|
Name |
Accession |
Description |
Interval |
E-value |
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
3-333 |
1.05e-122 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 356.87 E-value: 1.05e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 3 KKYTANTIQDAMNLAKMELGDNITLIDKKEVRKSGIrgifsKKDIELTIGWE-------------------KKDNLEQKD 63
Cdd:COG1419 4 KKFVAKDMREALRKVKEELGPDAVILSTRKVKKGGF-----LKKVEVTAAVDedeaekapaaaaapaaasaAAEEEELEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 64 LKREIEQLKSIINNMGFDNKNDND-----IDKICKNLLNLDLNQEIVEFIKADLQEmKFNGIDTSKNLVESLKKKIKIEN 138
Cdd:COG1419 79 LRRELAELKELLEEQLSGLAGESArlppeLAELLERLLEAGVSPELARELLEKLPE-DLSAEEAWRALLEALARRLPVAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 139 QAIN---GKIALVGPPGVGKTTTIAKLAAKLVFEENKKVGVITIDTYRIGAVEQLKIYTDIMNIPFKGVISPDEMELALD 215
Cdd:COG1419 158 DPLLdegGVIALVGPTGVGKTTTIAKLAARFVLRGKKKVALITTDTYRIGAVEQLKTYARILGVPVEVAYDPEELKEALE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 216 EMKDCDVVLIDTTGRGYKNSMQILEIKNLIDKAETDNIHLVLNCTTRESDTKAIIDSYRNVNFKSLIITKLDETITYGSI 295
Cdd:COG1419 238 RLRDKDLVLIDTAGRSPRDPELIEELKALLDAGPPIEVYLVLSATTKYEDLKEIVEAFSSLGLDGLILTKLDETASLGSI 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 544970261 296 FNIMNYAQKPISYITTGQNVPDDIIKPNEDKIIRLLLG 333
Cdd:COG1419 318 LNLLIRTGLPLSYITNGQRVPEDIEVADPERLARLLLG 355
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
3-337 |
5.98e-118 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 346.88 E-value: 5.98e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 3 KKYTANTIQDAMNLAKMELGDNITLIDKKEVRKsgiRGIFSKKDIELTIGWE---------------------------- 54
Cdd:PRK05703 4 KKFTAKDMREALKQIKEELGADAVILSNKKVRK---GGFLGKKLVEVTAAVDedetpkknpvlreekrkpaksilslqal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 55 ---------------------------------------------KKDNLEQKDLKREIEQLKSIINNMGFDNKNDNDID 89
Cdd:PRK05703 81 lekrpsrtnsqdallqaenalpewkkelekpsepkeeepkaaaesKVVQKELDELRDELKELKNLLEDQLSGLRQVERIP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 90 ----KICKNLLNLDLNQEIVEFIKADLQE-MKFNGIDTSKNLVESLKKKIKIENQAI---NGKIALVGPPGVGKTTTIAK 161
Cdd:PRK05703 161 pefaELYKRLKRSGLSPEIAEKLLKLLLEhMPPRERTAWRYLLELLANMIPVRVEDIlkqGGVVALVGPTGVGKTTTLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 162 LAAKLVF-EENKKVGVITIDTYRIGAVEQLKIYTDIMNIPFKGVISPDEMELALDEMKDCDVVLIDTTGRGYKNSMQILE 240
Cdd:PRK05703 241 LAARYALlYGKKKVALITLDTYRIGAVEQLKTYAKIMGIPVEVVYDPKELAKALEQLRDCDVILIDTAGRSQRDKRLIEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 241 IKNLID-KAETDNIHLVLNCTTRESDTKAIIDSYRNVNFKSLIITKLDETITYGSIFNIMNYAQKPISYITTGQNVPDDI 319
Cdd:PRK05703 321 LKALIEfSGEPIDVYLVLSATTKYEDLKDIYKHFSRLPLDGLIFTKLDETSSLGSILSLLIESGLPISYLTNGQRVPDDI 400
|
410
....*....|....*...
gi 544970261 320 IKPNEDKIIRLLLGVESI 337
Cdd:PRK05703 401 KVANPEELVRLLLGGFNK 418
|
|
| FlhF |
cd17873 |
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ... |
143-331 |
5.04e-87 |
|
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: 259.79 E-value: 5.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 143 GKIALVGPPGVGKTTTIAKLAAKLVFEENKKVGVITIDTYRIGAVEQLKIYTDIMNIPFKGVISPDEMELALDEMKDCDV 222
Cdd:cd17873 1 RVIALVGPTGVGKTTTLAKLAARYVLKKGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEVAEDPEDLADALERLSDRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 223 VLIDTTGRGYKNSMQILEIKNLIDKAETDNIHLVLNCTTRESDTKAIIDSYRNVNFKSLIITKLDETITYGSIFNIMNYA 302
Cdd:cd17873 81 ILIDTAGRSPRDKEQLEELKELLGAGEDIEVHLVLSATTKAKDLKEIIERFSPLGYRGLILTKLDETTSLGSVLSVLAES 160
|
170 180
....*....|....*....|....*....
gi 544970261 303 QKPISYITTGQNVPDDIIKPNEDKIIRLL 331
Cdd:cd17873 161 QLPVSYVTTGQRVPEDIEVASPLRLARLL 189
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
3-229 |
4.97e-69 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 217.20 E-value: 4.97e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 3 KKYTANTIQDAMNLAKMELGDNITLIDKKEVRKsgirGIFSKKDIELTIGWEKKDN------------------------ 58
Cdd:TIGR03499 4 KKFTAPTMREALKKVKEELGPDAVILSTRKVRK----GLFGKKFVEVTAAIDEEEAaaasaeeeaskaleqadpkplsat 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 59 ------------------------LEQKDLKREIEQLKSIINNM---GFDNKNDNDIDKICKNLLNLDLNQEIVEFIKAD 111
Cdd:TIGR03499 80 aeplelpapqeepaapaaqaaeplLPEEELRKELEALRELLERLlagLAWLQRPPERAKLYERLLEAGVSEELARELLEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 112 LQEmKFNGIDTSKNLVESLKKKI---KIENQAINGK--IALVGPPGVGKTTTIAKLAAKLVFE-ENKKVGVITIDTYRIG 185
Cdd:TIGR03499 160 LPE-DADAEDAWRWLREALEGMLpvkPEEDPILEQGgvIALVGPTGVGKTTTLAKLAARFALEhGKKKVALITTDTYRIG 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 544970261 186 AVEQLKIYTDIMNIPFKGVISPDEMELALDEMKDCDVVLIDTTG 229
Cdd:TIGR03499 239 AVEQLKTYAEILGIPVKVARDPKELREALDRLRDKDLILIDTAG 282
|
|
| SRP54 |
smart00962 |
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ... |
143-333 |
2.22e-63 |
|
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: 199.56 E-value: 2.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 143 GKIALVGPPGVGKTTTIAKLAAKLVFEENKKVGVITIDTYRIGAVEQLKIYTDIMNI-PFKGVISPDEMELALDEMK--- 218
