|
Name |
Accession |
Description |
Interval |
E-value |
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
1-435 |
0e+00 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 723.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 1 MFESLSDRLTGALRGLGGKGRLTEADINATAREIRLALLEADVSLEVVRTFIKRIKERA--NEIIGSqtVNPANQIIEVV 78
Cdd:COG0541 1 MFENLSERLQGAFKKLRGKGRLTEENIKEALREVRRALLEADVNLKVVKDFIERVKERAlgEEVLKS--LTPGQQVIKIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 79 NEELINILGGETRRLNMSKQPPTVIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQLEIVAERAGVPC 158
Cdd:COG0541 79 HDELVELLGGENEELNLAKKPPTVIMMVGLQGSGKTTTAAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 159 FAPfpgtsldsthemgTSEDNPVDAAFRGLAYARQHRHDVVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVIDSMIG 238
Cdd:COG0541 159 FPE-------------EDGKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAAVNPDETLLVVDAMTG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 239 QDAVETAKAFRDGVDFTGVVLTKLDGDARGGAALSIREVTGKPILFASTGEKLEDFDVFHPDRMASRILGMGDLKTLVEV 318
Cdd:COG0541 226 QDAVNVAKAFNEALGLTGVILTKLDGDARGGAALSIRAVTGKPIKFIGTGEKLDDLEPFHPDRMASRILGMGDVLSLIEK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 319 ASKEIDHEQAAKSAQKIGSGELTLEDFLEQMMMVRKMGPIGNILKMLPGGAEMSKAAEM-VDEKQLDRIEAIIRGMTPEE 397
Cdd:COG0541 306 AQEAIDEEEAEKLAKKLKKGKFDLEDFLEQLQQMKKMGPLKKLLGMLPGMGKLKQLKDLdIDEKELKRIEAIINSMTPEE 385
|
410 420 430
....*....|....*....|....*....|....*...
gi 740843391 398 RENPKILNASRRRRIANGSGVSVSEVNQLIERFNEARK 435
Cdd:COG0541 386 RRNPDIINGSRKRRIAKGSGTTVQDVNRLLKQFEQMKK 423
|
|
| ffh |
TIGR00959 |
signal recognition particle protein; This model represents Ffh (Fifty-Four Homolog), the ... |
2-437 |
0e+00 |
|
signal recognition particle protein; This model represents Ffh (Fifty-Four Homolog), the protein component that forms the bacterial (and organellar) signal recognition particle together with a 4.5S RNA. Ffh is a GTPase homologous to eukaryotic SRP54 and also to the GTPase FtsY (TIGR00064) that is the receptor for the signal recognition particle. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273364 [Multi-domain] Cd Length: 428 Bit Score: 600.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 2 FESLSDRLTGALRGLGGKGRLTEADINATAREIRLALLEADVSLEVVRTFIKRIKERA--NEIIGSqtVNPANQIIEVVN 79
Cdd:TIGR00959 1 FESLSERLQRIFKKLSGRGTITEKNIKEALREIRLALLEADVNLQVVKDFIKKVKEKAlgQEVLKS--LSPGQQFIKIVH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 80 EELINILGGETRRLNMSKQPPTVIMLAGLQGAGKTTLAGKLARYLT-DQGHTPVLVACDLQRPGAVQQLEIVAERAGVPC 158
Cdd:TIGR00959 79 EELVAILGGENAELNLAKKPPTVILMVGLQGSGKTTTCGKLAYYLKkKQGKKVLLVACDLYRPAAIEQLKVLGQQVGVPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 159 FAPFPGTSldsthemgtsednPVDAAFRGLAYARQHRHDVVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVIDSMIG 238
Cdd:TIGR00959 159 FALGKGQS-------------PVEIARRALEYAKENGFDVVIVDTAGRLQIDEELMEELAAIKEILNPDEILLVVDAMTG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 239 QDAVETAKAFRDGVDFTGVVLTKLDGDARGGAALSIREVTGKPILFASTGEKLEDFDVFHPDRMASRILGMGDLKTLVEV 318
Cdd:TIGR00959 226 QDAVNTAKTFNERLGLTGVVLTKLDGDARGGAALSVRSVTGKPIKFIGVGEKIDDLEPFHPERMASRILGMGDILSLVEK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 319 ASKEIDHEQAAKSAQKIGSGELTLEDFLEQMMMVRKMGPIGNILKMLPGGAEMSKAAEMVD--EKQLDRIEAIIRGMTPE 396
Cdd:TIGR00959 306 AQEVVDEEEAKKLAEKMKKGQFDLEDFLEQLRQIKKMGPLSSLLKMIPGMGGVKPSLSDADldEKQFKRIEAIISSMTPE 385
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 740843391 397 ERENPKILNASRRRRIANGSGVSVSEVNQLIERFNEARKMM 437
Cdd:TIGR00959 386 ERRNPKILNPSRRKRIAAGSGTTVQDVNKLIKRFEQMKKMM 426
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
5-448 |
9.62e-166 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 477.01 E-value: 9.62e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 5 LSDRLTGALRGLGGKGRLTEADINATAREIRLALLEADVSLEVVRTFIKRIKERANEIIGSQTVNPANQIIEVVNEELIN 84
Cdd:PRK00771 1 LGESLRDALKKLAGKSRIDEKTVKEVVKDIQRALLQADVNVKLVKELSKSIKERALEEEPPKGLTPREHVIKIVYEELVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 85 ILGGETRRLNMSKQPpTVIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQLEIVAERAGVPCFApfpg 164
Cdd:PRK00771 81 LLGEETEPLVLPLKP-QTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYG---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 165 tsldsthemGTSEDNPVDAAFRGLAYARQHrhDVVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVIDSMIGQDAVET 244
Cdd:PRK00771 156 ---------DPDNKDAVEIAKEGLEKFKKA--DVIIVDTAGRHALEEDLIEEMKEIKEAVKPDEVLLVIDATIGQQAKNQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 245 AKAFRDGVDFTGVVLTKLDGDARGGAALSIREVTGKPILFASTGEKLEDFDVFHPDRMASRILGMGDLKTLVEVASKEID 324
Cdd:PRK00771 225 AKAFHEAVGIGGIIITKLDGTAKGGGALSAVAETGAPIKFIGTGEKIDDLERFDPDRFISRLLGMGDLESLLEKVEEALD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 325 HEQAAKSAQKIGSGELTLEDFLEQMMMVRKMGPIGNILKMLPG-GAEMSKAAEMVDEKQLDRIEAIIRGMTPEERENPKI 403
Cdd:PRK00771 305 EEEEEKDVEKMMKGKFTLKDMYKQLEAMNKMGPLKQILQMLPGlGGKLPDEALEVTEEKLKKYKAIMDSMTEEELENPEI 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 740843391 404 LNASRRRRIANGSGVSVSEVNQLIERFNEARKMMAQMAGRFGMGG 448
Cdd:PRK00771 385 INASRIRRIARGSGTTVEDVRELLKYYKMMKKAMKQLKKGKGKMG 429
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
101-306 |
1.23e-101 |
|
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: 304.14 E-value: 1.23e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 101 TVIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQLEIVAERAGVPCFAPFPGTSldsthemgtsednP 180
