|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
1-561 |
0e+00 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 862.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 1 MKIKRFVAPDMRTAFRMVREEHGPDAVILSNRRTAEGIEIVAASNYDEELVQRALETARSETSAAAHNAAAPIQQApapq 80
Cdd:PRK12727 1 MKIKRFVAPDMRTAFRMVREEHGPDAVILSNRRTAEGIEIVAASNYDEELVQRALETARSDTPATAAAPAPAPQAP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 81 apTKPAAPVHAPLKLAANANVSQRQRVANAAEDMIAAMALRQPVNVPRQAPAAAPVRTASIPSPAAQALAHAVAVTTAPR 160
Cdd:PRK12727 77 --TKPAAPVHAPLKLSANANMSQRQRVASAAEDMIAAMALRQPVSVPRQAPAAAPVRAASIPSPAAQALAHAAAVRTAPR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 161 QEHALSAVPEQLFADFLTTAPMQAPVQAPvHAAPVQACTPIMAAALATHASYG-QDDDEQDDDGFDMDDALPQILPPAAL 239
Cdd:PRK12727 155 QEHALSAVPEQLFADFLTTAPVPRAPVQA-PVVAAPAPVPAIAAALAAHAAYAqDDDEQLDDDGFDLDDALPQILPPAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 240 ----PPIVVAPAAVAVAAAAPAPQNDEELKQLRGELALMRQMIEREMNRLTDERLRGSPARAQALELMDDYGFDAGLTRD 315
Cdd:PRK12727 234 ppivVAPAAPAALAAVAAAAPAPQNDEELKQLRGELALMRQMIEREMNRLTDERLRGSPVRAQALELMDDYGFDAGLTRD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 316 VAMQIPADTELHRGRGLMLGLLSKRLPVAPVDPLERGGVIALVGPTGAGKTTTIAKLAQRFAAQHTPRDVALVTTDTQRV 395
Cdd:PRK12727 314 VAMQIPADTELHRGRGLMLGLLSKRLPVAPVDPLERGGVIALVGPTGAGKTTTIAKLAQRFAAQHAPRDVALVTTDTQRV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 396 GGREQLHSYGRQLGIAVHEADSAESLLDLFERLRDYKLVLIDTAGMGQRDRALAAQLNWLRAAQQVTSLLVLPANAHFSD 475
Cdd:PRK12727 394 GGREQLHSYGRQLGIAVHEADSAESLLDLLERLRDYKLVLIDTAGMGQRDRALAAQLNWLRAARQVTSLLVLPANAHFSD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 476 LDEVVRRFAHAKPQGVVLTKLDETGSFGSALSVVVDHQMPITWVTDGQRVPDDLHRANAASLVLRLEDLRRAADKPCTPE 555
Cdd:PRK12727 474 LDEVVRRFAHAKPQGVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVPDDLHRANAASLVLRLEDLRRAADKPCTPE 553
|
....*.
gi 1126961737 556 HNHAVA 561
Cdd:PRK12727 554 HNHAVA 559
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
1-541 |
2.60e-105 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 320.66 E-value: 2.60e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 1 MKIKRFVAPDMRTAFRMVREEHGPDAVILSNRRTAEG-----IEIVAASNYDEElvqraletarsetsaaahnaaapiqq 75
Cdd:COG1419 1 MKIKKFVAKDMREALRKVKEELGPDAVILSTRKVKKGgflkkVEVTAAVDEDEA-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 76 apapqapTKPAAPVHAPLKLAANANvsqrqrvanaaedmiaamalrqpvnvprqapaaapvrtasipspaaqalahavav 155
Cdd:COG1419 55 -------EKAPAAAAAPAAASAAAE------------------------------------------------------- 72
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 156 ttaprqehalsavpeqlfadflttapmqapvqapvhaapvqactpimaaalathasygqdddeqdddgfdmddalpqilp 235
Cdd:COG1419 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 236 paalppivvapaavavaaaapapqnDEELKQLRGELALMRQMIEREMNRLTDERLRGSPARAQALELMDDYGFDAGLTRD 315
Cdd:COG1419 73 -------------------------EEELEELRRELAELKELLEEQLSGLAGESARLPPELAELLERLLEAGVSPELARE 127
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 316 VAMQIPADTELHRGRGLMLGLLSKRLPVAPVDPLERGGVIALVGPTGAGKTTTIAKLAQRFAAQHtPRDVALVTTDTQRV 395
Cdd:COG1419 128 LLEKLPEDLSAEEAWRALLEALARRLPVAEDPLLDEGGVIALVGPTGVGKTTTIAKLAARFVLRG-KKKVALITTDTYRI 206
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 396 GGREQLHSYGRQLGIAVHEADSAESLLDLFERLRDYKLVLIDTAGMGQRDRALAAQL-NWLRAAQQVTSLLVLPANAHFS 474
Cdd:COG1419 207 GAVEQLKTYARILGVPVEVAYDPEELKEALERLRDKDLVLIDTAGRSPRDPELIEELkALLDAGPPIEVYLVLSATTKYE 286
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1126961737 475 DLDEVVRRFAHAKPQGVVLTKLDETGSFGSALSVVVDHQMPITWVTDGQRVPDDLHRANAASLVLRL 541
Cdd:COG1419 287 DLKEIVEAFSSLGLDGLILTKLDETASLGSILNLLIRTGLPLSYITNGQRVPEDIEVADPERLARLL 353
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
1-543 |
1.26e-97 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 302.97 E-value: 1.26e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 1 MKIKRFVAPDMRTAFRMVREEHGPDAVILSNRRTAEG-------IEIVAAsnYDEELVQRALETARSETSaaahnaaapi 73
Cdd:PRK05703 1 MKIKKFTAKDMREALKQIKEELGADAVILSNKKVRKGgflgkklVEVTAA--VDEDETPKKNPVLREEKR---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 74 qqapapqaptKPAAPVhaplkLAANANVSQRQRVANAAEDMIAAMALRQPVNVPRQAPAAAPVRTASIPSPAAqalahav 153
Cdd:PRK05703 69 ----------KPAKSI-----LSLQALLEKRPSRTNSQDALLQAENALPEWKKELEKPSEPKEEEPKAAAESK------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 154 avttaprqehalsavpeqlfadflttapmqapvqapvhaapvqactpimaaalathasygqdddeqdddgfdmddalpqi 233
Cdd:PRK05703 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 234 lppaalppivvapaavavaaaapapQNDEELKQLRGELALMRQMIEREMNRLTDErLRGSPARAQALELMDDYGFDAGLT 313
Cdd:PRK05703 127 -------------------------VVQKELDELRDELKELKNLLEDQLSGLRQV-ERIPPEFAELYKRLKRSGLSPEIA 180
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 314 RDVAMQIPADTELHRGRGL--MLGLLSKRLPVAPVDPLERGGVIALVGPTGAGKTTTIAKLAQRFAAQHTPRDVALVTTD 391
Cdd:PRK05703 181 EKLLKLLLEHMPPRERTAWryLLELLANMIPVRVEDILKQGGVVALVGPTGVGKTTTLAKLAARYALLYGKKKVALITLD 260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 392 TQRVGGREQLHSYGRQLGIAVHEADSAESLLDLFERLRDYKLVLIDTAGMGQRDRALAAQLNWL--RAAQQVTSLLVLPA 469
Cdd:PRK05703 261 TYRIGAVEQLKTYAKIMGIPVEVVYDPKELAKALEQLRDCDVILIDTAGRSQRDKRLIEELKALieFSGEPIDVYLVLSA 340
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1126961737 470 NAHFSDLDEVVRRFAHAKPQGVVLTKLDETGSFGSALSVVVDHQMPITWVTDGQRVPDDLHRANA---ASLVLRLED 543
Cdd:PRK05703 341 TTKYEDLKDIYKHFSRLPLDGLIFTKLDETSSLGSILSLLIESGLPISYLTNGQRVPDDIKVANPeelVRLLLGGFN 417
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
1-540 |
1.25e-87 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 279.16 E-value: 1.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 1 MKIKRFVAPDMRTAFRMVREEHGPDAVILSNRRTAEGIEIVAASNYDEELVQRALETArsetsaaahnaaapiqqapapq 80
