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Conserved domains on  [gi|158635983|ref|NP_001103611|]
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eukaryotic translation initiation factor 5B [Rattus norvegicus]

Protein Classification

eukaryotic translation initiation factor 5B( domain architecture ID 1903529)

eukaryotic translation initiation factor 5B (eIF-5B) plays a role in translation initiation by serving as a ribosome-dependent GTPase that promotes the joining of the 60S ribosomal subunit with the pre-initiation complex, forming the 80S initiation complex, with the initiator methionine-tRNA positioned in the P-site and base-paired to the start codon

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK04004 super family cl44330
translation initiation factor IF-2; Validated
623-1198 0e+00

translation initiation factor IF-2; Validated


The actual alignment was detected with superfamily member PRK04004:

Pssm-ID: 457675 [Multi-domain]  Cd Length: 586  Bit Score: 559.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  623 EKLRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGH 702
Cdd:PRK04004    2 KKLRQPIVVVLGHVDHGKTTLLDKIRGTAVAAKEAGGITQHIGATEVPIDVIEKIAGPLKKPLPIKLKIPGLLFIDTPGH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  703 ESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLYDWKKSPDSDVAVTLKKQKKNTKDE 782
Cdd:PRK04004   82 EAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDRIPGWKSTEDAPFLESIEKQSQRVQQE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  783 FEERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEE--LRAQVMEVK 860
Cdd:PRK04004  162 LEEKLYELIGQLSELGFSADRFDRVKDFTKTVAIVPVSAKTGEGIPDLLMVLAGLAQRYLEERLKIDVEgpGKGTVLEVK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  861 ALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELR-VKNQYEKHKEVEAAQGVKILGKDLEKTLA 939
Cdd:PRK04004  242 EERGLGTTIDVILYDGTLRKGDTIVVGGKDGPIVTKVRALLKPRPLDEMRdPEDKFKPVDEVVAAAGVKISAPDLEDALA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  940 GLPLLVAyKDDEIPVLKDELIHELKQtlNAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASV 1019
Cdd:PRK04004  322 GSPLRVV-RDEDVEEVKEEVEEEIEE--IRIETDEEGVVVKADTLGSLEALVNELREEGIPIRKADVGDISKRDVIEAST 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983 1020 MLEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYK-KQKQEEFKHIaVFPCKMKILPQYIF 1098
Cdd:PRK04004  399 VAEKDPLYGVILAFNVKVLPDAEEEAEKSDVKIFTGDVIYQLIEDYEKWVKEQKeAEKEKILEKI-VRPAKIRILPGYVF 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983 1099 NSRDPIVIGVTVEAGQVKQGTPmcVPSKNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEpipgesPKMFGRHFEATDIL 1178
Cdd:PRK04004  478 RQSDPAIVGVEVLGGTIKPGVP--LIKEDGKRVGTIKQIQDQGENVKEAKAGMEVAISID------GPTVGRQIKEGDIL 549
                         570       580
                  ....*....|....*....|
gi 158635983 1179 VSKISRQSIDALKDWFRDEM 1198
Cdd:PRK04004  550 YVDIPEEHAKILEQELKDEL 569
 
Name Accession Description Interval E-value
PRK04004 PRK04004
translation initiation factor IF-2; Validated
623-1198 0e+00

translation initiation factor IF-2; Validated


Pssm-ID: 235195 [Multi-domain]  Cd Length: 586  Bit Score: 559.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  623 EKLRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGH 702
Cdd:PRK04004    2 KKLRQPIVVVLGHVDHGKTTLLDKIRGTAVAAKEAGGITQHIGATEVPIDVIEKIAGPLKKPLPIKLKIPGLLFIDTPGH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  703 ESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLYDWKKSPDSDVAVTLKKQKKNTKDE 782
Cdd:PRK04004   82 EAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDRIPGWKSTEDAPFLESIEKQSQRVQQE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  783 FEERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEE--LRAQVMEVK 860
Cdd:PRK04004  162 LEEKLYELIGQLSELGFSADRFDRVKDFTKTVAIVPVSAKTGEGIPDLLMVLAGLAQRYLEERLKIDVEgpGKGTVLEVK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  861 ALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELR-VKNQYEKHKEVEAAQGVKILGKDLEKTLA 939
Cdd:PRK04004  242 EERGLGTTIDVILYDGTLRKGDTIVVGGKDGPIVTKVRALLKPRPLDEMRdPEDKFKPVDEVVAAAGVKISAPDLEDALA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  940 GLPLLVAyKDDEIPVLKDELIHELKQtlNAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASV 1019
Cdd:PRK04004  322 GSPLRVV-RDEDVEEVKEEVEEEIEE--IRIETDEEGVVVKADTLGSLEALVNELREEGIPIRKADVGDISKRDVIEAST 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983 1020 MLEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYK-KQKQEEFKHIaVFPCKMKILPQYIF 1098
Cdd:PRK04004  399 VAEKDPLYGVILAFNVKVLPDAEEEAEKSDVKIFTGDVIYQLIEDYEKWVKEQKeAEKEKILEKI-VRPAKIRILPGYVF 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983 1099 NSRDPIVIGVTVEAGQVKQGTPmcVPSKNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEpipgesPKMFGRHFEATDIL 1178
Cdd:PRK04004  478 RQSDPAIVGVEVLGGTIKPGVP--LIKEDGKRVGTIKQIQDQGENVKEAKAGMEVAISID------GPTVGRQIKEGDIL 549
                         570       580
                  ....*....|....*....|
gi 158635983 1179 VSKISRQSIDALKDWFRDEM 1198
Cdd:PRK04004  550 YVDIPEEHAKILEQELKDEL 569
aIF-2 TIGR00491
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ...
624-1211 4.68e-138