Cdd:cd18539 1 TVILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQS-------------P 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 181 VDAAFRGLAYARQHRHDVVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVIDSMIGQDAVETAKAFRDGVDFTGVVLT 260
Cdd:cd18539 68 VDIAKRALEKAKEEGFDVVIVDTAGRLHIDEELMDELKEIKEVLNPDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 740843391 261 KLDGDARGGAALSIREVTGKPILFASTGEKLEDFDVFHPDRMASRI 306
Cdd:cd18539 148 KLDGDARGGAALSIRHVTGKPIKFIGVGEKIEDLEPFHPDRMASRI 193
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
100-308 |
8.80e-98 |
|
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: 294.32 E-value: 8.80e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 100 PTVIMLAGLQGAGKTTLAGKLARYLTDQG-HTPVLVACDLQRPGAVQQLEIVAERAGVPCFAPFPGTsldsthemgtsed 178
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGA------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 179 NPVDAAFRGLAYARQHRHDVVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVIDSMIGQDAVETAKAFRDGVDFTGVV 258
Cdd:smart00962 68 DPVAVAKDAVELAKARGYDVVLIDTAGRLHNDENLMEELKKIKRVIKPDEVLLVSDATTGQDAVEQAKAFNEALGLTGII 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 740843391 259 LTKLDGDARGGAALSIREVTGKPILFASTGEKLEDFDVFHPDRMASRILG 308
Cdd:smart00962 148 LTKLDGTAKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLLG 197
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
5-440 |
8.32e-97 |
|
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: 300.21 E-value: 8.32e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 5 LSDRLTGALRGLGGKGRLTEADINATAREIRLALLEADVSLEVVRTFIKRIKERANEIIGSQTVNPANQIIEVVNEELIN 84
Cdd:TIGR01425 5 LGSSLVTALRSMSSATVIDEEVINTMLKEICTALLESDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQDAVFEELCN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 85 ILGGETRRLNMSKQPPTVIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQLEIVAERAGVPCFAPFpg 164
Cdd:TIGR01425 85 LVDPGVEAFTPKKGKTCVIMFVGLQGAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYGSY-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 165 tsldsthemgtSEDNPVDAAFRGLAYARQHRHDVVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVIDSMIGQDAVET 244
Cdd:TIGR01425 163 -----------EESDPVKIASEGVEKFRKEKFDIIIVDTSGRHKQEKELFEEMQQVREAIKPDSIIFVMDGSIGQAAFGQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 245 AKAFRDGVDFTGVVLTKLDGDARGGAALSIREVTGKPILFASTGEKLEDFDVFHPDRMASRILGMGDLKTLVEVASKEID 324
Cdd:TIGR01425 232 AKAFKDSVEVGSVIITKLDGHAKGGGALSAVAATKSPIIFIGTGEHVDEFEIFDAEPFVSKLLGMGDLKGLIDKVQDLAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 325 HEQAAKSAQKIGSGELTLEDFLEQMMMVRKMGPIGNILKMLPGGAE--MSKAAEMVDEKQLDRIEAIIRGMTPEERE-NP 401
Cdd:TIGR01425 312 NDEEKTLIEHLKEGTFTLRDWYEQFQNLLKMGPLGNIMSMIPGLSHpmMSKGNEEETSAKIKVFMTIMDSMTDRELDsTA 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 740843391 402 KIL--NASRRRRIANGSGVSVSEVNQLIERFnearKMMAQM 440
Cdd:TIGR01425 392 KTMlkDPSRIRRVARGSGRDIREVNELLEQY----KLFAQM 428
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
101-306 |
1.22e-92 |
|
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: 280.97 E-value: 1.22e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 101 TVIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQLEIVAERAGVPCFAPFPGTSldsthemgtsednP 180
Cdd:pfam00448 1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGAD-------------P 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 181 VDAAFRGLAYARQHRHDVVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVIDSMIGQDAVETAKAFRDGVDFTGVVLT 260
Cdd:pfam00448 68 AAVAFDAVEKAKAENYDVVLVDTAGRLQNDKNLMDELKKIKRVVAPDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 740843391 261 KLDGDARGGAALSIREVTGKPILFASTGEKLEDFDVFHPDRMASRI 306
Cdd:pfam00448 148 KLDGDAKGGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
1-308 |
1.83e-84 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 263.81 E-value: 1.83e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 1 MFESLSDRL-------TGALRGL-GGKGRLTEADINatarEIRLALLEADVSLEVVRTFIKRIKERANEiigsQTVNPAN 72
Cdd:COG0552 1 FFERLKEGLsktrsglGEKLKSLfSGKKKIDEDLLE----ELEELLIEADVGVETTEEIIEELRERVKR----KKLKDPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 73 QIIEVVNEELINILGGETRRLNMSKQPPTVIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQLEIVAE 152
Cdd:COG0552 73 ELKEALKEELLEILDPVDKPLAIEEKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 153 RAGVPCFApfpgtsldstHEMGTsednpvDAA---FRGLAYARQHRHDVVIIDTAGRLGIDEVLMKQARDIRDAIN---- 225
Cdd:COG0552 153 RVGVPVIA----------QKEGA------DPAavaFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKkldp 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 226 --PHEVLFVIDSMIGQDAVETAKAFRDGVDFTGVVLTKLDGDARGGAALSIREVTGKPILFASTGEKLEDFDVFHPDRMA 303
Cdd:COG0552 217 daPHEVLLVLDATTGQNALSQAKVFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFV 296
|
....*
gi 740843391 304 SRILG 308
Cdd:COG0552 297 DALFG 301
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
21-308 |
3.92e-72 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 233.33 E-value: 3.92e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 21 RLTEADINATAREIRLALLEADVSLEVVRTFIKRIKERANEIIGSQTVNPANQIIEVVNEELINILGgETRRLNM----- 95
Cdd:PRK14974 57 EIKEKDIEDLLEELELELLESDVALEVAEEILESLKEKLVGKKVKRGEDVEEIVKNALKEALLEVLS-VGDLFDLieeik 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 96 SKQPPTVIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQLEIVAERAGVPCFapfpgtsldsTHEMGT 175
Cdd:PRK14974 136 SKGKPVVIVFVGVNGTGKTTTIAKLAYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVI----------KHKYGA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 176 sedNPVDAAFRGLAYARQHRHDVVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVIDSMIGQDAVETAKAFRDGVDFT 255
