|
Name |
Accession |
Description |
Interval |
E-value |
| SelB |
COG3276 |
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ... |
6-615 |
0e+00 |
|
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 442507 [Multi-domain] Cd Length: 630 Bit Score: 597.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGIETDRLEEEKRRGISIALGFAWLEVPGG-EIDLIDMPGHERFVRTMVAGAAGIRAVVLAV 84
Cdd:COG3276 3 IGTAGHIDHGKTTLVKALTGIDTDRLKEEKKRGITIDLGFAYLPLPDGrRLGFVDVPGHEKFIKNMLAGAGGIDLVLLVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 85 SAAEGIRPQTREHVEIAGLLGVEAGVVAVTQCDLADEARAAEVGADAARLLAAHGMADAPVVHTSALDGRGLPELRATLA 164
Cdd:COG3276 83 AADEGVMPQTREHLAILDLLGIKRGIVVLTKADLVDEEWLELVEEEIRELLAGTFLEDAPIVPVSAVTGEGIDELRAALD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 165 ELMQRVPAPAEQGLAYLPVDRTFAVAGFGTVVTGTLQRGRLSVGEEVELTPGGKRARIRALQVHGRQVQQAIPGGRTAVN 244
Cdd:COG3276 163 ALAAAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVALN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 245 LRGVESAEVGRGCALATPGLLHASDWLDVHLRALPGDHRPLETGREYKLLLAAGEIPARLRLLDREILHPGEAAPAQLRC 324
Cdd:COG3276 243 LAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLPSAPRPLKHWQRVHLHHGTAEVLARVVLLDREELAPGEEALAQLRL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 325 AGPVAVPAREGFVLRAGSPARTVAGGRVLDPQTRRHRRNDPAVLDRLLSLAGAGPQEVVSQLLTGTgPAGVLLDEAARLS 404
Cdd:COG3276 323 EEPLVAARGDRFILRDYSPRRTIGGGRVLDPNPPKRKRRSPERLAWLEALAKGDPAELLAALLALA-PGGLSLAELARLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 405 GHAPSWVISWLPELQARQV-----GPLLVTAAALEGLKRDIRTALAEHHHSAPASPGLMFEDVLDRL--RAARPVLELAV 477
Cdd:COG3276 402 GLSEEELAALLEELGARVVvlgggDRLLVSAAALEALKERLLAALAEFHEKNPLRPGLSREELRRRLlpRLPEKLFDALL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 478 QELLAGGELARTQGCLRLPGFRPSTLAAEGELSRRIEAAIRAGGLQPPDLKELPGGGSVAIKAIQRLLAggVLVRARDRV 557
Cdd:COG3276 482 EELLAEGELVLTGGWLHLPGHKVTLSAEEEALWQRLLPLLAAGGFPPPWLRELAAELGLEEEAVRELLR--LLLRLGELV 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1481165581 558 QKRELLFHRDAVADAAERLATAFAARPEGFLVGEAGRVLGISRKYSVPLLEYLDGVGI 615
Cdd:COG3276 560 KVVDDLFYLAAALAALAALLAALLAETGAAAAADRRDLLGGRRKLLLLLLEFFDRRRR 617
|
|
| selB |
TIGR00475 |
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ... |
6-615 |
5.53e-88 |
|
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]
Pssm-ID: 129567 [Multi-domain] Cd Length: 581 Bit Score: 285.23 E-value: 5.53e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGIETDRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRTMVAGAAGIRAVVLAVS 85
Cdd:TIGR00475 3 IATAGHVDHGKTTLLKALTGIAADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAIAGGGGIDAALLVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 86 AAEGIRPQTREHVEIAGLLGVEAGVVAVTQCDLADEARAAEVGADAARLLAAHGMA-DAPVVHTSALDGRGLPELRATLA 164
Cdd:TIGR00475 83 ADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEEIKRTEMFMKQILNSYIFLkNAKIFKTSAKTGQGIGELKKELK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 165 ELMQRVPAPAEQGLAYLPVDRTFAVAGFGTVVTGTLQRGRLSVGEEVELTPGGKRARIRALQVHGRQVQQAIPGGRTAVN 244
Cdd:TIGR00475 163 NLLESLDIKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQRIALN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 245 LRGVESAEVGRGCALATPglLHASDWLDVHLRAlpgdHRPLETGREYKLLLAAGEIPARLRLLDREIlhpgeaapAQLRC 324
Cdd:TIGR00475 243 LMDVEPESLKRGLLILTP--EDPKLRVVVKFIA----EVPLLELQPYHIAHGMSVTTGKISLLDKGI--------ALLTL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 325 AGPVAVPAREGFVLRAgSPARTVAGGRVLDPQTRRHRRNdpavldRLLSLAGAGPQEVVSQLLTGTGPAGVLLDEAARLS 404
Cdd:TIGR00475 309 DAPLILAKGDKLVLRD-SSGNFLAGARVLEPPVRVKRKA------FIAELIKAGDSCYCIFLLLERGAVDLGLEWFKQLT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 405 GHAPSWViswLPELQARQVGPLLVTAAALEGLKRDIRTALAEHHHSAPAspglmfedvLDRLRAAR------PVLELAVQ 478
Cdd:TIGR00475 382 GILIMRL---LLPPTTIRICGFGENIDFGEVEVKKILVKLGTEQHDVKG---------VDKERLERmaslneELLKTAIE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 479 ELLaggELARTQGCLRLPGfRPSTLAAEGELSRRIEAAIRAGGLQPPDLKELPGGGSVAIKAIQRLLA--GGVLVRARDR 556
Cdd:TIGR00475 450 KLI---GTYKIGGWLHIPD-HKSDFEKEEDIWQKIKGTFGTKGAWVREFAEEVNGDEKVMLKRVRKAGhrGGETLIVKDR 525
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1481165581 557 vqkrellFHRDAVADAAERLATafaarpegFLVGEAGRVLGISRKYSVPLLEYLDGVGI 615
Cdd:TIGR00475 526 -------LLKKYINELKEEGGT--------FNVQQARDKLGLGRKLLIQLLEYFDRLGF 569
|
|
| PRK10512 |
PRK10512 |
selenocysteinyl-tRNA-specific translation factor; Provisional |
10-514 |
2.48e-76 |
|
selenocysteinyl-tRNA-specific translation factor; Provisional
Pssm-ID: 182508 [Multi-domain] Cd Length: 614 Bit Score: 255.36 E-value: 2.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 10 GHVDHGKTALVRALTGIETDRLEEEKRRGISIALGFAWLEVPGGE-IDLIDMPGHERFVRTMVAGAAGIRAVVLAVSAAE 88
Cdd:PRK10512 7 GHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYAYWPQPDGRvLGFIDVPGHEKFLSNMLAGVGGIDHALLVVACDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 89 GIRPQTREHVEIAGLLGVEAGVVAVTQCDLADEARAAEVGADAARLLAAHGMADAPVVHTSALDGRGLPELRATLAELMQ 168
Cdd:PRK10512 87 GVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEVRRQVKAVLREYGFAEAKLFVTAATEGRGIDALREHLLQLPE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 169 RVPAPAEQglAYLPVDRTFAVAGFGTVVTGTLQRGRLSVGEEVELTPGGKRARIRALQVHGRQVQQAIPGGRTAVNLRG- 247
Cdd:PRK10512 167 REHAAQHR--FRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNIAGd 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 248 VESAEVGRGCALATPGLLHASDWLDVHLRAlpgdHRPLETGREYKLLLAAGEIPARLRLLdreilhpgEAAPAQLRCAGP 327
Cdd:PRK10512 245 AEKEQINRGDWLLADAPPEPFTRVIVELQT----HTPLTQWQPLHIHHAASHVTGRVSLL--------EDNLAELVLDTP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 328 VAVPAREGFVLRAGSPARTVAGGRVLDPQTRRHRRNDPAVLDRLLSLAGAGPQEVVSQLLTGTGPagVLLDE---AARLS 404
Cdd:PRK10512 313 LWLADNDRLVLRDISARNTLAGARVVMLNPPRRGKRKPEYLQWLAALARAQDDAEALALHLERGA--VNLADfawARQLN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 405 GHAPSWVISWLPELQArqvGPLLVTAAALEGLKRDIRTALAEHHHSAPASPGLMfedvLDRLR------AARPVLELAVQ 478
Cdd:PRK10512 391 GEGMRALLQQPGYIQA---GDSLLSAPVAARWQRKLLDTLATYHEQHRDEPGPG----RERLRrmalpmEDEALVLLLIE 463
|
490 500 510
....*....|....*....|....*....|....*.
gi 1481165581 479 ELLAGGELARTQGCLRLPGFRPSTLAAEGELSRRIE 514
Cdd:PRK10512 464 KMRESGDIHSHHGWLHLPDHKAGFSEEQQALWQKAE 499
|
|
| SelB |
cd04171 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
6-172 |
8.65e-71 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.
Pssm-ID: 206734 [Multi-domain] Cd Length: 170 Bit Score: 226.33 E-value: 8.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGIETDRLEEEKRRGISIALGFAWLEVPGGE-IDLIDMPGHERFVRTMVAGAAGIRAVVLAV 84
Cdd:cd04171 2 IGTAGHIDHGKTTLIKALTGIETDRLPEEKKRGITIDLGFAYLDLPDGKrLGFIDVPGHEKFVKNMLAGAGGIDAVLLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 85 SAAEGIRPQTREHVEIAGLLGVEAGVVAVTQCDLADEARAAEVGADAARLLAAHGMADAPVVHTSALDGRGLPELRATLA 164
Cdd:cd04171 82 AADEGIMPQTREHLEILELLGIKKGLVVLTKADLVDEDRLELVEEEILELLAGTFLADAPIFPVSSVTGEGIEELKNYLD 161
|
....*...