Cdd:smart00962 2 GVILLVGPNGVGKTTTIAKLAARLKLKGGKKVLLVAADTFRAAAVEQLKTYAEILGVvPVAGGEGADPVAVAKDAVElak 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 219 --DCDVVLIDTTGRGYKNSMQILEIKNLIDKAETDNIhLVLNCTTRESDTKAIIDSYRN-VNFKSLIITKLDETITYGSI 295
Cdd:smart00962 82 arGYDVVLIDTAGRLHNDENLMEELKKIKRVIKPDEV-LLVSDATTGQDAVEQAKAFNEaLGLTGIILTKLDGTAKGGAA 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 544970261 296 FNIMNYAQKPISYITTGQNVPdDIIKPNEDKIIRLLLG 333
Cdd:smart00962 161 LSIAAETGLPIKFIGTGEKVP-DLEPFDPERFVSRLLG 197
|
|
| PRK12723 |
PRK12723 |
flagellar biosynthesis regulator FlhF; Provisional |
7-333 |
1.83e-44 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183702 [Multi-domain] Cd Length: 388 Bit Score: 156.60 E-value: 1.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 7 ANTIQDAMNLAKMELGDNITLIDKKEVRKSGIRGIFSKKDIELT------IGWEKKDNLEQK-----DLKRE-------- 67
Cdd:PRK12723 9 GPTYNEVIETIKKKYGKNARVMTYKTIPHGGILGLFSRDWVEVSgyvrydIGQQQINVEDEKrkilqSIKKEenssiedv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 68 IEQLKSIINNM--GFDNKNDNDIDKICKNLLNLDLNQ----EIVEFIKADLQEMKFNGIDTSKNLV-----ESLKKKIKI 136
Cdd:PRK12723 89 LKEVKSLKNELahKKEEINHPTILKIEDILRENDFSEsyikDINEFIKKEFSLSDLDDYDKVRDSViiyiaKTIKCSGSI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 137 ENQAINGKIALVGPPGVGKTTTIAKLAAKLVF---EENKKVGVITIDTYRIGAVEQLKIYTDIMNIPFKGVISPDEMELA 213
Cdd:PRK12723 169 IDNLKKRVFILVGPTGVGKTTTIAKLAAIYGInsdDKSLNIKIITIDNYRIGAKKQIQTYGDIMGIPVKAIESFKDLKEE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 214 LDEMKDCDVVLIDTTGRGYKNSMQILEIKNLIDKAETD-NIHLVLNCTTRESDTKAIIDSYRNVNFKSLIITKLDETITY 292
Cdd:PRK12723 249 ITQSKDFDLVLVDTIGKSPKDFMKLAEMKELLNACGRDaEFHLAVSSTTKTSDVKEIFHQFSPFSYKTVIFTKLDETTCV 328
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 544970261 293 GSIFNIMNYAQKPISYITTGQNVPDDIIKPNEDKIIRLLLG 333
Cdd:PRK12723 329 GNLISLIYEMRKEVSYVTDGQIVPHNISIAEPLTFIKKING 369
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
145-331 |
9.42e-43 |
|
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: 146.53 E-value: 9.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 145 IALVGPPGVGKTTTIAKLAAKLVfEENKKVGVITIDTYRIGAVEQLKIYTDIMNIP-FKGVISPDEMELALDEMK----- 218
Cdd:pfam00448 3 ILLVGLQGSGKTTTIAKLAAYLK-KKGKKVLLVAADTFRAAAIEQLKQLAEKLGVPvFGSKTGADPAAVAFDAVEkakae 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 219 DCDVVLIDTTGRGYKNSMQILEIKNLIDKAETDNIHLVLNCTTRESDTKAIIDSYRNVNFKSLIITKLDETITYGSIFNI 298
Cdd:pfam00448 82 NYDVVLVDTAGRLQNDKNLMDELKKIKRVVAPDEVLLVLDATTGQNAVNQAKAFNEAVGITGVILTKLDGDAKGGAALSI 161
|
170 180 190
....*....|....*....|....*....|...
gi 544970261 299 MNYAQKPISYITTGQNVpDDIIKPNEDKIIRLL 331
Cdd:pfam00448 162 VAETGKPIKFIGVGEKI-DDLEPFDPERFVSRL 193
|
|
| PRK12724 |
PRK12724 |
flagellar biosynthesis regulator FlhF; Provisional |
4-328 |
1.64e-36 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183703 [Multi-domain] Cd Length: 432 Bit Score: 136.25 E-value: 1.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 4 KYTANTIQDAMNLAKMELGDNITLIDKKEVRKSGI--RGIFSKKDIELTIGWEKKDNLEQKdLKREIEQLKSIINNMGF- 80
Cdd:PRK12724 5 KIRGKSYQDCLMEMKMKYGSEATVISQTVVTEGGVmgTGLLAKKMIEIQIGIPEKQASREK-IERKLQDLKELLKQKSYt 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 81 ------------------------------------------------------------------DNKNDNDIDKICKN 94
Cdd:PRK12724 84 eperkktlqtlkplserleekesaiyeiesfeleeviteperpvglsfekelfeknsflesettivRKEKDSPLQRLGER 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 95 LLNLDLNQEIVEFIKADLQEmKFNGIDTSKN------LVESLKKKIKIENQAINGK-------IALVGPPGVGKTTTIAK 161
Cdd:PRK12724 164 LVREGMSQSYVEEMASKLEE-RLSPVDQGRNhnvterAVTYLEERVSVDSDLFSGTgknqrkvVFFVGPTGSGKTTSIAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 162 LAAKLVFEENKKVGVITIDTYRIGAVEQLKIYTDIMNIPFKGV--ISPDEMELALDemkDCDVVLIDTTGRGYKNSMQIL 239
Cdd:PRK12724 243 LAAKYFLHMGKSVSLYTTDNYRIAAIEQLKRYADTMGMPFYPVkdIKKFKETLARD---GSELILIDTAGYSHRNLEQLE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 240 EIKNLIDK-AETDNIH--LVLNCTTRESDTKAIIDSYRNVNFKSLIITKLDETITYGSIFNIMNYAQKPISYITTGQNVP 316
Cdd:PRK12724 320 RMQSFYSCfGEKDSVEnlLVLSSTSSYHHTLTVLKAYESLNYRRILLTKLDEADFLGSFLELADTYSKSFTYLSVGQEVP 399
|
410
....*....|..
gi 544970261 317 DDIIkPNEDKII 328
Cdd:PRK12724 400 FDIL-NATKNLM 410
|
|
| flhF |
PRK06995 |
flagellar biosynthesis protein FlhF; |
143-323 |
5.54e-36 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235904 [Multi-domain] Cd Length: 484 Bit Score: 135.86 E-value: 5.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 143 GKIALVGPPGVGKTTTIAKLAAKLVFEEN-KKVGVITIDTYRIGAVEQLKIYTDIMNIPFKGVISPDEMELALDEMKDCD 221
Cdd:PRK06995 257 GVFALMGPTGVGKTTTTAKLAARCVMRHGaSKVALLTTDSYRIGGHEQLRIYGKILGVPVHAVKDAADLRLALSELRNKH 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 222 VVLIDTTGRGYKNSM---QI-------LEIKNLidkaetdnihLVLNCTTReSDT-KAIIDSYRNVNFKSLIITKLDETI 290
Cdd:PRK06995 337 IVLIDTIGMSQRDRMvseQIamlhgagAPVKRL----------LLLNATSH-GDTlNEVVQAYRGPGLAGCILTKLDEAA 405
|
170 180 190
....*....|....*....|....*....|...