Cdd:PRK14974 206 ---DPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDANLMDELKKIVRVTKPDLVIFVGDALAGNDAVEQAREFNEAVGID 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 740843391 256 GVVLTKLDGDARGGAALSIREVTGKPILFASTGEKLEDFDVFHPDRMASRILG 308
Cdd:PRK14974 283 GVILTKVDADAKGGAALSIAYVIGKPILFLGVGQGYDDLIPFDPDWFVDKLLG 335
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
102-306 |
6.63e-71 |
|
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: 224.95 E-value: 6.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 102 VIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQLEIVAERAGVPCFAPFPGTSldsthemgtsednPV 181
Cdd:cd03115 2 VILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGTD-------------PA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 182 DAAFRGLAYARQHRHDVVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVIDSMIGQDAVETAKAFRDGVDFTGVVLTK 261
Cdd:cd03115 69 SIAQEAVEKAKLEGYDVLLVDTAGRLQKDEPLMEELKKVKEVESPDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTK 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 740843391 262 LDGDARGGAALSIREVTGKPILFASTGEKLEDFDVFHPDRMASRI 306
Cdd:cd03115 149 LDGTAKGGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
6-308 |
3.78e-70 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 227.29 E-value: 3.78e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 6 SDRLTGALRGLGGKGRLTEADINatarEIRLALLEADVSLEVVRTFIKRIKERANEiigsQTVNPANQIIEVVNEELINI 85
Cdd:PRK10416 28 RENFGEGINGLFAKKKIDEDLLE----ELEELLIEADVGVETTEEIIEELRERVKR----KNLKDPEELKELLKEELAEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 86 LGGETRRLNMSKQPPTVIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQLEIVAERAGVPCFAPFPGT 165
Cdd:PRK10416 100 LEPVEKPLNIEEKKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQVWGERVGVPVIAQKEGA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 166 sldsthemgtsednpvDAA---FRGLAYARQHRHDVVIIDTAGRLGIDEVLMKQARDIRDAIN------PHEVLFVIDSM 236
Cdd:PRK10416 180 ----------------DPAsvaFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKkadpdaPHEVLLVLDAT 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740843391 237 IGQDAVETAKAFRDGVDFTGVVLTKLDGDARGGAALSIREVTGKPILFASTGEKLEDFDVFHPDRMASRILG 308
Cdd:PRK10416 244 TGQNALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLG 315
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
33-307 |
1.27e-67 |
|
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: 219.44 E-value: 1.27e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 33 EIRLALLEADVSLEVVRTFIKRIKERANEiigsQTVNPANQIIEVVNEELINIL-----GGETRRLNMSKQPPTVIMLAG 107
Cdd:TIGR00064 9 ELEEILLESDVGYEVVEKIIEALKKELKG----KKVKDAEKLKEILKEYLKEILkedllKNTDLELIVEENKPNVILFVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 108 LQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQLEIVAERAGVPCFAPFPGTsldsthemgtsedNPVDAAFRG 187
Cdd:TIGR00064 85 VNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGA-------------DPAAVAFDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 188 LAYARQHRHDVVIIDTAGRLGIDEVLMKQARDI------RDAINPHEVLFVIDSMIGQDAVETAKAFRDGVDFTGVVLTK 261
Cdd:TIGR00064 152 IQKAKARNIDVVLIDTAGRLQNKVNLMDELKKIkrvikkVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILTK 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 740843391 262 LDGDARGGAALSIREVTGKPILFASTGEKLEDFDVFHPDRMASRIL 307
Cdd:TIGR00064 232 LDGTAKGGIILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
102-306 |
2.18e-65 |
|
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: 210.51 E-value: 2.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 102 VIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQLEIVAERAGVPCFAPFpgtsldsthemgtSEDNPV 181
Cdd:cd17875 2 VIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSY-------------TEKDPV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 182 DAAFRGLAYARQHRHDVVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVIDSMIGQDAVETAKAFRDGVDFTGVVLTK 261
Cdd:cd17875 69 KIAKEGVEKFKKEKFDIIIVDTSGRHKQEEELFEEMKQISDAVKPDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITK 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 740843391 262 LDGDARGGAALSIREVTGKPILFASTGEKLEDFDVFHPDRMASRI 306
Cdd:cd17875 149 LDGHAKGGGALSAVAATGAPIIFIGTGEHIDDLEPFDPKRFVSRL 193
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
101-306 |
3.51e-63 |
|
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: 205.11 E-value: 3.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 101 TVIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQLEIVAERAGVPCFAPFPGTsldsthemgtsedNP 180
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGA-------------DP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 181 VDAAFRGLAYARQHRHDVVIIDTAGRLGIDEVLMKQARDIRDAIN------PHEVLFVIDSMIGQDAVETAKAFRDGVDF 254
Cdd:cd17874 68 AAVAFDAIQAAKARGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKkkdpeaPHEVLLVLDATTGQNALEQAKEFNEAVGL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 740843391 255 TGVVLTKLDGDARGGAALSIREVTGKPILFASTGEKLEDFDVFHPDRMASRI 306
Cdd:cd17874 148 TGIILTKLDGTAKGGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SRP_SPB |
pfam02978 |
Signal peptide binding domain; |
339-435 |
8.84e-43 |
|
Signal peptide binding domain;
Pssm-ID: 460771 [Multi-domain] Cd Length: 95 Bit Score: 147.54 E-value: 8.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 339 ELTLEDFLEQMMMVRKMGPIGNILKMLPGgaeMSKAAEMVD-EKQLDRIEAIIRGMTPEERENPKILNASRRRRIANGSG 417
Cdd:pfam02978 1 KFTLRDFLEQLQQIKKMGPLSKILSMIPG---MGKKDDDIDsEKKLKRIEAIIDSMTPKERDNPDIINASRKRRIARGSG 77
|
90
....*....|....*...