Cdd:PRK06995 1 MNIKKFFGKTSRDALRLVREALGADAVILSNRAVDGGVEIVALADSDLAALAPPAAAA---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 81 aptkPAAPVHAPLKLAANANVSQRQRVANAAEDMIAAMALRQPVNVPRQAPAAAPVRTASIPSPAAQALAHAVAVTTAPR 160
Cdd:PRK06995 59 ----PAAAQPPPAAAPAAVSRPAAPAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAAENAARRLAR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 161 QEhalsavpeqlfadfltTAPMQAPVQAPVHAAPVQACTPIMAAALATHasygqdddeqdddgfdmddalpqilppaalp 240
Cdd:PRK06995 135 AA----------------AAAPRPRVPADAAAAVADAVKARIERIVNDT------------------------------- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 241 pivvapaavavaaaapapqndeelkqLRGELALMRQMIEREMNRLT-DERLRGSPARAQALELMDDYGFDAGLTRDVAMQ 319
Cdd:PRK06995 168 --------------------------VMQELRSLRGMLEEQLASLAwGERQRRDPVRAALLKHLLAAGFSAQLVRMLVDN 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 320 IPADTELHRGRGLMLGLLSKRLPVAPV--DPLERGGVIALVGPTGAGKTTTIAKLAQRFAAQHTPRDVALVTTDTQRVGG 397
Cdd:PRK06995 222 LPEGDDAEAALDWVQSALAKNLPVLDSedALLDRGGVFALMGPTGVGKTTTTAKLAARCVMRHGASKVALLTTDSYRIGG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 398 REQLHSYGRQLGIAVHEADSAESLLDLFERLRDYKLVLIDTAGMGQRDRALAAQLNWLRAA-QQVTSLLVLPANAHFSDL 476
Cdd:PRK06995 302 HEQLRIYGKILGVPVHAVKDAADLRLALSELRNKHIVLIDTIGMSQRDRMVSEQIAMLHGAgAPVKRLLLLNATSHGDTL 381
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1126961737 477 DEVVRRFAHAKPQGVVLTKLDETGSFGSALSVVVDHQMPITWVTDGQRVPDDLHRANAASLVLR 540
Cdd:PRK06995 382 NEVVQAYRGPGLAGCILTKLDEAASLGGALDVVIRYKLPLHYVSNGQRVPEDLHLANKKFLLHR 445
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
353-541 |
2.96e-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: 2.96e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 353 GVIALVGPTGAGKTTTIAKLAQRFAAQHTPRdVALVTTDTQRVGGREQLHSYGRQLGIAVHEADSAESLLDLFERLRDYK 432
Cdd:cd17873 1 RVIALVGPTGVGKTTTLAKLAARYVLKKGKK-VALITTDTYRIGAVEQLKTYAEIMGIPVEVAEDPEDLADALERLSDRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 433 LVLIDTAGMGQRDRALAAQLNWL-RAAQQVTSLLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDETGSFGSALSVVVD 511
Cdd:cd17873 80 LILIDTAGRSPRDKEQLEELKELlGAGEDIEVHLVLSATTKAKDLKEIIERFSPLGYRGLILTKLDETTSLGSVLSVLAE 159
|
170 180 190
....*....|....*....|....*....|
gi 1126961737 512 HQMPITWVTDGQRVPDDLHRANAASLVLRL 541
Cdd:cd17873 160 SQLPVSYVTTGQRVPEDIEVASPLRLARLL 189
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
1-440 |
2.12e-63 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 209.11 E-value: 2.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 1 MKIKRFVAPDMRTAFRMVREEHGPDAVILSNRRTAEG------IEIVAASNYDEelvqraletarsetsaaahnaaapiq 74
Cdd:TIGR03499 1 MKIKKFTAPTMREALKKVKEELGPDAVILSTRKVRKGlfgkkfVEVTAAIDEEE-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 75 qapapqaptkpaapvhaplklaanANVSQRQRVANAAedmiaamalrQPVNVPRQAPAAAPvrtasipspaaqalahava 154
Cdd:TIGR03499 55 ------------------------AAAASAEEEASKA----------LEQADPKPLSATAE------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 155 vttaprqehalsavpeqlfadflttaPMQAPVQAPVHAAPVQActpimaaalathasygqdddeqdddgfdmddalpqil 234
Cdd:TIGR03499 82 --------------------------PLELPAPQEEPAAPAAQ------------------------------------- 98
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 235 ppaalppivvapaavavaaaapAPQNDEELKQLRGELALMRQMIEREMNRLTDERLrgSPARAQALELMDDYGFDAGLTR 314
Cdd:TIGR03499 99 ----------------------AAEPLLPEEELRKELEALRELLERLLAGLAWLQR--PPERAKLYERLLEAGVSEELAR 154
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 315 DVAMQIPADTELHRGRGLMLGLLSKRLPVAP--VDPLERGGVIALVGPTGAGKTTTIAKLAQRFAAQHTPRDVALVTTDT 392
Cdd:TIGR03499 155 ELLEKLPEDADAEDAWRWLREALEGMLPVKPeeDPILEQGGVIALVGPTGVGKTTTLAKLAARFALEHGKKKVALITTDT 234
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1126961737 393 QRVGGREQLHSYGRQLGIAVHEADSAESLLDLFERLRDYKLVLIDTAG 440
Cdd:TIGR03499 235 YRIGAVEQLKTYAEILGIPVKVARDPKELREALDRLRDKDLILIDTAG 282
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
270-546 |
1.06e-58 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 201.33 E-value: 1.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 270 ELALMRQMIEREMNRL--TDERLRgSPARAQALELMDDYGFDAGLTRDVAMQIPADTELHRGRGLMLGLLSKRLPVAPVD 347
Cdd:PRK14721 107 EIRAMRQMLEEQLTTMgwSNFSQR-DPGGMKVLRTLLSAGFSPLLSRHLLEKLPADRDFEQSLKKTISLLTLNLRTIGGD 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 348 P-LERGGVIALVGPTGAGKTTTIAKLAQRFAAQHTPRDVALVTTDTQRVGGREQLHSYGRQLGIAVHEADSAESLLDLFE 426
Cdd:PRK14721 186 EiIEQGGVYALIGPTGVGKTTTTAKLAARAVIRHGADKVALLTTDSYRIGGHEQLRIYGKLLGVSVRSIKDIADLQLMLH 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 427 RLRDYKLVLIDTAGMGQRDRALAAQLNWL-RAAQQVTSLLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDETGSFGSA 505
Cdd:PRK14721 266 ELRGKHMVLIDTVGMSQRDQMLAEQIAMLsQCGTQVKHLLLLNATSSGDTLDEVISAYQGHGIHGCIITKVDEAASLGIA 345
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1126961737 506 LSVVVDHQMPITWVTDGQRVPDDLHRANAASLVLRLEDLRR 546
Cdd:PRK14721 346 LDAVIRRKLVLHYVTNGQKVPEDLHEANSRYLLHRIFKPSR 386
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
352-541 |
1.72e-55 |
|
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: 185.31 E-value: 1.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 352 GGVIALVGPTGAGKTTTIAKLAQRFAAQHTPRdVALVTTDTQRVGGREQLHSYGRQLGIAV-------HEADSAESLLDL 424
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGGKK-VLLVAADTFRAAAVEQLKTYAEILGVVPvaggegaDPVAVAKDAVEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 425 FeRLRDYKLVLIDTAGMGQRDRALAAQLNWLRAAQQVTSLLVLPANAHFSDLDEVVRRFAHA-KPQGVVLTKLDETGSFG 503
