|
Name |
Accession |
Description |
Interval |
E-value |
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
391-607 |
2.04e-143 |
|
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: 413.93 E-value: 2.04e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 391 YVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLsalhppekhggrtMVQLFEKGYGKDA 470
Cdd:cd17876 1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRL-------------GVELYEKGYGKDP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 471 AGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALADHSMAQT 550
Cdd:cd17876 68 AAVAKEAIKYARDQGFDVVLIDTAGRMQNNEPLMRALAKLIKENNPDLVLFVGEALVGNDAVDQLKKFNQALADYSPSDN 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 966988840 551 PRLIDGIVLTKFDTIDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 607
Cdd:cd17876 148 PRLIDGIVLTKFDTIDDKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
269-608 |
1.02e-86 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 273.39 E-value: 1.02e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 269 SSDDEGAAQNSTKPSATKGTLGGMFGMLKglvgSKSLSREDMESVLDKMRDHLIAKNVAADIAVQLCESVANKLEGKVMG 348
Cdd:PRK14974 26 EEAPEAEEEEEEEDEEEKKEKPGFFDKAK----ITEIKEKDIEDLLEELELELLESDVALEVAEEILESLKEKLVGKKVK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 349 TFSTVTSTVKQALQESLVQILQPQRRVDMLRDImdaQRRQRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDT 428
Cdd:PRK14974 102 RGEDVEEIVKNALKEALLEVLSVGDLFDLIEEI---KSKGKPVVIVFVGVNGTGKTTTIAKLAYYLKKNGFSVVIAAGDT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 429 FRAGAVEQLRTHTRRLSalhppekhggrtmVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALA 508
Cdd:PRK14974 179 FRAGAIEQLEEHAERLG-------------VKVIKHKYGADPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDANLMDELK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 509 KLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGT 588
Cdd:PRK14974 246 KIVRVTKPDLVIFVGDALAGNDAVEQAREFNEAVG----------IDGVILTKVDA-DAKGGAALSIAYVIGKPILFLGV 314
|
330 340
....*....|....*....|
gi 966988840 589 GQTYCDLRSLNAKAVVAALM 608
Cdd:PRK14974 315 GQGYDDLIPFDPDWFVDKLL 334
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
390-609 |
2.89e-73 |
|
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: 233.07 E-value: 2.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 390 PYVVTFCGVNGVGKSTNLAKISFWLLENG-FSVLIAACDTFRAGAVEQLRTHTRRLSalhppekhggrtmVQLFEKGYGK 468
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEILG-------------VVPVAGGEGA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 469 DAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsma 548
Cdd:smart00962 68 DPVAVAKDAVELAKARGYDVVLIDTAGRLHNDENLMEELKKIKRVIKPDEVLLVSDATTGQDAVEQAKAFNEALG----- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966988840 549 qtprlIDGIVLTKFDtIDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAALMK 609
Cdd:smart00962 143 -----LTGIILTKLD-GTAKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLLG 197
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
285-607 |
1.70e-68 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 224.52 E-value: 1.70e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 285 TKGTLGGmfGMLKGLVGSKSLSredmESVLDKMRDHLIAKNVAADIAVQLCESVANKLEGKVMGTfstvTSTVKQALQES 364
Cdd:COG0552 12 TRSGLGE--KLKSLFSGKKKID----EDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKD----PEELKEALKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 365 LVQILQP-QRRVDMLRDimdaqrrqRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRThtrr 443
Cdd:COG0552 82 LLEILDPvDKPLAIEEK--------KPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEV---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 444 lsalhppekHGGRTMVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITV------NTPD 517
Cdd:COG0552 150 ---------WGERVGVPVIAQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVikkldpDAPH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 518 LVLFVGEALVGNEAVDQLVKFNRALAdhsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRS 597
Cdd:COG0552 221 EVLLVLDATTGQNALSQAKVFNEAVG----------VTGIVLTKLDG-TAKGGVVLAIADELGIPIKFIGVGEGIDDLRP 289
|
330
....*....|
gi 966988840 598 LNAKAVVAAL 607
Cdd:COG0552 290 FDAEEFVDAL 299
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
308-607 |
2.17e-62 |
|
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: 207.49 E-value: 2.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 308 EDMESVLDKMRDHLIAknvaADIAVQLCESVANKLEGKVMGTFSTVTSTVKQALQESLVQILQPQRRVDmlRDIMDAQRR 387
Cdd:TIGR00064 1 KDDEDFFEELEEILLE----SDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLLKN--TDLELIVEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 388 QRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLrthtrrlsalhppEKHGGRTMVQLFEKGYG 467
Cdd:TIGR00064 75 NKPNVILFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQL-------------EEWAKRLGVDVIKQKEG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 468 KDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITV------NTPDLVLFVGEALVGNEAVDQLVKFNRA 541
Cdd:TIGR00064 142 ADPAAVAFDAIQKAKARNIDVVLIDTAGRLQNKVNLMDELKKIKRVikkvdkDAPDEVLLVLDATTGQNALEQAKVFNEA 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966988840 542 LAdhsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 607
Cdd:TIGR00064 222 VG----------LTGIILTKLDG-TAKGGIILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEAL 276
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
392-607 |
1.39e-60 |
|
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: 199.69 E-value: 1.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 392 VVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHtrrlsalhppekhGGRTMVQLFEKGYGKDAA 471
Cdd:pfam00448 2 VILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQL-------------AEKLGVPVFGSKTGADPA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 472 GIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsmaqtp 551
Cdd:pfam00448 69 AVAFDAVEKAKAENYDVVLVDTAGRLQNDKNLMDELKKIKRVVAPDEVLLVLDATTGQNAVNQAKAFNEAVG-------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 966988840 552 rlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 607
Cdd:pfam00448 141 --ITGVILTKLDG-DAKGGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| SRP-alpha_N |
pfam04086 |
Signal recognition particle, alpha subunit, N-terminal; SRP is a complex of six distinct ... |
28-268 |
2.55e-60 |
|
Signal recognition particle, alpha subunit, N-terminal; SRP is a complex of six distinct polypeptides and a 7S RNA that is essential for transferring nascent polypeptide chains that are destined for export from the cell to the translocation apparatus of the endoplasmic reticulum (ER) membrane. SRP binds hydrophobic signal sequences as they emerge from the ribosome, and arrests translation.