gi 740843391 418 VSVSEVNQLIERFNEARK 435
Cdd:pfam02978 78 TSVQEVNRLLKQFKQMKK 95
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
102-300 |
1.34e-34 |
|
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: 129.27 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 102 VIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQLEIVAERAGVPCFapfpgtsldsthEMGTSEDnPV 181
Cdd:cd17876 2 VIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELY------------EKGYGKD-PA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 182 DAAFRGLAYARQHRHDVVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVIDSMIGQDAVETAK----AFRDGVDFT-- 255
Cdd:cd17876 69 AVAKEAIKYARDQGFDVVLIDTAGRMQNNEPLMRALAKLIKENNPDLVLFVGEALVGNDAVDQLKkfnqALADYSPSDnp 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 740843391 256 ----GVVLTKLDG-DARGGAALSIREVTGKPILFASTGEKLEDFDVFHPD 300
Cdd:cd17876 149 rlidGIVLTKFDTiDDKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVK 198
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
9-308 |
2.59e-33 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 129.99 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 9 LTGALRGLGGKGRLTEADINATAREIRLALLEADVSLEVVRTFIKRIKERANeiigsqtvnpANQIIEVVNEELINILGG 88
Cdd:COG1419 86 LKELLEEQLSGLAGESARLPPELAELLERLLEAGVSPELARELLEKLPEDLS----------AEEAWRALLEALARRLPV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 89 ETRRLNmskQPPTVIMLAGLQGAGKTTLAGKLA-RYLTDQGHTPVLVACDLQRPGAVQQLEIVAERAGVPCFAPFPGTSL 167
Cdd:COG1419 156 AEDPLL---DEGGVIALVGPTGVGKTTTIAKLAaRFVLRGKKKVALITTDTYRIGAVEQLKTYARILGVPVEVAYDPEEL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 168 DSThemgtsednpvdaafrglayARQHRH-DVVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVID-SMIGQDAVETA 245
Cdd:COG1419 233 KEA--------------------LERLRDkDLVLIDTAGRSPRDPELIEELKALLDAGPPIEVYLVLSaTTKYEDLKEIV 292
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740843391 246 KAFRDgVDFTGVVLTKLDGDARGGAALSIREVTGKPILFASTGEKL-EDFDVFHPDRMASRILG 308
Cdd:COG1419 293 EAFSS-LGLDGLILTKLDETASLGSILNLLIRTGLPLSYITNGQRVpEDIEVADPERLARLLLG 355
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
102-306 |
5.09e-24 |
|
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: 99.16 E-value: 5.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 102 VIMLAGLQGAGKTTLAGKLA-RYLTDQGHTPVLVACDLQRPGAVQQLEIVAERAGVPCFAPFPGTSLDSthemgtsednp 180
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAaRYVLKKGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEVAEDPEDLAD----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 181 vdaafrglAYARQHRHDVVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVIDS-MIGQDAVETAKAFRdGVDFTGVVL 259
Cdd:cd17873 71 --------ALERLSDRDLILIDTAGRSPRDKEQLEELKELLGAGEDIEVHLVLSAtTKAKDLKEIIERFS-PLGYRGLIL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 740843391 260 TKLDGDARGGAALSIREVTGKPILFASTGEKL-EDFDVFHPDRMASRI 306
Cdd:cd17873 142 TKLDETTSLGSVLSVLAESQLPVSYVTTGQRVpEDIEVASPLRLARLL 189
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
5-82 |
1.12e-21 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 88.68 E-value: 1.12e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740843391 5 LSDRLTGALRGLGGKGRLTEADINATAREIRLALLEADVSLEVVRTFIKRIKERAneiIGSQTVNPANQIIEVVNEEL 82
Cdd:pfam02881 1 LGEKLSSLFKGLRGKGKIDEEDLEEALKELEEALLEADVGVEVVKKIIERLREKA---VGEKKLKPPQEVKKILKEEL 75
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
9-86 |
7.22e-18 |
|
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle 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.