gi 544970261 291 TYGSIFNIMNYAQKPISYITTGQNVPDDIIKPN 323
Cdd:PRK06995 406 SLGGALDVVIRYKLPLHYVSNGQRVPEDLHLAN 438
|
|
| flhF |
PRK14723 |
flagellar biosynthesis regulator FlhF; Provisional |
143-328 |
9.61e-36 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 237802 [Multi-domain] Cd Length: 767 Bit Score: 137.24 E-value: 9.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 143 GKIALVGPPGVGKTTTIAKLAAKLVFEENK-KVGVITIDTYRIGAVEQLKIYTDIMNIPFKGVISPDEMELALDEMKDCD 221
Cdd:PRK14723 186 GVLALVGPTGVGKTTTTAKLAARCVAREGAdQLALLTTDSFRIGALEQLRIYGRILGVPVHAVKDAADLRFALAALGDKH 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 222 VVLIDTTG---RGYKNSMQILEIKNLidKAETDNIhLVLNCTTRESDTKAIIDSYRN---VNFKSLIITKLDETITYGSI 295
Cdd:PRK14723 266 LVLIDTVGmsqRDRNVSEQIAMLCGV--GRPVRRL-LLLNAASHGDTLNEVVHAYRHgagEDVDGCIITKLDEATHLGPA 342
|
170 180 190
....*....|....*....|....*....|...
gi 544970261 296 FNIMNYAQKPISYITTGQNVPDDIIKPNEDKII 328
Cdd:PRK14723 343 LDTVIRHRLPVHYVSTGQKVPEHLELAQADELV 375
|
|
| SRP_G_like |
cd03115 |
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ... |
145-331 |
4.43e-34 |
|
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349769 [Multi-domain] Cd Length: 193 Bit Score: 123.64 E-value: 4.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 145 IALVGPPGVGKTTTIAKLAAKLVfEENKKVGVITIDTYRIGAVEQLKIYTDIMNIPF----KGVISPDEMELALDEMKDC 220
Cdd:cd03115 3 ILLVGLQGSGKTTTLAKLARYYQ-EKGKKVLLIAADTFRAAAVEQLKTLAEKLGVPVfesyTGTDPASIAQEAVEKAKLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 221 --DVVLIDTTGRGYKNSMQILEIKNLIDKAETDNIHLVLNCTTRESDTKAIIDSYRNVNFKSLIITKLDETITYGSIFNI 298
Cdd:cd03115 82 gyDVLLVDTAGRLQKDEPLMEELKKVKEVESPDEVLLVLDATTGQEALSQAKAFNEAVGLTGVILTKLDGTAKGGAALSI 161
|
170 180 190
....*....|....*....|....*....|...
gi 544970261 299 MNYAQKPISYITTGQNvPDDIIKPNEDKIIRLL 331
Cdd:cd03115 162 VAETKKPIKFIGVGEK-PEDLEPFDPERFVSAL 193
|
|
| flhF |
PRK14721 |
flagellar biosynthesis regulator FlhF; Provisional |
143-324 |
2.16e-33 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173184 [Multi-domain] Cd Length: 420 Bit Score: 127.76 E-value: 2.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 143 GKIALVGPPGVGKTTTIAKLAAKLVFEEN-KKVGVITIDTYRIGAVEQLKIYTDIMNIPFKGVISPDEMELALDEMKDCD 221
Cdd:PRK14721 192 GVYALIGPTGVGKTTTTAKLAARAVIRHGaDKVALLTTDSYRIGGHEQLRIYGKLLGVSVRSIKDIADLQLMLHELRGKH 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 222 VVLIDTTGRGYKNSMQILEIKnLIDKAETDNIHLV-LNCTTRESDTKAIIDSYRNVNFKSLIITKLDETITYGSIFNIMN 300
Cdd:PRK14721 272 MVLIDTVGMSQRDQMLAEQIA-MLSQCGTQVKHLLlLNATSSGDTLDEVISAYQGHGIHGCIITKVDEAASLGIALDAVI 350
|
170 180
....*....|....*....|....
gi 544970261 301 YAQKPISYITTGQNVPDDIIKPNE 324
Cdd:PRK14721 351 RRKLVLHYVTNGQKVPEDLHEANS 374
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
143-323 |
1.41e-29 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 118.55 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 143 GKIALVGPPGVGKTTTIAKLAAKLVfEEN--KKVGVITIDTYRIGAVEQLKIYTDIMNIPFKGVISPDEMELALDEMKDC 220
Cdd:PRK12727 351 GVIALVGPTGAGKTTTIAKLAQRFA-AQHapRDVALVTTDTQRVGGREQLHSYGRQLGIAVHEADSAESLLDLLERLRDY 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 221 DVVLIDTTGRGYKNSMQILEIkNLIDKAETDNIHLVLNCTTRESDTKAIIDSYRNVNFKSLIITKLDETITYGSIFNIMN 300
Cdd:PRK12727 430 KLVLIDTAGMGQRDRALAAQL-NWLRAARQVTSLLVLPANAHFSDLDEVVRRFAHAKPQGVVLTKLDETGRFGSALSVVV 508
|
170 180
....*....|....*....|...
gi 544970261 301 YAQKPISYITTGQNVPDDIIKPN 323
Cdd:PRK12727 509 DHQMPITWVTDGQRVPDDLHRAN 531
|
|
| PRK12726 |
PRK12726 |
flagellar biosynthesis regulator FlhF; Provisional |
121-335 |
2.05e-29 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 183704 [Multi-domain] Cd Length: 407 Bit Score: 116.37 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 121 DTSKNLVESLKKKIKIENQ-AINGK--IALVGPPGVGKTTTIAKLAAKLVfEENKKVGVITIDTYRIGAVEQLKIYTDIM 197
Cdd:PRK12726 182 DITDWFVPYLSGKLAVEDSfDLSNHriISLIGQTGVGKTTTLVKLGWQLL-KQNRTVGFITTDTFRSGAVEQFQGYADKL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 198 NIPFKGVISPDEMELALDEMK--DC-DVVLIDTTGRGYKNSMQILEIKnlidkAETDNIHLVLNCTT-----RESDTKAI 269
Cdd:PRK12726 261 DVELIVATSPAELEEAVQYMTyvNCvDHILIDTVGRNYLAEESVSEIS-----AYTDVVHPDLTCFTfssgmKSADVMTI 335
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544970261 270 IDSYRNVNFKSLIITKLDETITYGSIFNIMNYAQKPISYITTGQNVPDDIIKPNEDKIIRLLLGVE 335
Cdd:PRK12726 336 LPKLAEIPIDGFIITKMDETTRIGDLYTVMQETNLPVLYMTDGQNITENIFRPKSRWLAERFVGTD 401
|
|
| flhF |
PRK11889 |
flagellar biosynthesis protein FlhF; |
13-319 |
8.00e-29 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 183360 [Multi-domain] Cd Length: 436 Bit Score: 115.16 E-value: 8.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 13 AMNLAKMELGDNITLIDKKE-VRKSGIRGIFSKKDIELTigwekKDNLEQKDLKREIEQLKSiinNMGFDNKNDNDIDKI 91
Cdd:PRK11889 108 PMSYAAMQTGNSEEWARKKEkLLKLFEKGIVVVKQTEET-----KVTKKQKAVKKVVPVKKE---EVVVKKEKQESVPFI 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 92 CKNLLNLdLNQEIVE--FIKADLQEMKFNGIDTS--------KNLVESLKKKIKIEN--QAINGKIALVGPPGVGKTTTI 159
Cdd:PRK11889 180 IQKVIRM-LEQNDVEqyFIHAYAEKLKVKFENATmiteeeviEYILEDMRSHFNTENvfEKEVQTIALIGPTGVGKTTTL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 160 AKLAAKLvFEENKKVGVITIDTYRIGAVEQLKIYTDIMNIPFKGVISPDEMELALDEMKD---CDVVLIDTTGRGYKNSM 236
Cdd:PRK11889 259 AKMAWQF-HGKKKTVGFITTDHSRIGTVQQLQDYVKTIGFEVIAVRDEAAMTRALTYFKEearVDYILIDTAGKNYRASE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 237 QILEIKNLIDKAETDNIHLVLNCTTRESDTKAIIDSYRNVNFKSLIITKLDETITYGSIFNIMNYAQKPISYITTGQNVP 316
Cdd:PRK11889 338 TVEEMIETMGQVEPDYICLTLSASMKSKDMIEIITNFKDIHIDGIVFTKFDETASSGELLKIPAVSSAPIVLMTDGQDVK 417
|
...
