|
Name |
Accession |
Description |
Interval |
E-value |
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
1-433 |
0e+00 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 720.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 1 MFESLSDRLTGALAGLRGKGRLTDADIDATTREIRLALLEADVSLPVVRAFVGRIKERARGAEVSGALNPAQQVVKIVNE 80
Cdd:COG0541 1 MFENLSERLQGAFKKLRGKGRLTEENIKEALREVRRALLEADVNLKVVKDFIERVKERALGEEVLKSLTPGQQVIKIVHD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 81 ELIGILGGQTRQLVFAKTPPTVIMLAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFA 160
Cdd:COG0541 81 ELVELLGGENEELNLAKKPPTVIMMVGLQGSGKTTTAAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVFP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 161 PhpgappsgpdtGPEGDPVAVAAAGLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDAMIGQDAV 240
Cdd:COG0541 161 E-----------EDGKDPVDIAKRALEYAKKNGYDVVIVDTAGRLHIDEELMDELKAIKAAVNPDETLLVVDAMTGQDAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 241 TTAEAFREGVGFTGVVLTKLDGDARGGAALSVREVTGVPILFASTGEKLEDFDVFHPDRMSSRILGMGDVLSLIEQAEQV 320
Cdd:COG0541 230 NVAKAFNEALGLTGVILTKLDGDARGGAALSIRAVTGKPIKFIGTGEKLDDLEPFHPDRMASRILGMGDVLSLIEKAQEA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 321 FDAEQAEAAAAKIGSGELTLEDFLEQMLAIRKMGPIGNLLGMLPGAGQMR-DALAEVDDRQLDRLQAIIRGMTPQERADP 399
Cdd:COG0541 310 IDEEEAEKLAKKLKKGKFDLEDFLEQLQQMKKMGPLKKLLGMLPGMGKLKqLKDLDIDEKELKRIEAIINSMTPEERRNP 389
|
410 420 430
....*....|....*....|....*....|....
gi 1207588923 400 KIINASRRLRIANGSGVTVAEVNQLVDRFFEARK 433
Cdd:COG0541 390 DIINGSRKRRIAKGSGTTVQDVNRLLKQFEQMKK 423
|
|
| ffh |
TIGR00959 |
signal recognition particle protein; This model represents Ffh (Fifty-Four Homolog), the ... |
2-437 |
0e+00 |
|
signal recognition particle protein; This model represents Ffh (Fifty-Four Homolog), the protein component that forms the bacterial (and organellar) signal recognition particle together with a 4.5S RNA. Ffh is a GTPase homologous to eukaryotic SRP54 and also to the GTPase FtsY (TIGR00064) that is the receptor for the signal recognition particle. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273364 [Multi-domain] Cd Length: 428 Bit Score: 633.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 2 FESLSDRLTGALAGLRGKGRLTDADIDATTREIRLALLEADVSLPVVRAFVGRIKERARGAEVSGALNPAQQVVKIVNEE 81
Cdd:TIGR00959 1 FESLSERLQRIFKKLSGRGTITEKNIKEALREIRLALLEADVNLQVVKDFIKKVKEKALGQEVLKSLSPGQQFIKIVHEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 82 LIGILGGQTRQLVFAKTPPTVIMLAGLQGSGKTTLAGKLAFWLRN-QGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFA 160
Cdd:TIGR00959 81 LVAILGGENAELNLAKKPPTVILMVGLQGSGKTTTCGKLAYYLKKkQGKKVLLVACDLYRPAAIEQLKVLGQQVGVPVFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 161 PHPGAPPsgpdtgpegdpVAVAAAGLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDAMIGQDAV 240
Cdd:TIGR00959 161 LGKGQSP-----------VEIARRALEYAKENGFDVVIVDTAGRLQIDEELMEELAAIKEILNPDEILLVVDAMTGQDAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 241 TTAEAFREGVGFTGVVLTKLDGDARGGAALSVREVTGVPILFASTGEKLEDFDVFHPDRMSSRILGMGDVLSLIEQAEQV 320
Cdd:TIGR00959 230 NTAKTFNERLGLTGVVLTKLDGDARGGAALSVRSVTGKPIKFIGVGEKIDDLEPFHPERMASRILGMGDILSLVEKAQEV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 321 FDAEQAEAAAAKIGSGELTLEDFLEQMLAIRKMGPIGNLLGMLPGAGQMRDAL--AEVDDRQLDRLQAIIRGMTPQERAD 398
Cdd:TIGR00959 310 VDEEEAKKLAEKMKKGQFDLEDFLEQLRQIKKMGPLSSLLKMIPGMGGVKPSLsdADLDEKQFKRIEAIISSMTPEERRN 389
|
410 420 430
....*....|....*....|....*....|....*....
