|
Name |
Accession |
Description |
Interval |
E-value |
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
417-633 |
9.29e-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: 413.16 E-value: 9.29e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 417 YVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLtalhppekhggrtMVQLFEKGYGKDA 496
Cdd:cd17876 1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRL-------------GVELYEKGYGKDP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 497 AGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALADHSMAQT 576
Cdd:cd17876 68 AAVAKEAIKYARDQGFDVVLIDTAGRMQNNEPLMRALAKLIKENNPDLVLFVGEALVGNDAVDQLKKFNQALADYSPSDN 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27229036 577 PRLIDGIVLTKFDTIDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 633
Cdd:cd17876 148 PRLIDGIVLTKFDTIDDKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| SRP-alpha_N |
pfam04086 |
Signal recognition particle, alpha subunit, N-terminal; SRP is a complex of six distinct ... |
28-295 |
3.27e-87 |
|
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: 273.52 E-value: 3.27e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 28 PVNALIRSVLLQERGGNNSFTHEALTLKYKLDNQFELVFVVGFQKILTLTYVDKLIDDVHRLFRDKYRTEIQQQSALSLL 107
Cdd:pfam04086 1 PINALIRDVLLEERSGNPSFKHDSYTLKWTLDNELGLVFVAVYQKILHLSYVDKLLDNVKTIFVDLYKDQLKPYTTLVEC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 108 NgtfDFQNDFLRLLREAEESSKI--RAPTTMKKFEDSEKAKKPVRSMIETRGEKTKEKAKNNKKRGAKKEGSDGTLATSK 185
Cdd:pfam04086 81 P---DFDEYFDQLLREAEESAAAqaKAPKAMKTFEESKKSQKTVKSMIEDRPPPPPGKKKKGAKKEAPAAGDAGSDDSTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 186 TAPAEKSGLS---AGPENGELSKEELIRRKREEFIQKHGKGL----DKSSKSTKSDTPKEKGKKaPRVWELGGCA-NKEV 257
Cdd:pfam04086 158 SATPDTSRPStplLTAKGAGPGAGDVSRRNRKALNKKRSGAGassgDESSKSPKPPKKKKKGKK-ARVWDADGSAdEADQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 27229036 258 LDYSTPTTNGTPEAALSEDINLIRGTGPG-------GQLQDLDCS 295
Cdd:pfam04086 237 LDYSAPADENGGEAEGESAVEAVDQSTWGsktgkgqFVLKDLDDE 281
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
326-634 |
1.49e-85 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 271.08 E-value: 1.49e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 326 VGSKSLSREDMESVLDKMRDHLIAKNVAADIAVQLCESVANKLEGKVMGTFSTVTSTVKQALQESLVQILQPQRRVDMLR 405
Cdd:PRK14974 53 AKITEIKEKDIEDLLEELELELLESDVALEVAEEILESLKEKLVGKKVKRGEDVEEIVKNALKEALLEVLSVGDLFDLIE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 406 DImdaQRRQRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLTalhppekhggrtmV 485
Cdd:PRK14974 133 EI---KSKGKPVVIVFVGVNGTGKTTTIAKLAYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLG-------------V 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 486 QLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFN 565
Cdd:PRK14974 197 KVIKHKYGADPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDANLMDELKKIVRVTKPDLVIFVGDALAGNDAVEQAREFN 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27229036 566 RALAdhsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAALM 634
Cdd:PRK14974 277 EAVG----------IDGVILTKVDA-DAKGGAALSIAYVIGKPILFLGVGQGYDDLIPFDPDWFVDKLL 334
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
416-635 |
7.32e-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: 232.68 E-value: 7.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 416 PYVVTFCGVNGVGKSTNLAKISFWLLENG-FSVLIAACDTFRAGAVEQLRTHTRRLTalhppekhggrtmVQLFEKGYGK 494
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEILG-------------VVPVAGGEGA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 495 DAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsma 574
Cdd:smart00962 68 DPVAVAKDAVELAKARGYDVVLIDTAGRLHNDENLMEELKKIKRVIKPDEVLLVSDATTGQDAVEQAKAFNEALG----- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27229036 575 qtprlIDGIVLTKFDtIDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAALMK 635
Cdd:smart00962 143 -----LTGIILTKLD-GTAKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLLG 197
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
311-633 |
8.32e-68 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 223.36 E-value: 8.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 311 TKGTLGGmfGMLKGLVGSKSLSredmESVLDKMRDHLIAKNVAADIAVQLCESVANKLEGKVMGTfstvTSTVKQALQES 390
Cdd:COG0552 12 TRSGLGE--KLKSLFSGKKKID----EDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKD----PEELKEALKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 391 LVQILQP-QRRVDMLRDimdaqrrqRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRThtrr 469
Cdd:COG0552 82 LLEILDPvDKPLAIEEK--------KPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEV---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 470 ltalhppekHGGRTMVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITV------NTPD 543
Cdd:COG0552 150 ---------WGERVGVPVIAQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVikkldpDAPH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 544 LVLFVGEALVGNEAVDQLVKFNRALAdhsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRS 623