Pssm-ID: 461165 Cd Length: 281 Bit Score: 202.26 E-value: 2.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 28 PVNALIRSVLLQ----------------------------VGFQKILTLTYVDKLIDDVHRLFRDKYRTEIQQQSALSLL 79
Cdd:pfam04086 1 PINALIRDVLLEersgnpsfkhdsytlkwtldnelglvfvAVYQKILHLSYVDKLLDNVKTIFVDLYKDQLKPYTTLVEC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 80 NgtfDFQNDFLRLLREAEESSKI--RAPTTMKKFEDSEKAKKPVRSMIETRGEKPKEKAKNSKKKGAKKEGSDGPLATSK 157
Cdd:pfam04086 81 P---DFDEYFDQLLREAEESAAAqaKAPKAMKTFEESKKSQKTVKSMIEDRPPPPPGKKKKGAKKEAPAAGDAGSDDSTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 158 AVPAEKSG--LPVGPENGVELSKEELIRRKREEFIQKHGRG----MEKSNKSTKSDAPKEKGKKaPRVWELGGCA-NKEV 230
Cdd:pfam04086 158 SATPDTSRpsTPLLTAKGAGPGAGDVSRRNRKALNKKRSGAgassGDESSKSPKPPKKKKKGKK-ARVWDADGSAdEADQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 966988840 231 LDYSTPTTNGSPEAALSEDINLIRGTGPG-------GQLQDLDCS 268
Cdd:pfam04086 237 LDYSAPADENGGEAEGESAVEAVDQSTWGsktgkgqFVLKDLDDE 281
|
|
| SR_alpha_SRX |
cd14826 |
SRX domain of signal recognition particle receptor subunit alpha; Signal recognition particle ... |
3-92 |
2.31e-30 |
|
SRX domain of signal recognition particle receptor subunit alpha; Signal recognition particle receptor subunit alpha (SR-alpha) is part of the membrane-associated heterodimeric receptor for the signal recognition particle (SRP). The signal recognition particle (SRP) pathway is highly conserved and plays an important role in the translocation of proteins across and insertion into membranes by targeting the translating ribosome to the endoplasmic reticulum. The N-terminal SRX domain of SR-alpha has a profilin-like fold and has been shown to be the interaction site with the second subunit, SR-beta.
Pssm-ID: 341430 Cd Length: 118 Bit Score: 114.99 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 3 DFFTIFSKGGLVLWCFQGVSDSCTGPVNALIRSVLLQ----------------------------VGFQKILTLTYVDKL 54
Cdd:cd14826 1 DQFSIFTKGGIVLWSFNFTGLFKGSPINALIKDVLLEersgessftydsytlkwtldnelglvfvVVYQKILQLQYIDEL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 966988840 55 IDDVHRLFRDKYRTEIQQQSALSLLNGTFDFQNDFLRL 92
Cdd:cd14826 81 LDLVKKLFVSLYKNELKNKNALGIDDDLFKFDEYFKQK 118
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
273-495 |
2.99e-14 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 73.52 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 273 EGAAQNSTKPSATKGTLGGMFGMLKGLVGSKSLSREDmeSVLDKMRDHLIAKNVAADIAVQLCESVANKLEGkvmgtfst 352
Cdd:TIGR03499 97 AQAAEPLLPEEELRKELEALRELLERLLAGLAWLQRP--PERAKLYERLLEAGVSEELARELLEKLPEDADA-------- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 353 vtSTVKQALQESLVQILQpqrrvdmlRDIMDAQRRQRPYVVTFCGVNGVGKSTNLAKISFWLLEN--GFSVLIAACDTFR 430
Cdd:TIGR03499 167 --EDAWRWLREALEGMLP--------VKPEEDPILEQGGVIALVGPTGVGKTTTLAKLAARFALEhgKKKVALITTDTYR 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966988840 431 AGAVEQLRTHtrrlsalhppekhgGRTMvqlfekgygkdaaGIAMEAI--------AFARNQGFDVVLVDTAG 495
Cdd:TIGR03499 237 IGAVEQLKTY--------------AEIL-------------GIPVKVArdpkelreALDRLRDKDLILIDTAG 282
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
290-361 |
1.37e-08 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 51.70 E-value: 1.37e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966988840 290 GGMFGMLKGLVGSKSLSREDMESVLDKMRDHLIAKNVAADIAVQLCESVANKLEG-KVMGTFSTVTSTVKQAL 361
Cdd:pfam02881 3 EKLSSLFKGLRGKGKIDEEDLEEALKELEEALLEADVGVEVVKKIIERLREKAVGeKKLKPPQEVKKILKEEL 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
391-607 |
2.04e-143 |
|
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: 413.93 E-value: 2.04e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 391 YVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLsalhppekhggrtMVQLFEKGYGKDA 470
Cdd:cd17876 1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRL-------------GVELYEKGYGKDP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 471 AGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALADHSMAQT 550
Cdd:cd17876 68 AAVAKEAIKYARDQGFDVVLIDTAGRMQNNEPLMRALAKLIKENNPDLVLFVGEALVGNDAVDQLKKFNQALADYSPSDN 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 966988840 551 PRLIDGIVLTKFDTIDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 607
Cdd:cd17876 148 PRLIDGIVLTKFDTIDDKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
391-607 |
1.59e-88 |
|
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: 272.71 E-value: 1.59e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 391 YVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLsalhppekhggrtMVQLFEKGYGKDA 470
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKL-------------GVPVFESYTGTDP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 471 AGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsmaqt 550
Cdd:cd03115 68 ASIAQEAVEKAKLEGYDVLLVDTAGRLQKDEPLMEELKKVKEVESPDEVLLVLDATTGQEALSQAKAFNEAVG------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 966988840 551 prlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 607
Cdd:cd03115 141 ---LTGVILTKLDG-TAKGGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
269-608 |
1.02e-86 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 273.39 E-value: 1.02e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 269 SSDDEGAAQNSTKPSATKGTLGGMFGMLKglvgSKSLSREDMESVLDKMRDHLIAKNVAADIAVQLCESVANKLEGKVMG 348
Cdd:PRK14974 26 EEAPEAEEEEEEEDEEEKKEKPGFFDKAK----ITEIKEKDIEDLLEELELELLESDVALEVAEEILESLKEKLVGKKVK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 349 TFSTVTSTVKQALQESLVQILQPQRRVDMLRDImdaQRRQRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDT 428