gi 1207588923 399 PKIINASRRLRIANGSGVTVAEVNQLVDRFFEARKMMSS 437
Cdd:TIGR00959 390 PKILNPSRRKRIAAGSGTTVQDVNKLIKRFEQMKKMMKK 428
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
5-443 |
5.02e-155 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 449.27 E-value: 5.02e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 5 LSDRLTGALAGLRGKGRLTDADIDATTREIRLALLEADVSLPVVRAFVGRIKERARGAEVSGALNPAQQVVKIVNEELIG 84
Cdd:PRK00771 1 LGESLRDALKKLAGKSRIDEKTVKEVVKDIQRALLQADVNVKLVKELSKSIKERALEEEPPKGLTPREHVIKIVYEELVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 85 ILGGQTRQLVFAKTPpTVIMLAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFAphpg 164
Cdd:PRK00771 81 LLGEETEPLVLPLKP-QTIMLVGLQGSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYG---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 165 appsGPDtgpEGDPVAVAAAGLAEAqaKHHDVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDAMIGQDAVTTAE 244
Cdd:PRK00771 156 ----DPD---NKDAVEIAKEGLEKF--KKADVIIVDTAGRHALEEDLIEEMKEIKEAVKPDEVLLVIDATIGQQAKNQAK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 245 AFREGVGFTGVVLTKLDGDARGGAALSVREVTGVPILFASTGEKLEDFDVFHPDRMSSRILGMGDVLSLIEQAEQVFDAE 324
Cdd:PRK00771 227 AFHEAVGIGGIIITKLDGTAKGGGALSAVAETGAPIKFIGTGEKIDDLERFDPDRFISRLLGMGDLESLLEKVEEALDEE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 325 QAEAAAAKIGSGELTLEDFLEQMLAIRKMGPIGNLLGMLPGAG-QMRDALAEVDDRQLDRLQAIIRGMTPQERADPKIIN 403
Cdd:PRK00771 307 EEEKDVEKMMKGKFTLKDMYKQLEAMNKMGPLKQILQMLPGLGgKLPDEALEVTEEKLKKYKAIMDSMTEEELENPEIIN 386
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1207588923 404 ASRRLRIANGSGVTVAEVNQLVDRFFEARKMMSSMLGGMG 443
Cdd:PRK00771 387 ASRIRRIARGSGTTVEDVRELLKYYKMMKKAMKQLKKGKG 426
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
101-304 |
3.74e-101 |
|
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349786 Cd Length: 193 Bit Score: 302.60 E-value: 3.74e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 101 TVIMLAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFAPHPGAppsgpdtgpegDPVA 180
Cdd:cd18539 1 TVILLVGLQGSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVFESGDGQ-----------SPVD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 181 VAAAGLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDAMIGQDAVTTAEAFREGVGFTGVVLTKL 260
Cdd:cd18539 70 IAKRALEKAKEEGFDVVIVDTAGRLHIDEELMDELKEIKEVLNPDEVLLVVDAMTGQDAVNVAKAFNERLGLTGVVLTKL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207588923 261 DGDARGGAALSVREVTGVPILFASTGEKLEDFDVFHPDRMSSRI 304
Cdd:cd18539 150 DGDARGGAALSIRHVTGKPIKFIGVGEKIEDLEPFHPDRMASRI 193
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
5-438 |
8.41e-92 |
|
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: 287.12 E-value: 8.41e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 5 LSDRLTGALAGLRGKGRLTDADIDATTREIRLALLEADVSLPVVRAFVGRIKERARGAEVSGALNPAQQVVKIVNEELIG 84
Cdd:TIGR01425 5 LGSSLVTALRSMSSATVIDEEVINTMLKEICTALLESDVNPKLVRQMRNNIKKKINLEDIASGINKRKLIQDAVFEELCN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 85 ILGGQTRQLVFAKTPPTVIMLAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFAPHPg 164
Cdd:TIGR01425 85 LVDPGVEAFTPKKGKTCVIMFVGLQGAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAFDQLKQNATKAGIPFYGSYE- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 165 appsgpdtgpEGDPVAVAAAGLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDAMIGQDAVTTAE 244
Cdd:TIGR01425 164 ----------ESDPVKIASEGVEKFRKEKFDIIIVDTSGRHKQEKELFEEMQQVREAIKPDSIIFVMDGSIGQAAFGQAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 245 AFREGVGFTGVVLTKLDGDARGGAALSVREVTGVPILFASTGEKLEDFDVFHPDRMSSRILGMGDVLSLIEQAEQVFDAE 324
Cdd:TIGR01425 234 AFKDSVEVGSVIITKLDGHAKGGGALSAVAATKSPIIFIGTGEHVDEFEIFDAEPFVSKLLGMGDLKGLIDKVQDLALND 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 325 QAEAAAAKIGSGELTLEDFLEQMLAIRKMGPIGNLLGMLPGAGQ--MRDALAEVDDRQLDRLQAIIRGMTPQE-RADPKI 401
Cdd:TIGR01425 314 EEKTLIEHLKEGTFTLRDWYEQFQNLLKMGPLGNIMSMIPGLSHpmMSKGNEEETSAKIKVFMTIMDSMTDRElDSTAKT 393
|
410 420 430
....*....|....*....|....*....|....*....