gi 1481165581 165 ELMQRVPA 172
Cdd:cd04171 162 ELAEPQSK 169
|
|
| TEF1 |
COG5256 |
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ... |
8-256 |
2.18e-46 |
|
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444074 [Multi-domain] Cd Length: 423 Bit Score: 169.34 E-value: 2.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 8 VIGHVDHGKTALV-RAL--------------------TGIET-------DRLEEEKRRGISIALGFAWLEVPGGEIDLID 59
Cdd:COG5256 12 VIGHVDHGKSTLVgRLLyetgaidehiiekyeeeaekKGKESfkfawvmDRLKEERERGVTIDLAHKKFETDKYYFTIID 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 60 MPGHERFVRTMVAGAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEAGVVAVTQCDLA--DEARAAEVGADAARLLAA 137
Cdd:COG5256 92 APGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVnySEKRYEEVKEEVSKLLKM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 138 HG--MADAPVVHTSALDGRGLPELRA--------TLAEL--MQRVPA-PAEQGLAyLPVDRTFAVAGFGTVVTGTLQRGR 204
Cdd:COG5256 172 VGykVDKIPFIPVSAWKGDNVVKKSDnmpwyngpTLLEAldNLKEPEkPVDKPLR-IPIQDVYSISGIGTVPVGRVETGV 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1481165581 205 LSVGEEVELTPGGKRARIRALQVHGRQVQQAIPGGRTAVNLRGVESAEVGRG 256
Cdd:COG5256 251 LKVGDKVVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRG 302
|
|
| PRK12736 |
PRK12736 |
elongation factor Tu; Reviewed |
6-352 |
2.84e-44 |
|
elongation factor Tu; Reviewed
Pssm-ID: 237184 [Multi-domain] Cd Length: 394 Bit Score: 162.81 E-value: 2.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGI-------------ETDRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRTMVA 72
Cdd:PRK12736 15 IGTIGHVDHGKTTLTAAITKVlaerglnqakdydSIDAAPEEKERGITINTAHVEYETEKRHYAHVDCPGHADYVKNMIT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 73 GAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEAGVVAVTQCDLADEARAAE-VGADAARLLAAHGMA--DAPVVHTS 149
Cdd:PRK12736 95 GAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLElVEMEVRELLSEYDFPgdDIPVIRGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 150 ALDG-RGLPELRATLAELMQRV----PAPA-EQGLAYL-PVDRTFAVAGFGTVVTGTLQRGRLSVGEEVE---LTPgGKR 219
Cdd:PRK12736 175 ALKAlEGDPKWEDAIMELMDAVdeyiPTPErDTDKPFLmPVEDVFTITGRGTVVTGRVERGTVKVGDEVEivgIKE-TQK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 220 ARIRALQVHGRQVQQAIPGGRTAVNLRGVESAEVGRGCALATPGLLHASDWLDVHLRALP----GDHRPLETGREYKLLL 295
Cdd:PRK12736 254 TVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTkeegGRHTPFFNNYRPQFYF 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1481165581 296 AAGEIPARLRLLD-REILHPGEAAPAQLRCAGPVAVPAREGFVLRAGspARTVAGGRV 352
Cdd:PRK12736 334 RTTDVTGSIELPEgTEMVMPGDNVTITVELIHPIAMEQGLKFAIREG--GRTVGAGTV 389
|
|
| EF-Tu |
TIGR00485 |
translation elongation factor TU; This model models orthologs of translation elongation factor ... |
6-352 |
7.63e-44 |
|
translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]
Pssm-ID: 129576 [Multi-domain] Cd Length: 394 Bit Score: 161.48 E-value: 7.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGI-------------ETDRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRTMVA 72
Cdd:TIGR00485 15 VGTIGHVDHGKTTLTAAITTVlakeggaaaraydQIDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVKNMIT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 73 GAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEAGVVAVTQCDLADEARAAE-VGADAARLLAAHGMA--DAPVVHTS 149
Cdd:TIGR00485 95 GAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLElVEMEVRELLSQYDFPgdDTPIIRGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 150 ALDG-RGLPELRATLAELMQRV----PAPAEQ--GLAYLPVDRTFAVAGFGTVVTGTLQRGRLSVGEEVELT--PGGKRA 220
Cdd:TIGR00485 175 ALKAlEGDAEWEAKILELMDAVdeyiPTPEREidKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVglKDTRKT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 221 RIRALQVHGRQVQQAIPGGRTAVNLRGVESAEVGRGCALATPGLLHASDWLDVHLRALP----GDHRPLETGREYKLLLA 296
Cdd:TIGR00485 255 TVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSkeegGRHTPFFSGYRPQFYFR 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1481165581 297 AGEIPARLRLLDR-EILHPGEAAPAQLRCAGPVAVPAREGFVLRAGspARTVAGGRV 352
Cdd:TIGR00485 335 TTDVTGTIELPEGvEMVMPGDNVKMTVELISPIALEQGMRFAIREG--GRTVGAGVV 389
|
|
| PLN03127 |
PLN03127 |
Elongation factor Tu; Provisional |
4-352 |
1.61e-42 |
|
Elongation factor Tu; Provisional
Pssm-ID: 178673 [Multi-domain] Cd Length: 447 Bit Score: 159.22 E-value: 1.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 4 LAVGVIGHVDHGKTALVRALTGI-------------ETDRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRTM 70
Cdd:PLN03127 62 VNVGTIGHVDHGKTTLTAAITKVlaeegkakavafdEIDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNM 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 71 VAGAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEAGVVAVTQCDLADEARAAE-VGADAARLLAAHGMA--DAPVVH 147
Cdd:PLN03127 142 ITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLElVEMELRELLSFYKFPgdEIPIIR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 148 TSAL---DGRGlPEL-RATLAELMQRV----PAPAEQ--GLAYLPVDRTFAVAGFGTVVTGTLQRGRLSVGEEVE---LT 214
Cdd:PLN03127 222 GSALsalQGTN-DEIgKNAILKLMDAVdeyiPEPVRVldKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEivgLR 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 215 PGG-KRARIRALQVHGRQVQQAIPGGRTAVNLRGVESAEVGRGCALATPGLLHASDWLDVHLRALP----GDHRPLETGR 289
Cdd:PLN03127 301 PGGpLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTkdegGRHTPFFSNY 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1481165581 290 EYKLLLAAGEIPARLRLLDR-EILHPGEAAPAQLRCAGPVAVPAREGFVLRAGSpaRTVAGGRV 352
Cdd:PLN03127 381 RPQFYLRTADVTGKVELPEGvKMVMPGDNVTAVFELISPVPLEPGQRFALREGG--RTVGAGVV 442
|
|
| PRK12317 |
PRK12317 |
elongation factor 1-alpha; Reviewed |
8-256 |
2.64e-42 |
|
elongation factor 1-alpha; Reviewed
Pssm-ID: 237055 [Multi-domain] Cd Length: 425 Bit Score: 158.17 E-value: 2.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 8 VIGHVDHGKTALVRAL---TG------IET-------------------DRLEEEKRRGISIALGFAWLEVPGGEIDLID 59
Cdd:PRK12317 11 VIGHVDHGKSTLVGRLlyeTGaidehiIEElreeakekgkesfkfawvmDRLKEERERGVTIDLAHKKFETDKYYFTIVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 60 MPGHERFVRTMVAGAAGIRAVVLAVSA--AEGIRPQTREHVEIAGLLGVEAGVVAVTQCDLA--DEARAAEVGADAARLL 135
Cdd:PRK12317 91 CPGHRDFVKNMITGASQADAAVLVVAAddAGGVMPQTREHVFLARTLGINQLIVAINKMDAVnyDEKRYEEVKEEVSKLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 136 AAHG--MADAPVVHTSALDGRGLPELRA--------TLAELMQRVPAPAEQGLAYL--PVDRTFAVAGFGTVVTGTLQRG 203
Cdd:PRK12317 171 KMVGykPDDIPFIPVSAFEGDNVVKKSEnmpwyngpTLLEALDNLKPPEKPTDKPLriPIQDVYSISGVGTVPVGRVETG 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1481165581 204 RLSVGEEVELTPGGKRARIRALQVHGRQVQQAIPGGRTAVNLRGVESAEVGRG 256
Cdd:PRK12317 251 VLKVGDKVVFMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRG 303
|
|
| TufA |
COG0050 |
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ... |
6-263 |
1.62e-41 |
|
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 439820 [Multi-domain] Cd Length: 396 Bit Score: 155.31 E-value: 1.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGI-------------ETDRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRTMVA 72
Cdd:COG0050 15 IGTIGHVDHGKTTLTAAITKVlakkggakakaydQIDKAPEEKERGITINTSHVEYETEKRHYAHVDCPGHADYVKNMIT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 73 GAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEAGVVAVTQCDLADEARAAE-VGADAARLLAAHGM--ADAPVVHTS 149
Cdd:COG0050 95 GAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLElVEMEVRELLSKYGFpgDDTPIIRGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 150 ---ALDGRGLPELRATLAELMQRV----PAPA-EQGLAYL-PVDRTFAVAGFGTVVTGTLQRGRLSVGEEVELTpgGKRA 220
Cdd:COG0050 175 alkALEGDPDPEWEKKILELMDAVdsyiPEPErDTDKPFLmPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIV--GIRD 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1481165581 221 RIRA----LQVHGRQVQQAIPGGRTAVNLRGVESAEVGRGCALATPG 263
Cdd:COG0050 253 TQKTvvtgVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPG 299
|
|
| eif2g_arch |
TIGR03680 |
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ... |
6-243 |
1.33e-40 |
|
translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
Pssm-ID: 274720 [Multi-domain] Cd Length: 406 Bit Score: 152.90 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGIETDRLEEEKRRGISIALGFAWLEV--------------------PGGE------IDLID 59
Cdd:TIGR03680 7 IGMVGHVDHGKTTLTKALTGVWTDTHSEELKRGISIRLGYADAEIykcpecdgpecyttepvcpnCGSEtellrrVSFVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 60 MPGHERFVRTMVAGAAGIRAVVLAVSAAEGI-RPQTREHVEIAGLLGVEAGVVAVTQCDLADEARAAEVGADAARLLAAH 138
Cdd:TIGR03680 87 APGHETLMATMLSGAALMDGALLVIAANEPCpQPQTKEHLMALEIIGIKNIVIVQNKIDLVSKEKALENYEEIKEFVKGT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 139 GMADAPVVHTSALDGRGLPELRATLAElmqRVPAPA--EQGLAYLPVDRTFAVAGFGT--------VVTGTLQRGRLSVG 208
Cdd:TIGR03680 167 VAENAPIIPVSALHNANIDALLEAIEK---FIPTPErdLDKPPLMYVARSFDVNKPGTppeklkggVIGGSLIQGKLKVG 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1481165581 209 EEVELTPGGKRAR------------IRALQVHGRQVQQAIPGGRTAV 243
Cdd:TIGR03680 244 DEIEIRPGIKVEKggktkwepiyteITSLRAGGYKVEEARPGGLVGV 290
|
|
| PRK00049 |
PRK00049 |
elongation factor Tu; Reviewed |
6-263 |
7.56e-39 |
|
elongation factor Tu; Reviewed
Pssm-ID: 234596 [Multi-domain] Cd Length: 396 Bit Score: 147.64 E-value: 7.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGI-------------ETDRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRTMVA 72
Cdd:PRK00049 15 VGTIGHVDHGKTTLTAAITKVlakkggaeakaydQIDKAPEEKARGITINTAHVEYETEKRHYAHVDCPGHADYVKNMIT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 73 GAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEAGVVAVTQCDLADEARAAE-VGADAARLLAAHGMA--DAPVVHTS 149
Cdd:PRK00049 95 GAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLElVEMEVRELLSKYDFPgdDTPIIRGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 150 ---ALDGRGLPELRATLAELMQRV----PAPA-EQGLAYL-PVDRTFAVAGFGTVVTGTLQRGRLSVGEEVELTpGgkra 220
Cdd:PRK00049 175 alkALEGDDDEEWEKKILELMDAVdsyiPTPErAIDKPFLmPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIV-G---- 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1481165581 221 rIRALQ---VHG-----RQVQQAIPGGRTAVNLRGVESAEVGRGCALATPG 263
Cdd:PRK00049 250 -IRDTQkttVTGvemfrKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPG 299
|
|
| PRK04000 |
PRK04000 |
translation initiation factor IF-2 subunit gamma; Validated |
6-243 |
1.86e-37 |
|
translation initiation factor IF-2 subunit gamma; Validated
Pssm-ID: 235194 [Multi-domain] Cd Length: 411 Bit Score: 144.22 E-value: 1.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGIETDRLEEEKRRGISIALGFA--------WLEVP------------GGE------IDLID 59
Cdd:PRK04000 12 IGMVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYAdatirkcpDCEEPeayttepkcpncGSEtellrrVSFVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 60 MPGHERFVRTMVAGAAGIRAVVLAVSAAEGI-RPQTREHVEIAGLLGVEAGVVAVTQCDLADEARAAEVGADAARLLAAH 138
Cdd:PRK04000 92 APGHETLMATMLSGAALMDGAILVIAANEPCpQPQTKEHLMALDIIGIKNIVIVQNKIDLVSKERALENYEQIKEFVKGT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 139 GMADAPVVHTSALDGRGLPELRATLAElmqRVPAPaEQGLAYLP---VDRTFAVAGFGT--------VVTGTLQRGRLSV 207
Cdd:PRK04000 172 VAENAPIIPVSALHKVNIDALIEAIEE---EIPTP-ERDLDKPPrmyVARSFDVNKPGTppeklkggVIGGSLIQGVLKV 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1481165581 208 GEEVELTPG------GK------RARIRALQVHGRQVQQAIPGGRTAV 243
Cdd:PRK04000 248 GDEIEIRPGikveegGKtkwepiTTKIVSLRAGGEKVEEARPGGLVGV 295
|
|
| PRK12735 |
PRK12735 |
elongation factor Tu; Reviewed |
6-263 |
2.07e-37 |
|
elongation factor Tu; Reviewed
Pssm-ID: 183708 [Multi-domain] Cd Length: 396 Bit Score: 143.44 E-value: 2.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGI-------------ETDRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRTMVA 72
Cdd:PRK12735 15 VGTIGHVDHGKTTLTAAITKVlakkgggeakaydQIDNAPEEKARGITINTSHVEYETANRHYAHVDCPGHADYVKNMIT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 73 GAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEAGVVAVTQCDLADEARAAE-VGADAARLLAAHGMA--DAPVVHTS 149
Cdd:PRK12735 95 GAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLElVEMEVRELLSKYDFPgdDTPIIRGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 150 A---LDGRGLPELRATLAELMQRV----PAPA-EQGLAYL-PVDRTFAVAGFGTVVTGTLQRGRLSVGEEVELTpgGKRA 220
Cdd:PRK12735 175 AlkaLEGDDDEEWEAKILELMDAVdsyiPEPErAIDKPFLmPIEDVFSISGRGTVVTGRVERGIVKVGDEVEIV--GIKE 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1481165581 221 RIR----ALQVHGRQVQQAIPGGRTAVNLRGVESAEVGRGCALATPG 263
Cdd:PRK12735 253 TQKttvtGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPG 299
|
|
| GTP_translation_factor |
cd00881 |
GTP translation factor family primarily contains translation initiation, elongation and ... |
6-173 |
3.54e-37 |
|
GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.