Cdd:PRK14974 102 RGEDVEEIVKNALKEALLEVLSVGDLFDLIEEI---KSKGKPVVIVFVGVNGTGKTTTIAKLAYYLKKNGFSVVIAAGDT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 429 FRAGAVEQLRTHTRRLSalhppekhggrtmVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALA 508
Cdd:PRK14974 179 FRAGAIEQLEEHAERLG-------------VKVIKHKYGADPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDANLMDELK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 509 KLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGT 588
Cdd:PRK14974 246 KIVRVTKPDLVIFVGDALAGNDAVEQAREFNEAVG----------IDGVILTKVDA-DAKGGAALSIAYVIGKPILFLGV 314
|
330 340
....*....|....*....|
gi 966988840 589 GQTYCDLRSLNAKAVVAALM 608
Cdd:PRK14974 315 GQGYDDLIPFDPDWFVDKLL 334
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
390-609 |
2.89e-73 |
|
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: 233.07 E-value: 2.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 390 PYVVTFCGVNGVGKSTNLAKISFWLLENG-FSVLIAACDTFRAGAVEQLRTHTRRLSalhppekhggrtmVQLFEKGYGK 468
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEILG-------------VVPVAGGEGA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 469 DAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsma 548
Cdd:smart00962 68 DPVAVAKDAVELAKARGYDVVLIDTAGRLHNDENLMEELKKIKRVIKPDEVLLVSDATTGQDAVEQAKAFNEALG----- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966988840 549 qtprlIDGIVLTKFDtIDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAALMK 609
Cdd:smart00962 143 -----LTGIILTKLD-GTAKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLLG 197
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
285-607 |
1.70e-68 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 224.52 E-value: 1.70e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 285 TKGTLGGmfGMLKGLVGSKSLSredmESVLDKMRDHLIAKNVAADIAVQLCESVANKLEGKVMGTfstvTSTVKQALQES 364
Cdd:COG0552 12 TRSGLGE--KLKSLFSGKKKID----EDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKD----PEELKEALKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 365 LVQILQP-QRRVDMLRDimdaqrrqRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRThtrr 443
Cdd:COG0552 82 LLEILDPvDKPLAIEEK--------KPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEV---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 444 lsalhppekHGGRTMVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITV------NTPD 517
Cdd:COG0552 150 ---------WGERVGVPVIAQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVikkldpDAPH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 518 LVLFVGEALVGNEAVDQLVKFNRALAdhsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRS 597
Cdd:COG0552 221 EVLLVLDATTGQNALSQAKVFNEAVG----------VTGIVLTKLDG-TAKGGVVLAIADELGIPIKFIGVGEGIDDLRP 289
|
330
....*....|
gi 966988840 598 LNAKAVVAAL 607
Cdd:COG0552 290 FDAEEFVDAL 299
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
308-607 |
2.17e-62 |
|
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: 207.49 E-value: 2.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 308 EDMESVLDKMRDHLIAknvaADIAVQLCESVANKLEGKVMGTFSTVTSTVKQALQESLVQILQPQRRVDmlRDIMDAQRR 387
Cdd:TIGR00064 1 KDDEDFFEELEEILLE----SDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLLKN--TDLELIVEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 388 QRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLrthtrrlsalhppEKHGGRTMVQLFEKGYG 467
Cdd:TIGR00064 75 NKPNVILFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQL-------------EEWAKRLGVDVIKQKEG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 468 KDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITV------NTPDLVLFVGEALVGNEAVDQLVKFNRA 541
Cdd:TIGR00064 142 ADPAAVAFDAIQKAKARNIDVVLIDTAGRLQNKVNLMDELKKIKRVikkvdkDAPDEVLLVLDATTGQNALEQAKVFNEA 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966988840 542 LAdhsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 607
Cdd:TIGR00064 222 VG----------LTGIILTKLDG-TAKGGIILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEAL 276
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
392-607 |
1.39e-60 |
|
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: 199.69 E-value: 1.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 392 VVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHtrrlsalhppekhGGRTMVQLFEKGYGKDAA 471
Cdd:pfam00448 2 VILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQL-------------AEKLGVPVFGSKTGADPA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 472 GIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsmaqtp 551
Cdd:pfam00448 69 AVAFDAVEKAKAENYDVVLVDTAGRLQNDKNLMDELKKIKRVVAPDEVLLVLDATTGQNAVNQAKAFNEAVG-------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 966988840 552 rlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 607
Cdd:pfam00448 141 --ITGVILTKLDG-DAKGGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| SRP-alpha_N |
pfam04086 |
Signal recognition particle, alpha subunit, N-terminal; SRP is a complex of six distinct ... |
28-268 |
2.55e-60 |
|
Signal recognition particle, alpha subunit, N-terminal; SRP is a complex of six distinct polypeptides and a 7S RNA that is essential for transferring nascent polypeptide chains that are destined for export from the cell to the translocation apparatus of the endoplasmic reticulum (ER) membrane. SRP binds hydrophobic signal sequences as they emerge from the ribosome, and arrests translation.