gi 1207588923 402 I--NASRRLRIANGSGVTVAEVNQLvdrfFEARKMMSSM 438
Cdd:TIGR01425 394 MlkDPSRIRRVARGSGRDIREVNEL----LEQYKLFAQM 428
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
100-306 |
4.28e-90 |
|
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: 274.29 E-value: 4.28e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 100 PTVIMLAGLQGSGKTTLAGKLAFWLRNQG-HTPLLVACDLQRPAAVNQLQVVGQRAGVPVFAPHPGAppsgpdtgpegDP 178
Cdd:smart00962 1 PGVILLVGPNGVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAVEQLKTYAEILGVVPVAGGEGA-----------DP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 179 VAVAAAGLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDAMIGQDAVTTAEAFREGVGFTGVVLT 258
Cdd:smart00962 70 VAVAKDAVELAKARGYDVVLIDTAGRLHNDENLMEELKKIKRVIKPDEVLLVSDATTGQDAVEQAKAFNEALGLTGIILT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207588923 259 KLDGDARGGAALSVREVTGVPILFASTGEKLEDFDVFHPDRMSSRILG 306
Cdd:smart00962 150 KLDGTAKGGAALSIAAETGLPIKFIGTGEKVPDLEPFDPERFVSRLLG 197
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
101-304 |
5.78e-88 |
|
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: 268.64 E-value: 5.78e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 101 TVIMLAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFAPHPGAppsgpdtgpegDPVA 180
Cdd:pfam00448 1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPVFGSKTGA-----------DPAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 181 VAAAGLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDAMIGQDAVTTAEAFREGVGFTGVVLTKL 260
Cdd:pfam00448 70 VAFDAVEKAKAENYDVVLVDTAGRLQNDKNLMDELKKIKRVVAPDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207588923 261 DGDARGGAALSVREVTGVPILFASTGEKLEDFDVFHPDRMSSRI 304
Cdd:pfam00448 150 DGDAKGGAALSIVAETGKPIKFIGVGEKIDDLEPFDPERFVSRL 193
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
1-306 |
1.46e-78 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 248.40 E-value: 1.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 1 MFESLSDRL-------TGALAGL-RGKGRLTDADIDattrEIRLALLEADVSLPVVRAFVGRIKERARGAEVSgalnPAQ 72
Cdd:COG0552 1 FFERLKEGLsktrsglGEKLKSLfSGKKKIDEDLLE----ELEELLIEADVGVETTEEIIEELRERVKRKKLK----DPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 73 QVVKIVNEELIGILGGQTRQLVFAKTPPTVIMLAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGQ 152
Cdd:COG0552 73 ELKEALKEELLEILDPVDKPLAIEEKKPFVILVVGVNGVGKTTTIGKLAHRLKAEGKSVLLAAGDTFRAAAIEQLEVWGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 153 RAGVPVFAPHPGAPPSGP--DTgpegdpvavaaagLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDAIN------P 224
Cdd:COG0552 153 RVGVPVIAQKEGADPAAVafDA-------------IQAAKARGADVVIIDTAGRLHNKKNLMEELKKIKRVIKkldpdaP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 225 DEVIFVLDAMIGQDAVTTAEAFREGVGFTGVVLTKLDGDARGGAALSVREVTGVPILFASTGEKLEDFDVFHPDRMSSRI 304
Cdd:COG0552 220 HEVLLVLDATTGQNALSQAKVFNEAVGVTGIVLTKLDGTAKGGVVLAIADELGIPIKFIGVGEGIDDLRPFDAEEFVDAL 299
|
..
gi 1207588923 305 LG 306
Cdd:COG0552 300 FG 301
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
102-304 |
6.69e-70 |
|
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: 222.25 E-value: 6.69e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 102 VIMLAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFAPHPGAppsgpdtgpegDPVAV 181
Cdd:cd03115 2 VILLVGLQGSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVFESYTGT-----------DPASI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 182 AAAGLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDAMIGQDAVTTAEAFREGVGFTGVVLTKLD 261
Cdd:cd03115 71 AQEAVEKAKLEGYDVLLVDTAGRLQKDEPLMEELKKVKEVESPDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207588923 262 GDARGGAALSVREVTGVPILFASTGEKLEDFDVFHPDRMSSRI 304
Cdd:cd03115 151 GTAKGGAALSIVAETKKPIKFIGVGEKPEDLEPFDPERFVSAL 193
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
6-306 |
6.18e-67 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 218.81 E-value: 6.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 6 SDRLTGALAGLRGKGRLTDADIDattrEIRLALLEADVSLPVVRAFVGRIKERARGAEVSGAlnpaQQVVKIVNEELIGI 85
Cdd:PRK10416 28 RENFGEGINGLFAKKKIDEDLLE----ELEELLIEADVGVETTEEIIEELRERVKRKNLKDP----EELKELLKEELAEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 86 LGGQTRQLVFAKTPPTVIMLAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFAPHPGA 165
Cdd:PRK10416 100 LEPVEKPLNIEEKKPFVILVVGVNGVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAIEQLQVWGERVGVPVIAQKEGA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 166 PPSGP--DTGPEGdpvavaaaglaeaQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDAIN------PDEVIFVLDAMIGQ 237