Pssm-ID: 206647 [Multi-domain] Cd Length: 183 Bit Score: 136.66 E-value: 3.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGI-------------ETDRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRTMVA 72
Cdd:cd00881 2 VGVIGHVDHGKTTLTGSLLYQtgaidrrgtrketFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 73 GAAGIRAVVLAVSAAEGIRPQTREHVEIAgLLGVEAGVVAVTQCDLADEARAAEVGADAARLLAAHGM-----ADAPVVH 147
Cdd:cd00881 82 GLAQADGALLVVDANEGVEPQTREHLNIA-LAGGLPIIVAVNKIDRVGEEDFDEVLREIKELLKLIGFtflkgKDVPIIP 160
|
170 180
....*....|....*....|....*.
gi 1481165581 148 TSALDGRGLPELratLAELMQRVPAP 173
Cdd:cd00881 161 ISALTGEGIEEL---LDAIVEHLPPP 183
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
6-168 |
1.82e-36 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 134.96 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRAL---TGIE-------------TDRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRT 69
Cdd:pfam00009 6 IGIIGHVDHGKTTLTDRLlyyTGAIskrgevkgegeagLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVDFVKE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 70 MVAGAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEAgVVAVTQCDLADEARAAEVGADAARLL---AAHGMADAPVV 146
Cdd:pfam00009 86 VIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPI-IVFINKMDRVDGAELEEVVEEVSRELlekYGEDGEFVPVV 164
|
170 180
....*....|....*....|..
gi 1481165581 147 HTSALDGRGLPELRATLAELMQ 168
Cdd:pfam00009 165 PGSALKGEGVQTLLDALDEYLP 186
|
|
| PLN03126 |
PLN03126 |
Elongation factor Tu; Provisional |
6-350 |
1.27e-35 |
|
Elongation factor Tu; Provisional
Pssm-ID: 215592 [Multi-domain] Cd Length: 478 Bit Score: 140.14 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGI-------------ETDRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRTMVA 72
Cdd:PLN03126 84 IGTIGHVDHGKTTLTAALTMAlasmggsapkkydEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNMIT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 73 GAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEAGVVAVTQCDLADEARAAE-VGADAARLLAAHGMA--DAPVVHTS 149
Cdd:PLN03126 164 GAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLElVELEVRELLSSYEFPgdDIPIISGS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 150 ALDG-----------RGLPELRATLAELMQRV----PAPAEQ-GLAYL-PVDRTFAVAGFGTVVTGTLQRGRLSVGEEVE 212
Cdd:PLN03126 244 ALLAlealmenpnikRGDNKWVDKIYELMDAVdsyiPIPQRQtDLPFLlAVEDVFSITGRGTVATGRVERGTVKVGETVD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 213 LTpGGKRAR---IRALQVHGRQVQQAIPGGRTAVNLRGVESAEVGRGCALATPGLLHASDWLDVHLRALP----GDHRPL 285
Cdd:PLN03126 324 IV-GLRETRsttVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKkeegGRHSPF 402
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1481165581 286 ETGREYKLLLAAGEIPARLRLL------DREILHPGEAAPAQLRCAGPVAVPAREGFVLRAGspARTVAGG 350
Cdd:PLN03126 403 FAGYRPQFYMRTTDVTGKVTSImndkdeESKMVMPGDRVKMVVELIVPVACEQGMRFAIREG--GKTVGAG 471
|
|
| tufA |
CHL00071 |
elongation factor Tu |
6-263 |
7.87e-35 |
|
elongation factor Tu
Pssm-ID: 177010 [Multi-domain] Cd Length: 409 Bit Score: 136.63 E-value: 7.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGI-------------ETDRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRTMVA 72
Cdd:CHL00071 15 IGTIGHVDHGKTTLTAAITMTlaakggakakkydEIDSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYVKNMIT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 73 GAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEAGVVAVTQCDLADEARAAE-VGADAARLLAAHGMA--DAPVVHTS 149
Cdd:CHL00071 95 GAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLElVELEVRELLSKYDFPgdDIPIVSGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 150 ALD-----------GRGLPELRATLAELMQRV----PAPA-EQGLAYL-PVDRTFAVAGFGTVVTGTLQRGRLSVGEEVE 212
Cdd:CHL00071 175 ALLalealtenpkiKRGENKWVDKIYNLMDAVdsyiPTPErDTDKPFLmAIEDVFSITGRGTVATGRIERGTVKVGDTVE 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1481165581 213 LTpGGKRAR---IRALQVHGRQVQQAIPGGRTAVNLRGVESAEVGRGCALATPG 263
Cdd:CHL00071 255 IV-GLRETKtttVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPG 307
|
|
| GCD11 |
COG5257 |
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ... |
6-243 |
1.50e-34 |
|
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 444075 [Multi-domain] Cd Length: 408 Bit Score: 135.73 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGIETDRLEEEKRRGISIALGFA--------WLEVP------------GGEIDL------ID 59
Cdd:COG5257 8 IGVVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYAdatfykcpNCEPPeayttepkcpncGSETELlrrvsfVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 60 MPGHERFVRTMVAGAAGIRAVVLAVSAAEGI-RPQTREHVEIAGLLGVEAGVVAVTQCDLADEARAAEVGADAARLLAAH 138
Cdd:COG5257 88 APGHETLMATMLSGAALMDGAILVIAANEPCpQPQTKEHLMALDIIGIKNIVIVQNKIDLVSKERALENYEQIKEFVKGT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 139 GMADAPVVHTSALDGRGLPELRATLAElmqRVPAPaEQGL---AYLPVDRTFAVAGFGT--------VVTGTLQRGRLSV 207
Cdd:COG5257 168 VAENAPIIPVSAQHKVNIDALIEAIEE---EIPTP-ERDLskpPRMLVARSFDVNKPGTppkdlkggVIGGSLIQGVLKV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1481165581 208 GEEVELTPG------GK------RARIRALQVHGRQVQQAIPGGRTAV 243
Cdd:COG5257 244 GDEIEIRPGikvekgGKtkyepiTTTVVSLRAGGEEVEEAKPGGLVAV 291
|
|
| CysN |
COG2895 |
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ... |
10-360 |
7.91e-31 |
|
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 442140 [Multi-domain] Cd Length: 430 Bit Score: 125.20 E-value: 7.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 10 GHVDHGKTALV------------------------RALTGIE----TDRLEEEKRRGISIalgfawlevpggeiD----- 56
Cdd:COG2895 24 GSVDDGKSTLIgrllydtksifedqlaalerdskkRGTQEIDlallTDGLQAEREQGITI--------------Dvayry 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 57 ---------LIDMPGHERFVRTMVAGAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEAGVVAVTQCDLAD--EARAA 125
Cdd:COG2895 90 fstpkrkfiIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDysEEVFE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 126 EVGADAARLLAAHGMADAPVVHTSALDG-------------RGlpelrATLAELMQRVPAPAEQGLA--YLPV------- 183
Cdd:COG2895 170 EIVADYRAFAAKLGLEDITFIPISALKGdnvversenmpwyDG-----PTLLEHLETVEVAEDRNDApfRFPVqyvnrpn 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 184 -D-RTFAvagfgtvvtGTLQRGRLSVGEEVELTPGGKRARIRALQVHGRQVQQAIPGgrTAVNLRGVESAEVGRGCALAT 261
Cdd:COG2895 245 lDfRGYA---------GTIASGTVRVGDEVVVLPSGKTSTVKSIVTFDGDLEEAFAG--QSVTLTLEDEIDISRGDVIVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 262 PG-LLHASDWLDVHLRALpgDHRPLETGREYKLLLAAGEIPARLRLLDREI------------LHPGEAAPAQLRCAGPV 328
Cdd:COG2895 314 ADaPPEVADQFEATLVWM--DEEPLLPGRKYLLKHGTRTVRATVTAIKYRIdvntleheaadsLELNDIGRVTLRLAEPI 391
|
410 420 430
....*....|....*....|....*....|....*...
gi 1481165581 329 AV-PARE-----GFVLRAGSPARTVAGGRVLDPQTRRH 360
Cdd:COG2895 392 AFdPYADnratgSFILIDRLTNATVGAGMIRGALRRAA 429
|
|
| GTPBP1 |
COG5258 |
GTPase [General function prediction only]; |
4-354 |
1.23e-29 |
|
GTPase [General function prediction only];
Pssm-ID: 444076 [Multi-domain] Cd Length: 531 Bit Score: 123.51 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 4 LAVGVIGHVDHGKTALVRAL-TG----------IETDRLEEEKRRGISIALGFAWLEVPGGE------------------ 54
Cdd:COG5258 123 IVVGVAGHVDHGKSTLVGTLvTGklddgnggtrSFLDVQPHEVERGLSADLSYAVYGFDDDGpvrmknplrktdrarvve 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 55 -----IDLIDMPGHERFVRTMVAGAAG--IRAVVLAVSAAEGIRPQTREHVEIAGLLGVEAgVVAVTQCDLADEARAAEV 127
Cdd:COG5258 203 esdklVSFVDTVGHEPWLRTTIRGLVGqkLDYGLLVVAADDGPTHTTREHLGILLAMDLPV-IVAITKIDKVDDERVEEV 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 128 GADAARLL------------------AAHGMAD--APVVHTSALDGRGLPELRATLAELMQRVPAPAEQGLAYlpVDRTF 187
Cdd:COG5258 282 EREIENLLrivgrtplevesrhdvdaAIEEINGrvVPILKTSAVTGEGLDLLDELFERLPKRATDEDEPFLMY--IDRIY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 188 AVAGFGTVVTGTLQRGRLSVGEEVELTPGG----KRARIRALQVHGRQVQQAIPGGRTAVNLRGVESAEVGRGCALATPG 263
Cdd:COG5258 360 NVTGVGTVVSGTVKSGKVEAGDELLIGPTKdgsfREVEVKSIEMHYHRVDKAEAGRIVGIALKGVEEEELERGMVLLPRD 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 264 LLHASDW-LDVHLRALpgdHRPLETGREYKLLLAAGEI--PARLRLLDREILHPGEAAPAQLRCA-GPVAVPAREGFVLR 339
Cdd:COG5258 440 ADPKAVReFEAEVMVL---NHPTTIKEGYEPVVHLETIseAVRFEPIDKGYLLPGDSGRVRLRFKyRPYYVEEGQRFVFR 516
|
410
....*....|....*
gi 1481165581 340 AGspaRTVAGGRVLD 354
Cdd:COG5258 517 EG---RSKGVGTVTD 528
|
|
| SelB_euk |
cd01889 |
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ... |
6-166 |
7.22e-29 |
|
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.