Pssm-ID: 214941 [Multi-domain] Cd Length: 77 Bit Score: 77.98 E-value: 7.22e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740843391 9 LTGALRGLGGKGRLTEADINATAREIRLALLEADVSLEVVRTFIKRIKERANEIIgSQTVNPANQIIEVVNEELINIL 86
Cdd:smart00963 1 LSKALGKLLGELFLTEKDDEELLEELEEALLEADVGVEVVKEIIERVKEKAKGEV-LKGLTPKQEVKKILKEELVKIL 77
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
33-308 |
3.41e-15 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 77.63 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 33 EIRLALLEADVSLEVVRTFIKRIKERANEIIGsqtvnpanQIIEVVNEELINILGGETRRLNMSKQpptVIMLAGLQGAG 112
Cdd:PRK05703 165 ELYKRLKRSGLSPEIAEKLLKLLLEHMPPRER--------TAWRYLLELLANMIPVRVEDILKQGG---VVALVGPTGVG 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 113 KTT-LAgKLA-RYLTDQGHTPV-LVACDLQRPGAVQQLEIVAERAGVP---CFapfpgtsldsthemgTSEDnpvdaafr 186
Cdd:PRK05703 234 KTTtLA-KLAaRYALLYGKKKVaLITLDTYRIGAVEQLKTYAKIMGIPvevVY---------------DPKE-------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 187 gLAYA-RQHRH-DVVIIDTAGRLGIDEVLMKQARD-IRDAINPHEVLFVIdSMIGQ--DAVETAKAFRDgVDFTGVVLTK 261
Cdd:PRK05703 290 -LAKAlEQLRDcDVILIDTAGRSQRDKRLIEELKAlIEFSGEPIDVYLVL-SATTKyeDLKDIYKHFSR-LPLDGLIFTK 366
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 740843391 262 LDGDARGGAALSIREVTGKPILFASTGEKL-EDFDVFHPDRMASRILG 308
Cdd:PRK05703 367 LDETSSLGSILSLLIESGLPISYLTNGQRVpDDIKVANPEELVRLLLG 414
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
85-313 |
1.23e-12 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 70.40 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 85 ILGGETRRLNMSKQPPT----VIMLAGLQGAGKTTLAGKLARYLTDQgHTP---VLVACDLQRPGAVQQLEIVAERAGVP 157
Cdd:PRK12727 331 MLGLLSKRLPVAPVDPLerggVIALVGPTGAGKTTTIAKLAQRFAAQ-HAPrdvALVTTDTQRVGGREQLHSYGRQLGIA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 158 CFAPFPGTSLDSTHEmgtsednpvdaafrglayaRQHRHDVVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVIDSMI 237
Cdd:PRK12727 410 VHEADSAESLLDLLE-------------------RLRDYKLVLIDTAGMGQRDRALAAQLNWLRAARQVTSLLVLPANAH 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740843391 238 GQDAVETAKAFrDGVDFTGVVLTKLDGDARGGAALSIREVTGKPILFASTGEKLEDfDVfHPDRMASRILGMGDLK 313
Cdd:PRK12727 471 FSDLDEVVRRF-AHAKPQGVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVPD-DL-HRANAASLVLRLEDLR 543
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
38-292 |
5.63e-12 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 67.78 E-value: 5.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 38 LLEADvslEVVRTFIKRIKERANEIIGSQTVNPANQIIEVVNEELINILGGEtrrlNMSKQPPTVIMLAGLQGAGKTTLA 117
Cdd:PRK11889 186 MLEQN---DVEQYFIHAYAEKLKVKFENATMITEEEVIEYILEDMRSHFNTE----NVFEKEVQTIALIGPTGVGKTTTL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 118 GKLARYLTDQGHTPVLVACDLQRPGAVQQLEIVAERAGVPCFApfpgtsldsthemgtSEDNPvdAAFRGLAYARQH-RH 196
Cdd:PRK11889 259 AKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIA---------------VRDEA--AMTRALTYFKEEaRV 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 197 DVVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVID-SMIGQDAVETAKAFRDgVDFTGVVLTKLDGDARGGAALSIR 275
Cdd:PRK11889 322 DYILIDTAGKNYRASETVEEMIETMGQVEPDYICLTLSaSMKSKDMIEIITNFKD-IHIDGIVFTKFDETASSGELLKIP 400
|
250
....*....|....*..
gi 740843391 276 EVTGKPILFASTGEKLE 292
Cdd:PRK11889 401 AVSSAPIVLMTDGQDVK 417
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
71-292 |
5.68e-11 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 63.23 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 71 ANQIIEVVNEELINILGGETRRLNMSKQPPTVIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQLEIV 150
Cdd:PRK06731 46 ATMITEEVIEYILEDMSSHFNTENVFEKEVQTIALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDY 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 151 AERAGVPCFApfpgtsldsthemgtSEDNPvdAAFRGLAYARQH-RHDVVIIDTAGRLGIDEVLMKQARDIRDAINPHEV 229
Cdd:PRK06731 126 VKTIGFEVIA---------------VRDEA--AMTRALTYFKEEaRVDYILIDTAGKNYRASETVEEMIETMGQVEPDYI 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740843391 230 LFVID-SMIGQDAVETAKAFRDgVDFTGVVLTKLDGDARGGAALSIREVTGKPILFASTGEKLE 292
Cdd:PRK06731 189 CLTLSaSMKSKDMIEIITNFKD-IHIDGIVFTKFDETASSGELLKIPAVSSAPIVLMTDGQDVK 251
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
32-205 |
1.23e-10 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 62.35 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 32 REIRLALLEADVSLEVVRTFIKRIKERANEIigsqtvnpanQIIEVVNEELINILGGETRRLNMSKQPpTVIMLAGLQGA 111
Cdd:TIGR03499 137 AKLYERLLEAGVSEELARELLEKLPEDADAE----------DAWRWLREALEGMLPVKPEEDPILEQG-GVIALVGPTGV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 112 GKTTLAGKLA-RYLTDQGHTPV-LVACDLQRPGAVQQLEIVAERAGVPCFApfpgtsLDSTHEMGTsednpvdaafrglA 189
Cdd:TIGR03499 206 GKTTTLAKLAaRFALEHGKKKVaLITTDTYRIGAVEQLKTYAEILGIPVKV------ARDPKELRE-------------A 266
|
170
....*....|....*.