Cdd:PRK10416 180 DPASVafDAIQAA-------------KARGIDVLIIDTAGRLHNKTNLMEELKKIKRVIKkadpdaPHEVLLVLDATTGQ 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207588923 238 DAVTTAEAFREGVGFTGVVLTKLDGDARGGAALSVREVTGVPILFASTGEKLEDFDVFHPDRMSSRILG 306
Cdd:PRK10416 247 NALSQAKAFHEAVGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGIDDLQPFDAEEFVDALLG 315
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
21-306 |
1.16e-66 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 218.69 E-value: 1.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 21 RLTDADIDATTREIRLALLEADVSLPVVRAFVGRIKERARGAEVSGALNPAQQVVKIVNEELIGILG-GQTRQLVF---A 96
Cdd:PRK14974 57 EIKEKDIEDLLEELELELLESDVALEVAEEILESLKEKLVGKKVKRGEDVEEIVKNALKEALLEVLSvGDLFDLIEeikS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 97 KTPPTVIMLAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFAPHPGAppsgpdtgpeg 176
Cdd:PRK14974 137 KGKPVVIVFVGVNGTGKTTTIAKLAYYLKKNGFSVVIAAGDTFRAGAIEQLEEHAERLGVKVIKHKYGA----------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 177 DPVAVAAAGLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDAMIGQDAVTTAEAFREGVGFTGVV 256
Cdd:PRK14974 206 DPAAVAYDAIEHAKARGIDVVLIDTAGRMHTDANLMDELKKIVRVTKPDLVIFVGDALAGNDAVEQAREFNEAVGIDGVI 285
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1207588923 257 LTKLDGDARGGAALSVREVTGVPILFASTGEKLEDFDVFHPDRMSSRILG 306
Cdd:PRK14974 286 LTKVDADAKGGAALSIAYVIGKPILFLGVGQGYDDLIPFDPDWFVDKLLG 335
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
26-305 |
2.45e-65 |
|
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: 213.27 E-value: 2.45e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 26 DIDATTREIRLALLEADVSLPVVRAFVGRIKERARGAEVSGALNPAQQVVKIVNEELIGILGGQTRQLVFAKTP-PTVIM 104
Cdd:TIGR00064 2 DDEDFFEELEEILLESDVGYEVVEKIIEALKKELKGKKVKDAEKLKEILKEYLKEILKEDLLKNTDLELIVEENkPNVIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 105 LAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFAPHPGAppsgpdtgpegDPVAVAAA 184
Cdd:TIGR00064 82 FVGVNGVGKTTTIAKLANKLKKQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVDVIKQKEGA-----------DPAAVAFD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 185 GLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAAI------RDAINPDEVIFVLDAMIGQDAVTTAEAFREGVGFTGVVLT 258
Cdd:TIGR00064 151 AIQKAKARNIDVVLIDTAGRLQNKVNLMDELKKIkrvikkVDKDAPDEVLLVLDATTGQNALEQAKVFNEAVGLTGIILT 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1207588923 259 KLDGDARGGAALSVREVTGVPILFASTGEKLEDFDVFHPDRMSSRIL 305
Cdd:TIGR00064 231 KLDGTAKGGIILSIAYELKLPIKFIGVGEKIDDLAPFDADWFVEALF 277
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
102-304 |
6.74e-60 |
|
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: 195.87 E-value: 6.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 102 VIMLAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFaphpgappsGPDTgpEGDPVAV 181
Cdd:cd17875 2 VIMFVGLQGSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFY---------GSYT--EKDPVKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 182 AAAGLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDAMIGQDAVTTAEAFREGVGFTGVVLTKLD 261
Cdd:cd17875 71 AKEGVEKFKKEKFDIIIVDTSGRHKQEEELFEEMKQISDAVKPDEVILVIDASIGQAAEDQAKAFKEAVDIGSVIITKLD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207588923 262 GDARGGAALSVREVTGVPILFASTGEKLEDFDVFHPDRMSSRI 304
Cdd:cd17875 151 GHAKGGGALSAVAATGAPIIFIGTGEHIDDLEPFDPKRFVSRL 193
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
101-298 |
1.83e-57 |
|
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: 189.70 E-value: 1.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 101 TVIMLAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFAPHPGAppsgpdtgpegDPVA 180
Cdd:cd17874 1 FVILFVGVNGVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAVEQLEEWAERLGVPVISQNEGA-----------DPAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 181 VAAAGLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDAIN------PDEVIFVLDAMIGQDAVTTAEAFREGVGFTG 254
Cdd:cd17874 70 VAFDAIQAAKARGIDVVLIDTAGRLHTKKNLMEELKKIKRVIKkkdpeaPHEVLLVLDATTGQNALEQAKEFNEAVGLTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1207588923 255 VVLTKLDGDARGGAALSVREVTGVPILFASTGEKLEDFDVFHPD 298
Cdd:cd17874 150 IILTKLDGTAKGGIVLSIADELKIPVKFVGVGEGIDDLRPFDPE 193
|
|
| SRP_SPB |
pfam02978 |
Signal peptide binding domain; |
337-433 |
3.38e-41 |
|
Signal peptide binding domain;
Pssm-ID: 460771 [Multi-domain] Cd Length: 95 Bit Score: 142.92 E-value: 3.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 337 ELTLEDFLEQMLAIRKMGPIGNLLGMLPGAGQMRDAlaEVDDRQLDRLQAIIRGMTPQERADPKIINASRRLRIANGSGV 416
Cdd:pfam02978 1 KFTLRDFLEQLQQIKKMGPLSKILSMIPGMGKKDDD--IDSEKKLKRIEAIIDSMTPKERDNPDIINASRKRRIARGSGT 78
|
90
....*....|....*..