Pssm-ID: 206676 [Multi-domain] Cd Length: 192 Bit Score: 113.61 E-value: 7.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGIET----DRLEEEKRRGISIALGFAWLEV-----------PGGE---IDLIDMPGHERFV 67
Cdd:cd01889 3 VGLLGHVDSGKTSLAKALSEIAStaafDKNPQSQERGITLDLGFSSFEVdkpkhlednenPQIEnyqITLVDCPGHASLI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 68 RTMVAGAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEaGVVAVTQCDLADEA-RAAEVGADAARLLAAHGMA---DA 143
Cdd:cd01889 83 RTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKP-LIVVLNKIDLIPEEeRKRKIEKMKKRLQKTLEKTrlkDS 161
|
170 180
....*....|....*....|...
gi 1481165581 144 PVVHTSALDGRGLPELRATLAEL 166
Cdd:cd01889 162 PIIPVSAKPGEGEAELGGELKNL 184
|
|
| EF_Tu |
cd01884 |
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ... |
6-170 |
5.64e-28 |
|
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.
Pssm-ID: 206671 [Multi-domain] Cd Length: 195 Bit Score: 111.14 E-value: 5.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGI-------------ETDRLEEEKRRGISIALgfAWLEVpggEIDL-----IDMPGHERFV 67
Cdd:cd01884 5 VGTIGHVDHGKTTLTAAITKVlakkggakakkydEIDKAPEEKARGITINT--AHVEY---ETANrhyahVDCPGHADYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 68 RTMVAGAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEAGVVAVTQCDLADEARAAE-VGADAARLLAAHGM--ADAP 144
Cdd:cd01884 80 KNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLElVEMEVRELLSKYGFdgDDTP 159
|
170 180
....*....|....*....|....*....
gi 1481165581 145 VVHTSAL---DGRGLPELRATLAELMQRV 170
Cdd:cd01884 160 IVRGSALkalEGDDPNKWVDKILELLDAL 188
|
|
| PTZ00327 |
PTZ00327 |
eukaryotic translation initiation factor 2 gamma subunit; Provisional |
6-243 |
3.19e-27 |
|
eukaryotic translation initiation factor 2 gamma subunit; Provisional
Pssm-ID: 240362 [Multi-domain] Cd Length: 460 Bit Score: 115.10 E-value: 3.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGIETDRLEEEKRRGISIALGFAWLEV--------P-------------------GGEIDL- 57
Cdd:PTZ00327 37 IGTIGHVAHGKSTVVKALSGVKTVRFKREKVRNITIKLGYANAKIykcpkcprPtcyqsygsskpdnppcpgcGHKMTLk 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 58 -----IDMPGHERFVRTMVAGAAGIRAVVLAVSAAEGI-RPQTREH---VEIAGLLGVeagVVAVTQCDLADEARAAEVG 128
Cdd:PTZ00327 117 rhvsfVDCPGHDILMATMLNGAAVMDAALLLIAANESCpQPQTSEHlaaVEIMKLKHI---IILQNKIDLVKEAQAQDQY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 129 ADAARLLAAHGMADAPVVHTSALDGRGLPELratLAELMQRVPAPAEQ--GLAYLPVDRTFAVAGFGT--------VVTG 198
Cdd:PTZ00327 194 EEIRNFVKGTIADNAPIIPISAQLKYNIDVV---LEYICTQIPIPKRDltSPPRMIVIRSFDVNKPGEdienlkggVAGG 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1481165581 199 TLQRGRLSVGEEVELTPG-------GK------RARIRALQVHGRQVQQAIPGGRTAV 243
Cdd:PTZ00327 271 SILQGVLKVGDEIEIRPGiiskdsgGEftcrpiRTRIVSLFAENNELQYAVPGGLIGV 328
|
|
| eIF2_gamma |
cd01888 |
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ... |
6-126 |
3.26e-27 |
|
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.
Pssm-ID: 206675 [Multi-domain] Cd Length: 197 Bit Score: 108.89 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGIETDRLEEEKRRGISIALGFA-------------------WLEVPGGE--------IDLI 58
Cdd:cd01888 3 IGTIGHVAHGKTTLVKALSGVWTVRHKEELKRNITIKLGYAnakiykcpncgcprpydtpECECPGCGgetklvrhVSFV 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1481165581 59 DMPGHERFVRTMVAGAAGIRAVVLAVSAAEGI-RPQTREH---VEIAGLLGVeagVVAVTQCDLADEARAAE 126
Cdd:cd01888 83 DCPGHEILMATMLSGAAVMDGALLLIAANEPCpQPQTSEHlaaLEIMGLKHI---IILQNKIDLVKEEQALE 151
|
|
| CysN |
TIGR02034 |
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ... |
29-359 |
4.40e-27 |
|
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 213679 [Multi-domain] Cd Length: 406 Bit Score: 114.01 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 29 DRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRTMVAGAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEA 108
Cdd:TIGR02034 56 DGLQAEREQGITIDVAYRYFSTDKRKFIVADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRH 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 109 GVVAVTQCDLA--DEARAAEVGADAARLLAAHGMADAPVVHTSALDGRGLPELRA--------TLAELMQRVPA-PAEQG 177
Cdd:TIGR02034 136 VVLAVNKMDLVdyDEEVFENIKKDYLAFAEQLGFRDVTFIPLSALKGDNVVSRSEsmpwysgpTLLEILETVEVeRDAQD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 178 LAY-LPVD---------RTFAvagfgtvvtGTLQRGRLSVGEEVELTPGGKRARIRALQVHGRQVQQAIPGgrTAVNLRG 247
Cdd:TIGR02034 216 LPLrFPVQyvnrpnldfRGYA---------GTIASGSVHVGDEVVVLPSGRSSRVARIVTFDGDLEQARAG--QAVTLTL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 248 VESAEVGRGCALATP-GLLHASDWLDVHLRALpgDHRPLETGREYKLLLAAGEIPARL----RLLDREILHPGEAAPAQL 322
Cdd:TIGR02034 285 DDEIDISRGDLLAAAdSAPEVADQFAATLVWM--AEEPLLPGRSYDLKLGTRKVRASVaaikHKVDVNTLEKGAAKSLEL 362
|
330 340 350
....*....|....*....|....*....|....*..
gi 1481165581 323 RCAGPVAVPAREGFVLRAGSPARTVAGGRVLDPQTRR 359
Cdd:TIGR02034 363 NEIGRVNLSLDEPIAFDPYAENRTTGAFILIDRLSNR 399
|
|
| SelB_II |
cd03696 |
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ... |
180-260 |
2.36e-25 |
|
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.
Pssm-ID: 293897 [Multi-domain] Cd Length: 83 Bit Score: 99.91 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 180 YLPVDRTFAVAGFGTVVTGTLQRGRLSVGEEVELTPGGKRARIRALQVHGRQVQQAIPGGRTAVNLRGVESAEVGRGCAL 259
Cdd:cd03696 2 RLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGFVL 81
|
.
gi 1481165581 260 A 260
Cdd:cd03696 82 S 82
|
|
| PTZ00141 |
PTZ00141 |
elongation factor 1- alpha; Provisional |
8-256 |
9.18e-24 |
|
elongation factor 1- alpha; Provisional
Pssm-ID: 185474 [Multi-domain] Cd Length: 446 Bit Score: 104.44 E-value: 9.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 8 VIGHVDHGKTA----LVRALTGIET------------------------DRLEEEKRRGISIALGFAWLEVPGGEIDLID 59
Cdd:PTZ00141 12 VIGHVDSGKSTttghLIYKCGGIDKrtiekfekeaaemgkgsfkyawvlDKLKAERERGITIDIALWKFETPKYYFTIID 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 60 MPGHERFVRTMVAGAAGIRAVVLAVSAAEGI-------RPQTREHVEIAGLLGVEAGVVAVTQCDLA----DEARAAEVG 128
Cdd:PTZ00141 92 APGHRDFIKNMITGTSQADVAILVVASTAGEfeagiskDGQTREHALLAFTLGVKQMIVCINKMDDKtvnySQERYDEIK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 129 ADAARLLAAHG--MADAPVVHTSALDGRGLPELRA--------TLAELMQRVPAP---AEQGLAyLPVDRTFAVAGFGTV 195
Cdd:PTZ00141 172 KEVSAYLKKVGynPEKVPFIPISGWQGDNMIEKSDnmpwykgpTLLEALDTLEPPkrpVDKPLR-LPLQDVYKIGGIGTV 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1481165581 196 VTGTLQRGRLSVGEEVELTPGGKRARIRALQVHGRQVQQAIPGGRTAVNLRGVESAEVGRG 256
Cdd:PTZ00141 251 PVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRG 311
|
|
| CysN_ATPS |
cd04166 |
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ... |
10-153 |
1.58e-21 |
|
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.
Pssm-ID: 206729 [Multi-domain] Cd Length: 209 Bit Score: 93.02 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 10 GHVDHGKTALV-------------------------RALTGIE----TDRLEEEKRRGISIALGFAWLEVPGGEIDLIDM 60
Cdd:cd04166 6 GSVDDGKSTLIgrllydsksifedqlaalerskssgTQGEKLDlallVDGLQAEREQGITIDVAYRYFSTPKRKFIIADT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 61 PGHERFVRTMVAGAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEAGVVAVTQCDLAD--EARAAEVGADAARLLAAH 138
Cdd:cd04166 86 PGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDydEEVFEEIKADYLAFAASL 165
|
170
....*....|....*
gi 1481165581 139 GMADAPVVHTSALDG 153
Cdd:cd04166 166 GIEDITFIPISALEG 180
|
|
| IF2_eIF5B |
cd01887 |
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ... |
6-169 |
2.57e-20 |
|
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.
Pssm-ID: 206674 [Multi-domain] Cd Length: 169 Bit Score: 88.30 E-value: 2.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGieTDRLEEEKrRGI--SIALGFAWLEVPGGEIDLIDMPGHERFVrTMVA-GAAGIRAVVL 82
Cdd:cd01887 3 VTVMGHVDHGKTTLLDKIRK--TNVAAGEA-GGItqHIGAYQVPIDVKIPGITFIDTPGHEAFT-NMRArGASVTDIAIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 83 AVSAAEGIRPQTREHVEIAGLLGVEAgVVAVTQCDladeaRAAEVGADAARL---LAAHGMA------DAPVVHTSALDG 153
Cdd:cd01887 79 VVAADDGVMPQTIEAINHAKAANVPI-IVAINKID-----KPYGTEADPERVkneLSELGLVgeewggDVSIVPISAKTG 152
|
170
....*....|....*.
gi 1481165581 154 RGLPELRATLAELMQR 169
Cdd:cd01887 153 EGIDDLLEAILLLAEV 168
|
|
| EF1_alpha |
cd01883 |
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ... |
8-156 |
3.26e-20 |
|
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.