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: 432.32  E-value: 4.68e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   624 KLRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGHE 703
Cdd:TIGR00491    1 RLRQPIVVVLGHVDHGKTTLLDKIRGTAVVKKEAGGITQHIGASEVPTDVIEKICGDLLKSFKIKLKIPGLLFIDTPGHE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   704 SFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLYDWKKSPDSDVAVTLKKQKKNTKDEF 783
Cdd:TIGR00491   81 AFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDRIPGWKSHEGYPFLESINKQEQRVRQNL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   784 EERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEE--LRAQVMEVKA 861
Cdd:TIGR00491  161 DKQVYNLVIQLAEQGFNAERFDRIRDFTKTVAIIPVSAKTGEGIPELLAILAGLAQNYLENKLKLAIEgpAKGTILEVKE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   862 LPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRV-KNQYEKHKEVEAAQGVKILGKDLEKTLAG 940
Cdd:TIGR00491  241 EQGLGYTIDAVIYDGILRKGDIIVLAGIDDVIVTRVRAILKPRPLQEMRLaRKKFAQVDEVYAAAGVKVAAPNLDTVLAG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   941 LPlLVAYKDDEIPVLKDELIHELKQTlnAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASVM 1020
Cdd:TIGR00491  321 SP-IVVENNEEIEKYKEEIQKEVEEI--KIYTDEEGIVVKADTLGSLEALVNELRRRGIPIKKADIGDVSKRDVVEAEIV 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  1021 LEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYKKQKQEEFKHIAVFPCKMKILPQYIFNS 1100
Cdd:TIGR00491  398 KQEAKEYGAIAAFNVKPLPGAEIEAEKYDIKLFSDNIIYQLMENFEKWIEDIEESEKRKTLEAIIKPGKIKIIPGYVFRR 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  1101 RDPIVIGVTVEAGQVKQGTPMCVPSKNFVdiGIVTSIEINHKQVDVAKKGQEVCVKIEPIpgespkMFGRHFEATDIL-- 1178
Cdd:TIGR00491  478 SDPAIVGVEVLGGIIRPGYPLIKKDGRRV--GEVRQIQDNGKNVKRASAGMEVAIAIEDV------VIGRQLEEGDELyv 549
                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 158635983  1179 ------VSKISRQSIDALKDWFRDEMQKsdwqlIVELKK 1211
Cdd:TIGR00491  550 dvperhAKVLERDLLDSLDEEEKRAFKE-----FLEIKR 583
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
628-841 1.39e-77

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: 252.78  E-value: 1.39e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  628 PIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLeaineqtkmiknfdreNVRIPGMLIIDTPGHESFSN 707
Cdd:cd01887     1 PVVTVMGHVDHGKTTLLDKIRKTNVAAGEAGGITQHIGAYQVPI----------------DVKIPGITFIDTPGHEAFTN 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  708 LRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLYDwkkspdsdvavtlkkqkkntKDEFEERA 787
Cdd:cd01887    65 MRARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYG--------------------TEADPERV 124
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 158635983  788 KAIIVEFAQQGLnaalfyenkDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTM 841
Cdd:cd01887   125 KNELSELGLVGE---------EWGGDVSIVPISAKTGEGIDDLLEAILLLAEVL 169
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
626-1063 2.52e-55

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: 201.01  E-value: 2.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  626 RAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEaineqTKMIknfdrenvripgmLIIDTPGHESF 705
Cdd:COG0532     3 RPPVVTVMGHVDHGKTSLLDAIRKTNVAAGEAGGITQHIGAYQVETN-----GGKI-------------TFLDTPGHEAF 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  706 SNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRlydwkksPDSDVavtlkkqkkntkdefeE 785
Cdd:COG0532    65 TAMRARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDK-------PGANP----------------D 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  786 RAKAiivEFAQQGLNA------ALFyenkdprtfvslVPTSAHTGDGMGSL---IYLLVELtqtmlskrlahcEELRAQ- 855
Cdd:COG0532   122 RVKQ---ELAEHGLVPeewggdTIF------------VPVSAKTGEGIDELlemILLQAEV------------LELKANp 174
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  856 -------VMEVKALPGMGTTIDVILINGRLKEGDTIIVpgveGPIVTQIRGLLlpppmkelrvkNqyEKHKEVEAA---Q 925
Cdd:COG0532   175 drpargtVIEAKLDKGRGPVATVLVQNGTLKVGDIVVA----GTAYGRVRAMF-----------D--DRGKRVKEAgpsT 237
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  926 GVKILGkdlektLAGLP----LLVAYKDD----EIpVLK--DELIHELKQTLNAIKLE------------EKGVYVQAST 983
Cdd:COG0532   238 PVEILG------LSGVPqagdEFVVVEDEkkarEI-AEKrqQKAREKKLARQKRVSLEdlfsqikegevkELNLILKADV 310
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  984 LGSLEAL---LEFLKTSEVpyaGINI-----GPVHKKDVM--KASvmlehdpqYAVILAFDVRIERDAQEMADSLGVRIF 1053
Cdd:COG0532   311 QGSVEALkdsLEKLSTDEV---KVNIihsgvGAITESDVNlaAAS--------NAIIIGFNVRPDAKARKLAEREGVDIR 379
                         490
                  ....*....|
gi 158635983 1054 SAEIIYHLFD 1063
Cdd:COG0532   380 YYSIIYDLID 389
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
626-840 4.39e-41

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: 149.60  E-value: 4.39e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   626 RAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGAT--NVPLEAINEQTKMIKN--FDRENVRIpgmLIIDTPG 701
Cdd:pfam00009    2 RHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEAGldNLPEERERGITIKSAAvsFETKDYLI---NLIDTPG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   702 HESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLYDwkkspdsdvaVTLKKQKKNTKD 781
Cdd:pfam00009   79 HVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDG----------AELEEVVEEVSR 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 158635983   782 EFeerakaiIVEFAQQGLnaalfyenkdprtFVSLVPTSAHTGDGMGSLIYLLVELTQT 840
Cdd:pfam00009  149 EL-------LEKYGEDGE-------------FVPVVPGSALKGEGVQTLLDALDEYLPS 187
 