Cdd:COG0552 221 EVLLVLDATTGQNALSQAKVFNEAVG----------VTGIVLTKLDG-TAKGGVVLAIADELGIPIKFIGVGEGIDDLRP 289
|
330
....*....|
gi 27229036 624 LNAKAVVAAL 633
Cdd:COG0552 290 FDAEEFVDAL 299
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
334-633 |
1.40e-61 |
|
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: 205.95 E-value: 1.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 334 EDMESVLDKMRDHLIAknvaADIAVQLCESVANKLEGKVMGTFSTVTSTVKQALQESLVQILQPQRRVDmlRDIMDAQRR 413
Cdd:TIGR00064 1 KDDEDFFEELEEILLE----SDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLLKN--TDLELIVEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 414 QRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLrthtrrltalhppEKHGGRTMVQLFEKGYG 493
Cdd:TIGR00064 75 NKPNVILFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQL-------------EEWAKRLGVDVIKQKEG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 494 KDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITV------NTPDLVLFVGEALVGNEAVDQLVKFNRA 567
Cdd:TIGR00064 142 ADPAAVAFDAIQKAKARNIDVVLIDTAGRLQNKVNLMDELKKIKRVikkvdkDAPDEVLLVLDATTGQNALEQAKVFNEA 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27229036 568 LAdhsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 633
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 ... |
418-633 |
4.70e-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: 198.92 E-value: 4.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 418 VVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHtrrltalhppekhGGRTMVQLFEKGYGKDAA 497
Cdd:pfam00448 2 VILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQL-------------AEKLGVPVFGSKTGADPA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 498 GIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsmaqtp 577
Cdd:pfam00448 69 AVAFDAVEKAKAENYDVVLVDTAGRLQNDKNLMDELKKIKRVVAPDEVLLVLDATTGQNAVNQAKAFNEAVG-------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27229036 578 rlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 633
Cdd:pfam00448 141 --ITGVILTKLDG-DAKGGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| SR_alpha_SRX |
cd14826 |
SRX domain of signal recognition particle receptor subunit alpha; Signal recognition particle ... |
3-120 |
8.95e-54 |
|
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: 179.32 E-value: 8.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 3 DFFTIFSKGGLVLWCFQGVSDSCTGPVNALIRSVLLQERGGNNSFTHEALTLKYKLDNQFELVFVVGFQKILTLTYVDKL 82
Cdd:cd14826 1 DQFSIFTKGGIVLWSFNFTGLFKGSPINALIKDVLLEERSGESSFTYDSYTLKWTLDNELGLVFVVVYQKILQLQYIDEL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 27229036 83 IDDVHRLFRDKYRTEIQQQSALSLLNGTFDFQNDFLRL 120
Cdd:cd14826 81 LDLVKKLFVSLYKNELKNKNALGIDDDLFKFDEYFKQK 118
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
316-387 |
2.28e-08 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 51.31 E-value: 2.28e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27229036 316 GGMFGMLKGLVGSKSLSREDMESVLDKMRDHLIAKNVAADIAVQLCESVANKLEG-KVMGTFSTVTSTVKQAL 387
Cdd:pfam02881 3 EKLSSLFKGLRGKGKIDEEDLEEALKELEEALLEADVGVEVVKKIIERLREKAVGeKKLKPPQEVKKILKEEL 75
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
122-249 |
2.00e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 122 REAEESSKiRAPTTMKKFEDSEKAKKPVRSMIETRGEKTKEKAKNNKKRGAKKEGsdgtlATSKTAPAEKSGLSAGPENG 201
Cdd:PTZ00121 1315 KKADEAKK-KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA-----AEKKKEEAKKKADAAKKKAE 1388
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 27229036 202 ELSKEELIRRKREEFIQKHGKGLDKSSKSTKSDTPKEKGKKAPRVWEL 249
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
417-633 |
9.29e-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: 413.16 E-value: 9.29e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 417 YVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLtalhppekhggrtMVQLFEKGYGKDA 496
Cdd:cd17876 1 YVIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRL-------------GVELYEKGYGKDP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 497 AGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALADHSMAQT 576
Cdd:cd17876 68 AAVAKEAIKYARDQGFDVVLIDTAGRMQNNEPLMRALAKLIKENNPDLVLFVGEALVGNDAVDQLKKFNQALADYSPSDN 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27229036 577 PRLIDGIVLTKFDTIDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 633
Cdd:cd17876 148 PRLIDGIVLTKFDTIDDKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVKAVVNSL 204
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
417-633 |
8.83e-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: 271.55 E-value: 8.83e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 417 YVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLtalhppekhggrtMVQLFEKGYGKDA 496
Cdd:cd03115 1 NVILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKL-------------GVPVFESYTGTDP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 497 AGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsmaqt 576