Pssm-ID: 206670 [Multi-domain] Cd Length: 219 Bit Score: 89.47 E-value: 3.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 8 VIGHVDHGKTALVRAL---TG------IET-------------------DRLEEEKRRGISIALGFAWLEVPGGEIDLID 59
Cdd:cd01883 4 VIGHVDAGKSTLTGHLlykLGgvdkrtIEKyekeakemgkesfkyawvlDKLKEERERGVTIDVGLAKFETEKYRFTIID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 60 MPGHERFVRTMVAGAAGIRAVVLAVSAAEG-------IRPQTREHVEIAGLLGVEAGVVAVTQCDLA----DEARAAEVG 128
Cdd:cd01883 84 APGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVtvnwSQERYDEIK 163
|
170 180 190
....*....|....*....|....*....|
gi 1481165581 129 ADAARLLAAHG--MADAPVVHTSALDGRGL 156
Cdd:cd01883 164 KKVSPFLKKVGynPKDVPFIPISGFTGDNL 193
|
|
| IF-2 |
TIGR00487 |
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ... |
2-237 |
1.20e-19 |
|
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]
Pssm-ID: 273102 [Multi-domain] Cd Length: 587 Bit Score: 92.91 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 2 RPLAVGVIGHVDHGKTALvraLTGIETDRLEEEKRRGISIALGFAWLEVPGGE-IDLIDMPGHERFVRTMVAGAAGIRAV 80
Cdd:TIGR00487 86 RPPVVTIMGHVDHGKTSL---LDSIRKTKVAQGEAGGITQHIGAYHVENEDGKmITFLDTPGHEAFTSMRARGAKVTDIV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 81 VLAVSAAEGIRPQTREHVEIAGLLGVEAgVVAVTQCDLADearaaevgADAARL---LAAHGM------ADAPVVHTSAL 151
Cdd:TIGR00487 163 VLVVAADDGVMPQTIEAISHAKAANVPI-IVAINKIDKPE--------ANPDRVkqeLSEYGLvpedwgGDTIFVPVSAL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 152 DGRGLPELRAT---LAELMQRVPAPAEQGLAYlpVDRTFAVAGFGTVVTGTLQRGRLSVGEEVELtpGGKRARIRAL-QV 227
Cdd:TIGR00487 234 TGDGIDELLDMillQSEVEELKANPNGQASGV--VIEAQLDKGRGPVATVLVQSGTLRVGDIVVV--GAAYGRVRAMiDE 309
|
250
....*....|
gi 1481165581 228 HGRQVQQAIP 237
Cdd:TIGR00487 310 NGKSVKEAGP 319
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
28-322 |
3.07e-19 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 91.91 E-value: 3.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 28 TDRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRTMVAGAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVE 107
Cdd:PRK05506 79 VDGLAAEREQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 108 AGVVAVTQCDLAD--EARAAEVGADAARLLAAHGMADAPVVHTSALDGRGLPELRA--------TLAELMQRVPAPAEQG 177
Cdd:PRK05506 159 HVVLAVNKMDLVDydQEVFDEIVADYRAFAAKLGLHDVTFIPISALKGDNVVTRSArmpwyegpSLLEHLETVEIASDRN 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 178 L--AYLPVD---------RTFAvagfgtvvtGTLQRGRLSVGEEVELTPGGKRARIRALQVHGRQVQQAIPGgrTAVNLR 246
Cdd:PRK05506 239 LkdFRFPVQyvnrpnldfRGFA---------GTVASGVVRPGDEVVVLPSGKTSRVKRIVTPDGDLDEAFAG--QAVTLT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 247 GVESAEVGRGCALATPGLL-HASDWLDVHLRALpgDHRPLETGREYKLLLAAGEIPARLRLLDREI----LHPGEAAPAQ 321
Cdd:PRK05506 308 LADEIDISRGDMLARADNRpEVADQFDATVVWM--AEEPLLPGRPYLLKHGTRTVPASVAAIKYRVdvntLERLAAKTLE 385
|
.
gi 1481165581 322 L 322
Cdd:PRK05506 386 L 386
|
|
| PLN00043 |
PLN00043 |
elongation factor 1-alpha; Provisional |
8-256 |
4.28e-19 |
|
elongation factor 1-alpha; Provisional
Pssm-ID: 165621 [Multi-domain] Cd Length: 447 Bit Score: 90.53 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 8 VIGHVDHGKTA----LVRALTGIET------------------------DRLEEEKRRGISIALGFAWLEVPGGEIDLID 59
Cdd:PLN00043 12 VIGHVDSGKSTttghLIYKLGGIDKrvierfekeaaemnkrsfkyawvlDKLKAERERGITIDIALWKFETTKYYCTVID 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 60 MPGHERFVRTMVAGAAGIRAVVLAVSAAEG-------IRPQTREHVEIAGLLGVEAGVVAVTQCDLA----DEARAAEVG 128
Cdd:PLN00043 92 APGHRDFIKNMITGTSQADCAVLIIDSTTGgfeagisKDGQTREHALLAFTLGVKQMICCCNKMDATtpkySKARYDEIV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 129 ADAARLLAAHGMA--DAPVVHTSALDGRGLPELRA--------TLAELMQRVPAP---AEQGLAyLPVDRTFAVAGFGTV 195
Cdd:PLN00043 172 KEVSSYLKKVGYNpdKIPFVPISGFEGDNMIERSTnldwykgpTLLEALDQINEPkrpSDKPLR-LPLQDVYKIGGIGTV 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1481165581 196 VTGTLQRGRLSVGEEVELTPGGKRARIRALQVHGRQVQQAIPGGRTAVNLRGVESAEVGRG 256
Cdd:PLN00043 251 PVGRVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRG 311
|
|
| selB_III |
cd15491 |
Domain III of selenocysteine-specific translation elongation factor; This family represents ... |
267-352 |
6.27e-19 |
|
Domain III of selenocysteine-specific translation elongation factor; This family represents domain III of bacterial selenocysteine (Sec)-specific elongation factor (EFSec), homologous to domain III of EF-Tu. SelB is a specialized translation elongation factor responsible for the co-translational incorporation of selenocysteine into proteins by recoding of a UGA stop codon in the presence of a downstream mRNA hairpin loop, called Sec insertion sequence (SECIS) element.
Pssm-ID: 294012 [Multi-domain] Cd Length: 87 Bit Score: 81.72 E-value: 6.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 267 ASDWLDVHLRALPGDHRPLETGREYKLLLAAGEIPARLRLLDREILHPGEAAPAQLRCAGPVAVPAREGFVLRAGSPART 346
Cdd:cd15491 2 PTYRIDVRLTLLKSAPRPLKHRTRVRLHLGTSEVLGRVVLLDRDELAPGEEALAQLRLEEPVVAKRGDRFILRSYSPMRT 81
|
....*.
gi 1481165581 347 VAGGRV 352
Cdd:cd15491 82 IGGGRV 87
|
|
| TypA_BipA |
cd01891 |
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ... |
6-173 |
6.90e-17 |
|
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.
Pssm-ID: 206678 [Multi-domain] Cd Length: 194 Bit Score: 79.17 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRAL---TGIET----------DRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERF------ 66
Cdd:cd01891 5 IAIIAHVDHGKTTLVDALlkqSGTFReneevgervmDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFggever 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 67 VRTMVAGaagiraVVLAVSAAEGIRPQTREHVEIAGLLGVEAgVVAVTQCDLADeARAAEVGADAARLLAAHG----MAD 142
Cdd:cd01891 85 VLSMVDG------VLLLVDASEGPMPQTRFVLKKALEAGLKP-IVVINKIDRPD-ARPEEVVDEVFDLFLELNatdeQLD 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 1481165581 143 APVVHTSALDGRG---LPELRATLAEL----MQRVPAP 173
Cdd:cd01891 157 FPIVYASAKNGWAslnLDDPSEDLDPLfetiIEHVPAP 194
|
|
| TypA_BipA |
TIGR01394 |
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ... |
6-254 |
1.63e-15 |
|
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]
Pssm-ID: 273597 [Multi-domain] Cd Length: 594 Bit Score: 80.04 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRAL---------TGIETDRL----EEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERF------ 66
Cdd:TIGR01394 4 IAIIAHVDHGKTTLVDALlkqsgtfraNEAVAERVmdsnDLERERGITILAKNTAIRYNGTKINIVDTPGHADFggever 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 67 VRTMVAGaagiraVVLAVSAAEGIRPQTREHVEIAGLLGVEAgVVAVTQCDLADeARAAEVGADAARLLAAHGMA----D 142
Cdd:TIGR01394 84 VLGMVDG------VLLLVDASEGPMPQTRFVLKKALELGLKP-IVVINKIDRPS-ARPDEVVDEVFDLFAELGADdeqlD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 143 APVVHTSALDGRG---LPELRATLAEL----MQRVPAPAE------QGLAYLpVDRTFAVagfGTVVTGTLQRGRLSVGE 209
Cdd:TIGR01394 156 FPIVYASGRAGWAsldLDDPSDNMAPLfdaiVRHVPAPKGdldeplQMLVTN-LDYDEYL---GRIAIGRVHRGTVKKGQ 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1481165581 210 EVEL-TPGGKRARIRALQVHG------RQVQQAIPGGRTAVNlrGVESAEVG 254
Cdd:TIGR01394 232 QVALmKRDGTIENGRISKLLGfeglerVEIDEAGAGDIVAVA--GLEDINIG 281
|
|
| cysN |
PRK05124 |
sulfate adenylyltransferase subunit 1; Provisional |
29-303 |
5.04e-15 |
|
sulfate adenylyltransferase subunit 1; Provisional
Pssm-ID: 235349 [Multi-domain] Cd Length: 474 Bit Score: 78.03 E-value: 5.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 29 DRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRTMVAGAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEA 108
Cdd:PRK05124 83 DGLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKH 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 109 GVVAVTQCDLAD--EARAAEVGAD----AARLlaaHGMADAPVVHTSALDGRGLPELRA--------TLAELMQRVP--A 172
Cdd:PRK05124 163 LVVAVNKMDLVDysEEVFERIREDyltfAEQL---PGNLDIRFVPLSALEGDNVVSQSEsmpwysgpTLLEVLETVDiqR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 173 PAEQGLAYLPVD---------RTFAvagfgtvvtGTLQRGRLSVGEEVELTPGGKRARIRALQVHGRQVQQAIPGgrTAV 243
Cdd:PRK05124 240 VVDAQPFRFPVQyvnrpnldfRGYA---------GTLASGVVKVGDRVKVLPSGKESNVARIVTFDGDLEEAFAG--EAI 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1481165581 244 NLRGVESAEVGRGCALATPG-LLHASDWLDVHLRALpgDHRPLETGREYKLLLAAGEIPAR 303
Cdd:PRK05124 309 TLVLEDEIDISRGDLLVAADeALQAVQHASADVVWM--AEQPLQPGQSYDIKIAGKKTRAR 367
|
|
| EFTU_II |
cd03697 |
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ... |
181-263 |
5.05e-15 |
|
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.