gi 1207588923 417 TVAEVNQLVDRFFEARK 433
Cdd:pfam02978 79 SVQEVNRLLKQFKQMKK 95
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
102-298 |
1.42e-33 |
|
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: 126.19 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 102 VIMLAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFaphpgappsgpDTGPEGDPVAV 181
Cdd:cd17876 2 VIVFCGVNGVGKSTNLAKIAYWLLSNGFRVLIAACDTFRSGAVEQLRTHARRLGVELY-----------EKGYGKDPAAV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 182 AAAGLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDAMIGQDAVTTAEAFREGV----------G 251
Cdd:cd17876 71 AKEAIKYARDQGFDVVLIDTAGRMQNNEPLMRALAKLIKENNPDLVLFVGEALVGNDAVDQLKKFNQALadyspsdnprL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207588923 252 FTGVVLTKLDG-DARGGAALSVREVTGVPILFASTGEKLEDFDVFHPD 298
Cdd:cd17876 151 IDGIVLTKFDTiDDKVGAALSMVYATGQPIVFVGTGQTYTDLKKLNVK 198
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
32-306 |
3.46e-30 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 121.13 E-value: 3.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 32 REIRLALLEADVSLPVVRAFVGRIKERArgaevsgalnPAQQVVKIVNEELIGILGGQTRQLVfakTPPTVIMLAGLQGS 111
Cdd:COG1419 109 AELLERLLEAGVSPELARELLEKLPEDL----------SAEEAWRALLEALARRLPVAEDPLL---DEGGVIALVGPTGV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 112 GKTTLAGKLAFWL-RNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFAPHpgappsgpdtgpegDPvavAAAGLAEAQ 190
Cdd:COG1419 176 GKTTTIAKLAARFvLRGKKKVALITTDTYRIGAVEQLKTYARILGVPVEVAY--------------DP---EELKEALER 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 191 AKHHDVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDA-MIGQDAVTTAEAFReGVGFTGVVLTKLDGDARGGAA 269
Cdd:COG1419 239 LRDKDLVLIDTAGRSPRDPELIEELKALLDAGPPIEVYLVLSAtTKYEDLKEIVEAFS-SLGLDGLILTKLDETASLGSI 317
|
250 260 270
....*....|....*....|....*....|....*...
gi 1207588923 270 LSVREVTGVPILFASTGEKL-EDFDVFHPDRMSSRILG 306
Cdd:COG1419 318 LNLLIRTGLPLSYITNGQRVpEDIEVADPERLARLLLG 355
|
|
| SRP54_N |
pfam02881 |
SRP54-type protein, helical bundle domain; |
5-82 |
4.24e-24 |
|
SRP54-type protein, helical bundle domain;
Pssm-ID: 460734 [Multi-domain] Cd Length: 75 Bit Score: 95.61 E-value: 4.24e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207588923 5 LSDRLTGALAGLRGKGRLTDADIDATTREIRLALLEADVSLPVVRAFVGRIKERARGAEvsgALNPAQQVVKIVNEEL 82
Cdd:pfam02881 1 LGEKLSSLFKGLRGKGKIDEEDLEEALKELEEALLEADVGVEVVKKIIERLREKAVGEK---KLKPPQEVKKILKEEL 75
|
|
| SRP54_N |
smart00963 |
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle ... |
9-86 |
3.92e-22 |
|
SRP54-type protein, helical bundle domain; This entry represents the N-terminal helical bundle domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species.