Pssm-ID: 461165 Cd Length: 281 Bit Score: 202.26 E-value: 2.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 28 PVNALIRSVLLQ----------------------------VGFQKILTLTYVDKLIDDVHRLFRDKYRTEIQQQSALSLL 79
Cdd:pfam04086 1 PINALIRDVLLEersgnpsfkhdsytlkwtldnelglvfvAVYQKILHLSYVDKLLDNVKTIFVDLYKDQLKPYTTLVEC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 80 NgtfDFQNDFLRLLREAEESSKI--RAPTTMKKFEDSEKAKKPVRSMIETRGEKPKEKAKNSKKKGAKKEGSDGPLATSK 157
Cdd:pfam04086 81 P---DFDEYFDQLLREAEESAAAqaKAPKAMKTFEESKKSQKTVKSMIEDRPPPPPGKKKKGAKKEAPAAGDAGSDDSTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 158 AVPAEKSG--LPVGPENGVELSKEELIRRKREEFIQKHGRG----MEKSNKSTKSDAPKEKGKKaPRVWELGGCA-NKEV 230
Cdd:pfam04086 158 SATPDTSRpsTPLLTAKGAGPGAGDVSRRNRKALNKKRSGAgassGDESSKSPKPPKKKKKGKK-ARVWDADGSAdEADQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 966988840 231 LDYSTPTTNGSPEAALSEDINLIRGTGPG-------GQLQDLDCS 268
Cdd:pfam04086 237 LDYSAPADENGGEAEGESAVEAVDQSTWGsktgkgqFVLKDLDDE 281
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
391-607 |
8.62e-59 |
|
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: 195.10 E-value: 8.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 391 YVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLSalhppekhggrtmVQLFEKGYGKDA 470
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLG-------------VPVISQNEGADP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 471 AGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITV------NTPDLVLFVGEALVGNEAVDQLVKFNRALAd 544
Cdd:cd17874 68 AAVAFDAIQAAKARGIDVVLIDTAGRLHTKKNLMEELKKIKRVikkkdpEAPHEVLLVLDATTGQNALEQAKEFNEAVG- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966988840 545 hsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 607
Cdd:cd17874 147 ---------LTGIILTKLDG-TAKGGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
288-610 |
1.67e-52 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 182.61 E-value: 1.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 288 TLGGMFGMLKGLVGSKSLSredmESVLDKMRDHLIAKNVAADIAVQLCESVANKLEGKVMgtfsTVTSTVKQALQESLVQ 367
Cdd:PRK10416 27 TRENFGEGINGLFAKKKID----EDLLEELEELLIEADVGVETTEEIIEELRERVKRKNL----KDPEELKELLKEELAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 368 ILQPQRRVDMLRDimdaqrrQRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRThtrrlsal 447
Cdd:PRK10416 99 ILEPVEKPLNIEE-------KKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQV-------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 448 hppekHGGRTMVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITV------NTPDLVLF 521
Cdd:PRK10416 164 -----WGERVGVPVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVikkadpDAPHEVLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 522 VGEALVGNEAVDQLVKFNRALAdhsmaqtprlIDGIVLTKFD-TidDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNA 600
Cdd:PRK10416 239 VLDATTGQNALSQAKAFHEAVG----------LTGIILTKLDgT--AKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDA 306
|
330
....*....|
gi 966988840 601 KAVVAALMKA 610
Cdd:PRK10416 307 EEFVDALLGG 316
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
296-589 |
2.07e-46 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 169.05 E-value: 2.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 296 LKGLVGSKSLSREDMESVLDKMRDHLIAKNVAADIAVQLCESVANKLEG-KVMGTFstvtsTVKQAL----QESLVQILQ 370
Cdd:COG0541 13 FKKLRGKGRLTEENIKEALREVRRALLEADVNLKVVKDFIERVKERALGeEVLKSL-----TPGQQVikivHDELVELLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 371 PQRRVDMLRDimdaqrrQRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLSalhpp 450
Cdd:COG0541 88 GENEELNLAK-------KPPTVIMMVGLQGSGKTTTAAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIG----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 451 ekhggrtmVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNE 530
Cdd:COG0541 156 --------VPVFPEEDGKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAAVNPDETLLVVDAMTGQD 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 966988840 531 AVDQLVKFNRALAdhsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTG 589
Cdd:COG0541 228 AVNVAKAFNEALG----------LTGVILTKLDG-DARGGAALSIRAVTGKPIKFIGTG 275
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
392-596 |
2.82e-44 |
|
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: 156.22 E-value: 2.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 392 VVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHtrrlsalhppekhGGRTMVQLFEKGYGKDAA 471
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTL-------------GEQVGVPVFESGDGQSPV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 472 GIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsmaqtp 551
Cdd:cd18539 69 DIAKRALEKAKEEGFDVVIVDTAGRLHIDEELMDELKEIKEVLNPDEVLLVVDAMTGQDAVNVAKAFNERLG-------- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 966988840 552 rlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLR 596
Cdd:cd18539 141 --LTGVVLTKLDG-DARGGAALSIRHVTGKPIKFIGVGEKIEDLE 182
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
391-607 |
1.19e-30 |
|