Pssm-ID: 293898 [Multi-domain] Cd Length: 87 Bit Score: 70.63 E-value: 5.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 181 LPVDRTFAVAGFGTVVTGTLQRGRLSVGEEVELTPGGK--RARIRALQVHGRQVQQAIPGGRTAVNLRGVESAEVGRGCA 258
Cdd:cd03697 3 MPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKEtlKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMV 82
|
....*
gi 1481165581 259 LATPG 263
Cdd:cd03697 83 LAKPG 87
|
|
| InfB |
COG0532 |
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
2-237 |
1.82e-14 |
|
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440298 [Multi-domain] Cd Length: 502 Bit Score: 76.21 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 2 RPLAVGVIGHVDHGKTALVRALtgietdrleeekrRGISIALGFA----------WLEVPGGEIDLIDMPGHERFVrTMV 71
Cdd:COG0532 3 RPPVVTVMGHVDHGKTSLLDAI-------------RKTNVAAGEAggitqhigayQVETNGGKITFLDTPGHEAFT-AMR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 72 A-GAAGIRAVVLAVSAAEGIRPQTREHVEIAGllgvEAGV---VAVTQCDLAdearaaevGADAARL---LAAHGMA--- 141
Cdd:COG0532 69 ArGAQVTDIVILVVAADDGVMPQTIEAINHAK----AAGVpiiVAINKIDKP--------GANPDRVkqeLAEHGLVpee 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 142 ---DAPVVHTSALDGRGLPELRATL---AELM--QRVP-APAEqGL---AYLpvDRtfavaGFGTVVTGTLQRGRLSVGE 209
Cdd:COG0532 137 wggDTIFVPVSAKTGEGIDELLEMIllqAEVLelKANPdRPAR-GTvieAKL--DK-----GRGPVATVLVQNGTLKVGD 208
|
250 260 270
....*....|....*....|....*....|.
gi 1481165581 210 EV--ELTPGgkraRIRALQ-VHGRQVQQAIP 237
Cdd:COG0532 209 IVvaGTAYG----RVRAMFdDRGKRVKEAGP 235
|
|
| TypA |
COG1217 |
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ... |
6-254 |
2.09e-14 |
|
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];
Pssm-ID: 440830 [Multi-domain] Cd Length: 606 Bit Score: 76.21 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRAL---TGI--ETDRLEE--------EKRRGISIalgFA------WLEVpggEIDLIDMPGH--- 63
Cdd:COG1217 9 IAIIAHVDHGKTTLVDALlkqSGTfrENQEVAErvmdsndlERERGITI---LAkntavrYKGV---KINIVDTPGHadf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 64 ----ERfVRTMVAGaagiraVVLAVSAAEGIRPQTREHVEIAgllgVEAG---VVAVTQCDLADeARAAEV--------- 127
Cdd:COG1217 83 ggevER-VLSMVDG------VLLLVDAFEGPMPQTRFVLKKA----LELGlkpIVVINKIDRPD-ARPDEVvdevfdlfi 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 128 --GADAARLlaahgmaDAPVVHTSALDG---RGLPELRATLAEL----MQRVPAPaeqglaylPVDRTfavAGF------ 192
Cdd:COG1217 151 elGATDEQL-------DFPVVYASARNGwasLDLDDPGEDLTPLfdtiLEHVPAP--------EVDPD---GPLqmlvtn 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1481165581 193 -------GTVVTGTLQRGRLSVGEEVEL-TPGGKRARIRALQVHG------RQVQQAIPGGRTAVNlrGVESAEVG 254
Cdd:COG1217 213 ldysdyvGRIAIGRIFRGTIKKGQQVALiKRDGKVEKGKITKLFGfeglerVEVEEAEAGDIVAIA--GIEDINIG 286
|
|
| infB |
CHL00189 |
translation initiation factor 2; Provisional |
2-237 |
2.57e-14 |
|
translation initiation factor 2; Provisional
Pssm-ID: 177089 [Multi-domain] Cd Length: 742 Bit Score: 76.41 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 2 RPLAVGVIGHVDHGKTALvraLTGIETDRLEEEKRRGISIALGFAWLEVP----GGEIDLIDMPGHERFVRTMVAGAAGI 77
Cdd:CHL00189 243 RPPIVTILGHVDHGKTTL---LDKIRKTQIAQKEAGGITQKIGAYEVEFEykdeNQKIVFLDTPGHEAFSSMRSRGANVT 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 78 RAVVLAVSAAEGIRPQTRE---HVEIAGLlgveAGVVAVTQCDLADearaaevgADAARL---LAAHGM------ADAPV 145
Cdd:CHL00189 320 DIAILIIAADDGVKPQTIEainYIQAANV----PIIVAINKIDKAN--------ANTERIkqqLAKYNLipekwgGDTPM 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 146 VHTSALDGRGLPELRAT---LAEL--MQRVPAPAEQGL---AYLpvDRTfavagFGTVVTGTLQRGRLSVGEevELTPGG 217
Cdd:CHL00189 388 IPISASQGTNIDKLLETillLAEIedLKADPTQLAQGIileAHL--DKT-----KGPVATILVQNGTLHIGD--IIVIGT 458
|
250 260
....*....|....*....|.
gi 1481165581 218 KRARIRA-LQVHGRQVQQAIP 237
Cdd:CHL00189 459 SYAKIRGmINSLGNKINLATP 479
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
7-165 |
1.79e-12 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 65.56 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 7 GVIGHVDHGKTALVRALTGIETDRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRTMVAGAA-----GIRAVV 81
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELArlllrGADLIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 82 LAVSAAEGIRPQTREHVEIAGLLGVEAGVVAV-TQCDLADEARAAEVgadaARLLAAHGMADAPVVHTSALDGRGLPELR 160
Cdd:cd00882 81 LVVDSTDRESEEDAKLLILRRLRKEGIPIILVgNKIDLLEEREVEEL----LRLEELAKILGVPVFEVSAKTGEGVDELF 156
|
....*
gi 1481165581 161 ATLAE 165
Cdd:cd00882 157 EKLIE 161
|
|
| GTPBP1_like |
cd04165 |
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ... |
6-169 |
5.38e-12 |
|
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.
Pssm-ID: 206728 [Multi-domain] Cd Length: 224 Bit Score: 65.77 E-value: 5.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGIETD------RL-------EEEKRRGISIA---LGFA-------WLEVPGGEID------ 56
Cdd:cd04165 2 VAVVGNVDAGKSTLLGVLTQGELDngrgkaRLnlfrhkhEVESGRTSSVSndiLGFDsdgevvnYPDNHLGELDveicek 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 57 ------LIDMPGHERFVRTMVAGAAGIRA--VVLAVSAAEGIRPQTREHVEIAGLLGVEAGVVaVTQCDLADEARAAEVG 128
Cdd:cd04165 82 sskvvtFIDLAGHERYLKTTVFGMTGYAPdyAMLVVGANAGIIGMTKEHLGLALALKVPVFVV-VTKIDMTPANVLQETL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1481165581 129 ADAARLLAAHG----------MADA-------------PVVHTSALDGRGLPELRATLAELMQR 169
Cdd:cd04165 161 KDLKRLLKSPGvrklpvpvksKDDVvlsasnlssgrvvPIFQVSNVTGEGLDLLRRFLNLLPPR 224
|
|
| EF2 |
cd01885 |
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ... |
6-95 |
7.14e-12 |
|
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.
Pssm-ID: 206672 [Multi-domain] Cd Length: 218 Bit Score: 65.33 E-value: 7.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRAL---TGIE----------TDRLEEEKRRGI-----SIALGF--AWLEVPGGE--IDLIDMPGH 63
Cdd:cd01885 3 ICIIAHVDHGKTTLSDSLlasAGIIseklagkaryLDTREDEQERGItikssAISLYFeyEEEKMDGNDylINLIDSPGH 82
|
90 100 110
....*....|....*....|....*....|....*
gi 1481165581 64 ERF---VRTMVAGAAGirAVVLaVSAAEGIRPQTR 95
Cdd:cd01885 83 VDFsseVTAALRLTDG--ALVV-VDAVEGVCVQTE 114
|
|
| PRK12740 |
PRK12740 |
elongation factor G-like protein EF-G2; |
9-137 |
7.07e-11 |
|
elongation factor G-like protein EF-G2;
Pssm-ID: 237186 [Multi-domain] Cd Length: 668 Bit Score: 65.15 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 9 IGHVDHGKTALVRAL---TG-------IE-----TDRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRTMVAG 73
Cdd:PRK12740 1 VGHSGAGKTTLTEAIlfyTGaihrigeVEdgtttMDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1481165581 74 AAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVeAGVVAVTQCDladearaaEVGADAARLLAA 137
Cdd:PRK12740 81 LRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGV-PRIIFVNKMD--------RAGADFFRVLAQ 135
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
1-167 |
9.26e-11 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 61.15 E-value: 9.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 1 MRPLAVGVIGHVDHGKTALVRALTGIETDRLEEEKRRGISIAlgFAWLEVPGGEID--LIDMPGHERF--VRTMVAGAAG 76
Cdd:COG1100 1 MGEKKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLSTNGVTID--KKELKLDGLDVDlvIWDTPGQDEFreTRQFYARQLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 77 IRAVVLAVsaAEGIRPQTREH-VEIAGLLgVEAG-----VVAVTQCDLADEARAAEVGADAARLLAAHGmadAPVVHTSA 150
Cdd:COG1100 79 GASLYLFV--VDGTREETLQSlYELLESL-RRLGkkspiILVLNKIDLYDEEEIEDEERLKEALSEDNI---VEVVATSA 152
|
170
....*....|....*..
gi 1481165581 151 LDGRGLPELRATLAELM 167
Cdd:COG1100 153 KTGEGVEELFAALAEIL 169
|
|
| LepA |
cd01890 |
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ... |
8-173 |
9.55e-11 |
|
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.
Pssm-ID: 206677 [Multi-domain] Cd Length: 179 Bit Score: 61.01 E-value: 9.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 8 VIGHVDHGKTALV------------RALTGIETDRLEEEKRRGISIALGFAWL--EVPGGE---IDLIDMPGHERF---V 67
Cdd:cd01890 5 IIAHIDHGKSTLAdrlleltgtvseREMKEQVLDSMDLERERGITIKAQAVRLfyKAKDGEeylLNLIDTPGHVDFsyeV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 68 RTMVAGAAGiraVVLAVSAAEGIRPQTREHVEIAGLLGVEAgVVAVTQCDL--ADEARAAE-----VGADAARllaahgm 140
Cdd:cd01890 85 SRSLAACEG---ALLVVDATQGVEAQTLANFYLALENNLEI-IPVINKIDLpaADPDRVKQeiedvLGLDASE------- 153
|
170 180 190
....*....|....*....|....*....|...
gi 1481165581 141 adapVVHTSALDGRGLPELratLAELMQRVPAP 173
Cdd:cd01890 154 ----AILVSAKTGLGVEDL---LEAIVERIPPP 179
|
|
| TetM_like |
cd04168 |
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ... |
7-95 |
3.51e-10 |
|
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.
Pssm-ID: 206731 [Multi-domain] Cd Length: 237 Bit Score: 60.71 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 7 GVIGHVDHGKTALVRAL---TG-IE-----------TDRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFV---- 67
Cdd:cd04168 3 GILAHVDAGKTTLTESLlytSGaIRelgsvdkgttrTDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIaeve 82
|
90 100 110
....*....|....*....|....*....|
gi 1481165581 68 RT--MVAGAagiravVLAVSAAEGIRPQTR 95
Cdd:cd04168 83 RSlsVLDGA------ILVISAVEGVQAQTR 106
|
|
| EF1_alpha_II |
cd03693 |
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ... |
181-256 |
6.84e-10 |
|
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.