Cdd:smart00962 80 A-KARGYDVVLIDTAGRLHNDENLMEELKKIKRVIKPDEVLLVSDATTGQDAVEQAKAFNEAlGLTGIILTKLDGTAKGG 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1126961737 504 SALSVVVDHQMPITWVTDGQRVPdDLHRANAASLVLRL 541
Cdd:smart00962 159 AALSIAAETGLPIKFIGTGEKVP-DLEPFDPERFVSRL 195
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
267-548 |
7.44e-55 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 198.10 E-value: 7.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 267 LRGELALMRQMIEREMNRL---TDERLRGSPARAQALELMDDYGFDAGLTRDVAMQIPADTELHRGRGLMLGLLSKRLPV 343
Cdd:PRK14723 95 LRGELQSMRGMLERQLAGLlwaAGEVAGRDPLRASLFRWLLGAGFSGQLARALLERLPVGYDRPAAMAWIRNELATHLPV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 344 A--PVDPLERGGVIALVGPTGAGKTTTIAKLAQRFAAQHTPRDVALVTTDTQRVGGREQLHSYGRQLGIAVHEADSAESL 421
Cdd:PRK14723 175 LrdEDALLAQGGVLALVGPTGVGKTTTTAKLAARCVAREGADQLALLTTDSFRIGALEQLRIYGRILGVPVHAVKDAADL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 422 LDLFERLRDYKLVLIDTAGMGQRDRALAAQLNWLRAAQ-QVTSLLVLPANAHFSDLDEVVRRFAHAKPQ---GVVLTKLD 497
Cdd:PRK14723 255 RFALAALGDKHLVLIDTVGMSQRDRNVSEQIAMLCGVGrPVRRLLLLNAASHGDTLNEVVHAYRHGAGEdvdGCIITKLD 334
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1126961737 498 ETGSFGSALSVVVDHQMPITWVTDGQRVPDDLHRANAASLVLR-LEDLRRAA 548
Cdd:PRK14723 335 EATHLGPALDTVIRHRLPVHYVSTGQKVPEHLELAQADELVDRaFATPRRGA 386
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
270-538 |
1.39e-46 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 167.59 E-value: 1.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 270 ELALMRQMIEREMNRLT-DERLRGSPARAQALELMDDYGFDAGLTRDVAMQIPA----DTeLHRGRGLMLGLLSKRLPVA 344
Cdd:PRK14722 49 ELGSLRELMEEQFAGLMwNERQRRNPVHGALTKYLFAAGFSAQLVRMIVDNLPEgegyDT-LDAAADWAQSVLAANLPVL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 345 PVDP--LERGGVIALVGPTGAGKTTTIAKLAQRFAAQHTPRDVALVTTDTQRVGGREQLHSYGRQLGIAVHEADSAESLL 422
Cdd:PRK14722 128 DSEDalMERGGVFALMGPTGVGKTTTTAKLAARCVMRFGASKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDLQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 423 DLFERLRDYKLVLIDTAGMGQRDRALAAQLNWLRAAQQ-VTSLLVLPANAHFSDLDEVVRRFAHAKPQ---------GVV 492
Cdd:PRK14722 208 LALAELRNKHMVLIDTIGMSQRDRTVSDQIAMLHGADTpVQRLLLLNATSHGDTLNEVVQAYRSAAGQpkaalpdlaGCI 287
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1126961737 493 LTKLDETGSFGSALSVVVDHQMPITWVTDGQRVPDDLHRANAASLV 538
Cdd:PRK14722 288 LTKLDEASNLGGVLDTVIRYKLPVHYVSTGQKVPENLYVATKKFLL 333
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
354-541 |
9.61e-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: 140.37 E-value: 9.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 354 VIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGIAV----HEADSAESLLDLFE--R 427
Cdd:pfam00448 2 VILLVGLQGSGKTTTIAKLAAYLKKKG--KKVLLVAADTFRAAAIEQLKQLAEKLGVPVfgskTGADPAAVAFDAVEkaK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 428 LRDYKLVLIDTAGMGQRDRALAAQL-NWLRAAQQVTSLLVLPANAHFSDLdEVVRRFAHAKP-QGVVLTKLDETGSFGSA 505
Cdd:pfam00448 80 AENYDVVLVDTAGRLQNDKNLMDELkKIKRVVAPDEVLLVLDATTGQNAV-NQAKAFNEAVGiTGVILTKLDGDAKGGAA 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1126961737 506 LSVVVDHQMPITWVTDGQRVpDDLHRANAASLVLRL 541
Cdd:pfam00448 159 LSIVAETGKPIKFIGVGEKI-DDLEPFDPERFVSRL 193
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
354-541 |
1.88e-32 |
|
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: 123.25 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 354 VIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGIAVHEADSAESLLDLFE------R 427
Cdd:cd03115 2 VILLVGLQGSGKTTTLAKLARYYQEKG--KKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTDPASIAQeavekaK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 428 LRDYKLVLIDTAGMGQRDRALAAQLNWLRAAQQ-VTSLLVLPANAHFSDLDeVVRRFAHAKP-QGVVLTKLDETGSFGSA 505
Cdd:cd03115 80 LEGYDVLLVDTAGRLQKDEPLMEELKKVKEVESpDEVLLVLDATTGQEALS-QAKAFNEAVGlTGVILTKLDGTAKGGAA 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1126961737 506 LSVVVDHQMPITWVTDGQRvPDDLHRANAASLVLRL 541
Cdd:cd03115 159 LSIVAETKKPIKFIGVGEK-PEDLEPFDPERFVSAL 193
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
354-549 |
2.35e-29 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 119.62 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 354 VIALVGPTGAGKTTTIAKLAQRFA--AQHTPRDVALVTTDTQRVGGREQLHSYGRQLGIAVHEADSAESLLDLFERLRDY 431
Cdd:PRK12723 176 VFILVGPTGVGKTTTIAKLAAIYGinSDDKSLNIKIITIDNYRIGAKKQIQTYGDIMGIPVKAIESFKDLKEEITQSKDF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 432 KLVLIDTAGMGQRDRALAAQLNWLRAA--QQVTSLLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDETGSFGSALSVV 509
Cdd:PRK12723 256 DLVLVDTIGKSPKDFMKLAEMKELLNAcgRDAEFHLAVSSTTKTSDVKEIFHQFSPFSYKTVIFTKLDETTCVGNLISLI 335
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1126961737 510 VDHQMPITWVTDGQRVPDDLHRANAASLVLRLEDLRRAAD 549
Cdd:PRK12723 336 YEMRKEVSYVTDGQIVPHNISIAEPLTFIKKINGYRISDD 375
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
355-537 |
2.03e-27 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 114.78 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 355 IALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLG---IAVHEADSAESLLDLF-ERLR- 429
Cdd:PRK11889 244 IALIGPTGVGKTTTLAKMAWQFHGKK--KTVGFITTDHSRIGTVQQLQDYVKTIGfevIAVRDEAAMTRALTYFkEEARv 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 430 DYklVLIDTAGMGQRDRALAAQLnwLRAAQQVTS---LLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDETGSFGSAL 506
Cdd:PRK11889 322 DY--ILIDTAGKNYRASETVEEM--IETMGQVEPdyiCLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDETASSGELL 397
|
170 180 190
....*....|....*....|....*....|.