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: 118.45 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 391 YVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLSalhppekhggrtmVQLFEKGYGKDA 470
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKAR-------------VPFYGSYTEKDP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 471 AGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsmaqt 550
Cdd:cd17875 68 VKIAKEGVEKFKKEKFDIIIVDTSGRHKQEEELFEEMKQISDAVKPDEVILVIDASIGQAAEDQAKAFKEAVD------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 966988840 551 prlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 607
Cdd:cd17875 141 ---IGSVIITKLDG-HAKGGGALSAVAATGAPIIFIGTGEHIDDLEPFDPKRFVSRL 193
|
|
| SR_alpha_SRX |
cd14826 |
SRX domain of signal recognition particle receptor subunit alpha; Signal recognition particle ... |
3-92 |
2.31e-30 |
|
SRX domain of signal recognition particle receptor subunit alpha; Signal recognition particle receptor subunit alpha (SR-alpha) is part of the membrane-associated heterodimeric receptor for the signal recognition particle (SRP). The signal recognition particle (SRP) pathway is highly conserved and plays an important role in the translocation of proteins across and insertion into membranes by targeting the translating ribosome to the endoplasmic reticulum. The N-terminal SRX domain of SR-alpha has a profilin-like fold and has been shown to be the interaction site with the second subunit, SR-beta.
Pssm-ID: 341430 Cd Length: 118 Bit Score: 114.99 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 3 DFFTIFSKGGLVLWCFQGVSDSCTGPVNALIRSVLLQ----------------------------VGFQKILTLTYVDKL 54
Cdd:cd14826 1 DQFSIFTKGGIVLWSFNFTGLFKGSPINALIKDVLLEersgessftydsytlkwtldnelglvfvVVYQKILQLQYIDEL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 966988840 55 IDDVHRLFRDKYRTEIQQQSALSLLNGTFDFQNDFLRL 92
Cdd:cd14826 81 LDLVKKLFVSLYKNELKNKNALGIDDDLFKFDEYFKQK 118
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
389-608 |
3.37e-29 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 120.70 E-value: 3.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 389 RPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLSalhppekhggrtmVQLFEKGYGK 468
Cdd:PRK00771 94 KPQTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIG-------------VPFYGDPDNK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 469 DAAGIAMEAIAFARNQgfDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsma 548
Cdd:PRK00771 161 DAVEIAKEGLEKFKKA--DVIIVDTAGRHALEEDLIEEMKEIKEAVKPDEVLLVIDATIGQQAKNQAKAFHEAVG----- 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 549 qtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAALM 608
Cdd:PRK00771 234 -----IGGIIITKLDG-TAKGGGALSAVAETGAPIKFIGTGEKIDDLERFDPDRFISRLL 287
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
289-590 |
3.41e-27 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 113.42 E-value: 3.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 289 LGGMFGMLKGLVGSKSLSREDMESVLDKMRDHLIAKNVAADIAVQLCESVANKLEgkvmgtfstvTSTVKQALQESLVQI 368
Cdd:COG1419 83 LAELKELLEEQLSGLAGESARLPPELAELLERLLEAGVSPELARELLEKLPEDLS----------AEEAWRALLEALARR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 369 LQPQRRvdmlrDIMDAQRrqrpyVVTFCGVNGVGKSTNLAKISFWL-LENGFSVLIAACDTFRAGAVEQLRTHTRRLsal 447
Cdd:COG1419 153 LPVAED-----PLLDEGG-----VIALVGPTGVGKTTTIAKLAARFvLRGKKKVALITTDTYRIGAVEQLKTYARIL--- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 448 hppekhggrtmvqlfekgygkdaaGIAMEAI--------AFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLV 519
Cdd:COG1419 220 ------------------------GVPVEVAydpeelkeALERLRDKDLVLIDTAGRSPRDPELIEELKALLDAGPPIEV 275
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966988840 520 LFV------GEALvgNEAVDQLVKFNraladhsmaqtprlIDGIVLTKFD-TidDKVGAAISMTYITSKPIVFVGTGQ 590
Cdd:COG1419 276 YLVlsattkYEDL--KEIVEAFSSLG--------------LDGLILTKLDeT--ASLGSILNLLIRTGLPLSYITNGQ 335
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
289-608 |
5.13e-24 |
|
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: 104.92 E-value: 5.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 289 LGG-MFGMLKGLVGSKSLSREDMESVLDKMRDHLIAKNVAADIAVQLCESVANKLEGKVMGTFSTVTSTVKQALQESLVQ 367
Cdd:TIGR01425 5 LGSsLVTALRSMSSATVIDEEVINTMLKEICTALLESDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQDAVFEELCN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 368 ILQPQRRVDMLRdimdaqrRQRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLSal 447
Cdd:TIGR01425 85 LVDPGVEAFTPK-------KGKTCVIMFVGLQGAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAG-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 448 hppekhggrtmVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALV 527
Cdd:TIGR01425 156 -----------IPFYGSYEESDPVKIASEGVEKFRKEKFDIIIVDTSGRHKQEKELFEEMQQVREAIKPDSIIFVMDGSI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 528 GNEAVDQLVKFNRALAdhsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 607
Cdd:TIGR01425 225 GQAAFGQAKAFKDSVE----------VGSVIITKLDG-HAKGGGALSAVAATKSPIIFIGTGEHVDEFEIFDAEPFVSKL 293
|
.