Pssm-ID: 293894 [Multi-domain] Cd Length: 91 Bit Score: 56.04 E-value: 6.84e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1481165581 181 LPVDRTFAVAGFGTVVTGTLQRGRLSVGEEVELTPGGKRARIRALQVHGRQVQQAIPGGRTAVNLRGVESAEVGRG 256
Cdd:cd03693 7 LPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIKRG 82
|
|
| small_GTP |
TIGR00231 |
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ... |
6-156 |
1.24e-09 |
|
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]
Pssm-ID: 272973 [Multi-domain] Cd Length: 162 Bit Score: 57.38 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALTGieTDRLEEEKRRGISIALGFAWLEVPGG--EIDLIDMPGHERFVR----TMVAGAAGIRA 79
Cdd:TIGR00231 4 IVIVGHPNVGKSTLLNSLLG--NKGSITEYYPGTTRNYVTTVIEEDGKtyKFNLLDTAGQEDYDAirrlYYPQVERSLRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 80 ---VVLAVSAAEGIRPQTRehvEIAGLLGVEAG-VVAVTQCDLADEARAAEVGADAARllaahgMADAPVVHTSALDGRG 155
Cdd:TIGR00231 82 fdiVILVLDVEEILEKQTK---EIIHHADSGVPiILVGNKIDLKDADLKTHVASEFAK------LNGEPIIPLSAETGKN 152
|
.
gi 1481165581 156 L 156
Cdd:TIGR00231 153 I 153
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
6-94 |
1.81e-09 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 60.83 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRAL---TGIeTDRL-------------EEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFV-- 67
Cdd:COG0480 12 IGIVAHIDAGKTTLTERIlfyTGA-IHRIgevhdgntvmdwmPEEQERGITITSAATTCEWKGHKINIIDTPGHVDFTge 90
|
90 100 110
....*....|....*....|....*....|
gi 1481165581 68 --RTM-VAGAAgiravVLAVSAAEGIRPQT 94
Cdd:COG0480 91 veRSLrVLDGA-----VVVFDAVAGVEPQT 115
|
|
| PRK07560 |
PRK07560 |
elongation factor EF-2; Reviewed |
6-98 |
2.93e-09 |
|
elongation factor EF-2; Reviewed
Pssm-ID: 236047 [Multi-domain] Cd Length: 731 Bit Score: 60.26 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRAL---TGIETDRL----------EEEKRRGISIALGFAWL--EVPGGE--IDLIDMPGHERF-- 66
Cdd:PRK07560 23 IGIIAHIDHGKTTLSDNLlagAGMISEELageqlaldfdEEEQARGITIKAANVSMvhEYEGKEylINLIDTPGHVDFgg 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1481165581 67 --VRTMvagaagiRAV---VLAVSAAEGIRPQT--------REHV 98
Cdd:PRK07560 103 dvTRAM-------RAVdgaIVVVDAVEGVMPQTetvlrqalRERV 140
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
6-95 |
7.00e-09 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 57.22 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRAL---TGIeTDRL-------------EEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRT 69
Cdd:cd04170 2 IALVGHSGSGKTTLAEALlyaTGA-IDRLgrvedgntvsdydPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGE 80
|
90 100
....*....|....*....|....*.
gi 1481165581 70 MVAGAAGIRAVVLAVSAAEGIRPQTR 95
Cdd:cd04170 81 TLSALRAVDAALIVVEAQSGVEVGTE 106
|
|
| Translation_Factor_II_like |
cd01342 |
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ... |
181-249 |
1.53e-08 |
|
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.
Pssm-ID: 293888 [Multi-domain] Cd Length: 80 Bit Score: 51.88 E-value: 1.53e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1481165581 181 LPVDRTFAVAGFGTVVTGTLQRGRLSVGEEVELTPGGKRARIRALQVHGRQVQQAIPGGRTAVNLRGVE 249
Cdd:cd01342 3 MQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK 71
|
|
| Snu114p |
cd04167 |
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ... |
6-96 |
1.87e-08 |
|
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.
Pssm-ID: 206730 [Multi-domain] Cd Length: 213 Bit Score: 54.97 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRALtgIE------------------TDRLEEEKRRGISIALGFAWLEVPGGE-----IDLIDMPG 62
Cdd:cd04167 3 VCIAGHLHHGKTSLLDML--IEqthkrtpsvklgwkplryTDTRKDEQERGISIKSNPISLVLEDSKgksylINIIDTPG 80
|
90 100 110
....*....|....*....|....*....|....
gi 1481165581 63 HERFVRTMVAGAAGIRAVVLAVSAAEGIRPQTRE 96
Cdd:cd04167 81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTER 114
|
|
| GTP_EFTU_D2 |
pfam03144 |
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ... |
193-260 |
9.10e-08 |
|
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.
Pssm-ID: 427163 [Multi-domain] Cd Length: 73 Bit Score: 49.57 E-value: 9.10e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1481165581 193 GTVVTGTLQRGRLSVGEEVELTPGGK-----RARIRALQVHGRQVQQAIPGGRTAVNLRGVESAEVGRGCALA 260
Cdd:pfam03144 1 GTVATGRVESGTLKKGDKVRILPNGTgkkkiVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
|
|
| PRK13351 |
PRK13351 |
elongation factor G-like protein; |
6-95 |
9.86e-08 |
|
elongation factor G-like protein;
Pssm-ID: 237358 [Multi-domain] Cd Length: 687 Bit Score: 55.34 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRAL---TG------------IETDRLEEEKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRTM 70
Cdd:PRK13351 11 IGILAHIDAGKTTLTERIlfyTGkihkmgevedgtTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDFTGEV 90
|
90 100
....*....|....*....|....*
gi 1481165581 71 VAGAAGIRAVVLAVSAAEGIRPQTR 95
Cdd:PRK13351 91 ERSLRVLDGAVVVFDAVTGVQPQTE 115
|
|
| aIF-2 |
TIGR00491 |
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ... |
1-169 |
1.17e-07 |
|
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]
Pssm-ID: 273104 [Multi-domain] Cd Length: 591 Bit Score: 54.82 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 1 MRPLAVGVIGHVDHGKTALvraLTGIETDRLEEEKRRGISIALGFAW--------------------LEVPGgeIDLIDM 60
Cdd:TIGR00491 2 LRQPIVVVLGHVDHGKTTL---LDKIRGTAVVKKEAGGITQHIGASEvptdviekicgdllksfkikLKIPG--LLFIDT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 61 PGHERFVRTMVAGAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEAgVVAVTQCDLADEARA---------------- 124
Cdd:TIGR00491 77 PGHEAFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPF-VVAANKIDRIPGWKShegypflesinkqeqr 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1481165581 125 ----------------AEVGADAARLLAAHGMAD-APVVHTSALDGRGLPELRATLAELMQR 169
Cdd:TIGR00491 156 vrqnldkqvynlviqlAEQGFNAERFDRIRDFTKtVAIIPVSAKTGEGIPELLAILAGLAQN 217
|
|
| PRK10218 |
PRK10218 |
translational GTPase TypA; |
6-221 |
1.39e-07 |
|
translational GTPase TypA;
Pssm-ID: 104396 [Multi-domain] Cd Length: 607 Bit Score: 54.71 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRAL---TGIETDRLEE----------EKRRGISIALGFAWLEVPGGEIDLIDMPGHERFVRTMVA 72
Cdd:PRK10218 8 IAIIAHVDHGKTTLVDKLlqqSGTFDSRAETqervmdsndlEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVER 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 73 GAAGIRAVVLAVSAAEGIRPQTREHVEIAGLLGVEAgVVAVTQCD--------LADEARAAEVGADaarllAAHGMADAP 144
Cdd:PRK10218 88 VMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKP-IVVINKVDrpgarpdwVVDQVFDLFVNLD-----ATDEQLDFP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 145 VVHTSALDG-RGL------PELRATLAELMQRVPAPAE--QGLAYLPVDRTFAVAGFGTVVTGTLQRGRLSVGEEVELTP 215
Cdd:PRK10218 162 IVYASALNGiAGLdhedmaEDMTPLYQAIVDHVPAPDVdlDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIID 241
|
....*.
gi 1481165581 216 GGKRAR 221
Cdd:PRK10218 242 SEGKTR 247
|
|
| aEF-2 |
TIGR00490 |
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ... |
6-94 |
2.88e-07 |
|
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]
Pssm-ID: 129581 [Multi-domain] Cd Length: 720 Bit Score: 53.75 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTAL---VRALTGIETDRL----------EEEKRRGISIALGFAWL--EVPGGE--IDLIDMPGHERFVR 68
Cdd:TIGR00490 22 IGIVAHIDHGKTTLsdnLLAGAGMISEELagqqlyldfdEQEQERGITINAANVSMvhEYEGNEylINLIDTPGHVDFGG 101
|
90 100
....*....|....*....|....*.
gi 1481165581 69 TMVAGAAGIRAVVLAVSAAEGIRPQT 94
Cdd:TIGR00490 102 DVTRAMRAVDGAIVVVCAVEGVMPQT 127
|
|
| RF3 |
cd04169 |
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ... |
8-95 |
3.45e-07 |
|
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.
Pssm-ID: 206732 [Multi-domain] Cd Length: 268 Bit Score: 52.21 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 8 VIGHVDHGKTALVRAL-----------------TGIET--DRLEEEKRRGISI---ALGFawlEVPGGEIDLIDMPGHER 65
Cdd:cd04169 7 IISHPDAGKTTLTEKLllfggaiqeagavkarkSRKHAtsDWMEIEKQRGISVtssVMQF---EYKGCVINLLDTPGHED 83
|
90 100 110
....*....|....*....|....*....|....
gi 1481165581 66 F----VRTMVAgaagIRAVVLAVSAAEGIRPQTR 95
Cdd:cd04169 84 FsedtYRTLTA----VDSAVMVIDAAKGVEPQTR 113
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
7-166 |
5.25e-07 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 49.94 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 7 GVIGHVDHGKTALVRALTGietdrleeEKRRGISIALG-------FAWLEVPGGEIDLIDMPG-------HERFVRTMVA 72
Cdd:cd00880 1 AIFGRPNVGKSSLLNALLG--------QNVGIVSPIPGttrdpvrKEWELLPLGPVVLIDTPGldeegglGRERVEEARQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 73 GAAGIRAVVLAVSAAEGIRPQTREHVEIAgllgvEAG---VVAVTQCDLADEARAAEVGADAARLLaahgMADAPVVHTS 149
Cdd:cd00880 73 VADRADLVLLVVDSDLTPVEEEAKLGLLR-----ERGkpvLLVLNKIDLVPESEEEELLRERKLEL----LPDLPVIAVS 143
|
170
....*....|....*..
gi 1481165581 150 ALDGRGLPELRATLAEL 166
Cdd:cd00880 144 ALPGEGIDELRKKIAEL 160
|
|
| PTZ00416 |
PTZ00416 |
elongation factor 2; Provisional |
8-94 |
2.16e-06 |
|
elongation factor 2; Provisional
Pssm-ID: 240409 [Multi-domain] Cd Length: 836 Bit Score: 50.82 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 8 VIGHVDHGKTALVRAL---TGI----------ETDRLEEEKRRGISI-----ALGFAW-LEVPGGE----IDLIDMPGHE 64
Cdd:PTZ00416 24 VIAHVDHGKSTLTDSLvckAGIissknagdarFTDTRADEQERGITIkstgiSLYYEHdLEDGDDKqpflINLIDSPGHV 103
|
90 100 110
....*....|....*....|....*....|
gi 1481165581 65 RFVRTMVAGAAGIRAVVLAVSAAEGIRPQT 94
Cdd:PTZ00416 104 DFSSEVTAALRVTDGALVVVDCVEGVCVQT 133
|
|
| GTPBP_II |
cd03694 |
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ... |
183-261 |
2.22e-06 |
|
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.
Pssm-ID: 293895 [Multi-domain] Cd Length: 87 Bit Score: 46.06 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 183 VDRTFAVAGFGTVVTGTLQRGRLSVGEEVELTP--GGK--RARIRALQVHGRQVQQAIPGGRTAVNLRGVESAEVGRGCA 258
Cdd:cd03694 5 IDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPdaDGKfrPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGMV 84
|
...
gi 1481165581 259 LAT 261
Cdd:cd03694 85 LVS 87
|
|
| SelB-wing_3 |
pfam09107 |
Elongation factor SelB, winged helix; Members of this family adopt a winged-helix fold, with ... |
580-615 |
7.34e-06 |
|
Elongation factor SelB, winged helix; Members of this family adopt a winged-helix fold, with an alpha/beta structure consisting of three alpha-helices and a twisted three-stranded antiparallel beta-sheet, with an alpha-beta-alpha-alpha-beta-beta connectivity. They are involved in both DNA and RNA binding.