Name Accession Description Interval E-value
PRK04004 PRK04004
translation initiation factor IF-2; Validated
623-1198 0e+00

translation initiation factor IF-2; Validated


Pssm-ID: 235195 [Multi-domain]  Cd Length: 586  Bit Score: 559.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  623 EKLRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGH 702
Cdd:PRK04004    2 KKLRQPIVVVLGHVDHGKTTLLDKIRGTAVAAKEAGGITQHIGATEVPIDVIEKIAGPLKKPLPIKLKIPGLLFIDTPGH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  703 ESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLYDWKKSPDSDVAVTLKKQKKNTKDE 782
Cdd:PRK04004   82 EAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDRIPGWKSTEDAPFLESIEKQSQRVQQE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  783 FEERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEE--LRAQVMEVK 860
Cdd:PRK04004  162 LEEKLYELIGQLSELGFSADRFDRVKDFTKTVAIVPVSAKTGEGIPDLLMVLAGLAQRYLEERLKIDVEgpGKGTVLEVK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  861 ALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELR-VKNQYEKHKEVEAAQGVKILGKDLEKTLA 939
Cdd:PRK04004  242 EERGLGTTIDVILYDGTLRKGDTIVVGGKDGPIVTKVRALLKPRPLDEMRdPEDKFKPVDEVVAAAGVKISAPDLEDALA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  940 GLPLLVAyKDDEIPVLKDELIHELKQtlNAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASV 1019
Cdd:PRK04004  322 GSPLRVV-RDEDVEEVKEEVEEEIEE--IRIETDEEGVVVKADTLGSLEALVNELREEGIPIRKADVGDISKRDVIEAST 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983 1020 MLEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYK-KQKQEEFKHIaVFPCKMKILPQYIF 1098
Cdd:PRK04004  399 VAEKDPLYGVILAFNVKVLPDAEEEAEKSDVKIFTGDVIYQLIEDYEKWVKEQKeAEKEKILEKI-VRPAKIRILPGYVF 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983 1099 NSRDPIVIGVTVEAGQVKQGTPmcVPSKNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEpipgesPKMFGRHFEATDIL 1178
Cdd:PRK04004  478 RQSDPAIVGVEVLGGTIKPGVP--LIKEDGKRVGTIKQIQDQGENVKEAKAGMEVAISID------GPTVGRQIKEGDIL 549
                         570       580
                  ....*....|....*....|
gi 158635983 1179 VSKISRQSIDALKDWFRDEM 1198
Cdd:PRK04004  550 YVDIPEEHAKILEQELKDEL 569
aIF-2 TIGR00491
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ...
624-1211 4.68e-138

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: 432.32  E-value: 4.68e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   624 KLRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGHE 703
Cdd:TIGR00491    1 RLRQPIVVVLGHVDHGKTTLLDKIRGTAVVKKEAGGITQHIGASEVPTDVIEKICGDLLKSFKIKLKIPGLLFIDTPGHE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   704 SFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLYDWKKSPDSDVAVTLKKQKKNTKDEF 783
Cdd:TIGR00491   81 AFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDRIPGWKSHEGYPFLESINKQEQRVRQNL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   784 EERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEE--LRAQVMEVKA 861
Cdd:TIGR00491  161 DKQVYNLVIQLAEQGFNAERFDRIRDFTKTVAIIPVSAKTGEGIPELLAILAGLAQNYLENKLKLAIEgpAKGTILEVKE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   862 LPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRV-KNQYEKHKEVEAAQGVKILGKDLEKTLAG 940
Cdd:TIGR00491  241 EQGLGYTIDAVIYDGILRKGDIIVLAGIDDVIVTRVRAILKPRPLQEMRLaRKKFAQVDEVYAAAGVKVAAPNLDTVLAG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   941 LPlLVAYKDDEIPVLKDELIHELKQTlnAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASVM 1020
Cdd:TIGR00491  321 SP-IVVENNEEIEKYKEEIQKEVEEI--KIYTDEEGIVVKADTLGSLEALVNELRRRGIPIKKADIGDVSKRDVVEAEIV 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  1021 LEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYKKQKQEEFKHIAVFPCKMKILPQYIFNS 1100
Cdd:TIGR00491  398 KQEAKEYGAIAAFNVKPLPGAEIEAEKYDIKLFSDNIIYQLMENFEKWIEDIEESEKRKTLEAIIKPGKIKIIPGYVFRR 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  1101 RDPIVIGVTVEAGQVKQGTPMCVPSKNFVdiGIVTSIEINHKQVDVAKKGQEVCVKIEPIpgespkMFGRHFEATDIL-- 1178
Cdd:TIGR00491  478 SDPAIVGVEVLGGIIRPGYPLIKKDGRRV--GEVRQIQDNGKNVKRASAGMEVAIAIEDV------VIGRQLEEGDELyv 549
                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 158635983  1179 ------VSKISRQSIDALKDWFRDEMQKsdwqlIVELKK 1211
Cdd:TIGR00491  550 dvperhAKVLERDLLDSLDEEEKRAFKE-----FLEIKR 583
PRK14845 PRK14845
translation initiation factor IF-2; Provisional
641-1212 3.11e-128

translation initiation factor IF-2; Provisional


Pssm-ID: 237833 [Multi-domain]  Cd Length: 1049  Bit Score: 420.06  E-value: 3.11e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  641 TKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGHESFSNLRNRGSSLCDIAI 720
Cdd:PRK14845  475 TTLLDKIRKTRVAKKEAGGITQHIGATEIPIDVIKKICGPLLKLLKAEIKIPGLLFIDTPGHEAFTSLRKRGGSLADLAV 554
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  721 LVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLYDWKKSPDSDVAVTLKKQKKNTKDEFEERAKAIIVEFAQQGLN 800
Cdd:PRK14845  555 LVVDINEGFKPQTIEAINILRQYKTPFVVAANKIDLIPGWNISEDEPFLLNFNEQDQHALTELEIKLYELIGKLYELGFD 634
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  801 AALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLA-HCE-ELRAQVMEVKALPGMGTTIDVILINGRL 878
Cdd:PRK14845  635 ADRFDRVQDFTRTVAIVPVSAKTGEGIPELLMMVAGLAQKYLEERLKlNVEgYAKGTILEVKEEKGLGTTIDAIIYDGTL 714
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  879 KEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRV-KNQYEKHKEVEAAQGVKILGKDLEKTLAGLPLLVAYKDDEIPVLKD 957
Cdd:PRK14845  715 RRGDTIVVGGPDDVIVTKVRALLKPKPLDEIRDpRDKFDPVDEVTAAAGVKIAAPGLEEVLAGSPIRIVPTKEKIEKAKE 794
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  958 ELIHELKQTlnAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASVMLEHDPQYAVILAFDVRI 1037
Cdd:PRK14845  795 EVMKEVEEA--KIETDKEGILIKADTLGSLEALANELRKAGIPIKKAEVGDITKKDVIEALSYKQENPLYGVILGFNVKV 872
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983 1038 ERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYK-KQKQEEFKHIaVFPCKMKILPQYIFNSRDPIVIGVTVEAGQVK 1116
Cdd:PRK14845  873 LPEAQEEAEKYGVKIFVDNIIYKLVEDYTEWVKEEEeKKKRELFEKL-IKPGIIRLLPDCIFRRSNPAIVGVEVLEGTLR 951
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983 1117 QGTPMCVPskNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEPIpgespkMFGRHFEATDILVSKISRQSIDALKDWFRD 1196
Cdd:PRK14845  952 VGVTLIKE--DGMKVGTVRSIKDRGENVKEAKAGKAVAIAIEGA------ILGRHVDEGETLYVDVPESHVRELYHKYMD 1023
                         570
                  ....*....|....*.
gi 158635983 1197 EMQKSDWQLIVELKKV 1212
Cdd:PRK14845 1024 RLRDDEKEALKMYMEL 1039
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
628-841 1.39e-77