gi 544970261 317 DDI 319
Cdd:PRK11889 418 KNI 420
|
|
| flhF |
PRK14722 |
flagellar biosynthesis regulator FlhF; Provisional |
143-319 |
5.66e-28 |
|
flagellar biosynthesis regulator FlhF; Provisional
Pssm-ID: 173185 [Multi-domain] Cd Length: 374 Bit Score: 112.12 E-value: 5.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 143 GKIALVGPPGVGKTTTIAKLAAKLVFEEN-KKVGVITIDTYRIGAVEQLKIYTDIMNIPFKGVISPDEMELALDEMKDCD 221
Cdd:PRK14722 138 GVFALMGPTGVGKTTTTAKLAARCVMRFGaSKVALLTTDSYRIGGHEQLRIFGKILGVPVHAVKDGGDLQLALAELRNKH 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 222 VVLIDTTGRGYKNSMQILEIKNLIDKAETDNIHLVLNCTTRESDTKAIIDSYRNV---------NFKSLIITKLDETITY 292
Cdd:PRK14722 218 MVLIDTIGMSQRDRTVSDQIAMLHGADTPVQRLLLLNATSHGDTLNEVVQAYRSAagqpkaalpDLAGCILTKLDEASNL 297
|
170 180
....*....|....*....|....*..
gi 544970261 293 GSIFNIMNYAQKPISYITTGQNVPDDI 319
Cdd:PRK14722 298 GGVLDTVIRYKLPVHYVSTGQKVPENL 324
|
|
| flhF |
PRK06731 |
flagellar biosynthesis regulator FlhF; Validated |
100-319 |
2.90e-25 |
|
flagellar biosynthesis regulator FlhF; Validated
Pssm-ID: 75717 [Multi-domain] Cd Length: 270 Bit Score: 102.52 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 100 LNQEIVEFIKADLQEmKFNgidtSKNLVEslkKKIKienqaingKIALVGPPGVGKTTTIAKLAAKLvFEENKKVGVITI 179
Cdd:PRK06731 49 ITEEVIEYILEDMSS-HFN----TENVFE---KEVQ--------TIALIGPTGVGKTTTLAKMAWQF-HGKKKTVGFITT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 180 DTYRIGAVEQLKIYTDIMNIPFKGVISPDEMELALDEMKD---CDVVLIDTTGRGYKNSMQILEIKNLIDKAETDNIHLV 256
Cdd:PRK06731 112 DHSRIGTVQQLQDYVKTIGFEVIAVRDEAAMTRALTYFKEearVDYILIDTAGKNYRASETVEEMIETMGQVEPDYICLT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544970261 257 LNCTTRESDTKAIIDSYRNVNFKSLIITKLDETITYGSIFNIMNYAQKPISYITTGQNVPDDI 319
Cdd:PRK06731 192 LSASMKSKDMIEIITNFKDIHIDGIVFTKFDETASSGELLKIPAVSSAPIVLMTDGQDVKKNI 254
|
|
| FtsY |
cd17874 |
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ... |
145-331 |
7.15e-25 |
|
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: 99.57 E-value: 7.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 145 IALVGPPGVGKTTTIAKLAAKLVfEENKKVGVITIDTYRIGAVEQLKIYTDIMNIPfkgVISPDE----MELALDEMK-- 218
Cdd:cd17874 3 ILFVGVNGVGKTTTIGKLAHYLK-NQGKKVVLAAGDTFRAAAVEQLEEWAERLGVP---VISQNEgadpAAVAFDAIQaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 219 ---DCDVVLIDTTGRGY--KNSMQILE-IKNLIDKAETDNIH---LVLNCTTRESDTKAIIDSYRNVNFKSLIITKLDET 289
Cdd:cd17874 79 karGIDVVLIDTAGRLHtkKNLMEELKkIKRVIKKKDPEAPHevlLVLDATTGQNALEQAKEFNEAVGLTGIILTKLDGT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 544970261 290 ITYGSIFNIMNYAQKPISYITTGQNVpDDIIKPNEDKIIRLL 331
Cdd:cd17874 159 AKGGIVLSIADELKIPVKFVGVGEGI-DDLRPFDPEAFVEAL 199
|
|
| PRK10416 |
PRK10416 |
signal recognition particle-docking protein FtsY; Provisional |
42-335 |
1.36e-24 |
|
signal recognition particle-docking protein FtsY; Provisional
Pssm-ID: 236686 [Multi-domain] Cd Length: 318 Bit Score: 101.71 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 42 FSKKDIELTIGWEKKdnLEQKdLKREIEQLKSIINNMGFDNKNDND-IDKICKNLLNLDLNQEIVEFIKADL-QEMKFNG 119
Cdd:PRK10416 5 LKKKKKEKKEGWFER--LKKG-LSKTRENFGEGINGLFAKKKIDEDlLEELEELLIEADVGVETTEEIIEELrERVKRKN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 120 IDTSKNLVESLKKKIKIENQAINGKIAL----------VGPPGVGKTTTIAKLAAKLVfEENKKVGVITIDTYRIGAVEQ 189
Cdd:PRK10416 82 LKDPEELKELLKEELAEILEPVEKPLNIeekkpfvilvVGVNGVGKTTTIGKLAHKYK-AQGKKVLLAAGDTFRAAAIEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 190 LKIYTDIMNIPfkgVISP-----------DEMELALDemKDCDVVLIDTTGR--GYKNSMQILE-IKNLIDKAETDNIH- 254
Cdd:PRK10416 161 LQVWGERVGVP---VIAQkegadpasvafDAIQAAKA--RGIDVLIIDTAGRlhNKTNLMEELKkIKRVIKKADPDAPHe 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 255 --LVLNCTTRE---SDTKAIIDSyrnVNFKSLIITKLDETITYGSIFNIMNYAQKPISYITTGQNVpDDIIKPNEDKIIR 329
Cdd:PRK10416 236 vlLVLDATTGQnalSQAKAFHEA---VGLTGIILTKLDGTAKGGVVFAIADELGIPIKFIGVGEGI-DDLQPFDAEEFVD 311
|
....*.