Cdd:cd03115 68 ASIAQEAVEKAKLEGYDVLLVDTAGRLQKDEPLMEELKKVKEVESPDEVLLVLDATTGQEALSQAKAFNEAVG------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27229036 577 prlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 633
Cdd:cd03115 141 ---LTGVILTKLDG-TAKGGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| SRP-alpha_N |
pfam04086 |
Signal recognition particle, alpha subunit, N-terminal; SRP is a complex of six distinct ... |
28-295 |
3.27e-87 |
|
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: 273.52 E-value: 3.27e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 28 PVNALIRSVLLQERGGNNSFTHEALTLKYKLDNQFELVFVVGFQKILTLTYVDKLIDDVHRLFRDKYRTEIQQQSALSLL 107
Cdd:pfam04086 1 PINALIRDVLLEERSGNPSFKHDSYTLKWTLDNELGLVFVAVYQKILHLSYVDKLLDNVKTIFVDLYKDQLKPYTTLVEC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 108 NgtfDFQNDFLRLLREAEESSKI--RAPTTMKKFEDSEKAKKPVRSMIETRGEKTKEKAKNNKKRGAKKEGSDGTLATSK 185
Cdd:pfam04086 81 P---DFDEYFDQLLREAEESAAAqaKAPKAMKTFEESKKSQKTVKSMIEDRPPPPPGKKKKGAKKEAPAAGDAGSDDSTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 186 TAPAEKSGLS---AGPENGELSKEELIRRKREEFIQKHGKGL----DKSSKSTKSDTPKEKGKKaPRVWELGGCA-NKEV 257
Cdd:pfam04086 158 SATPDTSRPStplLTAKGAGPGAGDVSRRNRKALNKKRSGAGassgDESSKSPKPPKKKKKGKK-ARVWDADGSAdEADQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 27229036 258 LDYSTPTTNGTPEAALSEDINLIRGTGPG-------GQLQDLDCS 295
Cdd:pfam04086 237 LDYSAPADENGGEAEGESAVEAVDQSTWGsktgkgqFVLKDLDDE 281
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
326-634 |
1.49e-85 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 271.08 E-value: 1.49e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 326 VGSKSLSREDMESVLDKMRDHLIAKNVAADIAVQLCESVANKLEGKVMGTFSTVTSTVKQALQESLVQILQPQRRVDMLR 405
Cdd:PRK14974 53 AKITEIKEKDIEDLLEELELELLESDVALEVAEEILESLKEKLVGKKVKRGEDVEEIVKNALKEALLEVLSVGDLFDLIE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 406 DImdaQRRQRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLTalhppekhggrtmV 485
Cdd:PRK14974 133 EI---KSKGKPVVIVFVGVNGTGKTTTIAKLAYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLG-------------V 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 486 QLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFN 565
Cdd:PRK14974 197 KVIKHKYGADPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDANLMDELKKIVRVTKPDLVIFVGDALAGNDAVEQAREFN 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27229036 566 RALAdhsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAALM 634
Cdd:PRK14974 277 EAVG----------IDGVILTKVDA-DAKGGAALSIAYVIGKPILFLGVGQGYDDLIPFDPDWFVDKLL 334
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
416-635 |
7.32e-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: 232.68 E-value: 7.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 416 PYVVTFCGVNGVGKSTNLAKISFWLLENG-FSVLIAACDTFRAGAVEQLRTHTRRLTalhppekhggrtmVQLFEKGYGK 494
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEILG-------------VVPVAGGEGA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 495 DAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsma 574
Cdd:smart00962 68 DPVAVAKDAVELAKARGYDVVLIDTAGRLHNDENLMEELKKIKRVIKPDEVLLVSDATTGQDAVEQAKAFNEALG----- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27229036 575 qtprlIDGIVLTKFDtIDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAALMK 635
Cdd:smart00962 143 -----LTGIILTKLD-GTAKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLLG 197
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
311-633 |
8.32e-68 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 223.36 E-value: 8.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 311 TKGTLGGmfGMLKGLVGSKSLSredmESVLDKMRDHLIAKNVAADIAVQLCESVANKLEGKVMGTfstvTSTVKQALQES 390
Cdd:COG0552 12 TRSGLGE--KLKSLFSGKKKID----EDLLEELEELLIEADVGVETTEEIIEELRERVKRKKLKD----PEELKEALKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 391 LVQILQP-QRRVDMLRDimdaqrrqRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRThtrr 469
Cdd:COG0552 82 LLEILDPvDKPLAIEEK--------KPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEV---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 470 ltalhppekHGGRTMVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITV------NTPD 543
Cdd:COG0552 150 ---------WGERVGVPVIAQKEGADPAAVAFDAIQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVikkldpDAPH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 544 LVLFVGEALVGNEAVDQLVKFNRALAdhsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRS 623
Cdd:COG0552 221 EVLLVLDATTGQNALSQAKVFNEAVG----------VTGIVLTKLDG-TAKGGVVLAIADELGIPIKFIGVGEGIDDLRP 289
|
330
....*....|
gi 27229036 624 LNAKAVVAAL 633
Cdd:COG0552 290 FDAEEFVDAL 299
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
334-633 |
1.40e-61 |
|
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: 205.95 E-value: 1.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 334 EDMESVLDKMRDHLIAknvaADIAVQLCESVANKLEGKVMGTFSTVTSTVKQALQESLVQILQPQRRVDmlRDIMDAQRR 413