gi 1126961737 507 SVVVDHQMPITWVTDGQRVPDDLHRANAASL 537
Cdd:PRK11889 398 KIPAVSSAPIVLMTDGQDVKKNIHIATAEHL 428
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
354-541 |
2.62e-25 |
|
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: 105.42 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 354 VIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGIAV----HEADSAESLLDLFE--R 427
Cdd:TIGR00064 79 VILFVGVNGVGKTTTIAKLANKLKKQG--KSVLLAAGDTFRAAAIEQLEEWAKRLGVDVikqkEGADPAAVAFDAIQkaK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 428 LRDYKLVLIDTAGMGQRDRALAAQLNWL-RAAQQVT------SLLVLPANAHFSDLdEVVRRFAHAKP-QGVVLTKLDET 499
Cdd:TIGR00064 157 ARNIDVVLIDTAGRLQNKVNLMDELKKIkRVIKKVDkdapdeVLLVLDATTGQNAL-EQAKVFNEAVGlTGIILTKLDGT 235
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1126961737 500 GSFGSALSVVVDHQMPITWVTDGQRVpDDLHRANAASLVLRL 541
Cdd:TIGR00064 236 AKGGIILSIAYELKLPIKFIGVGEKI-DDLAPFDADWFVEAL 276
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
355-541 |
7.96e-25 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 104.06 E-value: 7.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 355 IALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLG---IAVHEADSAESLLDLFERLRDY 431
Cdd:PRK06731 78 IALIGPTGVGKTTTLAKMAWQFHGKK--KTVGFITTDHSRIGTVQQLQDYVKTIGfevIAVRDEAAMTRALTYFKEEARV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 432 KLVLIDTAGMGQRDRALAAQLnwLRAAQQVTS---LLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDETGSFGSALSV 508
Cdd:PRK06731 156 DYILIDTAGKNYRASETVEEM--IETMGQVEPdyiCLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDETASSGELLKI 233
|
170 180 190
....*....|....*....|....*....|...
gi 1126961737 509 VVDHQMPITWVTDGQRVPDDLHRANAASLVLRL 541
Cdd:PRK06731 234 PAVSSAPIVLMTDGQDVKKNIHIATAEHLAKQM 266
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
354-529 |
3.49e-23 |
|
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: 97.26 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 354 VIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGIAV--HE--ADSAESLLD--LFER 427
Cdd:cd17874 2 VILFVGVNGVGKTTTIGKLAHYLKNQG--KKVVLAAGDTFRAAAVEQLEEWAERLGVPVisQNegADPAAVAFDaiQAAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 428 LRDYKLVLIDTAGMGQRDRALAAQLNWL-RAAQQVT------SLLVLPANAHfSDLDEVVRRFA-HAKPQGVVLTKLDET 499
Cdd:cd17874 80 ARGIDVVLIDTAGRLHTKKNLMEELKKIkRVIKKKDpeapheVLLVLDATTG-QNALEQAKEFNeAVGLTGIILTKLDGT 158
|
170 180 190
....*....|....*....|....*....|
gi 1126961737 500 GSFGSALSVVVDHQMPITWVTDGQRVpDDL 529
Cdd:cd17874 159 AKGGIVLSIADELKIPVKFVGVGEGI-DDL 187
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
354-533 |
3.46e-21 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 96.19 E-value: 3.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 354 VIALVGPTGAGKTTTIAKLAQRFAAqHTPRDVALVTTDTQRVGGREQLHSYGRQLGIAVHEADSAESLLDLFerLRD-YK 432
Cdd:PRK12724 225 VVFFVGPTGSGKTTSIAKLAAKYFL-HMGKSVSLYTTDNYRIAAIEQLKRYADTMGMPFYPVKDIKKFKETL--ARDgSE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 433 LVLIDTAGMGQRDRALAAQLNWLRAA----QQVTSLLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDETGSFGSALSV 508
Cdd:PRK12724 302 LILIDTAGYSHRNLEQLERMQSFYSCfgekDSVENLLVLSSTSSYHHTLTVLKAYESLNYRRILLTKLDEADFLGSFLEL 381
|
170 180
....*....|....*....|....*
gi 1126961737 509 VVDHQMPITWVTDGQRVPDDLHRAN 533
Cdd:PRK12724 382 ADTYSKSFTYLSVGQEVPFDILNAT 406
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
354-541 |
4.09e-21 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 94.65 E-value: 4.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 354 VIALVGPTGAGKTTTIAKLAQRFaaQHTPRDVALVTTDTQRVGGREQLHSYGRQLGIAV--HE--ADSAESLLDLFE--R 427
Cdd:PRK14974 142 VIVFVGVNGTGKTTTIAKLAYYL--KKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVikHKygADPAAVAYDAIEhaK 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 428 LRDYKLVLIDTAGMGQRDRALAAQlnwLRAAQQVT----SLLVLPANAHfSDLDEVVRRFAHA-KPQGVVLTKLDETGSF 502
Cdd:PRK14974 220 ARGIDVVLIDTAGRMHTDANLMDE---LKKIVRVTkpdlVIFVGDALAG-NDAVEQAREFNEAvGIDGVILTKVDADAKG 295
|
170 180 190
....*....|....*....|....*....|....*....
gi 1126961737 503 GSALSVVVDHQMPITWVTDGQRVpDDLHRANAASLVLRL 541
Cdd:PRK14974 296 GAALSIAYVIGKPILFLGVGQGY-DDLIPFDPDWFVDKL 333
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
354-527 |
5.89e-19 |
|
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: 84.96 E-value: 5.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 354 VIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGIAVHEADSAESLLDLFER------ 427
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKG--KKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQSPVDIAKRalekak 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 428 LRDYKLVLIDTAGMGQRDRALAAQLNWLRAAQQVTS-LLVLPAnAHFSDLDEVVRRFAHA-KPQGVVLTKLDETGSFGSA 505
Cdd:cd18539 80 EEGFDVVIVDTAGRLHIDEELMDELKEIKEVLNPDEvLLVVDA-MTGQDAVNVAKAFNERlGLTGVVLTKLDGDARGGAA 158
|
170 180
....*....|....*....|..