gi 544970261 330 LLLGVE 335
Cdd:PRK10416 312 ALLGGE 317
|
|
| ftsY |
TIGR00064 |
signal recognition particle-docking protein FtsY; There is a weak division between FtsY and ... |
95-332 |
3.16e-24 |
|
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: 99.64 E-value: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 95 LLNLDLNQEIVEFIKADL-QEMKFNGIDTSKNLVESLKKKIK------------IENQAINGK---IALVGPPGVGKTTT 158
Cdd:TIGR00064 14 LLESDVGYEVVEKIIEALkKELKGKKVKDAEKLKEILKEYLKeilkedllkntdLELIVEENKpnvILFVGVNGVGKTTT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 159 IAKLAAKLVfEENKKVGVITIDTYRIGAVEQLKIYTDIMNIPfkgVISP----DEMELALDEM-----KDCDVVLIDTTG 229
Cdd:TIGR00064 94 IAKLANKLK-KQGKSVLLAAGDTFRAAAIEQLEEWAKRLGVD---VIKQkegaDPAAVAFDAIqkakaRNIDVVLIDTAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 230 R--GYKNSMQILE-IKNLIDKAETDNIH---LVLNCTTRESDTKAIIDSYRNVNFKSLIITKLDETITYGSIFNIMNYAQ 303
Cdd:TIGR00064 170 RlqNKVNLMDELKkIKRVIKKVDKDAPDevlLVLDATTGQNALEQAKVFNEAVGLTGIILTKLDGTAKGGIILSIAYELK 249
|
250 260
....*....|....*....|....*....
gi 544970261 304 KPISYITTGQNVpDDIIKPNEDKIIRLLL 332
Cdd:TIGR00064 250 LPIKFIGVGEKI-DDLAPFDADWFVEALF 277
|
|
| FtsY |
COG0552 |
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ... |
102-335 |
1.25e-22 |
|
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440318 [Multi-domain] Cd Length: 303 Bit Score: 95.86 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 102 QEIVEFIKADLQEMKFNGIDTSKN-LVESLKKKIKIENQAIN---GK---IALVGPPGVGKTTTIAKLAAKLVfEENKKV 174
Cdd:COG0552 53 EEIIEELRERVKRKKLKDPEELKEaLKEELLEILDPVDKPLAieeKKpfvILVVGVNGVGKTTTIGKLAHRLK-AEGKSV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 175 GVITIDTYRIGAVEQLKIYTDIMNIPfkgVISPDE-----------MELALDemKDCDVVLIDTTGRGY--KNSMQILE- 240
Cdd:COG0552 132 LLAAGDTFRAAAIEQLEVWGERVGVP---VIAQKEgadpaavafdaIQAAKA--RGADVVIIDTAGRLHnkKNLMEELKk 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 241 IKNLIDKAETDNIH---LVLNCTT-----------RESdtkaiidsyrnVNFKSLIITKLDETITYGSIFNIMNYAQKPI 306
Cdd:COG0552 207 IKRVIKKLDPDAPHevlLVLDATTgqnalsqakvfNEA-----------VGVTGIVLTKLDGTAKGGVVLAIADELGIPI 275
|
250 260
....*....|....*....|....*....
gi 544970261 307 SYITTGQNVpDDIIKPNEDKIIRLLLGVE 335
Cdd:COG0552 276 KFIGVGEGI-DDLRPFDAEEFVDALFGEE 303
|
|
| PRK00771 |
PRK00771 |
signal recognition particle protein Srp54; Provisional |
144-333 |
5.77e-22 |
|
signal recognition particle protein Srp54; Provisional
Pssm-ID: 179118 [Multi-domain] Cd Length: 437 Bit Score: 95.66 E-value: 5.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 144 KIALVGPPGVGKTTTIAKLAaKLVFEENKKVGVITIDTYRIGAVEQLKIYTDIMNIPFKG-VISPDEMELA---LDEMKD 219
Cdd:PRK00771 97 TIMLVGLQGSGKTTTAAKLA-RYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGVPFYGdPDNKDAVEIAkegLEKFKK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 220 CDVVLIDTTGRGYKNSMQILEIKNLIDKAETDNIHLVLNCTT----RESdTKAIIDSyrnVNFKSLIITKLDETITYGSI 295
Cdd:PRK00771 176 ADVIIVDTAGRHALEEDLIEEMKEIKEAVKPDEVLLVIDATIgqqaKNQ-AKAFHEA---VGIGGIIITKLDGTAKGGGA 251
|
170 180 190
....*....|....*....|....*....|....*...
gi 544970261 296 FNIMNYAQKPISYITTGQNVpDDIIKPNEDKIIRLLLG 333
Cdd:PRK00771 252 LSAVAETGAPIKFIGTGEKI-DDLERFDPDRFISRLLG 288
|
|
| PRK14974 |
PRK14974 |
signal recognition particle-docking protein FtsY; |
98-333 |
3.84e-21 |
|
signal recognition particle-docking protein FtsY;
Pssm-ID: 237875 [Multi-domain] Cd Length: 336 Bit Score: 92.34 E-value: 3.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 98 LDLNQEIVEFIKADLQEMKFN-GIDTSKNLVESLKKKIK-----------IENQAINGK---IALVGPPGVGKTTTIAKL 162
Cdd:PRK14974 81 LEVAEEILESLKEKLVGKKVKrGEDVEEIVKNALKEALLevlsvgdlfdlIEEIKSKGKpvvIVFVGVNGTGKTTTIAKL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 163 AAKLvfEENKKVGVITI-DTYRIGAVEQLKIYTDIMNIP-FKGVISPDEMELALD-----EMKDCDVVLIDTTGRGYKNS 235
Cdd:PRK14974 161 AYYL--KKNGFSVVIAAgDTFRAGAIEQLEEHAERLGVKvIKHKYGADPAAVAYDaiehaKARGIDVVLIDTAGRMHTDA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 236 MQILEIKNLIDKAETDNIHLVLNCTTRESDTKAIIDSYRNVNFKSLIITKLDETITYGSIFNIMNYAQKPISYITTGQNV 315
Cdd:PRK14974 239 NLMDELKKIVRVTKPDLVIFVGDALAGNDAVEQAREFNEAVGIDGVILTKVDADAKGGAALSIAYVIGKPILFLGVGQGY 318
|
250
....*....|....*...
gi 544970261 316 pDDIIKPNEDKIIRLLLG 333
Cdd:PRK14974 319 -DDLIPFDPDWFVDKLLG 335
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
144-317 |
5.62e-21 |
|
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: 88.79 E-value: 5.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 144 KIALVGPPGVGKTTTIAKLAAklvFEENK--KVGVITIDTYRIGAVEQLKIYTDIMNIPFKGviSPDEM---ELA---LD 215
Cdd:cd17875 2 VIMFVGLQGSGKTTTAAKLAY---YYQKKgyKVGLVCADTFRAGAFDQLKQNATKARVPFYG--SYTEKdpvKIAkegVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 216 EMKD--CDVVLIDTTGRGYKNSMQILEIKNLIDKAETDNIHLVLNCT---TRESDTKAIIDSyrnVNFKSLIITKLDETI 290
Cdd:cd17875 77 KFKKekFDIIIVDTSGRHKQEEELFEEMKQISDAVKPDEVILVIDASigqAAEDQAKAFKEA---VDIGSVIITKLDGHA 153
|
170 180
....*....|....*....|....*..