Cdd:TIGR00064 1 KDDEDFFEELEEILLE----SDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLLKN--TDLELIVEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 414 QRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLrthtrrltalhppEKHGGRTMVQLFEKGYG 493
Cdd:TIGR00064 75 NKPNVILFVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQL-------------EEWAKRLGVDVIKQKEG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 494 KDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITV------NTPDLVLFVGEALVGNEAVDQLVKFNRA 567
Cdd:TIGR00064 142 ADPAAVAFDAIQKAKARNIDVVLIDTAGRLQNKVNLMDELKKIKRVikkvdkDAPDEVLLVLDATTGQNALEQAKVFNEA 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27229036 568 LAdhsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 633
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 ... |
418-633 |
4.70e-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: 198.92 E-value: 4.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 418 VVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHtrrltalhppekhGGRTMVQLFEKGYGKDAA 497
Cdd:pfam00448 2 VILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQL-------------AEKLGVPVFGSKTGADPA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 498 GIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsmaqtp 577
Cdd:pfam00448 69 AVAFDAVEKAKAENYDVVLVDTAGRLQNDKNLMDELKKIKRVVAPDEVLLVLDATTGQNAVNQAKAFNEAVG-------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27229036 578 rlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 633
Cdd:pfam00448 141 --ITGVILTKLDG-DAKGGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
417-633 |
6.59e-58 |
|
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: 193.56 E-value: 6.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 417 YVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLTalhppekhggrtmVQLFEKGYGKDA 496
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLG-------------VPVISQNEGADP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 497 AGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITV------NTPDLVLFVGEALVGNEAVDQLVKFNRALAd 570
Cdd:cd17874 68 AAVAFDAIQAAKARGIDVVLIDTAGRLHTKKNLMEELKKIKRVikkkdpEAPHEVLLVLDATTGQNALEQAKEFNEAVG- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27229036 571 hsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 633
Cdd:cd17874 147 ---------LTGIILTKLDG-TAKGGIVLSIADELKIPVKFVGVGEGIDDLRPFDPEAFVEAL 199
|
|
| SR_alpha_SRX |
cd14826 |
SRX domain of signal recognition particle receptor subunit alpha; Signal recognition particle ... |
3-120 |
8.95e-54 |
|
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: 179.32 E-value: 8.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 3 DFFTIFSKGGLVLWCFQGVSDSCTGPVNALIRSVLLQERGGNNSFTHEALTLKYKLDNQFELVFVVGFQKILTLTYVDKL 82
Cdd:cd14826 1 DQFSIFTKGGIVLWSFNFTGLFKGSPINALIKDVLLEERSGESSFTYDSYTLKWTLDNELGLVFVVVYQKILQLQYIDEL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 27229036 83 IDDVHRLFRDKYRTEIQQQSALSLLNGTFDFQNDFLRL 120
Cdd:cd14826 81 LDLVKKLFVSLYKNELKNKNALGIDDDLFKFDEYFKQK 118
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
314-636 |
9.58e-52 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 181.06 E-value: 9.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 314 TLGGMFGMLKGLVGSKSLSredmESVLDKMRDHLIAKNVAADIAVQLCESVANKLEGKVMgtfsTVTSTVKQALQESLVQ 393
Cdd:PRK10416 27 TRENFGEGINGLFAKKKID----EDLLEELEELLIEADVGVETTEEIIEELRERVKRKNL----KDPEELKELLKEELAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 394 ILQPQRRVDMLRDimdaqrrQRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRThtrrltal 473
Cdd:PRK10416 99 ILEPVEKPLNIEE-------KKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQV-------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 474 hppekHGGRTMVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITV------NTPDLVLF 547
Cdd:PRK10416 164 -----WGERVGVPVIAQKEGADPASVAFDAIQAAKARGIDVLIIDTAGRLHNKTNLMEELKKIKRVikkadpDAPHEVLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 548 VGEALVGNEAVDQLVKFNRALAdhsmaqtprlIDGIVLTKFD-TidDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNA 626
Cdd:PRK10416 239 VLDATTGQNALSQAKAFHEAVG----------LTGIILTKLDgT--AKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDA 306
|
330
....*....|
gi 27229036 627 KAVVAALMKA 636
Cdd:PRK10416 307 EEFVDALLGG 316
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
322-615 |
4.36e-46 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 168.66 E-value: 4.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 322 LKGLVGSKSLSREDMESVLDKMRDHLIAKNVAADIAVQLCESVANKLEG-KVMGTFstvtsTVKQAL----QESLVQILQ 396
Cdd:COG0541 13 FKKLRGKGRLTEENIKEALREVRRALLEADVNLKVVKDFIERVKERALGeEVLKSL-----TPGQQVikivHDELVELLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 397 PQRRVDMLRDimdaqrrQRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRThtrrltaLhpp 476
Cdd:COG0541 88 GENEELNLAK-------KPPTVIMMVGLQGSGKTTTAAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKT-------L--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 477 ekhGGRTMVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNE 556