gi 1126961737 506 LSVVVDHQMPITWVTDGQRVPD 527
Cdd:cd18539 159 LSIRHVTGKPIKFIGVGEKIED 180
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
354-509 |
8.93e-18 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 85.84 E-value: 8.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 354 VIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGIAVHEADSAESLLDLFE------R 427
Cdd:COG0541 102 VIMMVGLQGSGKTTTAAKLAKYLKKKG--KKPLLVAADVYRPAAIEQLKTLGEQIGVPVFPEEDGKDPVDIAKraleyaK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 428 LRDYKLVLIDTAGMGQRDRALAAQLNWLRAAQQVT-SLLVLPA-------NahfsdldeVVRRFAHAKP-QGVVLTKLDE 498
Cdd:COG0541 180 KNGYDVVIVDTAGRLHIDEELMDELKAIKAAVNPDeTLLVVDAmtgqdavN--------VAKAFNEALGlTGVILTKLDG 251
|
170
....*....|.
gi 1126961737 499 TGSFGSALSVV 509
Cdd:COG0541 252 DARGGAALSIR 262
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
333-529 |
1.65e-17 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 83.61 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 333 MLGLLSKRLPVAPVDPLerggVIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGIAV 412
Cdd:PRK10416 99 ILEPVEKPLNIEEKKPF----VILVVGVNGVGKTTTIGKLAHKYKAQG--KKVLLAAGDTFRAAAIEQLQVWGERVGVPV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 413 ----HEADSAeSLldLFE-----RLRDYKLVLIDTAGmgqRdraLAAQLNwL--------RAAQQV------TSLLVLPA 469
Cdd:PRK10416 173 iaqkEGADPA-SV--AFDaiqaaKARGIDVLIIDTAG---R---LHNKTN-LmeelkkikRVIKKAdpdaphEVLLVLDA 242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126961737 470 ----NAhFSDldevVRRFAHAKP-QGVVLTKLDETGSFGSALSVVVDHQMPITWVTDGQRVpDDL 529
Cdd:PRK10416 243 ttgqNA-LSQ----AKAFHEAVGlTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGI-DDL 301
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
354-541 |
4.25e-17 |
|
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: 79.54 E-value: 4.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 354 VIALVGPTGAGKTTTIAKLAQRFaaQHTPRDVALVTTDTQRVGGREQLHSYGRQLGIAVH----EADSAESLLDLFERLR 429
Cdd:cd17875 2 VIMFVGLQGSGKTTTAAKLAYYY--QKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYgsytEKDPVKIAKEGVEKFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 430 D--YKLVLIDTAGMGQRDRALAAQLNWLRAAQQVTS-LLVLPA----NAHfsdldEVVRRFAHAKPQG-VVLTKLDETGS 501
Cdd:cd17875 80 KekFDIIIVDTSGRHKQEEELFEEMKQISDAVKPDEvILVIDAsigqAAE-----DQAKAFKEAVDIGsVIITKLDGHAK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1126961737 502 FGSALSVVVDHQMPITWVTDGQRVpDDLHRANAASLVLRL 541
Cdd:cd17875 155 GGGALSAVAATGAPIIFIGTGEHI-DDLEPFDPKRFVSRL 193
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
261-541 |
4.71e-17 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 83.25 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 261 DEELKQLRGELALMRQMI------EREMNRLTDERLRGspaRAQALELMDDYgFDAGltRDVAMQIPAdTELHRGRGLML 334
Cdd:PRK12726 116 EEELSAMRLELAALNRELavkmreEREQNSDFVKFLKG---RGISDTYVADF-MQAG--RKQFKQVET-AHLDDITDWFV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 335 GLLSKRLPVAPVDPLERGGVIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGIAVHE 414
Cdd:PRK12726 189 PYLSGKLAVEDSFDLSNHRIISLIGQTGVGKTTTLVKLGWQLLKQN--RTVGFITTDTFRSGAVEQFQGYADKLDVELIV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 415 ADSAESLLDLFERLRDYKLV---LIDTAGmgqRDRALAAQLNWLRAAQQVT----SLLVLPANAHFSDLDEVVRRFAHAK 487
Cdd:PRK12726 267 ATSPAELEEAVQYMTYVNCVdhiLIDTVG---RNYLAEESVSEISAYTDVVhpdlTCFTFSSGMKSADVMTILPKLAEIP 343
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1126961737 488 PQGVVLTKLDETGSFGSALSVVVDHQMPITWVTDGQRVPDDLHRANAASLVLRL 541
Cdd:PRK12726 344 IDGFIITKMDETTRIGDLYTVMQETNLPVLYMTDGQNITENIFRPKSRWLAERF 397
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
333-541 |
9.08e-17 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 82.56 E-value: 9.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 333 MLGLLSKRLPVaPVDPLERGgVIALVGPTGAGKTTTIAKLAQRFaaQHTPRDVALVTTDTQRVGGREQLHSYGRQLGIAV 412
Cdd:PRK00771 78 LVKLLGEETEP-LVLPLKPQ-TIMLVGLQGSGKTTTAAKLARYF--KKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 413 H----EADSAESLLDLFERLRDYKLVLIDTAGmgqRDRALAAQLNWLRAAQQVTS----LLVLPA----NAHfsdldEVV 480
Cdd:PRK00771 154 YgdpdNKDAVEIAKEGLEKFKKADVIIVDTAG---RHALEEDLIEEMKEIKEAVKpdevLLVIDAtigqQAK-----NQA 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1126961737 481 RRFAHAKP-QGVVLTKLDETGSFGSALSVVVDHQMPITWVTDGQRVpDDLHRANAASLVLRL 541
Cdd:PRK00771 226 KAFHEAVGiGGIIITKLDGTAKGGGALSAVAETGAPIKFIGTGEKI-DDLERFDPDRFISRL 286
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
354-541 |
9.91e-17 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 80.84 E-value: 9.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 354 VIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHSYGRQLGIAV---HE-ADSAeSLldLFE--- 426
Cdd:COG0552 102 VILVVGVNGVGKTTTIGKLAHRLKAEG--KSVLLAAGDTFRAAAIEQLEVWGERVGVPViaqKEgADPA-AV--AFDaiq 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 427 --RLRDYKLVLIDTAGMGQRDRALAAQL-------NWLRAAQQVTSLLVLPA----NAHfsdldEVVRRFAHA-KPQGVV 492
Cdd:COG0552 177 aaKARGADVVIIDTAGRLHNKKNLMEELkkikrviKKLDPDAPHEVLLVLDAttgqNAL-----SQAKVFNEAvGVTGIV 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1126961737 493 LTKLDETGSFGSALSVVVDHQMPITWVTDGQRVpDDLHRANAASLVLRL 541
Cdd:COG0552 252 LTKLDGTAKGGVVLAIADELGIPIKFIGVGEGI-DDLRPFDAEEFVDAL 299
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
354-556 |
2.76e-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: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 354 VIALVGPTGAGKTTTIAKLAQRFaaQHTPRDVALVTTDTQRVGGREQLHSYGRQLGIAVH----EADSAESLLDLFERLR 429