gi 544970261 291 TYGSIFNIMNYAQKPISYITTGQNVPD 317
Cdd:cd17875 154 KGGGALSAVAATGAPIIFIGTGEHIDD 180
|
|
| SRP54_euk |
TIGR01425 |
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ... |
88-337 |
1.31e-18 |
|
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: 86.04 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 88 IDKICKNLLNLDLN----QEIVEFIK--ADLQEMKfNGIDTSK-----------NLVESLKKKIKIENQAINgKIALVGP 150
Cdd:TIGR01425 31 LKEICTALLESDVNpklvRQMRNNIKkkINLEDIA-SGINKRKliqdavfeelcNLVDPGVEAFTPKKGKTC-VIMFVGL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 151 PGVGKTTTIAKLAaklVFEENK--KVGVITIDTYRIGAVEQLKIYTDIMNIPFKGV-ISPDEMELALDEMK-----DCDV 222
Cdd:TIGR01425 109 QGAGKTTTCTKLA---YYYKRRgfKPALVCADTFRAGAFDQLKQNATKAGIPFYGSyEESDPVKIASEGVEkfrkeKFDI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 223 VLIDTTGRGYKNSMQILEIKNLIDKAETDNIHLVLNCT---TRESDTKAIIDSyrnVNFKSLIITKLDETITYGSIFNIM 299
Cdd:TIGR01425 186 IIVDTSGRHKQEKELFEEMQQVREAIKPDSIIFVMDGSigqAAFGQAKAFKDS---VEVGSVIITKLDGHAKGGGALSAV 262
|
250 260 270
....*....|....*....|....*....|....*....
gi 544970261 300 NYAQKPISYITTGQNVPD-DIIKPneDKIIRLLLGVESI 337
Cdd:TIGR01425 263 AATKSPIIFIGTGEHVDEfEIFDA--EPFVSKLLGMGDL 299
|
|
| SRP_G |
cd18539 |
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ... |
145-317 |
2.17e-18 |
|
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: 81.88 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 145 IALVGPPGVGKTTTIAKLAaKLVFEENKKVGVITIDTYRIGAVEQLKIYTDIMNIPF----KGVISPDEMELALDEMKD- 219
Cdd:cd18539 3 ILLVGLQGSGKTTTAAKLA-LYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGVPVfesgDGQSPVDIAKRALEKAKEe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 220 -CDVVLIDTTGRgyknsMQI-----LEIKNLIDKAETDNIHLVLNCTTREsDTKAIIDSYRN-VNFKSLIITKLDETITY 292
Cdd:cd18539 82 gFDVVIVDTAGR-----LHIdeelmDELKEIKEVLNPDEVLLVVDAMTGQ-DAVNVAKAFNErLGLTGVVLTKLDGDARG 155
|
170 180
....*....|....*....|....*
gi 544970261 293 GSIFNIMNYAQKPISYITTGQNVPD 317
Cdd:cd18539 156 GAALSIRHVTGKPIKFIGVGEKIED 180
|
|
| Ffh |
COG0541 |
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ... |
144-319 |
1.88e-16 |
|
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440307 [Multi-domain] Cd Length: 423 Bit Score: 79.68 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 144 KIALVGPPGVGKTTTIAKLAAKLVfEENKKVGVITIDTYRIGAVEQLKIYTDIMNIPF---KGVISPDEM-ELALDEMKD 219
Cdd:COG0541 102 VIMMVGLQGSGKTTTAAKLAKYLK-KKGKKPLLVAADVYRPAAIEQLKTLGEQIGVPVfpeEDGKDPVDIaKRALEYAKK 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 220 --CDVVLIDTTGRgyknsMQI-----LEIKNLIDKAETDNIHLVLNCTTREsDTKAIIDSYRN-VNFKSLIITKLDETIT 291
Cdd:COG0541 181 ngYDVVIVDTAGR-----LHIdeelmDELKAIKAAVNPDETLLVVDAMTGQ-DAVNVAKAFNEaLGLTGVILTKLDGDAR 254
|
170 180
....*....|....*....|....*...
gi 544970261 292 YGSIFNIMNYAQKPISYITTGQNVpDDI 319
Cdd:COG0541 255 GGAALSIRAVTGKPIKFIGTGEKL-DDL 281
|
|
| SRalpha_C |
cd17876 |
C-terminal domain of signal recognition particle receptor alpha subunit; The ... |
145-317 |
9.05e-15 |
|
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: 71.88 E-value: 9.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 145 IALVGPPGVGKTTTIAKLAAKLVfEENKKVGVITIDTYRIGAVEQLKIYTDIMNIPF--KG------VISPDEMELALDE 216
Cdd:cd17876 3 IVFCGVNGVGKSTNLAKIAYWLL-SNGFRVLIAACDTFRSGAVEQLRTHARRLGVELyeKGygkdpaAVAKEAIKYARDQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 217 mkDCDVVLIDTTGRGYKNSMQILEIKNLIDKAETDNI-----HLVLNCTTRESDT--KAIIDSYRNVNFKSL---IITKL 286
Cdd:cd17876 82 --GFDVVLIDTAGRMQNNEPLMRALAKLIKENNPDLVlfvgeALVGNDAVDQLKKfnQALADYSPSDNPRLIdgiVLTKF 159
|
170 180 190
....*....|....*....|....*....|....
gi 544970261 287 DeTI--TYGSIFNiMNYAQ-KPISYITTGQNVPD 317
Cdd:cd17876 160 D-TIddKVGAALS-MVYATgQPIVFVGTGQTYTD 191
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
142-263 |
2.40e-07 |
|
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: 49.68 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 142 NGKIALVGPPGVGKTTTIAKLAAKLvfeENKKVGVITIDTYRIGAVEQLKIYTDIMNIPFKGVISPDEMELALDEMK--D 219
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAREL---GPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARklK 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 544970261 220 CDVVLIDTTGRGYKNSMQILEIKN-----LIDKAETDNIHLVLNCTTRE 263
Cdd:smart00382 79 PDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKNLTVILTTNDEK 127
|
|
| MobB |
COG1763 |
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ... |
145-235 |
7.12e-06 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 441369 [Multi-domain] Cd Length: 162 Bit Score: 45.56 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 145 IALVGPPGVGKTTTIAKLAAKLVfEENKKVGVI-------TI-----DTYRI---GAVEQLkiytdimnipfkgVISPDE 209
Cdd:COG1763 4 LGIVGYSGSGKTTLLEKLIPELK-ARGLRVGTIkhahhdfDIdtpgkDSYRHreaGADEVL-------------VASPER 69
|
90 100 110
....*....|....*....|....*....|....*...
gi 544970261 210 M--------ELALDE----MKDCDVVLIDttgrGYKNS 235
Cdd:COG1763 70 WalmtelpeEPSLDEllarLDDVDLVLVE----GFKHE 103
|
|
| THEP1 |
COG1618 |
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism]; |
144-178 |
8.14e-05 |
|
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
Pssm-ID: 441225 [Multi-domain] Cd Length: 175 Bit Score: 42.58 E-value: 8.14e-05
10 20 30
....*....|....*....|....*....|....*
gi 544970261 144 KIALVGPPGVGKTTTIAKLAAKLVFEENKKVGVIT 178
Cdd:COG1618 2 KIFITGRPGVGKTTLLLKVVEELRDEGLRVGGFIT 36
|
|
| HypB |
COG0378 |
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ... |
145-229 |
1.10e-04 |
|
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440147 [Multi-domain] Cd Length: 200 Bit Score: 42.74 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 145 IALVGPPGVGKTTTIAKLAAKLvfEENKKVGVITIDTY------RIGA--VEQLKIYT------DIMNIpfkgvispdem 210
Cdd:COG0378 16 VNLMGSPGSGKTTLLEKTIRAL--KDRLRIAVIEGDIYttedaeRLRAagVPVVQINTggcchlDASMV----------- 82
|
90 100
....*....|....*....|.