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: 252.78  E-value: 1.39e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  628 PIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLeaineqtkmiknfdreNVRIPGMLIIDTPGHESFSN 707
Cdd:cd01887     1 PVVTVMGHVDHGKTTLLDKIRKTNVAAGEAGGITQHIGAYQVPI----------------DVKIPGITFIDTPGHEAFTN 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  708 LRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLYDwkkspdsdvavtlkkqkkntKDEFEERA 787
Cdd:cd01887    65 MRARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYG--------------------TEADPERV 124
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 158635983  788 KAIIVEFAQQGLnaalfyenkDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTM 841
Cdd:cd01887   125 KNELSELGLVGE---------EWGGDVSIVPISAKTGEGIDDLLEAILLLAEVL 169
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
626-1063 2.52e-55

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: 201.01  E-value: 2.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  626 RAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEaineqTKMIknfdrenvripgmLIIDTPGHESF 705
Cdd:COG0532     3 RPPVVTVMGHVDHGKTSLLDAIRKTNVAAGEAGGITQHIGAYQVETN-----GGKI-------------TFLDTPGHEAF 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  706 SNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRlydwkksPDSDVavtlkkqkkntkdefeE 785
Cdd:COG0532    65 TAMRARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDK-------PGANP----------------D 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  786 RAKAiivEFAQQGLNA------ALFyenkdprtfvslVPTSAHTGDGMGSL---IYLLVELtqtmlskrlahcEELRAQ- 855
Cdd:COG0532   122 RVKQ---ELAEHGLVPeewggdTIF------------VPVSAKTGEGIDELlemILLQAEV------------LELKANp 174
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  856 -------VMEVKALPGMGTTIDVILINGRLKEGDTIIVpgveGPIVTQIRGLLlpppmkelrvkNqyEKHKEVEAA---Q 925
Cdd:COG0532   175 drpargtVIEAKLDKGRGPVATVLVQNGTLKVGDIVVA----GTAYGRVRAMF-----------D--DRGKRVKEAgpsT 237
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  926 GVKILGkdlektLAGLP----LLVAYKDD----EIpVLK--DELIHELKQTLNAIKLE------------EKGVYVQAST 983
Cdd:COG0532   238 PVEILG------LSGVPqagdEFVVVEDEkkarEI-AEKrqQKAREKKLARQKRVSLEdlfsqikegevkELNLILKADV 310
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  984 LGSLEAL---LEFLKTSEVpyaGINI-----GPVHKKDVM--KASvmlehdpqYAVILAFDVRIERDAQEMADSLGVRIF 1053
Cdd:COG0532   311 QGSVEALkdsLEKLSTDEV---KVNIihsgvGAITESDVNlaAAS--------NAIIIGFNVRPDAKARKLAEREGVDIR 379
                         490
                  ....*....|
gi 158635983 1054 SAEIIYHLFD 1063
Cdd:COG0532   380 YYSIIYDLID 389
aeIF5B_II cd03703
Domain II of archaeal and eukaryotic Initiation Factor 5; This family represents domain II of ...
851-961 5.96e-50

Domain II of archaeal and eukaryotic Initiation Factor 5; This family represents domain II of archaeal and eukaryotic IF5B. aIF5B and eIF5B are homologs of prokaryotic Initiation Factor 2 (IF2). Disruption of the eIF5B gene (FUN12) in yeast causes a severe slow-growth phenotype, associated with a defect in translation. eIF5B has a function analogous to prokaryotic IF2 in mediating the joining of joining of 60S subunits. The eIF5B consists of three N-terminal domains (I, II, II) connected by a long helix to domain IV. Domain I is a G domain, domain II and IV are beta-barrels and domain III has a novel alpha-beta-alpha sandwich fold. The G domain and the beta-barrel domain II display a similar structure and arrangement to the homologous domains of EF1A, eEF1A and aeIF2gamma.


Pssm-ID: 293904 [Multi-domain]  Cd Length: 111  Bit Score: 171.95  E-value: 5.96e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  851 ELRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRVKNQYEKHKEVEAAQGVKIL 930
Cdd:cd03703     1 PGKGTVLEVKEEEGLGTTIDVILYDGTLREGDTIVVGGLNGPIVTKVRALLKPKPLKEMRVKSRFIHVKEVVAAAGVKIA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 158635983  931 GKDLEKTLAGLPLLVAYKDDEIPVLKDELIH 961
Cdd:cd03703    81 APDLEKAIAGSPLRVVGNEDEIEELIEEVME 111
IF2_IF5B_II cd03701
Domain II of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; ...
851-946 9.80e-44

Domain II of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; This family represents domain II of prokaryotic Initiation Factor 2 (IF2) and its archaeal and eukaryotic homologue aeIF5B. IF2, the largest initiation factor, is an essential GTP binding protein. In E. coli, three natural forms of IF2 exist in the cell, IF2alpha, IF2beta1, and IF2beta2. Disruption of the eIF5B gene (FUN12) in yeast causes a severe slow-growth phenotype, associated with a defect in translation. eIF5B has a function analogous to prokaryotic IF2 in mediating the joining of the 60S ribosomal subunit. The eIF5B consists of three N-terminal domains (I, II, II) connected by a long helix to domain IV. Domain I is a G domain, domain II and IV are beta-barrels and domain III has a novel alpha-beta-alpha sandwich fold. The G domain and the beta-barrel domain II display a similar structure and arrangement to the homologous domains in EF1A, eEF1A and aeIF2gamma.