gi 966988840 608 M 608
Cdd:TIGR01425 294 L 294
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
392-591 |
1.28e-20 |
|
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: 89.92 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 392 VVTFCGVNGVGKSTNLAKI-SFWLLENGFSVLIAACDTFRAGAVEQLRTHtrrlsalhppekhgGRTMVQLFEKGYGKDA 470
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLaARYVLKKGKKVALITTDTYRIGAVEQLKTY--------------AEIMGIPVEVAEDPED 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 471 AgiameAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPD---LVLFVG-EALVGNEAVDQLVKFNraladhs 546
Cdd:cd17873 68 L-----ADALERLSDRDLILIDTAGRSPRDKEQLEELKELLGAGEDIevhLVLSATtKAKDLKEIIERFSPLG------- 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 966988840 547 maqtprlIDGIVLTKFDTIdDKVGAAISMTYITSKPIVFVGTGQT 591
Cdd:cd17873 136 -------YRGLILTKLDET-TSLGSVLSVLAESQLPVSYVTTGQR 172
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
334-590 |
2.82e-16 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 81.48 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 334 LCESVANKLEGKVMGTFSTVTSTVKQALQESLVQILQPQrrvdmLRDIMDAQRrqrpyVVTFCGVNGVGKSTNLAKI--S 411
Cdd:PRK05703 175 LSPEIAEKLLKLLLEHMPPRERTAWRYLLELLANMIPVR-----VEDILKQGG-----VVALVGPTGVGKTTTLAKLaaR 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 412 FWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLSA----LHPPEKhggrtmvqlFEKgygkdaagiAMEaiAFARnqgFD 487
Cdd:PRK05703 245 YALLYGKKKVALITLDTYRIGAVEQLKTYAKIMGIpvevVYDPKE---------LAK---------ALE--QLRD---CD 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 488 VVLVDTAGRMQDNAPLMTALAKLI-TVNTPD---LVLfvgEALVGNEAVDQLVK-FNRaladhsmaqTPrlIDGIVLTKF 562
Cdd:PRK05703 302 VILIDTAGRSQRDKRLIEELKALIeFSGEPIdvyLVL---SATTKYEDLKDIYKhFSR---------LP--LDGLIFTKL 367
|
250 260
....*....|....*....|....*....
gi 966988840 563 D-TidDKVGAAISMTYITSKPIVFVGTGQ 590
Cdd:PRK05703 368 DeT--SSLGSILSLLIESGLPISYLTNGQ 394
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
273-495 |
2.99e-14 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 73.52 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 273 EGAAQNSTKPSATKGTLGGMFGMLKGLVGSKSLSREDmeSVLDKMRDHLIAKNVAADIAVQLCESVANKLEGkvmgtfst 352
Cdd:TIGR03499 97 AQAAEPLLPEEELRKELEALRELLERLLAGLAWLQRP--PERAKLYERLLEAGVSEELARELLEKLPEDADA-------- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 353 vtSTVKQALQESLVQILQpqrrvdmlRDIMDAQRRQRPYVVTFCGVNGVGKSTNLAKISFWLLEN--GFSVLIAACDTFR 430
Cdd:TIGR03499 167 --EDAWRWLREALEGMLP--------VKPEEDPILEQGGVIALVGPTGVGKTTTLAKLAARFALEhgKKKVALITTDTYR 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966988840 431 AGAVEQLRTHtrrlsalhppekhgGRTMvqlfekgygkdaaGIAMEAI--------AFARNQGFDVVLVDTAG 495
Cdd:TIGR03499 237 IGAVEQLKTY--------------AEIL-------------GIPVKVArdpkelreALDRLRDKDLILIDTAG 282
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
389-528 |
4.95e-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: 55.46 E-value: 4.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 389 RPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRthtrrlsalhppekhggrtMVQLFEKGYGK 468
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLL-------------------LIIVGGKKASG 61
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 469 DAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVG 528
Cdd:smart00382 62 SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVIL 121
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
392-590 |
1.30e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 57.44 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 392 VVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLSAlhppEKHGGRTMVQLFEkgygkdaa 471
Cdd:PRK12726 208 IISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLDV----ELIVATSPAELEE-------- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 472 giAMEAIAFArnQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEAlvGNEAVDQLVKFNRaladhsMAQTP 551
Cdd:PRK12726 276 --AVQYMTYV--NCVDHILIDTVGRNYLAEESVSEISAYTDVVHPDLTCFTFSS--GMKSADVMTILPK------LAEIP 343
|
170 180 190
....*....|....*....|....*....|....*....