gi 544970261 211 ELALDEM--KDCDVVLIDTTG 229
Cdd:COG0378 83 LEALEELdlPDLDLLFIENVG 103
|
|
| AAA_28 |
pfam13521 |
AAA domain; |
144-259 |
1.36e-04 |
|
AAA domain;
Pssm-ID: 433278 [Multi-domain] Cd Length: 164 Bit Score: 41.87 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 144 KIALVGPPGVGKTTTIAKLAAKL---VFEENkkVGVITIDTYRIGAvEQLKIYTDIMNIPfKGVIspDEMELALDEMKDC 220
Cdd:pfam13521 1 RIVITGGPSTGKTTLAEALAARFgypVVPEA--AREILEELGADGG-DALPWVEDLLAFA-RGVL--EAQLEDEAAAAAN 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 544970261 221 DVVLIDT---TGRGYknsMQILEIKN---LIDKAETDNIHLVLNC 259
Cdd:pfam13521 75 DLLFFDRgplDTLAY---SRAYGGPCppeLEAAARASRYDLVFLL 116
|
|
| Rad51B |
cd19493 |
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ... |
138-228 |
2.52e-04 |
|
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51B, together with the other RAD51 paralogs, RAD51C, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site.
Pssm-ID: 410901 [Multi-domain] Cd Length: 222 Bit Score: 41.92 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 138 NQAINGKIAL------VGPPGVGKTT---TIAKLAAKLVFEENKKVGVITIDTYRIGAVEQLKIYTdIMNIPFKGVISPD 208
Cdd:cd19493 1 DTALAGGLPLgaiteiTGASGSGKTQfalTLASSAAMPARKGGLDGGVLYIDTESKFSAERLAEIA-EARFPEAFSGFME 79
|
90 100
....*....|....*....|
gi 544970261 209 EMELALDEMKDCDVVLIDTT 228
Cdd:cd19493 80 ENERAEEMLKRVAVVRVTTL 99
|
|
| MMAA-like |
cd03114 |
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ... |
145-180 |
2.92e-04 |
|
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: 41.79 E-value: 2.92e-04
10 20 30
....*....|....*....|....*....|....*.
gi 544970261 145 IALVGPPGVGKTTTIAKLAAKLVfEENKKVGVITID 180
Cdd:cd03114 49 VGITGPPGAGKSTLIEALGRLLR-EQGHRVAVLAVD 83
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
144-258 |
3.22e-04 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 39.72 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 144 KIALVGP-PGVGKTTTIAKLAAKLVfEENKKVGVITIDTYrigaveqlkIYTDIMNIPFKGVISPDEMELALDEMKDCDV 222
Cdd:cd01983 2 VIAVTGGkGGVGKTTLAAALAVALA-AKGYKVLLIDLDDY---------VLIDGGGGLETGLLLGTIVALLALKKADEVI 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 544970261 223 VLIDTTGRGYKNSMQILEIKNLIDKAETdNIHLVLN 258
Cdd:cd01983 72 VVVDPELGSLLEAVKLLLALLLLGIGIR-PDGIVLN 106
|
|
| PRK13695 |
PRK13695 |
NTPase; |
144-229 |
5.45e-04 |
|
NTPase;
Pssm-ID: 237475 Cd Length: 174 Bit Score: 40.28 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 144 KIALVGPPGVGKTTTIAKLAAKL--------------VFEENKKVG--VITIDT------YRIGAVEQLKIYtdimnipf 201
Cdd:PRK13695 2 KIGITGPPGVGKTTLVLKIAELLkeegykvggfyteeVREGGKRIGfkIIDLDTgeegilARVGFPSRPRVG-------- 73
|
90 100 110
....*....|....*....|....*....|...
gi 544970261 202 KGVISPDEMELALDE-----MKDCDVVLIDTTG 229
Cdd:PRK13695 74 KYVVNLEDLERIGIPaleraLEEADVIIIDEIG 106
|
|
| DEXXQc_Upf1-like |
cd17934 |
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ... |
145-176 |
5.81e-04 |
|
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438708 [Multi-domain] Cd Length: 121 Bit Score: 39.14 E-value: 5.81e-04
10 20 30
....*....|....*....|....*....|....
gi 544970261 145 IALV-GPPGVGKTTTIAKLAAKLVFEE-NKKVGV 176
Cdd:cd17934 1 ISLIqGPPGTGKTTTIAAIVLQLLKGLrGKRVLV 34
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
144-227 |
7.00e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 40.00 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 144 KIALVGPPGVGKTTTIAKLAAKLVFEENKkvGVITIDTYRIGAVEQLKIYTDIMNipfkgvispDEMELALDEMKDCDVV 223
Cdd:pfam13479 4 KILIYGPSGIGKTTFAKTLPKPLFLDTEK--GSKALDGDRFPDIVIRDSWQDFLD---------AIDELTAAELADYKTI 72
|
....
gi 544970261 224 LIDT 227
Cdd:pfam13479 73 VIDT 76
|
|
| DEXXQc_SMUBP2 |
cd18044 |
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
125-172 |
9.01e-04 |
|
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350802 [Multi-domain] Cd Length: 191 Bit Score: 39.90 E-value: 9.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 544970261 125 NLVESLKKKIKIenqAINGK-IALV-GPPGVGKTTTIAKLAAKLVFEENK 172
Cdd:cd18044 1 NLNDSQKEAVKF---ALSQKdVALIhGPPGTGKTTTVVEIILQAVKRGEK 47
|
|
| mobB |
TIGR00176 |
molybdopterin-guanine dinucleotide biosynthesis protein MobB; This molybdenum cofactor ... |
145-257 |
9.54e-04 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobB; This molybdenum cofactor biosynthesis enzyme is similar to the urease accessory protein UreG and to the hydrogenase accessory protein HypB, both GTP hydrolases involved in loading nickel into the metallocenters of their respective target enzymes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]
Pssm-ID: 272943 [Multi-domain] Cd Length: 155 Bit Score: 39.28 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 145 IALVGPPGVGKTTTIAKLaAKLVFEENKKVGVI------------TIDTYRI---GAVEQLKIYTDIMNIPFKGVISPDe 209
Cdd:TIGR00176 2 LQIVGPKNSGKTTLIERL-VKALKARGYRVATIkhdhhdfdidknGKDSYRHreaGADQVIVASSRRYAFMHETQEERD- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 544970261 210 MELALDEMKDCDVVLIDttgrGYKNSM--QILEIKN--LIDKAETDNIHLVL 257
Cdd:TIGR00176 80 LEALLDRLPDLDIILVE----GFKDSPlpKIVVFRNpaEESEIIRPKIIAIA 127
|
|
| NTPase_1 |
pfam03266 |
NTPase; This domain is found across all species from bacteria to human, and the function was ... |
144-175 |
9.60e-04 |
|
NTPase; This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme. The sequence carries both a Walker A and Walker B motif which together are characteriztic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue.
