELLEL-----LLGREGEPLTPEERAA-----IDRAV 308
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 450 QQVTSLLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDETGRFGSALsvvvDHQMPITW 509
Cdd:COG3451 309 RALYRRADPEERTTLSDLYELLKEQPEAKDLAARLEPYTKGGSYGWLF----DGPTNLDL 364
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
341-435 |
8.36e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 38.55 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499727958 341 ERGGVIALVGPTGAGKTTTIAKLAQRFAA-------QHTPRDVAlvttDTQRVGG-------------REQLHSYGRQLG 400
Cdd:COG4152 25 PKGEIFGLLGPNGAGKTTTIRIILGILAPdsgevlwDGEPLDPE----DRRRIGYlpeerglypkmkvGEQLVYLARLKG 100
|
90 100 110
....*....|....*....|....*....|....*....
gi 499727958 401 VAVHEADsaESLLDLFERLR--DYKLVLIDT--AGMGQR 435
Cdd:COG4152 101 LSKAEAK--RRADEWLERLGlgDRANKKVEElsKGNQQK 137
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
343-401 |
9.39e-03 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 37.98 E-value: 9.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499727958 343 GGVIALVGPTGAGKtTTIAKLAQRFAaqhtprDVA--LVTTDTQRVggRE-QLHSYGRQLGV 401
Cdd:cd03253 27 GKKVAIVGPSGSGK-STILRLLFRFY------DVSsgSILIDGQDI--REvTLDSLRRAIGV 79
|
|
| |