Pssm-ID: 293902 [Multi-domain]  Cd Length: 96  Bit Score: 153.59  E-value: 9.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  851 ELRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRVKNQYEKHKEVEAAQGVKIL 930
Cdd:cd03701     1 EPRGVILEVKLDKGAGITIDMLVQEGTLRVGDTIVAGESKDVIYTRIRALLDPDPLEEMESRKKGNKRKEVGAASGVKIL 80
                          90
                  ....*....|....*.
gi 158635983  931 GKDLEKTLAGLPLLVA 946
Cdd:cd03701    81 GFGQELPHAGDPLEVV 96
IF-2 TIGR00487
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ...
626-1063 3.90e-43

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: 166.87  E-value: 3.90e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   626 RAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVpleaINEQTKMIKnfdrenvripgmlIIDTPGHESF 705
Cdd:TIGR00487   86 RPPVVTIMGHVDHGKTSLLDSIRKTKVAQGEAGGITQHIGAYHV----ENEDGKMIT-------------FLDTPGHEAF 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   706 SNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRlydwkksPDSDvavtlkkqkkntkdefee 785
Cdd:TIGR00487  149 TSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDK-------PEAN------------------ 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   786 rAKAIIVEFAQQGLNAALFYENkdprtfVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHcEELRAQVMEVKALPGM 865
Cdd:TIGR00487  204 -PDRVKQELSEYGLVPEDWGGD------TIFVPVSALTGDGIDELLDMILLQSEVEELKANPN-GQASGVVIEAQLDKGR 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   866 GTTIDVILINGRLKEGDTIIVpgveGPIVTQIRGLllpppmkelrVKNQYEKHKEVEAAQGVKILGKDlEKTLAGLPLLV 945
Cdd:TIGR00487  276 GPVATVLVQSGTLRVGDIVVV----GAAYGRVRAM----------IDENGKSVKEAGPSKPVEILGLS-DVPAAGDEFIV 340
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   946 aYKDDEIPVL----------KDELIHELKQTLNAIK-------LEEKGVYVQASTLGSLEAL---LEFLKTSEVPYAGIN 1005
Cdd:TIGR00487  341 -FKDEKDARLvaekragklrQKALSRSVKVTLDNLFeqikegeLKELNIILKADVQGSLEAIknsLEKLNNEEVKVKVIH 419
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  1006 --IGPVHKKDVMKASVmlehdpQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFD 1063
Cdd:TIGR00487  420 sgVGGITETDISLASA------SNAIIIGFNVRPDATAKNVAEAENVDIRYYSVIYKLID 473
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
626-840 4.39e-41

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: 149.60  E-value: 4.39e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   626 RAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGAT--NVPLEAINEQTKMIKN--FDRENVRIpgmLIIDTPG 701
Cdd:pfam00009    2 RHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEAGldNLPEERERGITIKSAAvsFETKDYLI---NLIDTPG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   702 HESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLYDwkkspdsdvaVTLKKQKKNTKD 781
Cdd:pfam00009   79 HVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDG----------AELEEVVEEVSR 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 158635983   782 EFeerakaiIVEFAQQGLnaalfyenkdprtFVSLVPTSAHTGDGMGSLIYLLVELTQT 840
Cdd:pfam00009  149 EL-------LEKYGEDGE-------------FVPVVPGSALKGEGVQTLLDALDEYLPS 187
infB CHL00189
translation initiation factor 2; Provisional
619-1152 7.10e-40

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 159.23  E-value: 7.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  619 NVNTEKlRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIknfdrenvripgmlIID 698
Cdd:CHL00189  237 TENSIN-RPPIVTILGHVDHGKTTLLDKIRKTQIAQKEAGGITQKIGAYEVEFEYKDENQKIV--------------FLD 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  699 TPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDrlydwkkspdsdvavtlkKQKKN 778
Cdd:CHL00189  302 TPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKID------------------KANAN 363
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  779 TkdefeERAKaiivefaQQGLNAALFYENKDPRTfvSLVPTSAHTGDGMGSLIYLLVELTQtMLSKRLAHCEELRAQVME 858
Cdd:CHL00189  364 T-----ERIK-------QQLAKYNLIPEKWGGDT--PMIPISASQGTNIDKLLETILLLAE-IEDLKADPTQLAQGIILE 428
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  859 VKALPGMGTTIDVILINGRLKEGDTIivpgVEGPIVTQIRGLllpppmkelrVKNQYEKHKEVEAAQGVKILGkdLEKTL 938
Cdd:CHL00189  429 AHLDKTKGPVATILVQNGTLHIGDII----VIGTSYAKIRGM----------INSLGNKINLATPSSVVEIWG--LSSVP 492
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  939 AGLPLLVAYKDDEIPVLKDELIHE--LKQTLNAIKLEEKGVY------------VQASTLGSLEALLEFLKTSEVPYAGI 1004
Cdd:CHL00189  493 ATGEHFQVFNSEKEAKLKIIKNKEnnKKDTTKRITLSTTKTInkkdnkkqinliIKTDTQGSIEAIINSISQIPQKKVQL 572
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983 1005 NI-----GPVHKKDVMKASVmlehdpQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQD-----YKK 1074
Cdd:CHL00189  573 NIlyaslGEVTETDVEFAST------TNAEILAFNTNLAPGAKKAARKLNIIIKEYQVIYDLLEYIEALMEDlldpeYKK 646
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158635983 1075 QKQEEFKHIAVFPckmkilpqyIFNSRdpiVIGVTVEAGQVKQGTPMCVPSKN-FVDIGIVTSIEINHKQVDVAKKGQE 1152
Cdd:CHL00189  647 VPIGEAEVKTVFP---------LAKRF---VAGCRVTEGKITKNALIKVIRENkLIYEGKITSLKRVKEDVEEAQEGNE 713
IF2_aeIF5B_IV cd16266
Domain IV of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; ...
1088-1182 7.14e-37

Domain IV of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; This family represents the domain IV of prokaryotic Initiation Factor 2 (IF2) and its archaeal and eukaryotic homologs IF5B. IF2, the largest initiation factor is an essential GTP binding protein. In E. coli three natural forms of IF2 exist in the cell, IF2alpha, IF2beta1, and IF2beta2. Disruption of the eIF5B gene (FUN12) in yeast causes a severe slow-growth phenotype, associated with a defect in translation. eIF5B has a function analogous to prokaryotic IF2 in mediating the joining of the 60S ribosomal subunit. The eIF5B consists of three N-terminal domains (I, II, II) connected by a long helix to domain IV. Domain I is a G domain, domain II and IV are beta-barrels and domain III has a novel alpha-beta-alpha sandwich fold. The G domain and the beta-barrel domain II display a similar structure and arrangement to the homologous domains in EF1A, eEF1A and aeIF2gamma.