Cdd:TIGR01425 102 VIMFVGLQGAGKTTTCTKLAYYY--KRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYgsyeESDPVKIASEGVEKFR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 430 DYK--LVLIDTAGMGQRDRALAAQLNWLRAAQQVTSLLVLPANAHFSDLDEVVRRFAHAKPQG-VVLTKLDETGSFGSAL 506
Cdd:TIGR01425 180 KEKfdIIIVDTSGRHKQEKELFEEMQQVREAIKPDSIIFVMDGSIGQAAFGQAKAFKDSVEVGsVIITKLDGHAKGGGAL 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1126961737 507 SVVVDHQMPITWVTDGQRVpDDLHRANAASLVLRL-------------EDLRRAADKPCTPEH 556
Cdd:TIGR01425 260 SAVAATKSPIIFIGTGEHV-DEFEIFDAEPFVSKLlgmgdlkglidkvQDLALNDEEKTLIEH 321
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
354-538 |
9.14e-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: 61.48 E-value: 9.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 354 VIALVGPTGAGKTTTIAKLAQRFAaQHTPRdVALVTTDTQRVGGREQLHSYGRQLGIAVHEA----DSAESLLDLFERLR 429
Cdd:cd17876 2 VIVFCGVNGVGKSTNLAKIAYWLL-SNGFR-VLIAACDTFRSGAVEQLRTHARRLGVELYEKgygkDPAAVAKEAIKYAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 430 D--YKLVLIDTAGMGQRDRALAAQLNWL-RAAQQVTSLLV---LPANAHFSDLDEVVRRFAHAKPQ-------GVVLTKL 496
Cdd:cd17876 80 DqgFDVVLIDTAGRMQNNEPLMRALAKLiKENNPDLVLFVgeaLVGNDAVDQLKKFNQALADYSPSdnprlidGIVLTKF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1126961737 497 DETGS-FGSALSVVVDHQMPITWVTDGQRVPdDLHRANAASLV 538
Cdd:cd17876 160 DTIDDkVGAALSMVYATGQPIVFVGTGQTYT-DLKKLNVKAVV 201
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
351-449 |
1.98e-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: 56.23 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 351 RGGVIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTDTQRVGGREQLHsyGRQLGIAVHEADSAESLLDLFERLR- 429
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPG--GGVIYIDGEDILEEVLDQLL--LIIVGGKKASGSGELRLRLALALARk 76
|
90 100
....*....|....*....|.
gi 1126961737 430 -DYKLVLIDTAGMGQRDRALA 449
Cdd:smart00382 77 lKPDVLILDEITSLLDAEQEA 97
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
350-456 |
2.05e-07 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 50.03 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 350 ERGGVIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTdTQRVGGREQLHSYGRQLGIAVHEADSAESLLDLFER-- 427
Cdd:pfam13401 3 FGAGILVLTGESGTGKTTLLRRLLEQLPEVR--DSVVFVDL-PSGTSPKDLLRALLRALGLPLSGRLSKEELLAALQQll 79
|
90 100 110
....*....|....*....|....*....|.
gi 1126961737 428 --LRDYKLVLIDTAgmgqrDRALAAQLNWLR 456
Cdd:pfam13401 80 laLAVAVVLIIDEA-----QHLSLEALEELR 105
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
349-516 |
2.52e-07 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 51.84 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 349 LERGGVIALVGPTGAGKTTtiakLAQRFAAQ--HTPRDVALVTTDTqrvgGREQLHSYGRQLG-----------IAVHEA 415
Cdd:COG0467 17 LPRGSSTLLSGPPGTGKTT----LALQFLAEglRRGEKGLYVSFEE----SPEQLLRRAESLGldleeyiesglLRIIDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 416 DSAESLLD---LFERLRDY------KLVLID--------TAGMGQRDRALAAQLNWLRaAQQVTSLLVLPANA-HFSDLD 477
Cdd:COG0467 89 SPEELGLDleeLLARLREAveefgaKRVVIDslsglllaLPDPERLREFLHRLLRYLK-KRGVTTLLTSETGGlEDEATE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1126961737 478 EVVRRFAHakpqGVVLTKLDET-GSFGSALSVV----VDHQMPI 516
Cdd:COG0467 168 GGLSYLAD----GVILLRYVELgGELRRALSVLkmrgSAHDRTI 207
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
350-439 |
4.16e-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: 48.63 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 350 ERGGVIALVGPTGAGKTTTIAKLAQRFaaqhtPRDVALVTTDTQRVGGREQLHSYGRQLGIAVHEADSAESLLDLFERLR 429
Cdd:COG3267 41 QGGGFVVLTGEVGTGKTTLLRRLLERL-----PDDVKVAYIPNPQLSPAELLRAIADELGLEPKGASKADLLRQLQEFLL 115
|
90
....*....|....*.
gi 1126961737 430 DYK------LVLIDTA 439
Cdd:COG3267 116 ELAaagrrvVLIIDEA 131
|
|
| CoaA |
COG1072 |
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ... |
268-391 |
8.17e-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: 8.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 268 RGELALMRQMIEREMNRLTDERLRGSPARAQALELMDDYgfdAGLTRDVAMQIPADTELHRGRGLMLGLLSKRLPVapvd 347
Cdd:COG1072 15 REEWAALRASTPLTLTEEELERLRGLNDPISLDEVEDIY---LPLSRLLNLYVAATQRLHRATSAFLGQADKKTPF---- 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1126961737 348 plerggVIALVGPTGAGKTTTIAKLAQRFAAQHTPRDVALVTTD 391
Cdd:COG1072 88 ------IIGIAGSVAVGKSTTARLLQALLSRWPEHPKVELVTTD 125
|
|
| MobB |
COG1763 |
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ... |
354-436 |
2.03e-05 |
|
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: 45.17 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 354 VIALVGPTGAGKTTTIAKLAQRFAAQ--------HTPRDVALVT--TDTQRvggreqlHsygRQLGIA------------ 411
Cdd:COG1763 3 VLGIVGYSGSGKTTLLEKLIPELKARglrvgtikHAHHDFDIDTpgKDSYR-------H---REAGADevlvasperwal 72
|
90 100
....*....|....*....|....*
gi 1126961737 412 VHEADSAESLLDLFERLRDYKLVLI 436
Cdd:COG1763 73 MTELPEEPSLDELLARLDDVDLVLV 97
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
349-452 |
9.07e-05 |
|
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: 44.08 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 349 LERGGVIALVGPTGAGKTTTIAKLA------------QRFAAQHTP----RDVALVTTDT---QRVGGREQLHSYGRQLG 409
Cdd:COG4555 24 AKDGEITGLLGPNGAGKTTLLRMLAgllkpdsgsiliDGEDVRKEPrearRQIGVLPDERglyDRLTVRENIRYFAELYG 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1126961737 410 IAVHEADS-AESLLDLFErLRDYKLVLIDTAGMGQRDR-ALAAQL 452
Cdd:COG4555 104 LFDEELKKrIEELIELLG-LEEFLDRRVGELSTGMKKKvALARAL 147
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
349-376 |
1.01e-04 |
|
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: 1.01e-04
10 20
....*....|....*....|....*...