gi 740843391 190 YARQHRHDVVIIDTAG 205
Cdd:TIGR03499 267 LDRLRDKDLILIDTAG 282
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
102-317 |
1.52e-09 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 60.14 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 102 VIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQLEIVAERagvpcfapfpgtsLDSTHEMGTSEDNpV 181
Cdd:PRK12726 208 IISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADK-------------LDVELIVATSPAE-L 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 182 DAAFRGLAYARQHRHdvVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVIDSMIGQDAVETAKAFRDGVDFTGVVLTK 261
Cdd:PRK12726 274 EEAVQYMTYVNCVDH--ILIDTVGRNYLAEESVSEISAYTDVVHPDLTCFTFSSGMKSADVMTILPKLAEIPIDGFIITK 351
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 740843391 262 LDGDARGGAALSIREVTGKPILFASTGEKLEDfDVFHPDR--MASRILGMgDLKTLVE 317
Cdd:PRK12726 352 MDETTRIGDLYTVMQETNLPVLYMTDGQNITE-NIFRPKSrwLAERFVGT-DRRQVLE 407
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
99-214 |
6.55e-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: 54.69 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 99 PPTVIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQLEIVAEragvpcfapfpgtsldsthEMGTSED 178
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV-------------------GGKKASG 61
|
90 100 110
....*....|....*....|....*....|....*.
gi 740843391 179 NPVDAAFRGLAYARQHRHDVVIIDTAGRLGIDEVLM 214
Cdd:smart00382 62 SGELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
102-290 |
9.97e-09 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 57.89 E-value: 9.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 102 VIMLAGLQGAGKTTLAGKL-ARYLTDQGHTPV-LVACDLQRPGAVQQLEIVAERAGVPCFApfpgtsldsthemgtsedn 179
Cdd:PRK14723 187 VLALVGPTGVGKTTTTAKLaARCVAREGADQLaLLTTDSFRIGALEQLRIYGRILGVPVHA------------------- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 180 PVDAA-FRGLAYARQHRHdVVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVIDSMIGQDAV-ETAKAFRDGV--DFT 255
Cdd:PRK14723 248 VKDAAdLRFALAALGDKH-LVLIDTVGMSQRDRNVSEQIAMLCGVGRPVRRLLLLNAASHGDTLnEVVHAYRHGAgeDVD 326
|
170 180 190
....*....|....*....|....*....|....*..
gi 740843391 256 GVVLTKLDGDARGGAAL--SIREVTgkPILFASTGEK 290
Cdd:PRK14723 327 GCIITKLDEATHLGPALdtVIRHRL--PVHYVSTGQK 361
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
38-293 |
1.81e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 56.65 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 38 LLEADVSLEVVRTFIKRIKERAneiiGSQTVNPANQIIEVVNEELINILGGETRRLNMSKqpptVIMLAGLQGAGKTTLA 117
Cdd:PRK14722 83 LFAAGFSAQLVRMIVDNLPEGE----GYDTLDAAADWAQSVLAANLPVLDSEDALMERGG----VFALMGPTGVGKTTTT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 118 GKLA-RYLTDQGHTPV-LVACDLQRPGAVQQLEIVAERAGVPCFAPFPGTSLDsthemgtsednpvdaafrgLAYARQHR 195
Cdd:PRK14722 155 AKLAaRCVMRFGASKVaLLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDLQ-------------------LALAELRN 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 196 HDVVIIDTAGRLGIDEVLMKQARDIRDAINPHEVLFVIDSMIGQDAV-ETAKAFRDGV--------DFTGVVLTKLDGDA 266
Cdd:PRK14722 216 KHMVLIDTIGMSQRDRTVSDQIAMLHGADTPVQRLLLLNATSHGDTLnEVVQAYRSAAgqpkaalpDLAGCILTKLDEAS 295
|
250 260
....*....|....*....|....*..
gi 740843391 267 RGGAALSIREVTGKPILFASTGEKLED 293
Cdd:PRK14722 296 NLGGVLDTVIRYKLPVHYVSTGQKVPE 322
|
|
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
110-290 |
1.28e-05 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 46.38 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 110 GAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAvqqlEIVAERAGvpcfapfpGTSLDSTHEMGTSEDNPVDAAFRGla 189
Cdd:PHA02518 11 GAGKTTVATNLASWLHADGHKVLLVDLDPQGSST----DWAEAREE--------GEPLIPVVRMGKSIRADLPKVASG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 190 yarqhrHDVVIIDTAGRlgiDEVLMKQARDIRDAI------NPHEVlFVIDSMIgqDAVETAKAFRDGVD-FTGVVLTKL 262
Cdd:PHA02518 77 ------YDYVVVDGAPQ---DSELARAALRIADMVlipvqpSPFDI-WAAPDLV--ELIKARQEVTDGLPkFAFIISRAI 144
|
170 180
....*....|....*....|....*...
gi 740843391 263 DGDARGGAALSIREVTGKPILFASTGEK 290
Cdd:PHA02518 145 KNTQLYREARKALAGYGLPILRNGTTQR 172
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
38-301 |
1.55e-05 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 47.27 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 38 LLEADVSLEVVRTFIKRIKERANEIIGSQTVNPANQIIEVVNEEL---INILGGETRrlNMSKqpptVIMLAGLQGAGKT 114
Cdd:PRK12724 164 LVREGMSQSYVEEMASKLEERLSPVDQGRNHNVTERAVTYLEERVsvdSDLFSGTGK--NQRK----VVFFVGPTGSGKT 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 115 TLAGKLA-RYLTDQGHTPVLVACDLQRPGAVQQLEIVAERAGVPCFAPFPGTSLDSTHEMGTSEdnpvdaafrglayarq 193
Cdd:PRK12724 238 TSIAKLAaKYFLHMGKSVSLYTTDNYRIAAIEQLKRYADTMGMPFYPVKDIKKFKETLARDGSE---------------- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 194 hrhdVVIIDTAGRLGIDEVLMKQARDI------RDAInphEVLFVIDSMIGQDAVETAKAFRDGVDFTGVVLTKLDGDAR 267
Cdd:PRK12724 302 ----LILIDTAGYSHRNLEQLERMQSFyscfgeKDSV---ENLLVLSSTSSYHHTLTVLKAYESLNYRRILLTKLDEADF 374
|
250 260 270
....*....|....*....|....*....|....
gi 740843391 268 GGAALSIREVTGKPILFASTGEKLEdFDVFHPDR 301
Cdd:PRK12724 375 LGSFLELADTYSKSFTYLSVGQEVP-FDILNATK 407
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
91-133 |
1.60e-05 |
|
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440295 [Multi-domain] Cd Length: 189 Bit Score: 45.85 E-value: 1.60e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 740843391 91 RRLNMSKQPPTVIMLAGLQGAGKTTLAGKLARYLTDQGHTPVL 133
Cdd:COG0529 7 ERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYL 49
|
|
| BY-kinase |
cd05387 |
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ... |
92-261 |
3.54e-05 |
|
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.