Pssm-ID: 214941 [Multi-domain] Cd Length: 77 Bit Score: 90.30 E-value: 3.92e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207588923 9 LTGALAGLRGKGRLTDADIDATTREIRLALLEADVSLPVVRAFVGRIKERARGaEVSGALNPAQQVVKIVNEELIGIL 86
Cdd:smart00963 1 LSKALGKLLGELFLTEKDDEELLEELEEALLEADVGVEVVKEIIERVKEKAKG-EVLKGLTPKQEVKKILKEELVKIL 77
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
102-304 |
4.73e-21 |
|
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: 90.69 E-value: 4.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 102 VIMLAGLQGSGKTTLAGKLA-FWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVfaphpgappsgpdtgpegDPVA 180
Cdd:cd17873 2 VIALVGPTGVGKTTTLAKLAaRYVLKKGKKVALITTDTYRIGAVEQLKTYAEIMGIPV------------------EVAE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 181 VAAA-GLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDA-MIGQDAVTTAEAFReGVGFTGVVLT 258
Cdd:cd17873 64 DPEDlADALERLSDRDLILIDTAGRSPRDKEQLEELKELLGAGEDIEVHLVLSAtTKAKDLKEIIERFS-PLGYRGLILT 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207588923 259 KLDGDARGGAALSVREVTGVPILFASTGEKL-EDFDVFHPDRMSSRI 304
Cdd:cd17873 143 KLDETTSLGSVLSVLAESQLPVSYVTTGQRVpEDIEVASPLRLARLL 189
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
102-306 |
1.96e-11 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 65.91 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 102 VIMLAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFAPhpgappsgpdtgpeGDPVAV 181
Cdd:PRK12726 208 IISLIGQTGVGKTTTLVKLGWQLLKQNRTVGFITTDTFRSGAVEQFQGYADKLDVELIVA--------------TSPAEL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 182 AAAGLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDA-MIGQDAVTTAEAFREgVGFTGVVLTKL 260
Cdd:PRK12726 274 EEAVQYMTYVNCVDHILIDTVGRNYLAEESVSEISAYTDVVHPDLTCFTFSSgMKSADVMTILPKLAE-IPIDGFIITKM 352
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207588923 261 DGDARGGAALSVREVTGVPILFASTGEKLEDfDVFHPDR--MSSRILG 306
Cdd:PRK12726 353 DETTRIGDLYTVMQETNLPVLYMTDGQNITE-NIFRPKSrwLAERFVG 399
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
34-290 |
1.37e-10 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 63.55 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 34 IRLaLLEADVSLPVVRAFVGRIKERARGAEVsgalnpaqqvvkIVNEELIGILGGQTR-----QLVFAKTPPTvIMLAGL 108
Cdd:PRK11889 184 IRM-LEQNDVEQYFIHAYAEKLKVKFENATM------------ITEEEVIEYILEDMRshfntENVFEKEVQT-IALIGP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 109 QGSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFAPHpgappsgpdtgpegDPVAVAAAGLAE 188
Cdd:PRK11889 250 TGVGKTTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVR--------------DEAAMTRALTYF 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 189 AQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDA-MIGQDAVTTAEAFREgVGFTGVVLTKLDGDARGG 267
Cdd:PRK11889 316 KEEARVDYILIDTAGKNYRASETVEEMIETMGQVEPDYICLTLSAsMKSKDMIEIITNFKD-IHIDGIVFTKFDETASSG 394
|
250 260
....*....|....*....|...
gi 1207588923 268 AALSVREVTGVPILFASTGEKLE 290
Cdd:PRK11889 395 ELLKIPAVSSAPIVLMTDGQDVK 417
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
34-290 |
2.12e-09 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 58.60 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 34 IRLaLLEADVSLPVVRAFVGRIKERARGAEVSgalnpAQQVVKIVNEELIGILGGQTrqlVFAKTPPTvIMLAGLQGSGK 113
Cdd:PRK06731 19 IRM-LEQNDVEQYFIHAYAEKLKVKFENATMI-----TEEVIEYILEDMSSHFNTEN---VFEKEVQT-IALIGPTGVGK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 114 TTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFAPHpgappsgpdtgpegDPVAVAAAGLAEAQAKH 193
Cdd:PRK06731 89 TTTLAKMAWQFHGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVR--------------DEAAMTRALTYFKEEAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 194 HDVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDA-MIGQDAVTTAEAFREgVGFTGVVLTKLDGDARGGAALSV 272
Cdd:PRK06731 155 VDYILIDTAGKNYRASETVEEMIETMGQVEPDYICLTLSAsMKSKDMIEIITNFKD-IHIDGIVFTKFDETASSGELLKI 233
|
250
....*....|....*...
gi 1207588923 273 REVTGVPILFASTGEKLE 290
Cdd:PRK06731 234 PAVSSAPIVLMTDGQDVK 251
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
33-306 |
8.31e-09 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 57.60 E-value: 8.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 33 EIRLALLEADVSLPVVRAFVGRIKER--ARGAEVSGALnpAQQVVKIVNEELIGILGGQTrqlvfaktpptVIMLAGLQG 110
Cdd:PRK05703 165 ELYKRLKRSGLSPEIAEKLLKLLLEHmpPRERTAWRYL--LELLANMIPVRVEDILKQGG-----------VVALVGPTG 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 111 SGKTT----LAGKLAfwLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPV--------FAphpgappsgpdtgpegdp 178
Cdd:PRK05703 232 VGKTTtlakLAARYA--LLYGKKKVALITLDTYRIGAVEQLKTYAKIMGIPVevvydpkeLA------------------ 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 179 vavaaagLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAA-IRDAINPDEVIFVLdAMIGQ--DAVTTAEAFREgVGFTGV 255
Cdd:PRK05703 292 -------KALEQLRDCDVILIDTAGRSQRDKRLIEELKAlIEFSGEPIDVYLVL-SATTKyeDLKDIYKHFSR-LPLDGL 362