gi 1126961737 349 LERGGVIALVGPTGAGKtTTIAKLAQRF 376
Cdd:cd03228 25 IKPGEKVAIVGPSGSGK-STLLKLLLRL 51
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
259-447 |
1.14e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 259 QNDEELKQLRGELALMRQMIEREMNRLTD----ERLRGSPARAQALELMDDYGFDAGLT------RDVAMQIPADTElhr 328
Cdd:TIGR00956 698 QKGEILVFRRGSLKRAKKAGETSASNKNDieagEVLGSTDLTDESDDVNDEKDMEKESGedifhwRNLTYEVKIKKE--- 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 329 grglmlgllsKRLPVAPVDPLERGGVI-ALVGPTGAGKTTTIAKLAQRfaaqhtpRDVALVTTDTQRVGGREQLHSYGRQ 407
Cdd:TIGR00956 775 ----------KRVILNNVDGWVKPGTLtALMGASGAGKTTLLNVLAER-------VTTGVITGGDRLVNGRPLDSSFQRS 837
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1126961737 408 LG-----------IAVHEA-------------------DSAESLLDLFErLRDYKLVLIDTAGMG----QRDRA 447
Cdd:TIGR00956 838 IGyvqqqdlhlptSTVRESlrfsaylrqpksvsksekmEYVEEVIKLLE-MESYADAVVGVPGEGlnveQRKRL 910
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
349-376 |
1.27e-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: 1.27e-04
10 20
....*....|....*....|....*...
gi 1126961737 349 LERGGVIALVGPTGAGKtTTIAKLAQRF 376
Cdd:COG1132 363 IPPGETVALVGPSGSGK-STLVNLLLRF 389
|
|
| ComEC |
COG2333 |
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ... |
434-543 |
3.28e-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: 42.54 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 434 VLIDTAGMGQRDRALAAQLNWLRAaQQVTSL--LVL--PANAHFSDLDEVVRRFahakPQGVVLT--KLDETGSFGSALS 507
Cdd:COG2333 24 ILIDTGPRPSFDAGERVVLPYLRA-LGIRRLdlLVLthPDADHIGGLAAVLEAF----PVGRVLVsgPPDTSETYERLLE 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1126961737 508 VVVDHQMPITWVTDGQRVPDD------LH---------RANAASLVLRLED 543
Cdd:COG2333 99 ALKEKGIPVRPCRAGDTWQLGgvrfevLWppedllegsDENNNSLVLRLTY 149
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
355-497 |
4.25e-04 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 41.51 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 355 IALVGPTGAGKTTtiakLAQRFAAQHTPRDVALVTtdtqrvggreqlhsygrqLGIAVHEADsaeslLDLFErlRDYKLV 434
Cdd:COG1100 6 IVVVGTGGVGKTS----LVNRLVGDIFSLEKYLST------------------NGVTIDKKE-----LKLDG--LDVDLV 56
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1126961737 435 LIDTAgmGQRDRALAAQL--NWLRAAqqvtSLLVL-------PANAHFSDLDEVVRRFAHAKPQGVVLTKLD 497
Cdd:COG1100 57 IWDTP--GQDEFRETRQFyaRQLTGA----SLYLFvvdgtreETLQSLYELLESLRRLGKKSPIILVLNKID 122
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
349-369 |
4.54e-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: 4.54e-04
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
354-391 |
5.29e-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: 5.29e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1126961737 354 VIALVGPTGAGKTTTIAKLAQRFAAQHtprdVALVTTD 391
Cdd:COG0572 9 IIGIAGPSGSGKTTFARRLAEQLGADK----VVVISLD 42
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
356-497 |
6.96e-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: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 356 ALVGPTGAGKTTTIAKLAQRFAAQhtPRDVALVTTDTQRvgGREQLHSYGrqlgiavheadsaeslldlferlrdYKLVL 435
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGE--VSDVPGTTRDPDV--YVKELDKGK-------------------------VKLVL 51
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1126961737 436 IDTAGMGQRDRALAAQLNWlRAAQQVTS-LLVLPANAHFSDLDE----VVRRFAHAKPQGVVLTKLD 497
Cdd:cd00882 52 VDTPGLDEFGGLGREELAR-LLLRGADLiLLVVDSTDRESEEDAklliLRRLRKEGIPIILVGNKID 117
|
|
| mobB |
TIGR00176 |
molybdopterin-guanine dinucleotide biosynthesis protein MobB; This molybdenum cofactor ... |
354-436 |
8.09e-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: 40.05 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 354 VIALVGPTGAGKTTTIAKLAQRFAAQ----------HTPRDVALVTTDTQRV--GGREQLHSYGRQLGIAVHEADSAESL 421
Cdd:TIGR00176 1 VLQIVGPKNSGKTTLIERLVKALKARgyrvatikhdHHDFDIDKNGKDSYRHreAGADQVIVASSRRYAFMHETQEERDL 80
|
90
....*....|....*
gi 1126961737 422 LDLFERLRDYKLVLI 436
Cdd:TIGR00176 81 EALLDRLPDLDIILV 95
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
349-376 |
9.26e-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: 9.26e-04
10 20
....*....|....*....|....*...
gi 1126961737 349 LERGGVIALVGPTGAGKtTTIAKLAQRF 376
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 ... |
339-451 |
1.48e-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: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 339 KRLPVAPVDPL----ERGGVIALVGPTGAGKTTTIAKLA------------QRFAAQHTPRDV----ALVTTDT---QRV 395
Cdd:cd03266 14 VKKTVQAVDGVsftvKPGEVTGLLGPNGAGKTTTLRMLAgllepdagfatvDGFDVVKEPAEArrrlGFVSDSTglyDRL 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1126961737 396 GGREQLHSYGRQLGIAVHEADSAesLLDLFERLRDYKLVLIDTAGM--GQRDRALAAQ 451
Cdd:cd03266 94 TARENLEYFAGLYGLKGDELTAR--LEELADRLGMEELLDRRVGGFstGMRQKVAIAR 149
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
312-518 |
1.58e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 41.09 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 312 LTRDVAMQIP-ADTELHRGRGLMLGLLSKRLPVApVDPLERGGV--IALVGPTGAGKTTTIAKLAQRFAAQHTprDVALV 388
Cdd:COG3451 162 TTSNLAALFPfHSFELGDPWGIYLLNTRSGTPVF-FDFHDGLDNgnTLILGPSGSGKSFLLKLLLLQLLRYGA--RIVIF 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 389 TTD------TQRVGGREQLHSYGRQLGIA----VHEADSAESLLDLFERlrdykLVLIDTAGMGQRDRALaaqlnWLRAA 458
Cdd:COG3451 239 DPGgsyeilVRALGGTYIDLSPGSPTGLNpfdlEDTEEKRDFLLELLEL-----LLGREGEPLTPEERAA-----IDRAV 308
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 459 QQVTSLLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDETGSFGSALsvvvDHQMPITW 518
Cdd:COG3451 309 RALYRRADPEERTTLSDLYELLKEQPEAKDLAARLEPYTKGGSYGWLF----DGPTNLDL 364
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
354-495 |
1.64e-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: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 354 VIALVGPT-GAGKTTTIAKLAQRFAAQHtpRDVALVTTDtqrvggreqlhsygrqlgiavheadsaeslldlferlrdyK 432
Cdd:cd01983 2 VIAVTGGKgGVGKTTLAAALAVALAAKG--YKVLLIDLD----------------------------------------D 39
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 433 LVLIDTAGMGQRDRALAAQLNWLRAaqQVTSLLVLPANAHFSDLDEVVRRFAHA-------KPQGVVLTK 495
Cdd:cd01983 40 YVLIDGGGGLETGLLLGTIVALLAL--KKADEVIVVVDPELGSLLEAVKLLLALlllgigiRPDGIVLNK 107
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
349-444 |
2.03e-03 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 40.05 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 349 LERGGVIALVGPTGAGKTTTI-------------AKLAQRFAAQHTP---RDVALVttdTQRVG------GREQLHSYGR 406
Cdd:COG1131 23 VEPGEIFGLLGPNGAGKTTTIrmllgllrptsgeVRVLGEDVARDPAevrRRIGYV---PQEPAlypdltVRENLRFFAR 99
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1126961737 407 QLGIAVHEADS-AESLLDLFErLRDYKLVLIDT--AGMGQR 444
Cdd:COG1131 100 LYGLPRKEARErIDELLELFG-LTDAADRKVGTlsGGMKQR 139
|
|
| MobB |
cd03116 |
molybdopterin-guanine dinucleotide biosynthesis protein B; Molybdenum is an essential trace ... |
354-436 |
2.59e-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: 38.77 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 354 VIALVGPTGAGKTTTIAKLAQRFAAQ--------HTPRDVALVT--TDT---QRVGGREQLHSYGRQLGIAVHEADSAES 420
Cdd:cd03116 2 IVGVVGKSGSGKTTLIEKLIPELKARglrvavikHTHHGFDIDTpgKDSyrhRQAGADAVLVSSPNRLALIHERPEWELT 81
|
90
....*....|....*.