Cdd:COG0541 151 ---GEQIGVPVFPEEDGKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAAVNPDETLLVVDAMTGQD 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 27229036 557 AVDQLVKFNRALAdhsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTG 615
Cdd:COG0541 228 AVNVAKAFNEALG----------LTGVILTKLDG-DARGGAALSIRAVTGKPIKFIGTG 275
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
418-622 |
4.58e-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: 155.83 E-value: 4.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 418 VVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHtrrltalhppekhGGRTMVQLFEKGYGKDAA 497
Cdd:cd18539 2 VILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTL-------------GEQVGVPVFESGDGQSPV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 498 GIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsmaqtp 577
Cdd:cd18539 69 DIAKRALEKAKEEGFDVVIVDTAGRLHIDEELMDELKEIKEVLNPDEVLLVVDAMTGQDAVNVAKAFNERLG-------- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27229036 578 rlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLR 622
Cdd:cd18539 141 --LTGVVLTKLDG-DARGGAALSIRHVTGKPIKFIGVGEKIEDLE 182
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
417-633 |
2.66e-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: 117.68 E-value: 2.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 417 YVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLTalhppekhggrtmVQLFEKGYGKDA 496
Cdd:cd17875 1 NVIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKAR-------------VPFYGSYTEKDP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 497 AGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsmaqt 576
Cdd:cd17875 68 VKIAKEGVEKFKKEKFDIIIVDTSGRHKQEEELFEEMKQISDAVKPDEVILVIDASIGQAAEDQAKAFKEAVD------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27229036 577 prlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 633
Cdd:cd17875 141 ---IGSVIITKLDG-HAKGGGALSAVAATGAPIIFIGTGEHIDDLEPFDPKRFVSRL 193
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
415-634 |
1.04e-28 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 119.16 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 415 RPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLTalhppekhggrtmVQLFEKGYGK 494
Cdd:PRK00771 94 KPQTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIG-------------VPFYGDPDNK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 495 DAAGIAMEAIAFARNQgfDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALAdhsma 574
Cdd:PRK00771 161 DAVEIAKEGLEKFKKA--DVIIVDTAGRHALEEDLIEEMKEIKEAVKPDEVLLVIDATIGQQAKNQAKAFHEAVG----- 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 575 qtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAALM 634
Cdd:PRK00771 234 -----IGGIIITKLDG-TAKGGGALSAVAETGAPIKFIGTGEKIDDLERFDPDRFISRLL 287
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
315-616 |
4.00e-27 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 113.04 E-value: 4.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 315 LGGMFGMLKGLVGSKSLSREDMESVLDKMRDHLIAKNVAADIAVQLCESVANKLEgkvmgtfstvTSTVKQALQESLVQI 394
Cdd:COG1419 83 LAELKELLEEQLSGLAGESARLPPELAELLERLLEAGVSPELARELLEKLPEDLS----------AEEAWRALLEALARR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 395 LQPQRRvdmlrDIMDAQRrqrpyVVTFCGVNGVGKSTNLAKISFWL-LENGFSVLIAACDTFRAGAVEQLRTHTRRLtal 473
Cdd:COG1419 153 LPVAED-----PLLDEGG-----VIALVGPTGVGKTTTIAKLAARFvLRGKKKVALITTDTYRIGAVEQLKTYARIL--- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 474 hppekhggrtmvqlfekgygkdaaGIAMEAI--------AFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLV 545
Cdd:COG1419 220 ------------------------GVPVEVAydpeelkeALERLRDKDLVLIDTAGRSPRDPELIEELKALLDAGPPIEV 275
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27229036 546 LFV------GEALvgNEAVDQLVKFNraladhsmaqtprlIDGIVLTKFD-TidDKVGAAISMTYITSKPIVFVGTGQ 616
Cdd:COG1419 276 YLVlsattkYEDL--KEIVEAFSSLG--------------LDGLILTKLDeT--ASLGSILNLLIRTGLPLSYITNGQ 335
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
315-634 |
1.10e-23 |
|
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: 104.15 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 315 LGG-MFGMLKGLVGSKSLSREDMESVLDKMRDHLIAKNVAADIAVQLCESVANKLEGKVMGTFSTVTSTVKQALQESLVQ 393
Cdd:TIGR01425 5 LGSsLVTALRSMSSATVIDEEVINTMLKEICTALLESDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQDAVFEELCN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 394 ILQPQRRVDMLRdimdaqrRQRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRrltal 473
Cdd:TIGR01425 85 LVDPGVEAFTPK-------KGKTCVIMFVGLQGAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNAT----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 474 hppekhggRTMVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALV 553
Cdd:TIGR01425 153 --------KAGIPFYGSYEESDPVKIASEGVEKFRKEKFDIIIVDTSGRHKQEKELFEEMQQVREAIKPDSIIFVMDGSI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 554 GNEAVDQLVKFNRALAdhsmaqtprlIDGIVLTKFDTiDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAAL 633
Cdd:TIGR01425 225 GQAAFGQAKAFKDSVE----------VGSVIITKLDG-HAKGGGALSAVAATKSPIIFIGTGEHVDEFEIFDAEPFVSKL 293
|
.