Pssm-ID: 293911 [Multi-domain]  Cd Length: 87  Bit Score: 133.83  E-value: 7.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983 1088 CKMKILPQYIFNSRDPIVIGVTVEAGQVKQGTPMCVPskNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEPIPgespkm 1167
Cdd:cd16266     1 AKIRILPGCVFRQSKPAIVGVEVLEGTLKPGVPLIVP--DGKDVGRVKSIQDNGENVKEAKKGQEVAVSIEGPT------ 72
                          90
                  ....*....|....*
gi 158635983 1168 FGRHFEATDILVSKI 1182
Cdd:cd16266    73 VGRHIEEGDILYVDI 87
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
629-837 8.67e-25

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: 102.76  E-value: 8.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  629 IICVLGHVDTGKTKILDKLRH---------------THVQDGE-AGGITQQIGATNVPLEaineqtkmiknfdreNVRIp 692
Cdd:cd00881     1 NVGVIGHVDHGKTTLTGSLLYqtgaidrrgtrketfLDTLKEErERGITIKTGVVEFEWP---------------KRRI- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  693 gmLIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLydwkksPDSDVAVTL 772
Cdd:cd00881    65 --NFIDTPGHEDFSKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRV------GEEDFDEVL 136
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158635983  773 KkqkkntkdEFEERAKAIIVEFaqqglnaalfyenkDPRTFVSLVPTSAHTGDGMGSLIYLLVEL 837
Cdd:cd00881   137 R--------EIKELLKLIGFTF--------------LKGKDVPIIPISALTGEGIEELLDAIVEH 179
IF-2 pfam11987
Translation-initiation factor 2; IF-2 is a translation initiator in each of the three main ...
962-1063 1.24e-20

Translation-initiation factor 2; IF-2 is a translation initiator in each of the three main phylogenetic domains (Eukaryotes, Bacteria and Archaea). IF2 interacts with formylmethionine-tRNA, GTP, IF1, IF3 and both ribosomal subunits. Through these interactions, IF2 promotes the binding of the initiator tRNA to the A site in the smaller ribosomal subunit and catalyzes the hydrolysis of GTP following initiation-complex formation.


Pssm-ID: 463421 [Multi-domain]  Cd Length: 116  Bit Score: 88.27  E-value: 1.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   962 ELKQTLNAIKLEEK--GVYVQASTLGSLEALLEFLKTSEVPYAGINI-----GPVHKKDVMKASvmlehdPQYAVILAFD 1034
Cdd:pfam11987   11 SLEDLFSQIKEEVKelNLIIKADVQGSLEALKESLEKLSNDEVKVNIihsgvGAITESDVMLAS------ASNAIIIGFN 84
                           90       100
                   ....*....|....*....|....*....
gi 158635983  1035 VRIERDAQEMADSLGVRIFSAEIIYHLFD 1063
Cdd:pfam11987   85 VRPDAKARKLAEKEGVDIRYYNIIYDLID 113
GTP_EFTU_D4 pfam14578
Elongation factor Tu domain 4; Elongation factor Tu consists of several structural domains, ...
1087-1178 4.13e-17

Elongation factor Tu domain 4; Elongation factor Tu consists of several structural domains, and this is usually the fourth.


Pssm-ID: 405293 [Multi-domain]  Cd Length: 86  Bit Score: 77.29  E-value: 4.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  1087 PCKMKILPQYIFNSRDPIVIGVTVEAGQVKQGTPMCVPSKNfvDIGIVTSIEINHKQVDVAKKGQEVCVKIepipgESPK 1166
Cdd:pfam14578    1 PGKIRILPGYVFRRSDPAIVGVEVLGGIIKPGYPLIREDGR--EVGEIMQIQDNGKSLDEAKAGQEVAISI-----EGKI 73
                           90
                   ....*....|..
gi 158635983  1167 MFGRHFEATDIL 1178
Cdd:pfam14578   74 MVGRQIKEGDIL 85
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
629-978 2.28e-15

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: 80.69  E-value: 2.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   629 IICVLGHVDTGKTKILDKLRHT---HVQDGEAGGITQQIGATNVPLEAineqtkmiknfdrenvRIPGmlIIDTPGHESF 705
Cdd:TIGR00475    2 IIATAGHVDHGKTTLLKALTGIaadRLPEEKKRGMTIDLGFAYFPLPD----------------YRLG--FIDVPGHEKF 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   706 snLRNRGSSLCDI--AILVVDIMHGLEPQTIESINILKSKKCPF-IVALNKIDRLYdwkkspdsdvavtlkkqkkntkde 782
Cdd:TIGR00475   64 --ISNAIAGGGGIdaALLVVDADEGVMTQTGEHLAVLDLLGIPHtIVVITKADRVN------------------------ 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   783 fEERAKaIIVEFAQQGLNAALFYENkdprtfVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHceELRAQVMEVKAL 862
Cdd:TIGR00475  118 -EEEIK-RTEMFMKQILNSYIFLKN------AKIFKTSAKTGQGIGELKKELKNLLESLDIKRIQK--PLRMAIDRAFKV 187
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   863 PGMGTTIDVILINGRLKEGDTIIVPGVEgpivtqirglllpppmKELRVKNQYEKHKEVEAAQ-----GVKILGKDLEKT 937
Cdd:TIGR00475  188 KGAGTVVTGTAFSGEVKVGDNLRLLPIN----------------HEVRVKAIQAQNQDVEIAYagqriALNLMDVEPESL 251
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 158635983   938 LAGLPLLVA--YKDDEIPVLKDE----------LIHELKQTLNAIKLEEKGVY 978
Cdd:TIGR00475  252 KRGLLILTPedPKLRVVVKFIAEvpllelqpyhIAHGMSVTTGKISLLDKGIA 304
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
629-925 5.80e-13