Pssm-ID: 430413 [Multi-domain] Cd Length: 46 Bit Score: 43.18 E-value: 7.34e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1481165581 580 FAARPEGFLVGEAGRVLGISRKYSVPLLEYLDGVGI 615
Cdd:pfam09107 1 HLKENGEITVAEFRDLLGTSRKYAIPLLEYLDRIGI 36
|
|
| EF-G |
cd01886 |
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ... |
6-94 |
9.29e-06 |
|
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.
Pssm-ID: 206673 [Multi-domain] Cd Length: 270 Bit Score: 47.87 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALV-RAL--TGI------------ETDRLEEEKRRGISI---ALGFAWlevPGGEIDLIDMPGH---- 63
Cdd:cd01886 2 IGIIAHIDAGKTTTTeRILyyTGRihkigevhgggaTMDWMEQERERGITIqsaATTCFW---KDHRINIIDTPGHvdft 78
|
90 100 110
....*....|....*....|....*....|....
gi 1481165581 64 ---ERFVRtMVAGAagiravVLAVSAAEGIRPQT 94
Cdd:cd01886 79 ievERSLR-VLDGA------VAVFDAVAGVQPQT 105
|
|
| HBS1-like_II |
cd16267 |
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ... |
181-259 |
1.12e-05 |
|
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.
Pssm-ID: 293912 [Multi-domain] Cd Length: 84 Bit Score: 44.04 E-value: 1.12e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1481165581 181 LPVDRTFAVAGFGTVVTGTLQRGRLSVGEEVELTPGGKRARIRALQVHGRQVQQAIPGGRTAVNLRGVESAEVGRGCAL 259
Cdd:cd16267 4 LSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGSIL 82
|
|
| PRK00093 |
PRK00093 |
GTP-binding protein Der; Reviewed |
2-171 |
5.21e-05 |
|
GTP-binding protein Der; Reviewed
Pssm-ID: 234628 [Multi-domain] Cd Length: 435 Bit Score: 46.20 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 2 RPLAVGVIGHVDHGKTALVRALTGietdrleeEKRrgiSIALgfawlEVPGGEIDLIDMP----GHE-RFVRTmvagaAG 76
Cdd:PRK00093 172 EPIKIAIIGRPNVGKSSLINALLG--------EER---VIVS-----DIAGTTRDSIDTPferdGQKyTLIDT-----AG 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 77 IR-------------------------AVVLAVSAAEGIRPQ-TRehveIAGLLgVEAG---VVAVTQCDLADEARAAEV 127
Cdd:PRK00093 231 IRrkgkvtegvekysvirtlkaieradVVLLVIDATEGITEQdLR----IAGLA-LEAGralVIVVNKWDLVDEKTMEEF 305
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1481165581 128 GADAARLLAAhgMADAPVVHTSALDGRGLPELRATL----AELMQRVP 171
Cdd:PRK00093 306 KKELRRRLPF--LDYAPIVFISALTGQGVDKLLEAIdeayENANRRIS 351
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
242-596 |
1.37e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 45.25 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 242 AVNLRGVESAEVGRGCALAT---------PGLLHASDWLDVHLRALPGDHRPLETGREYKLLLAAGEIPARLRLLDREIL 312
Cdd:COG3321 846 PVDWSALYPGRGRRRVPLPTypfqredaaAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAA 925
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 313 HPGEAAPAQLRCAGPVAVPAREGFVLRAGSPARTVAGGRVLDPQTRRHRRNDPAVLDRLLSLAGAGPQEVVSQLLTGTGP 392
Cdd:COG3321 926 LAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALL 1005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 393 AGVLLDEAARLSGHAPSWVISWLPELQARQVGPLLVTAAALEGLKRDIRTALAEHHHSAPASPGLMFEDVLDRLRAARPV 472
Cdd:COG3321 1006 AAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALA 1085
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 473 LELAVQELLAGGELARTQGCLRLPGFRPSTLAAEGELSRRIEAAIRAGGLQPPDLKELPGGGSVAIKAIQRLLAGGVLVR 552
Cdd:COG3321 1086 LAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAA 1165
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1481165581 553 ARDRVQKRELLFHRDAVADAAERLATAFAARPEGFLVGEAGRVL 596
Cdd:COG3321 1166 ALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALL 1209
|
|
| eIF2_gamma_II |
cd03688 |
Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily ... |
179-243 |
1.51e-04 |
|
Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily represents domain II of the gamma subunit of eukaryotic translation initiation factor 2 (eIF2-gamma) found in eukaryota and archaea. eIF2 is a G protein that delivers the methionyl initiator tRNA to the small ribosomal subunit and releases it upon GTP hydrolysis after the recognition of the initiation codon. eIF2 is composed of three subunits, alpha, beta and gamma. Subunit gamma shows strongest conservation, and it confers both tRNA binding and GTP/GDP binding.
Pssm-ID: 293889 [Multi-domain] Cd Length: 113 Bit Score: 41.40 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 179 AYLPVDRTFAVAGFGT--------VVTGTLQRGRLSVGEEVELTPGGK------------RARIRALQVHGRQVQQAIPG 238
Cdd:cd03688 6 PRMIVIRSFDVNKPGTevddlkggVIGGSLIQGVLKVGDEIEIRPGIVvkkggkttcrpiFTKIVSLFAEGNDLEEAVPG 85
|
....*
gi 1481165581 239 GRTAV 243
Cdd:cd03688 86 GLIGV 90
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
255-597 |
3.12e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 44.09 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 255 RGCALATPGLLHASDWLDVHLRALPGDHRPLETGREYKLLLAAGEIPARLRLLDREILHPGEAAPAQLRCAGPVAVPARE 334
Cdd:COG3321 843 AGVPVDWSALYPGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALA 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 335 GFVLRAGSPARTVAGGRVLDPQTRRHRRNDPAVLDRLLSLAGAGPQEVVSQLLTGTGPAGVLLDEAARLSGHAPSWVISW 414
Cdd:COG3321 923 AAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAL 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 415 LPELQARQVGPLLVTAAALEGLKRDIRTALAEHHHSAPASPGLMFEDVLDRLRAARP---VLELAVQELLAGGELARTQG 491
Cdd:COG3321 1003 ALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAalaLALAALLLLAALAELALAAA 1082
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 492 CLRLPGFRPSTLAAEGELSRRIEAAIRAGGLQPPDLKELPGGGSVAIKAIQRLLAGGVLVRARDRVQKRELLFHRDAVAD 571
Cdd:COG3321 1083 ALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAA 1162
|
330 340
....*....|....*....|....*.
gi 1481165581 572 AAERLATAFAARPEGFLVGEAGRVLG 597
Cdd:COG3321 1163 LAAALLAAAALLLALALALAAALAAA 1188
|
|
| EngA2 |
cd01895 |
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ... |
3-159 |
5.59e-04 |
|
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.
Pssm-ID: 206682 [Multi-domain] Cd Length: 174 Bit Score: 41.26 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 3 PLAVGVIGHVDHGKTALVRALTGietdrleeEKRRGISialgfawlEVPGGEIDLIDMP--------------------- 61
Cdd:cd01895 2 PIKIAIIGRPNVGKSSLLNALLG--------EERVIVS--------DIAGTTRDSIDVPfeydgqkytlidtagirkkgk 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 62 ---GHERF--VRTMVAgaagIRA---VVLAVSAAEGIRPQ-TRehveIAGLLgVEAG---VVAVTQCDL--ADEARAAEV 127
Cdd:cd01895 66 vteGIEKYsvLRTLKA----IERadvVLLVLDASEGITEQdLR----IAGLI-LEEGkalIIVVNKWDLveKDEKTMKEF 136
|
170 180 190
....*....|....*....|....*....|..
gi 1481165581 128 GADAARLLaaHGMADAPVVHTSALDGRGLPEL 159
Cdd:cd01895 137 EKELRRKL--PFLDYAPIVFISALTGQGVDKL 166
|
|
| prfC |
PRK00741 |
peptide chain release factor 3; Provisional |
29-95 |
8.67e-04 |
|
peptide chain release factor 3; Provisional
Pssm-ID: 179105 [Multi-domain] Cd Length: 526 Bit Score: 42.43 E-value: 8.67e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1481165581 29 DRLEEEKRRGISIA---LGFAWlevPGGEIDLIDMPGHERF----VRTMVAgaagIRAVVLAVSAAEGIRPQTR 95
Cdd:PRK00741 55 DWMEMEKQRGISVTssvMQFPY---RDCLINLLDTPGHEDFsedtYRTLTA----VDSALMVIDAAKGVEPQTR 121
|
|
| PLN00116 |
PLN00116 |
translation elongation factor EF-2 subunit; Provisional |
6-94 |
1.03e-03 |
|
translation elongation factor EF-2 subunit; Provisional
Pssm-ID: 177730 [Multi-domain] Cd Length: 843 Bit Score: 42.40 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 6 VGVIGHVDHGKTALVRAL---TGI----------ETDRLEEEKRRGISIA---------LGFAWLEVPGGEID------- 56
Cdd:PLN00116 22 MSVIAHVDHGKSTLTDSLvaaAGIiaqevagdvrMTDTRADEAERGITIKstgislyyeMTDESLKDFKGERDgneylin 101
|
90 100 110
....*....|....*....|....*....|....*...
gi 1481165581 57 LIDMPGHERFVRTMVAGAAGIRAVVLAVSAAEGIRPQT 94
Cdd:PLN00116 102 LIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQT 139
|
|
| Der |
COG1160 |
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis]; |
62-171 |
1.49e-03 |
|
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440774 [Multi-domain] Cd Length: 438 Bit Score: 41.55 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 62 GHERF--VRTMVAgaagIRA---VVLAVSAAEGIRPQ-TRehveIAGLLgVEAG---VVAVTQCDLADEARAA--EVGAD 130
Cdd:COG1160 242 GIEKYsvLRTLRA----IERadvVLLVIDATEGITEQdLK----IAGLA-LEAGkalVIVVNKWDLVEKDRKTreELEKE 312
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1481165581 131 AARLLAAhgMADAPVVHTSALDGRG----LPELRATLAELMQRVP 171
Cdd:COG1160 313 IRRRLPF--LDYAPIVFISALTGQGvdklLEAVDEVYESANKRIS 355
|
|
| PRK14845 |
PRK14845 |
translation initiation factor IF-2; Provisional |
46-100 |
2.50e-03 |
|
translation initiation factor IF-2; Provisional
Pssm-ID: 237833 [Multi-domain] Cd Length: 1049 Bit Score: 41.02 E-value: 2.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1481165581 46 AWLEVPGgeIDLIDMPGHERFVRTMVAGAAGIRAVVLAVSAAEGIRPQTREHVEI 100
Cdd:PRK14845 521 AEIKIPG--LLFIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINI 573
|
|
| Translation_Factor_II |
cd16265 |
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ... |
183-254 |
3.31e-03 |
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Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.
Pssm-ID: 293910 [Multi-domain] Cd Length: 80 Bit Score: 36.89 E-value: 3.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1481165581 183 VDRTFAVAGfGTVVTGTLQRGRLSVGEEVELtpGGKRARIRALQVHGRQVQQAIPGGRTAVNLRGVESAEVG 254
Cdd:cd16265 5 VEKVFKILG-RQVLTGEVESGVIYVGYKVKG--DKGVALIRAIEREHRKVDFAVAGDEVALILEGKIKVKEG 73
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| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
82-164 |
3.64e-03 |
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Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.30 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1481165581 82 LAVSAAEGIRPqtrehveiagllgveagVVAVTQCDLADEARAAEVGADAARLlaahgmaDAPVVHTSALDGRGLPELRA 161
Cdd:cd01854 26 LVAAEASGIEP-----------------VIVLNKADLVDDEELEELLEIYEKL-------GYPVLAVSAKTGEGLDELRE 81
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...
gi 1481165581 162 TLA 164
Cdd:cd01854 82 LLK 84
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