gi 27229036 634 M 634
Cdd:TIGR01425 294 L 294
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
418-617 |
1.69e-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: 89.53 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 418 VVTFCGVNGVGKSTNLAKI-SFWLLENGFSVLIAACDTFRAGAVEQLRTHtrrltalhppekhgGRTMVQLFEKGYGKDA 496
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLaARYVLKKGKKVALITTDTYRIGAVEQLKTY--------------AEIMGIPVEVAEDPED 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 497 AgiameAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPD---LVLFVG-EALVGNEAVDQLVKFNraladhs 572
Cdd:cd17873 68 L-----ADALERLSDRDLILIDTAGRSPRDKEQLEELKELLGAGEDIevhLVLSATtKAKDLKEIIERFSPLG------- 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27229036 573 maqtprlIDGIVLTKFDTIdDKVGAAISMTYITSKPIVFVGTGQT 617
Cdd:cd17873 136 -------YRGLILTKLDET-TSLGSVLSVLAESQLPVSYVTTGQR 172
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
360-616 |
6.23e-16 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 80.32 E-value: 6.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 360 LCESVANKLEGKVMGTFSTVTSTVKQALQESLVQILQPQrrvdmLRDIMDAQRrqrpyVVTFCGVNGVGKSTNLAKI--S 437
Cdd:PRK05703 175 LSPEIAEKLLKLLLEHMPPRERTAWRYLLELLANMIPVR-----VEDILKQGG-----VVALVGPTGVGKTTTLAKLaaR 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 438 FWLLENGFSVLIAACDTFRAGAVEQLRTHTRRL----TALHPPEKhggrtmvqlFEKgygkdaagiAMEaiAFARnqgFD 513
Cdd:PRK05703 245 YALLYGKKKVALITLDTYRIGAVEQLKTYAKIMgipvEVVYDPKE---------LAK---------ALE--QLRD---CD 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 514 VVLVDTAGRMQDNAPLMTALAKLI-TVNTPD---LVLfvgEALVGNEAVDQLVK-FNRaladhsmaqTPrlIDGIVLTKF 588
Cdd:PRK05703 302 VILIDTAGRSQRDKRLIEELKALIeFSGEPIdvyLVL---SATTKYEDLKDIYKhFSR---------LP--LDGLIFTKL 367
|
250 260
....*....|....*....|....*....
gi 27229036 589 D-TidDKVGAAISMTYITSKPIVFVGTGQ 616
Cdd:PRK05703 368 DeT--SSLGSILSLLIESGLPISYLTNGQ 394
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
315-521 |
1.05e-13 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 71.98 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 315 LGGMFGMLKGLVGSKSLSREDmeSVLDKMRDHLIAKNVAADIAVQLCESVANKLEGkvmgtfstvtSTVKQALQESLVQI 394
Cdd:TIGR03499 113 LEALRELLERLLAGLAWLQRP--PERAKLYERLLEAGVSEELARELLEKLPEDADA----------EDAWRWLREALEGM 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 395 LQpqrrvdmlRDIMDAQRRQRPYVVTFCGVNGVGKSTNLAKISFWLLEN--GFSVLIAACDTFRAGAVEQLRTHtrrlta 472
Cdd:TIGR03499 181 LP--------VKPEEDPILEQGGVIALVGPTGVGKTTTLAKLAARFALEhgKKKVALITTDTYRIGAVEQLKTY------ 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27229036 473 lhppekhgGRTMvqlfekgygkdaaGIAMEAI--------AFARNQGFDVVLVDTAG 521
Cdd:TIGR03499 247 --------AEIL-------------GIPVKVArdpkelreALDRLRDKDLILIDTAG 282
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
415-554 |
5.20e-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: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 415 RPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRthtrrltalhppekhggrtMVQLFEKGYGK 494
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLL-------------------LIIVGGKKASG 61
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 495 DAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVG 554
Cdd:smart00382 62 SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVIL 121
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
316-387 |
2.28e-08 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 51.31 E-value: 2.28e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27229036 316 GGMFGMLKGLVGSKSLSREDMESVLDKMRDHLIAKNVAADIAVQLCESVANKLEG-KVMGTFSTVTSTVKQAL 387
Cdd:pfam02881 3 EKLSSLFKGLRGKGKIDEEDLEEALKELEEALLEADVGVEVVKKIIERLREKAVGeKKLKPPQEVKKILKEEL 75
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
418-616 |