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: 73.41  E-value: 5.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  629 IICVLGHVDTGKT---KIL-----DKL-----RhthvqdgeagGITQQIGATNVPLEaineqtkmiknfdreNVRIPGml 695
Cdd:COG3276     2 IIGTAGHIDHGKTtlvKALtgidtDRLkeekkR----------GITIDLGFAYLPLP---------------DGRRLG-- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  696 IIDTPGHESFsnLRN--RGSSLCDIAILVVD----IMhglePQTIESINILKS---KKCpfIVALNKIDRlydwkkspds 766
Cdd:COG3276    55 FVDVPGHEKF--IKNmlAGAGGIDLVLLVVAadegVM----PQTREHLAILDLlgiKRG--IVVLTKADL---------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  767 dvaVTlkkqkkntkDEFEERAKAIIVEFAqqglnAALFYENKDprtfvsLVPTSAHTGDGMGSLIYLLVELTQTMLSKRL 846
Cdd:COG3276   117 ---VD---------EEWLELVEEEIRELL-----AGTFLEDAP------IVPVSAVTGEGIDELRAALDALAAAVPARDA 173
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  847 AHCeeLRAQVMEVKALPGMGTtidVI---LINGRLKEGDTiivpgvegpivtqirgLLLPPPMKELRVKN---QYEKHKE 920
Cdd:COG3276   174 DGP--FRLPIDRVFSIKGFGT---VVtgtLLSGTVRVGDE----------------LELLPSGKPVRVRGiqvHGQPVEE 232

                  ....*
gi 158635983  921 VEAAQ 925
Cdd:COG3276   233 AYAGQ 237
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
630-784 9.84e-13

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: 68.16  E-value: 9.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  630 ICVLGHVDTGKTKI------------LDKLRHTHVQdgeagGITQQIG--ATNVPLEAINEQTKmikNFDRENVRIPgml 695
Cdd:cd01889     3 VGLLGHVDSGKTSLakalseiastaaFDKNPQSQER-----GITLDLGfsSFEVDKPKHLEDNE---NPQIENYQIT--- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  696 IIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLydwkksPDSDVAVTLKKQ 775
Cdd:cd01889    72 LVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLI------PEEERKRKIEKM 145

                  ....*....
gi 158635983  776 KKNTKDEFE 784
Cdd:cd01889   146 KKRLQKTLE 154
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
629-837 2.59e-12

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: 66.47  E-value: 2.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  629 IICVLGHVDTGKTKILDKLRHT---HVQDGEAGGITQQIGATNVPLEaineqtkmiknfdreNVRIPGmlIIDTPGHESF 705
Cdd:cd04171     1 IIGTAGHIDHGKTTLIKALTGIetdRLPEEKKRGITIDLGFAYLDLP---------------DGKRLG--FIDVPGHEKF 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  706 snLRNRGSSLC--DIAILVVDIMHGLEPQTIESINILKS---KKCpfIVALNKIDRLydwkkspdsdvavtlkkqkkntK 780
Cdd:cd04171    64 --VKNMLAGAGgiDAVLLVVAADEGIMPQTREHLEILELlgiKKG--LVVLTKADLV----------------------D 117
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 158635983  781 DEFEERAKAIIVEFAqqglnAALFYENkdprtfVSLVPTSAHTGDGMGSLIYLLVEL 837
Cdd:cd04171   118 EDRLELVEEEILELL-----AGTFLAD------APIFPVSSVTGEGIEELKNYLDEL 163
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
630-835 6.05e-12

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: 65.09  E-value: 6.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   630 ICVLGHVDTGKTKILDKLRHTHVQDGEAG-GITQQIGATnvpLEAINEQTKMIKnfdrenvripgmlIIDTPGHESFSNL 708
Cdd:TIGR00231    4 IVIVGHPNVGKSTLLNSLLGNKGSITEYYpGTTRNYVTT---VIEEDGKTYKFN-------------LLDTAGQEDYDAI 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   709 R-------NRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKcPFIVALNKIDRlydwkksPDSDVavtlkkqKKNTKD 781
Cdd:TIGR00231   68 RrlyypqvERSLRVFDIVILVLDVEEILEKQTKEIIHHADSGV-PIILVGNKIDL-------KDADL-------KTHVAS 132
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 158635983   782 EFEERAKAIIvefaqqglnaalfyenkdprtfvslVPTSAHTGDGMGSLIYLLV 835
Cdd:TIGR00231  133 EFAKLNGEPI-------------------------IPLSAETGKNIDSAFKIVE 161
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
1088-1179 3.19e-11

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: 60.36  E-value: 3.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983 1088 CKMKIlpQYIFNSR-DPIVIGVTVEAGQVKQGTPMCVPSKNfvDIGIVTSIEINHKQVDVAKKGQEVCVKIEPIpgespk 1166
Cdd:cd01342     1 LVMQV--FKVFYIPgRGRVAGGRVESGTLKVGDEIRILPKG--ITGRVTSIERFHEEVDEAKAGDIVGIGILGV------ 70
                          90
                  ....*....|...
gi 158635983 1167 mfgRHFEATDILV 1179
Cdd:cd01342    71 ---KDILTGDTLT 80
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
630-757 6.70e-11

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: 63.40  E-value: 6.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  630 ICVLGHVDTGKTKILD---------------KLRHT-HVQDGEAGGITqqIGATNVPLEAINEQTKMIKNfdrenvripG 693
Cdd:cd01885     3 ICIIAHVDHGKTTLSDsllasagiiseklagKARYLdTREDEQERGIT--IKSSAISLYFEYEEEKMDGN---------D 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158635983  694 MLI--IDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTiESI--NILKSKKCPFIVaLNKIDRL 757
Cdd:cd01885    72 YLInlIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT-ETVlrQALEERVKPVLV-INKIDRL 137
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
630-757 1.86e-09

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: 59.20  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  630 ICVLGHVDTGKTKILDKLRH-THVQDGEAGGITQQIGATN--------------VPLEAINEQTKmiknfDRENVripgM 694
Cdd:cd04167     3 VCIAGHLHHGKTSLLDMLIEqTHKRTPSVKLGWKPLRYTDtrkdeqergisiksNPISLVLEDSK-----GKSYL----I 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158635983  695 LIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRL 757
Cdd:cd04167    74 NIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDRL 136
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
630-756 2.12e-09