gi 1126961737 421 LLDLFERLRDYKLVLI 436
Cdd:cd03116 82 LLELLARFSDVDLVLV 97
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
352-376 |
4.11e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 39.94 E-value: 4.11e-03
10 20
....*....|....*....|....*
gi 1126961737 352 GGVIALVGPTGAGKTTTIAkLAQRF 376
Cdd:PRK13657 361 GQTVAIVGPTGAGKSTLIN-LLQRV 384
|
|
| Kti12 |
COG4088 |
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ... |
349-391 |
4.41e-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: 4.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1126961737 349 LERGGVIALVGPTGAGKTTTIAKLAQRFAAQHtpRDVALVTTD 391
Cdd:COG4088 1 MDSPMLLILTGPPGSGKTTFAKALAQRLYAEG--IAVALLHSD 41
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
350-376 |
4.65e-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: 4.65e-03
10 20
....*....|....*....|....*..
gi 1126961737 350 ERGGVIALVGPTGAGKtTTIAKLAQRF 376
Cdd:cd03251 26 PAGETVALVGPSGSGK-STLVNLIPRF 51
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
349-456 |
4.75e-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: 38.01 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 349 LERGGVIALVGPTGAGKTTtiakLAQRFAAQHTPrDVALVTTDTQRVGGREqLHSYGRQLGIaVHEADSAESLLDLFERL 428
Cdd:pfam00005 8 LNPGEILALVGPNGAGKST----LLKLIAGLLSP-TEGTILLDGQDLTDDE-RKSLRKEIGY-VFQDPQLFPRLTVRENL 80
|
90 100
....*....|....*....|....*...
gi 1126961737 429 RdYKLVLIDTAGMGQRDRALAAqLNWLR 456
Cdd:pfam00005 81 R-LGLLLKGLSKREKDARAEEA-LEKLG 106
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
349-485 |
5.49e-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: 37.61 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 349 LERGGVIALVGPTGAGKTT---TIAKLAQRFA--AQHTPRDVALVTTDTQR--VGGREQLhSYG-RQLgIAVheadsAES 420
Cdd:cd00267 22 LKAGEIVALVGPNGSGKSTllrAIAGLLKPTSgeILIDGKDIAKLPLEELRrrIGYVPQL-SGGqRQR-VAL-----ARA 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1126961737 421 LldlferLRDYKLVLID--TAGMGQRDRALAAQLnwLR--AAQQVTSLLVLPanaHFSDLDEVVRRFAH 485
Cdd:cd00267 95 L------LLNPDLLLLDepTSGLDPASRERLLEL--LRelAEEGRTVIIVTH---DPELAELAADRVIV 152
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
349-474 |
7.77e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 38.73 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 349 LERGGVIALVGPTGAGKTTTIAKLAQRFAA-------QHTPRDVALVTTDTQRVGGREQLHSYGRQLGIAVHEADS---- 417
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLAAAVAAggpwlgrRVPPGKVLYLAAEDDRGELRRRLKALGADLGLPFADLDGrlrl 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1126961737 418 --------AESLLDLFERL---RDYKLVLIDTAG--MG------QRDRALAAQLNWLRAAQQVTSLLVlpanAHFS 474
Cdd:COG3598 90 lslagdldDTDDLEALERAieeEGPDLVVIDPLArvFGgdendaEEMRAFLNPLDRLAERTGAAVLLV----HHTG 161
|
|
| KaiC-like |
cd01124 |
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. ... |
349-462 |
9.28e-03 |
|
Circadian Clock Protein KaiC; KaiC is a circadian clock protein, most studied in cyanobacteria. KaiC, an autokinase, autophosphatase, and ATPase, is part of the core oscillator, composed of three proteins: KaiA, KaiB, and KaiC. The circadian oscillation is regulated via KaiC phosphorylation.
Pssm-ID: 410869 [Multi-domain] Cd Length: 222 Bit Score: 38.01 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 349 LERGGVIALVGPTGAGKTTtiakLAQRFAAQHTPRD--VALVTTDTQRVGGREQLHSYGRQLG-------IAVHEADSAE 419
Cdd:cd01124 16 IPKGSVTLLTGGPGTGKTL----FGLQFLYAGAKNGepGLFFTFEESPERLLRNAKSFGWDFDemedegkLIIVDAPPTE 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1126961737 420 SLLDLFERLR----------DYKLVLIDTAG---MGQRD-----RALAAQLNWLRAAQQVT 462
Cdd:cd01124 92 AGRFSLDELLsrilsiiksfKAKRVVIDSLSglrRAKEDqmrarRIVIALLNELRAAGVTT 152
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
350-444 |
9.84e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 38.17 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126961737 350 ERGGVIALVGPTGAGKTTTIAKLAQRFAA-------QHTPRDVAlvttDTQRVGG-------------REQLHSYGRQLG 409
Cdd:COG4152 25 PKGEIFGLLGPNGAGKTTTIRIILGILAPdsgevlwDGEPLDPE----DRRRIGYlpeerglypkmkvGEQLVYLARLKG 100
|
90 100 110
....*....|....*....|....*....|....*....
gi 1126961737 410 IAVHEADsaESLLDLFERLR--DYKLVLIDT--AGMGQR 444
Cdd:COG4152 101 LSKAEAK--RRADEWLERLGlgDRANKKVEElsKGNQQK 137
|
|
| |