Pssm-ID: 460869 Cd Length: 168 Bit Score: 39.53 E-value: 9.60e-04
10 20 30
....*....|....*....|....*....|..
gi 544970261 144 KIALVGPPGVGKTTTIAKLAAKLVfEENKKVG 175
Cdd:pfam03266 1 RIFITGPPGVGKTTLVLKVAELLK-SSGVKVG 31
|
|
| DExxQc_SF1-N |
cd17914 |
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ... |
147-199 |
1.45e-03 |
|
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. Their helicase core is surrounded by C and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains or domains engaged in protein-protein interactions. SF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438706 [Multi-domain] Cd Length: 121 Bit Score: 37.85 E-value: 1.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 544970261 147 LVGPPGVGKTTTIAKLAAKLVFEENKKVGVITIDTYRIGAVEQLKI-----YTDIMNI 199
Cdd:cd17914 4 IQGPPGTGKTRVLVKIVAALMQNKNGEPGRILLVTPTNKAAAQLDNilvdeAAQILEP 61
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
145-180 |
2.02e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 37.71 E-value: 2.02e-03
10 20 30
....*....|....*....|....*....|....*.
gi 544970261 145 IALVGPPGVGKTTTIAKLAAKLVFEEnkkVGVITID 180
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLLEQLPEVR---DSVVFVD 40
|
|
| RecA-like_Thep1 |
cd19482 |
RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the ... |
145-229 |
3.18e-03 |
|
RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the THEP1 family ATPase domain. It includes nucleoside-triphosphatase THEP 1 from Aquifex aeolicus (aaTHEP1) a nucleoside-phosphatase, with activity towards ATP, GTP, CTP, TTP and UTP; and which may hydrolyze nucleoside diphosphates with lower efficiency. The catalytic function of aaTHEP1 remains unclear, it may be a DNA/RNA modifying enzyme. Human THEP1 (hsTHEP1) may have a general function in many human tissues, as it is widely expressed in most examined tissues (such as in brain, heart, lymph node, skin, pancreas); it is especially highly expressed in embryonic and various tumor tissues. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410890 [Multi-domain] Cd Length: 164 Bit Score: 37.97 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 145 IALVGPPGVGKTTTIAKLAAKL--------------VFEENKKVG--VITIDT------YRIGAVEQlKIYTDIMNIPFK 202
Cdd:cd19482 1 IFITGPPGVGKTTLVLKVAELLkesglkvggfytpeVREGGKRIGfkIVDLASgergwlARVGAGSP-KVGKYGVDVDEL 79
|
90 100
....*....|....*....|....*..
gi 544970261 203 GVISPDEMELALDEmkdCDVVLIDTTG 229
Cdd:cd19482 80 EEIAVPALRRALEE---ADVIIIDEIG 103
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
145-274 |
4.12e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 37.13 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 145 IALVGPPGVGKtTTIAKLAAKLVFEENKKVGVITIDTYRIGAVEQLKIYTDIMNIPFKgvispdemelaLDEMKDCDVVL 224
Cdd:cd00009 22 LLLYGPPGTGK-TTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFE-----------LAEKAKPGVLF 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 544970261 225 IDTTGRGYKNS----MQILEIKNlIDKAETDNIHLVLNCTTRESDTKAIIDSYR 274
Cdd:cd00009 90 IDEIDSLSRGAqnalLRVLETLN-DLRIDRENVRVIGATNRPLLGDLDRALYDR 142
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
144-258 |
4.57e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 36.44 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 144 KIALVGPPGVGKTTTIAKLAAKLVFEENKKvGViTID-TYRIGAVEQLKIYtdIMNIP--FKGVISPDEMELALDEMKDC 220
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVSDYP-GT-TRDpNEGRLELKGKQII--LVDTPglIEGASEGEGLGRAFLAIIEA 76
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 544970261 221 DVVL--IDTTGrGYKNsmQILEIKNLIDKAETDnIHLVLN 258
Cdd:pfam01926 77 DLILfvVDSEE-GITP--LDEELLELLRENKKP-IILVLN 112
|
|
| DEXXQc_UPF1 |
cd18039 |
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ... |
149-259 |
4.79e-03 |
|
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of Nonsense Transcripts, or ATP-Dependent Helicase RENT1) is an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. It is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. It is recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) located downstream from the termination codon through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Diseases associated with UPF1 include juvenile amyotrophic lateral sclerosis and epidermolysis bullosa, junctional, non-Herlitz type. UPF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350797 [Multi-domain] Cd Length: 234 Bit Score: 38.00 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 149 GPPGVGKTTTIAKLAAKLVFEENKKVGVIT---IdtyrigAVEQLKiyTDIMNIPFK----------GVISPDEmELALD 215
Cdd:cd18039 23 GPPGTGKTVTSATIVYHLVKQGNGPVLVCApsnV------AVDQLT--EKIHQTGLKvvrlcaksreAVESPVS-FLALH 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 544970261 216 EMKDCdvvlIDTTGRGYKNSMQILEIKNLIDKAETDNIHLVLNC 259
Cdd:cd18039 94 NQVRN----LDSAEKLELLKLLKLETGELSSADEKRYRKLKRKA 133
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
145-180 |
5.30e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 38.40 E-value: 5.30e-03
10 20 30
....*....|....*....|....*....|....*.
gi 544970261 145 IALVGPPGVGKTTTIAKLaaKLVFEenKKVGVITID 180
Cdd:PRK13657 364 VAIVGPTGAGKSTLINLL--QRVFD--PQSGRILID 395
|
|
| CDC6 |
COG1474 |
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair]; |
145-225 |
6.11e-03 |
|
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
Pssm-ID: 441083 [Multi-domain] Cd Length: 389 Bit Score: 38.29 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544970261 145 IALVGPPGVGKTTTIAKLAAKL---VFEENKKVGVITID------TYRI--GAVEQLKiytDIMNIPFKGvISPDEMELA 213
Cdd:COG1474 54 VLIYGPTGTGKTAVAKYVLEELeeeAEERGVDVRVVYVNcrqastRYRVlsRILEELG---SGEDIPSTG-LSTDELFDR 129
|
90
....*....|...
gi 544970261 214 L-DEMKDCDVVLI 225
Cdd:COG1474 130 LyEALDERDGVLV 142
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
145-177 |
6.34e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.84 E-value: 6.34e-03
10 20 30
....*....|....*....|....*....|...
gi 544970261 145 IALVGPPGVGKTTTIAKLAAKLvfEENKKVGVI 177
Cdd:COG3267 46 VVLTGEVGTGKTTLLRRLLERL--PDDVKVAYI 76
|
|
| recD |
PRK10875 |
exodeoxyribonuclease V subunit alpha; |
140-167 |
8.50e-03 |
|
exodeoxyribonuclease V subunit alpha;
Pssm-ID: 236783 [Multi-domain] Cd Length: 615 Bit Score: 38.00 E-value: 8.50e-03
10 20
....*....|....*....|....*....
gi 544970261 140 AINGKIALV-GPPGVGKTTTIAKLAAKLV 167
Cdd:PRK10875 164 ALTRRISVIsGGPGTGKTTTVAKLLAALI 192
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
144-190 |
8.78e-03 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 36.27 E-value: 8.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 544970261 144 KIALVGPPGVGKTTTIAKLAAKLVFEENKkvgVITIDTYRIGAVEQL 190
Cdd:cd03221 28 RIGLVGRNGAGKSTLLKLIAGELEPDEGI---VTWGSTVKIGYFEQL 71
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