2.38e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 56.67 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 418 VVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRL-----TALHPPEKHggrtmvqlfekgy 492
Cdd:PRK12726 208 IISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLdveliVATSPAELE------------- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 493 gkdaagiamEAIAFARN-QGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEAlvGNEAVDQLVKFNRaladh 571
Cdd:PRK12726 275 ---------EAVQYMTYvNCVDHILIDTVGRNYLAEESVSEISAYTDVVHPDLTCFTFSS--GMKSADVMTILPK----- 338
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27229036 572 sMAQTPrlIDGIVLTKFDTIdDKVGAAISMTYITSKPIVFVGTGQ 616
Cdd:PRK12726 339 -LAEIP--IDGFIITKMDET-TRIGDLYTVMQETNLPVLYMTDGQ 379
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
418-633 |
2.76e-08 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 56.92 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 418 VVTFCGVNGVGKSTNLAKISFWLLENGF--SVLIAACDTFRAGAVEQLRTHTRRL-TALHppEKHGGRTMVQLFEkgygk 494
Cdd:PRK12727 352 VIALVGPTGAGKTTTIAKLAQRFAAQHAprDVALVTTDTQRVGGREQLHSYGRQLgIAVH--EADSAESLLDLLE----- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 495 daagiameaiafaRNQGFDVVLVDTAGRMQDNAPLMTAL-----AKLITvntpDLVLFVGEALVGNeaVDQLVkfnRALA 569
Cdd:PRK12727 425 -------------RLRDYKLVLIDTAGMGQRDRALAAQLnwlraARQVT----SLLVLPANAHFSD--LDEVV---RRFA 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27229036 570 dHSMAQtprlidGIVLTKFDTIdDKVGAAISMTYITSKPIVFVGTGQTYC-DLRSLNAKAVVAAL 633
Cdd:PRK12727 483 -HAKPQ------GVVLTKLDET-GRFGSALSVVVDHQMPITWVTDGQRVPdDLHRANAASLVLRL 539
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
419-616 |
4.86e-08 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 55.84 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 419 VTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLtalhppekhgGRTMVQLfekgygKDAAG 498
Cdd:PRK11889 244 IALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTI----------GFEVIAV------RDEAA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 499 IAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLV-LFVGEALVGNEAVDQLVKFNRAladHsmaqtp 577
Cdd:PRK11889 308 MTRALTYFKEEARVDYILIDTAGKNYRASETVEEMIETMGQVEPDYIcLTLSASMKSKDMIEIITNFKDI---H------ 378
|
170 180 190
....*....|....*....|....*....|....*....
gi 27229036 578 rlIDGIVLTKFDTIDDKvGAAISMTYITSKPIVFVGTGQ 616
Cdd:PRK11889 379 --IDGIVFTKFDETASS-GELLKIPAVSSAPIVLMTDGQ 414
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
414-616 |
6.98e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 55.11 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 414 QRPYVVTFCGVNGVGKSTNLAKISF-WLLENGFS-VLIAACDTFRAGAVEQLRTHTRRLTALHPPEKHGGRtmVQLfekg 491
Cdd:PRK14722 135 ERGGVFALMGPTGVGKTTTTAKLAArCVMRFGASkVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGD--LQL---- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 492 ygkdaagiameAIAFARNQgfDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALADH 571
Cdd:PRK14722 209 -----------ALAELRNK--HMVLIDTIGMSQRDRTVSDQIAMLHGADTPVQRLLLLNATSHGDTLNEVVQAYRSAAGQ 275
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27229036 572 SMAQTPRLIdGIVLTKFDTIDDkVGAAISMTYITSKPIVFVGTGQ 616
Cdd:PRK14722 276 PKAALPDLA-GCILTKLDEASN-LGGVLDTVIRYKLPVHYVSTGQ 318
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
419-616 |
5.16e-07 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 51.67 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 419 VTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLTalhppekhggrtmvqlFEKGYGKDAAG 498
Cdd:PRK06731 78 IALIGPTGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIG----------------FEVIAVRDEAA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 499 IAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLV-LFVGEALVGNEAVDQLVKFNRAladhsmaqtp 577
Cdd:PRK06731 142 MTRALTYFKEEARVDYILIDTAGKNYRASETVEEMIETMGQVEPDYIcLTLSASMKSKDMIEIITNFKDI---------- 211
|
170 180 190
....*....|....*....|....*....|....*....