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1207588923 256 VLTKLDGDARGGAALSVREVTGVPILFASTGEKL-EDFDVFHPDRMSSRILG 306
Cdd:PRK05703 363 IFTKLDETSSLGSILSLLIESGLPISYLTNGQRVpDDIKVANPEELVRLLLG 414
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
32-160 |
7.07e-08 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 53.88 E-value: 7.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 32 REIRLALLEADVSLPVVRAFVGRIKERARgaevsgalnpAQQVVKIVNEELIGILGGQTRQlVFAKTPPTVIMLAGLQGS 111
Cdd:TIGR03499 137 AKLYERLLEAGVSEELARELLEKLPEDAD----------AEDAWRWLREALEGMLPVKPEE-DPILEQGGVIALVGPTGV 205
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1207588923 112 GKTTLAGKLA--FWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFA 160
Cdd:TIGR03499 206 GKTTTLAKLAarFALEHGKKKVALITTDTYRIGAVEQLKTYAEILGIPVKV 256
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
102-291 |
8.82e-08 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 54.34 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 102 VIMLAGLQGSGKTTLAGKLAFW--LRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFAPHPGappsgpdtgpeGDpv 179
Cdd:PRK14722 139 VFALMGPTGVGKTTTTAKLAARcvMRFGASKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDG-----------GD-- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 180 avaaAGLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDAMIGQDAVT-TAEAFREGVG------- 251
Cdd:PRK14722 206 ----LQLALAELRNKHMVLIDTIGMSQRDRTVSDQIAMLHGADTPVQRLLLLNATSHGDTLNeVVQAYRSAAGqpkaalp 281
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1207588923 252 -FTGVVLTKLDGDARGGAALSVREVTGVPILFASTGEKLED 291
Cdd:PRK14722 282 dLAGCILTKLDEASNLGGVLDTVIRYKLPVHYVSTGQKVPE 322
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
102-288 |
1.97e-07 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 53.65 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 102 VIMLAGLQGSGKTTLAGKLA--FWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPVFAPHPGAppsgpdtgpegdpv 179
Cdd:PRK14723 187 VLALVGPTGVGKTTTTAKLAarCVAREGADQLALLTTDSFRIGALEQLRIYGRILGVPVHAVKDAA-------------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 180 aVAAAGLAEAQAKHhdVVIVDTAGRLGIDDELMSQAAAIRDAINPDEVIFVLDAMIGQDAVT-TAEAFREGVG--FTGVV 256
Cdd:PRK14723 253 -DLRFALAALGDKH--LVLIDTVGMSQRDRNVSEQIAMLCGVGRPVRRLLLLNAASHGDTLNeVVHAYRHGAGedVDGCI 329
|
170 180 190
....*....|....*....|....*....|..
gi 1207588923 257 LTKLDGDARGGAALSVREVTGVPILFASTGEK 288
Cdd:PRK14723 330 ITKLDEATHLGPALDTVIRHRLPVHYVSTGQK 361
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
85-291 |
3.87e-06 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 49.60 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 85 ILGGQTRQLVFAKTPPT----VIMLAGLQGSGKTTLAGKLA--FWLRNQGHTPLLVACDLQRPAAVNQLQVVGQRAGVPV 158
Cdd:PRK12727 331 MLGLLSKRLPVAPVDPLerggVIALVGPTGAGKTTTIAKLAqrFAAQHAPRDVALVTTDTQRVGGREQLHSYGRQLGIAV 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 159 FAPHPGAppsgpdtgpegdpvavaAAGLAEAQAKHHDVVIVDTAGRLGIDDELMSQAAAIRDA-------INPDEVIFV- 230
Cdd:PRK12727 411 HEADSAE-----------------SLLDLLERLRDYKLVLIDTAGMGQRDRALAAQLNWLRAArqvtsllVLPANAHFSd 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207588923 231 LDAMIGQDAVTTAEafregvgftGVVLTKLDGDARGGAALSVREVTGVPILFASTGEKLED 291
Cdd:PRK12727 474 LDEVVRRFAHAKPQ---------GVVLTKLDETGRFGSALSVVVDHQMPITWVTDGQRVPD 525
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
102-259 |
2.63e-05 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 43.19 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 102 VIMLAGLQ-GSGKTTLAGKLAFWLRNQGHTPLLVACDlqrpaavnqlqvvgqragvpvfaphpgappsgpdtgpegdpva 180
Cdd:cd01983 2 VIAVTGGKgGVGKTTLAAALAVALAAKGYKVLLIDLD------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 181 vaaaglaeaqakhhDVVIVDTAGRLGIDDELMSQAAAIRDaINPDEVIFVLDAMIG--QDAVTTA---EAFREGVGFTGV 255
Cdd:cd01983 39 --------------DYVLIDGGGGLETGLLLGTIVALLAL-KKADEVIVVVDPELGslLEAVKLLlalLLLGIGIRPDGI 103
|
....
gi 1207588923 256 VLTK 259
Cdd:cd01983 104 VLNK 107
|
|
| PHA02518 |
PHA02518 |
ParA-like protein; Provisional |
110-288 |
2.93e-05 |
|
ParA-like protein; Provisional
Pssm-ID: 222854 [Multi-domain] Cd Length: 211 Bit Score: 45.23 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 110 GSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAvnqlqvvgqragvpvfaphpgappSGPDTGPEGDPVAVAAAGLAEA 189
Cdd:PHA02518 11 GAGKTTVATNLASWLHADGHKVLLVDLDPQGSST------------------------DWAEAREEGEPLIPVVRMGKSI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 190 QAKHH------DVVIVDTAGRlgiDDELMSQAAAIRDAI----NPDEV-IFVLDAMIgqDAVTTAEAFREGV-GFTGVVL 257
Cdd:PHA02518 67 RADLPkvasgyDYVVVDGAPQ---DSELARAALRIADMVlipvQPSPFdIWAAPDLV--ELIKARQEVTDGLpKFAFIIS 141
|
170 180 190
....*....|....*....|....*....|.
gi 1207588923 258 TKLDGDARGGAALSVREVTGVPILFASTGEK 288
Cdd:PHA02518 142 RAIKNTQLYREARKALAGYGLPILRNGTTQR 172
|
|
| UMPK_like |
cd02028 |
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ... |
102-137 |
6.14e-05 |
|
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK).