gi 966988840 552 rlIDGIVLTKFDTIdDKVGAAISMTYITSKPIVFVGTGQ 590
Cdd:PRK12726 344 --IDGFIITKMDET-TRIGDLYTVMQETNLPVLYMTDGQ 379
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
290-361 |
1.37e-08 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 51.70 E-value: 1.37e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966988840 290 GGMFGMLKGLVGSKSLSREDMESVLDKMRDHLIAKNVAADIAVQLCESVANKLEG-KVMGTFSTVTSTVKQAL 361
Cdd:pfam02881 3 EKLSSLFKGLRGKGKIDEEDLEEALKELEEALLEADVGVEVVKKIIERLREKAVGeKKLKPPQEVKKILKEEL 75
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
388-590 |
4.42e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 55.50 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 388 QRPYVVTFCGVNGVGKSTNLAKISF-WLLENGFS-VLIAACDTFRAGAVEQLRTHTRRLSALHPPEKHGGRtmVQLfekg 465
Cdd:PRK14722 135 ERGGVFALMGPTGVGKTTTTAKLAArCVMRFGASkVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGD--LQL---- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 466 ygkdaagiameAIAFARNQgfDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALADH 545
Cdd:PRK14722 209 -----------ALAELRNK--HMVLIDTIGMSQRDRTVSDQIAMLHGADTPVQRLLLLNATSHGDTLNEVVQAYRSAAGQ 275
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 966988840 546 SMAQTPRLIdGIVLTKFDTIDDkVGAAISMTYITSKPIVFVGTGQ 590
Cdd:PRK14722 276 PKAALPDLA-GCILTKLDEASN-LGGVLDTVIRYKLPVHYVSTGQ 318
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
393-590 |
4.53e-08 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 55.84 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 393 VTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLsalhppekhgGRTMVQLfekgygKDAAG 472
Cdd:PRK11889 244 IALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTI----------GFEVIAV------RDEAA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 473 IAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLV-LFVGEALVGNEAVDQLVKFNRAladHsmaqtp 551
Cdd:PRK11889 308 MTRALTYFKEEARVDYILIDTAGKNYRASETVEEMIETMGQVEPDYIcLTLSASMKSKDMIEIITNFKDI---H------ 378
|
170 180 190
....*....|....*....|....*....|....*....
gi 966988840 552 rlIDGIVLTKFDTIDDKvGAAISMTYITSKPIVFVGTGQ 590
Cdd:PRK11889 379 --IDGIVFTKFDETASS-GELLKIPAVSSAPIVLMTDGQ 414
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
392-607 |
6.89e-08 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 55.38 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 392 VVTFCGVNGVGKSTNLAKISFWLLENGF--SVLIAACDTFRAGAVEQLRTHTRRLS-ALHppEKHGGRTMVQLFEkgygk 468
Cdd:PRK12727 352 VIALVGPTGAGKTTTIAKLAQRFAAQHAprDVALVTTDTQRVGGREQLHSYGRQLGiAVH--EADSAESLLDLLE----- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 469 daagiameaiafaRNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLfvgeALVGNEAVDQLVKFNRALAdHSMA 548
Cdd:PRK12727 425 -------------RLRDYKLVLIDTAGMGQRDRALAAQLNWLRAARQVTSLL----VLPANAHFSDLDEVVRRFA-HAKP 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 549 QtprlidGIVLTKFDTIdDKVGAAISMTYITSKPIVFVGTGQTYC-DLRSLNAKAVVAAL 607
Cdd:PRK12727 487 Q------GVVLTKLDET-GRFGSALSVVVDHQMPITWVTDGQRVPdDLHRANAASLVLRL 539
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
393-590 |
1.85e-07 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 52.83 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 393 VTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLSalhppekhggrtmvqlFEKGYGKDAAG 472
Cdd:PRK06731 78 IALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIG----------------FEVIAVRDEAA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 473 IAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLV-LFVGEALVGNEAVDQLVKFNRAladHsmaqtp 551
Cdd:PRK06731 142 MTRALTYFKEEARVDYILIDTAGKNYRASETVEEMIETMGQVEPDYIcLTLSASMKSKDMIEIITNFKDI---H------ 212
|
170 180 190
....*....|....*....|....*....|....*....