gi 27229036 578 rLIDGIVLTKFDTIDDKvGAAISMTYITSKPIVFVGTGQ 616
Cdd:PRK06731 212 -HIDGIVFTKFDETASS-GELLKIPAVSSAPIVLMTDGQ 248
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
329-616 |
7.03e-07 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 51.89 E-value: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 329 KSLSREDMESVLDKMRDHLIAKNVAADIAvqlcESVANKLEGKVmgtfSTVTSTVKQALQESLVQILQPQRRVDmlRDIM 408
Cdd:PRK12724 146 TTIVRKEKDSPLQRLGERLVREGMSQSYV----EEMASKLEERL----SPVDQGRNHNVTERAVTYLEERVSVD--SDLF 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 409 DAQRRQRPYVVTFCGVNGVGKSTNLAKISF-WLLENGFSVLIAACDTFRAGAVEQLRTHTRRLTALHPPEKHggrtmVQL 487
Cdd:PRK12724 216 SGTGKNQRKVVFFVGPTGSGKTTSIAKLAAkYFLHMGKSVSLYTTDNYRIAAIEQLKRYADTMGMPFYPVKD-----IKK 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 488 FEKGYGKDaagiameaiafarnqGFDVVLVDTAGRMQDNAPLMTALAKLITVntpdlvlfVGEalvgNEAVDQLVKFNRA 567
Cdd:PRK12724 291 FKETLARD---------------GSELILIDTAGYSHRNLEQLERMQSFYSC--------FGE----KDSVENLLVLSST 343
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 27229036 568 LADHSMAQTPRLIDG-----IVLTKFDTIdDKVGAAISMTYITSKPIVFVGTGQ 616
Cdd:PRK12724 344 SSYHHTLTVLKAYESlnyrrILLTKLDEA-DFLGSFLELADTYSKSFTYLSVGQ 396
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
426-589 |
4.56e-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: 48.11 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 426 GVGKSTNLAKISFWLLENGFSVLIAACD-----TFRAGAVEQLRTHTRRLTALHPPEKH------------------GGR 482
Cdd:pfam01656 9 GVGKTTLAANLARALARRGLRVLLIDLDpqsnnSSVEGLEGDIAPALQALAEGLKGRVNldpillkeksdeggldliPGN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 483 TMVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNapLMTAL---AKLITVNTPDLVLFVGealvgneaVD 559
Cdd:pfam01656 89 IDLEKFEKELLGPRKEERLREALEALKEDYDYVIIDGAPGLGEL--LRNALiaaDYVIIPLEPEVILVED--------AK 158
|
170 180 190
....*....|....*....|....*....|
gi 27229036 560 QLVKFNRALADHSMAQTPRLIdGIVLTKFD 589
Cdd:pfam01656 159 RLGGVIAALVGGYALLGLKII-GVVLNKVD 187
|
|
| MeaB |
pfam03308 |
Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ... |
401-576 |
6.40e-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: 45.12 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 401 VDMLRDIMdaQRRQRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACD---TFRAGAVEQLRTHTRRLTAlHP-- 475
Cdd:pfam03308 20 RELLRRLM--PRAGRAHRVGVTGVPGAGKSTLIEALGMELRRRGHRVAVLAVDpssPRTGGSILGDKTRMDRLAV-DPga 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 476 ---PEKHGGRtmvqlfekgygkdAAGIAM---EAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTP----DL- 544
Cdd:pfam03308 97 firPSPSRGA-------------LGGLSRktrEVVLLLEAAGFDVIIIETVGVGQSEVDVANMVDTFVLLTMPgggdELq 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 27229036 545 -----VLFVGEALVGNEAVDQLVKFNRALADHSMAQT 576
Cdd:pfam03308 164 gikagIMEIADIYVVNKADGNLPGAERAARELRAALH 200
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
122-249 |
2.00e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 122 REAEESSKiRAPTTMKKFEDSEKAKKPVRSMIETRGEKTKEKAKNNKKRGAKKEGsdgtlATSKTAPAEKSGLSAGPENG 201
Cdd:PTZ00121 1315 KKADEAKK-KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA-----AEKKKEEAKKKADAAKKKAE 1388
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 27229036 202 ELSKEELIRRKREEFIQKHGKGLDKSSKSTKSDTPKEKGKKAPRVWEL 249
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
|
| MMAA-like |
cd03114 |
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ... |
390-606 |
5.68e-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: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 390 SLVQILQPQRRVdMLRDIMDAQRRQ--RPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACD---TFRAGAVEQLR 464
Cdd:cd03114 19 TLVESGRPDHRE-LAQELLDALLPQagRAFRVGITGPPGAGKSTLIEALGRLLREQGHRVAVLAVDpssPRSGGSILGDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229036 465 THTRRLTAlhppekHGGRTMVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNaplmTALAKLItvntpDL 544
Cdd:cd03114 98 TRMQRLAR------DPNAFIRPSPSRGTLGGVARATREAILLCEAAGYDVVLVETVGVGQSE----VAVADMV-----DT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27229036 545 VLFVGEALVGNEAvdQLVKfnRALADHSmaqtprliDGIVLTKFDTiDDKVGAAISMTYITS 606
Cdd:cd03114 163 FVLLLPPGGGDEL--QGIK--AGIMEIA--------DLVVVNKADG-DLKTGARRAQRELTS 211
|
|
| |