Pssm-ID: 349772 [Multi-domain] Cd Length: 190 Bit Score: 44.87 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 92 RLNMSKQPPTVIMLAG-LQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQLEIVAERaGV-----------PCF 159
Cdd:cd05387 11 LFAGSDAGPKVIAVTSaSPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEP-GLsevlsgqasleDVI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 160 APFPGTSLD---SthemGTSEDNPVD----AAFRGLAYARQHRHDVVIIDTAGRLGIDE--VLMKQArdirDAinpheVL 230
Cdd:cd05387 90 QSTNIPNLDvlpA----GTVPPNPSEllssPRFAELLEELKEQYDYVIIDTPPVLAVADalILAPLV----DG-----VL 156
|
170 180 190
....*....|....*....|....*....|....
gi 740843391 231 FVIDS-MIGQDAVETAKA--FRDGVDFTGVVLTK 261
Cdd:cd05387 157 LVVRAgKTRRREVKEALErlEQAGAKVLGVVLNK 190
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
100-232 |
1.42e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 42.49 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 100 PTVIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACD-----------LQRPGAVQQLEIVAERAGVPCFAPFPGTSLD 168
Cdd:pfam13191 24 PPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDenlpysplleaLTREGLLRQLLDELESSLLEAWRAALLEALA 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740843391 169 STHEMGTSEDNPVDAAFRG-LAYARQHRHDVVI-IDTAGRLgiDEVLMKQARDIRDAINPHEVLFV 232
Cdd:pfam13191 104 PVPELPGDLAERLLDLLLRlLDLLARGERPLVLvLDDLQWA--DEASLQLLAALLRLLESLPLLVV 167
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
102-137 |
2.76e-04 |
|
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: 40.49 E-value: 2.76e-04
10 20 30
....*....|....*....|....*....|....*..
gi 740843391 102 VIMLAGLQ-GAGKTTLAGKLARYLTDQGHTPVLVACD 137
Cdd:cd01983 2 VIAVTGGKgGVGKTTLAAALAVALAAKGYKVLLIDLD 38
|
|
| UMPK_like |
cd02028 |
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ... |
102-137 |
7.05e-04 |
|
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK).
Pssm-ID: 238986 [Multi-domain] Cd Length: 179 Bit Score: 40.75 E-value: 7.05e-04
10 20 30
....*....|....*....|....*....|....*.
gi 740843391 102 VIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACD 137
Cdd:cd02028 1 VVGIAGPSGSGKTTFAKKLSNQLRVNGIGPVVISLD 36
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
102-133 |
8.62e-04 |
|
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.
Pssm-ID: 238985 [Multi-domain] Cd Length: 149 Bit Score: 39.77 E-value: 8.62e-04
10 20 30
....*....|....*....|....*....|..
gi 740843391 102 VIMLAGLQGAGKTTLAGKLARYLTDQGHTPVL 133
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYV 32
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
100-129 |
8.73e-04 |
|
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
Pssm-ID: 396247 [Multi-domain] Cd Length: 154 Bit Score: 39.99 E-value: 8.73e-04
10 20 30
....*....|....*....|....*....|
gi 740843391 100 PTVIMLAGLQGAGKTTLAGKLARYLTDQGH 129
Cdd:pfam01583 2 GCTIWLTGLSGAGKSTIANALERKLFEQGR 31
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
92-223 |
9.56e-04 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 40.42 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 92 RLNMSKQPPTVIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACDLQR--PGAVQqleivaeragvpCFAPFPGTSLDS 169
Cdd:pfam06414 3 DKTTSQERPKAILLGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRElhPHYRE------------LQAADPKTASEY 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 740843391 170 THEmgtsednpvDAAF---RGLAYARQHRHDvVIIDTAGRLGidEVLMKQARDIRDA 223
Cdd:pfam06414 71 TQP---------DASRwveKLLQHAIENGYN-IILEGTLRSP--DVAKKIARALKAA 115
|
|
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
90-133 |
2.38e-03 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 39.54 E-value: 2.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 740843391 90 TRRLNMSKQPPTVIMLAGLQGAGKTTLAGKLARYLTDQG-HTPVL 133
Cdd:PRK03846 14 AQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGvSTYLL 58
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
101-267 |
3.25e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 39.88 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 101 TVIMLAGLQGAGKTTLAGKLARYL----------TDQGhtPVL-VACDLQRPGAVQQLEIVAERAGVPCFAPFPGTSLDS 169
Cdd:COG3598 14 GVTLLAGPPGTGKSFLALQLAAAVaaggpwlgrrVPPG--KVLyLAAEDDRGELRRRLKALGADLGLPFADLDGRLRLLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 170 thEMGTSEDNPVDAAFRglAYARQHRHDVVIIDTAGRL-GIDEV-------LMKQARDIRDAINPHeVLFV------IDS 235
Cdd:COG3598 92 --LAGDLDDTDDLEALE--RAIEEEGPDLVVIDPLARVfGGDENdaeemraFLNPLDRLAERTGAA-VLLVhhtgkgGAG 166
|
170 180 190
....*....|....*....|....*....|..
gi 740843391 236 MIGQDAVETAKAFRDGVDfTGVVLTKLDGDAR 267
Cdd:COG3598 167 KDSGDRARGSSALRGAAR-SVLVLSREKGEDL 197
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
110-267 |
3.50e-03 |
|
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.