gi 966988840 552 rlIDGIVLTKFDTIDDKvGAAISMTYITSKPIVFVGTGQ 590
Cdd:PRK06731 213 --IDGIVFTKFDETASS-GELLKIPAVSSAPIVLMTDGQ 248
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
303-590 |
2.09e-07 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 53.81 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 303 KSLSREDMESVLDKMRDHLIAKNVAADIAvqlcESVANKLEGKVmgtfSTVTSTVKQALQESLVQILQPQRRVDmlRDIM 382
Cdd:PRK12724 146 TTIVRKEKDSPLQRLGERLVREGMSQSYV----EEMASKLEERL----SPVDQGRNHNVTERAVTYLEERVSVD--SDLF 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 383 DAQRRQRPYVVTFCGVNGVGKSTNLAKISF-WLLENGFSVLIAACDTFRAGAVEQLRTHTRRLSALHPPEKHggrtmVQL 461
Cdd:PRK12724 216 SGTGKNQRKVVFFVGPTGSGKTTSIAKLAAkYFLHMGKSVSLYTTDNYRIAAIEQLKRYADTMGMPFYPVKD-----IKK 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 462 FEKGYGKDaagiameaiafarnqGFDVVLVDTAGRMQDNAPLMTALAKLITVntpdlvlfVGEalvgNEAVDQLVKFNRA 541
Cdd:PRK12724 291 FKETLARD---------------GSELILIDTAGYSHRNLEQLERMQSFYSC--------FGE----KDSVENLLVLSST 343
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 966988840 542 LADHSMAQTPRLIDG-----IVLTKFDTIdDKVGAAISMTYITSKPIVFVGTGQ 590
Cdd:PRK12724 344 SSYHHTLTVLKAYESlnyrrILLTKLDEA-DFLGSFLELADTYSKSFTYLSVGQ 396
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
400-563 |
2.49e-06 |
|
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.
Pssm-ID: 426369 [Multi-domain] Cd Length: 228 Bit Score: 48.88 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 400 GVGKSTNLAKISFWLLENGFSVLIAACD-----TFRAGAVEQLRTHTRRLSALHPPEKH------------------GGR 456
Cdd:pfam01656 9 GVGKTTLAANLARALARRGLRVLLIDLDpqsnnSSVEGLEGDIAPALQALAEGLKGRVNldpillkeksdeggldliPGN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 457 TMVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNapLMTAL---AKLITVNTPDLVLFVGealvgneaVD 533
Cdd:pfam01656 89 IDLEKFEKELLGPRKEERLREALEALKEDYDYVIIDGAPGLGEL--LRNALiaaDYVIIPLEPEVILVED--------AK 158
|
170 180 190
....*....|....*....|....*....|
gi 966988840 534 QLVKFNRALADHSMAQTPRLIdGIVLTKFD 563
Cdd:pfam01656 159 RLGGVIAALVGGYALLGLKII-GVVLNKVD 187
|
|
| MeaB |
pfam03308 |
Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ... |
375-550 |
9.75e-05 |
|
Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ArgK proteins acting as ATPase enzymes and kinases. They are now believed to be methylmalonyl Co-A mutase-associated GTPase MeaB. Structural studies of MeaB and the human ortholog (methylmalonyl associated protein A) MMAA, reveal alpha-helical domains at the N- and C-termini as well as a Ras-like GTPase domain. Mutational analysis of MeaB, show prohibited growth in Methylobacterium due to the inability to convert methylmalonyl-CoA to succinyl-CoA caused by an inactive form of methylmalonyl-CoA mutatase (mcm). In humans, mutations in (MMAA) are associated with the fatal disease methylmalonyl aciduria.
Pssm-ID: 281323 [Multi-domain] Cd Length: 272 Bit Score: 44.35 E-value: 9.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 375 VDMLRDIMdaQRRQRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACD---TFRAGAVEQLRTHTRRLSAlHP-- 449
Cdd:pfam03308 20 RELLRRLM--PRAGRAHRVGVTGVPGAGKSTLIEALGMELRRRGHRVAVLAVDpssPRTGGSILGDKTRMDRLAV-DPga 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 450 ---PEKHGGRtmvqlfekgygkdAAGIAM---EAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTP----DL- 518
Cdd:pfam03308 97 firPSPSRGA-------------LGGLSRktrEVVLLLEAAGFDVIIIETVGVGQSEVDVANMVDTFVLLTMPgggdELq 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 966988840 519 -----VLFVGEALVGNEAVDQLVKFNRALADHSMAQT 550
Cdd:pfam03308 164 gikagIMEIADIYVVNKADGNLPGAERAARELRAALH 200
|
|
| MMAA-like |
cd03114 |
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ... |
364-580 |
5.30e-03 |
|
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB and its human homolog, methylmalonic aciduria associated protein (MMAA) are metallochaperones that function as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) and reactivation of the enzyme during catalysis. A member of the family, Escherichia coli ArgK, was previously thought to be a membrane ATPase which is required for transporting arginine, ornithine and lysine into the cells by the arginine and ornithine (AO system) and lysine, arginine and ornithine (LAO) transport systems.
Pssm-ID: 349768 Cd Length: 252 Bit Score: 39.09 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 364 SLVQILQPQRRVdMLRDIMDAQRRQ--RPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACD---TFRAGAVEQLR 438
Cdd:cd03114 19 TLVESGRPDHRE-LAQELLDALLPQagRAFRVGITGPPGAGKSTLIEALGRLLREQGHRVAVLAVDpssPRSGGSILGDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966988840 439 THTRRLSAlhppekHGGRTMVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNaplmTALAKLItvntpDL 518
Cdd:cd03114 98 TRMQRLAR------DPNAFIRPSPSRGTLGGVARATREAILLCEAAGYDVVLVETVGVGQSE----VAVADMV-----DT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966988840 519 VLFVGEALVGNEAvdQLVKfnRALADHSmaqtprliDGIVLTKFDTiDDKVGAAISMTYITS 580
Cdd:cd03114 163 FVLLLPPGGGDEL--QGIK--AGIMEIA--------DLVVVNKADG-DLKTGARRAQRELTS 211
|
|
| |