Pssm-ID: 238986 [Multi-domain] Cd Length: 179 Bit Score: 43.83 E-value: 6.14e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1207588923 102 VIMLAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACD 137
Cdd:cd02028 1 VVGIAGPSGSGKTTFAKKLSNQLRVNGIGPVVISLD 36
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
110-281 |
1.10e-04 |
|
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: 43.87 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 110 GSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGQR-------AGVP--------VFAPH---------PGA 165
Cdd:pfam01656 9 GVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIApalqalaEGLKgrvnldpiLLKEKsdeggldliPGN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 166 PP-SGPDTGPEGDPVAVAAAGLAEAQAKHHDVVIVDTAGRLGID--DELMSQAAAIRdAINPdEVIFVLDAmigQDAVTT 242
Cdd:pfam01656 89 IDlEKFEKELLGPRKEERLREALEALKEDYDYVIIDGAPGLGELlrNALIAADYVII-PLEP-EVILVEDA---KRLGGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207588923 243 AEAFREGVG-----FTGVVLTKLDGDARGGAALSV--REVTGVPIL 281
Cdd:pfam01656 164 IAALVGGYAllglkIIGVVLNKVDGDNHGKLLKEAleELLRGLPVL 209
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
99-212 |
1.35e-04 |
|
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: 42.36 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 99 PPTVIMLAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAVNQLQVVGqragvpvfaphpgappsGPDTGPEGDP 178
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII-----------------VGGKKASGSG 63
|
90 100 110
....*....|....*....|....*....|....
gi 1207588923 179 VAVAAAGLAEAQAKHHDVVIVDTAGRLGIDDELM 212
Cdd:smart00382 64 ELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
|
| ParAB_family |
cd02042 |
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ... |
110-274 |
4.43e-04 |
|
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.
Pssm-ID: 349760 [Multi-domain] Cd Length: 130 Bit Score: 40.22 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 110 GSGKTTLAGKLAFWLRNQGHTPLLVACDLQRPAAvnqlqvvgqragvpvfaphpgappsgpdtgpegdpvavaaaglaea 189
Cdd:cd02042 11 GVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLT---------------------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207588923 190 qAKHHDVVIVDTAGRLGIddeLMSQAAAIRDAI----NPDEviFVLDAMigQDAVTTAEAFREGVG----FTGVVLTKLd 261
Cdd:cd02042 45 -SWLYDYILIDTPPSLGL---LTRNALAAADLVlipvQPSP--FDLDGL--AKLLDTLEELKKQLNppllILGILLTRV- 115
|
170
....*....|...
gi 1207588923 262 gDARGGAALSVRE 274
Cdd:cd02042 116 -DPRTKLAREVLE 127
|
|
| arsen_driv_ArsA |
TIGR04291 |
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ... |
96-149 |
3.64e-03 |
|
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).
Pssm-ID: 275109 [Multi-domain] Cd Length: 566 Bit Score: 40.07 E-value: 3.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207588923 96 AKTPPTVIMLAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACDlqrPAA---------VNQLQV 149
Cdd:TIGR04291 317 AKSEKGLIMTMGKGGVGKTTVAAAIAVRLANKGLDVHLTTSD---PAAhlsvtltgsLNNLQV 376
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
97-133 |
4.47e-03 |
|
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440295 [Multi-domain] Cd Length: 189 Bit Score: 38.53 E-value: 4.47e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1207588923 97 KTPPTVIMLAGLQGSGKTTLAGKLAFWLRNQG-HTPLL 133
Cdd:COG0529 13 GQKGFVVWFTGLSGSGKSTLANALERRLFERGrHVYLL 50
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
99-121 |
8.77e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 36.73 E-value: 8.77e-03
|
| GPN1 |
cd17870 |
GPN-loop GTPase 1; GPN-loop GTPase 1 (GPN1, also kown as MBD2-interacting protein or MBDin, ... |
101-143 |
8.78e-03 |
|
GPN-loop GTPase 1; GPN-loop GTPase 1 (GPN1, also kown as MBD2-interacting protein or MBDin, RNAPII-associated protein 4, and XPA-binding protein 1) is a GTPase is required for nuclear targeting of RNA polymerase II. It forms heterodimers with GPN3.
Pssm-ID: 349779 [Multi-domain] Cd Length: 241 Bit Score: 37.93 E-value: 8.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1207588923 101 TVIMLAGLQGSGKTTLAGKLAFWLRNQGHTPLLVACDlqrPAA 143
Cdd:cd17870 1 VVIIVVGMAGSGKTTFVQRLNAYLHDNKKPPYVINLD---PAV 40
|
|
|