Pssm-ID: 349760 [Multi-domain] Cd Length: 130 Bit Score: 37.90 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 110 GAGKTTLAGKLARYLTDQGHTPVLVACDLQrpgavqqleivaeragvpcfapfpgtsldsthemgtsednpvdaafrglA 189
Cdd:cd02042 11 GVGKTTLAVNLAAALALRGKRVLLIDLDPQ-------------------------------------------------G 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 190 YARQHRHDVVIIDTAGRLGIdevLMKQARDIRDAI----NPHEvlFVIDSMIG-QDAVETAKAFRD-GVDFTGVVLTKLD 263
Cdd:cd02042 42 SLTSWLYDYILIDTPPSLGL---LTRNALAAADLVlipvQPSP--FDLDGLAKlLDTLEELKKQLNpPLLILGILLTRVD 116
|
....
gi 740843391 264 GDAR 267
Cdd:cd02042 117 PRTK 120
|
|
| PRK00889 |
PRK00889 |
adenylylsulfate kinase; Provisional |
97-129 |
5.26e-03 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179157 Cd Length: 175 Bit Score: 38.08 E-value: 5.26e-03
10 20 30
....*....|....*....|....*....|...
gi 740843391 97 KQPPTVIMLAGLQGAGKTTLAGKLARYLTDQGH 129
Cdd:PRK00889 1 KQRGVTVWFTGLSGAGKTTIARALAEKLREAGY 33
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
21-268 |
6.41e-03 |
|
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440255 [Multi-domain] Cd Length: 289 Bit Score: 38.63 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 21 RLTEADINATAREIRLALLEADVSLEVVRTFIKRIKERANEIIGSQTVNPANQII---EVVNEELINILGGETRRLNMSK 97
Cdd:COG0489 10 LLREEAQALLLLLLLLLLLLRLEEAAAAAALAAAAPAAAAPAPLPPAPALLLLLLlllGLLLLLLLALALLLLLLLLLLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 98 QPPTVIMLA-GLQGAGKTTLAGKLARYLTDQGHTPVLVACDLQRPGAVQQL---------EIVAERAGVP-CFAPFPGTS 166
Cdd:COG0489 90 LLLEVIAVTsGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLglenrpglsDVLAGEASLEdVIQPTEVEG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 167 LD--StheMGTSEDNPVD----AAFRGLAYARQHRHDVVIIDTA-GRLGIDEVLMKQARDirdainphEVLFVIDS-MIG 238
Cdd:COG0489 170 LDvlP---AGPLPPNPSEllasKRLKQLLEELRGRYDYVIIDTPpGLGVADATLLASLVD--------GVLLVVRPgKTA 238
|
250 260 270
....*....|....*....|....*....|..
gi 740843391 239 QDAVETAKAF--RDGVDFTGVVLTKLDGDARG 268
Cdd:COG0489 239 LDDVRKALEMleKAGVPVLGVVLNMVCPKGER 270
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
99-222 |
7.01e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 37.12 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 99 PPTVIMLAGLQGAGKTTLAGKLARyltdqgHTPVlVACDLQR------------PGAVQQL--EIVAE--RAGVPcfapf 162
Cdd:COG4639 1 MLSLVVLIGLPGSGKSTFARRLFA------PTEV-VSSDDIRallggdendqsaWGDVFQLahEIARArlRAGRL----- 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740843391 163 pgTSLDSTHemgtsednpVDAAFRG--LAYARQHRHDVVII--DT---------AGRLGI--DEVLMKQARDIRD 222
Cdd:COG4639 69 --TVVDATN---------LQREARRrlLALARAYGALVVAVvlDVplevclarnAARDRQvpEEVIRRMLRRLRR 132
|
|
| GPN1 |
cd17870 |
GPN-loop GTPase 1; GPN-loop GTPase 1 (GPN1, also kown as MBD2-interacting protein or MBDin, ... |
101-137 |
7.58e-03 |
|
GPN-loop GTPase 1; GPN-loop GTPase 1 (GPN1, also kown as MBD2-interacting protein or MBDin, RNAPII-associated protein 4, and XPA-binding protein 1) is a GTPase is required for nuclear targeting of RNA polymerase II. It forms heterodimers with GPN3.
Pssm-ID: 349779 [Multi-domain] Cd Length: 241 Bit Score: 38.32 E-value: 7.58e-03
10 20 30
....*....|....*....|....*....|....*..
gi 740843391 101 TVIMLAGLQGAGKTTLAGKLARYLTDQGHTPVLVACD 137
Cdd:cd17870 1 VVIIVVGMAGSGKTTFVQRLNAYLHDNKKPPYVINLD 37
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
95-127 |
7.90e-03 |
|
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: 37.90 E-value: 7.90e-03
10 20 30
....*....|....*....|....*....|...
gi 740843391 95 MSKQPPTVIMLAGLQGAGKTTLAGKLARYLTDQ 127
Cdd:COG0572 2 ARSGKPRIIGIAGPSGSGKTTFARRLAEQLGAD 34
|
|
| CooC |
COG3640 |
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ... |
103-283 |
7.97e-03 |
|
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442857 [Multi-domain] Cd Length: 249 Bit Score: 38.22 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 103 IMLAGLQGAGKTTLAGKLARYLTDQGHtPVLV-----------ACDLQRPGA-----VQQLEIVAERAGVPCFAPFPGT- 165
Cdd:COG3640 3 IAVAGKGGVGKTTLSALLARYLAEKGK-PVLAvdadpnanlaeALGLEVEADlikplGEMRELIKERTGAPGGGMFKLNp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843391 166 SLDSTHE-------------MGTSEDN------PVDAAFRG-LAYARQHRHDVVIIDT-AG-----RLGIDEVlmkqard 219
Cdd:COG3640 82 KVDDIPEeylvegdgvdllvMGTIEEGgsgcycPENALLRAlLNHLVLGNYEYVVVDMeAGiehlgRGTAEGV------- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740843391 220 irDAInphevLFVIDSmiGQDAVETAKAFRD-----GVDFTGVVLTKLDGDArggAALSIREVTGKPIL 283
Cdd:COG3640 155 --DLL-----LVVSEP--SRRSIETARRIKElaeelGIKKIYLVGNKVREEE---DEEFLRELLGLELL 211
|
|
| |