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: 58.37  E-value: 2.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  630 ICVLGHVDTGKTKILDK-LRHTHVQDgEAGGITQQIGATNvPLEAINEQTKMIKN--FDRENVRIPgmlIIDTPGHESFS 706
Cdd:cd01891     5 IAIIAHVDHGKTTLVDAlLKQSGTFR-ENEEVGERVMDSN-DLERERGITILAKNtaITYKDTKIN---IIDTPGHADFG 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 158635983  707 NLRNRGSSLCDIAILVVDIMHGLEPQTiesINILK---SKKCPFIVALNKIDR 756
Cdd:cd01891    80 GEVERVLSMVDGVLLLVDASEGPMPQT---RFVLKkalEAGLKPIVVINKIDR 129
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
629-936 2.81e-09

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 61.22  E-value: 2.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  629 IICVLGHVDTGKTKILDKL---RHTHVQDGEAGGITQQIGATNVPleaineqtkmiknfdRENVRIPGMliIDTPGHESF 705
Cdd:PRK10512    2 IIATAGHVDHGKTTLLQAItgvNADRLPEEKKRGMTIDLGYAYWP---------------QPDGRVLGF--IDVPGHEKF 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  706 -SNLRNrGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFI-VALNKIDRLydwkkspDSDVAVTLKKQkkntkdef 783
Cdd:PRK10512   65 lSNMLA-GVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLtVALTKADRV-------DEARIAEVRRQ-------- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  784 eerakaIIVEFAQQGLNAAlfyenkdprtfvSLVPTSAHTGDGMGSLIYLLVELTQT--MLSKRlahceeLRAQVMEVKA 861
Cdd:PRK10512  129 ------VKAVLREYGFAEA------------KLFVTAATEGRGIDALREHLLQLPERehAAQHR------FRLAIDRAFT 184
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158635983  862 LPGMGTTIDVILINGRLKEGDTIIVPGVEGPIvtQIRGlllpppmkeLRVKNQyekhkEVEAAQ-GVKI---LGKDLEK 936
Cdd:PRK10512  185 VKGAGLVVTGTALSGEVKVGDTLWLTGVNKPM--RVRG---------LHAQNQ-----PTEQAQaGQRIalnIAGDAEK 247
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
630-836 4.49e-09

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 57.30  E-value: 4.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  630 ICVLGHVDTGKTKILDKLRHTHVQDGEAGGItqqIGATnvpleaineQTKMIKNFDRENVRIpgmLIIDTPG-------H 702
Cdd:COG1100     6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLST---NGVT---------IDKKELKLDGLDVDL---VIWDTPGqdefretR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  703 ESF-SNLRNRgsslcDIAILVVDimhGLEPQTIESINIL------KSKKCPFIVALNKIDRLYDWKKSPDSDVAVTLKKQ 775
Cdd:COG1100    71 QFYaRQLTGA-----SLYLFVVD---GTREETLQSLYELleslrrLGKKSPIILVLNKIDLYDEEEIEDEERLKEALSED 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158635983  776 KkntkdefeerakaiivefaqqglnaalfyenkdprtFVSLVPTSAHTGDGMGSLIYLLVE 836
Cdd:COG1100   143 N------------------------------------IVEVVATSAKTGEGVEELFAALAE 167
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
631-757 1.06e-08

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: 55.54  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  631 CVLGHVDTGKTKILDKLrhthvqdgeaggitqqIGATNVPLEAINEQTKMIknfDRENVRIP----GMLIIDTPGHESFS 706
Cdd:cd00882     1 VVVGRGGVGKSSLLNAL----------------LGGEVGEVSDVPGTTRDP---DVYVKELDkgkvKLVLVDTPGLDEFG 61
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 158635983  707 NLRNRGSSL-----CDIAILVVDIMHG--LEPQTIESINILKSKKCPFIVALNKIDRL 757
Cdd:cd00882    62 GLGREELARlllrgADLILLVVDSTDResEEDAKLLILRRLRKEGIPIILVGNKIDLL 119
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
696-756 1.14e-08

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: 57.61  E-value: 1.14e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158635983  696 IIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDR 756
Cdd:cd04169    75 LLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDR 135
PRK13351 PRK13351
elongation factor G-like protein;
630-756 2.01e-08

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 58.81  E-value: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  630 ICVLGHVDTGKTKILDKLRH----TH----VQDGEA----------GGITQQIGATNVpleaineqtkmiknfDRENVRI 691
Cdd:PRK13351   11 IGILAHIDAGKTTLTERILFytgkIHkmgeVEDGTTvtdwmpqeqeRGITIESAATSC---------------DWDNHRI 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158635983  692 PgmlIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDR 756
Cdd:PRK13351   76 N---LIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDR 137
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
631-755 3.13e-08

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: 54.85  E-value: 3.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  631 CVLGHVDTGKTKILDK-LRHTHVQDGEAG--------------GITqqIGATNVPLeaineqtkMIKNFDRENVRIPgml 695
Cdd:cd01890     4 SIIAHIDHGKSTLADRlLELTGTVSEREMkeqvldsmdlererGIT--IKAQAVRL--------FYKAKDGEEYLLN--- 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  696 IIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKID 755
Cdd:cd01890    71 LIDTPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKID 130
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
696-762 6.20e-08

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: 54.50  E-value: 6.20e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158635983  696 IIDTPGHESFsnLRN--RGSSLCDIAILVVDIMHGLEPQT-----IESinILKSKKcpFIVALNKIDrLYDWKK 762
Cdd:cd04166    82 IADTPGHEQY--TRNmvTGASTADLAILLVDARKGVLEQTrrhsyIAS--LLGIRH--VVVAVNKMD-LVDYDE 148
TypA_BipA TIGR01394
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ...
630-756 6.62e-08

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: 56.93  E-value: 6.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   630 ICVLGHVDTGKTKILDK-LRHTHVQDgEAGGITQQIGATNvPLEAINEQTKMIKN--FDRENVRIPgmlIIDTPGHESFS 706
Cdd:TIGR01394    4 IAIIAHVDHGKTTLVDAlLKQSGTFR-ANEAVAERVMDSN-DLERERGITILAKNtaIRYNGTKIN---IVDTPGHADFG 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 158635983   707 NLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDR 756
Cdd:TIGR01394   79 GEVERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDR 128
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
695-886 4.49e-07

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: 53.53  E-value: 4.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   695 LIIDTPGHESFSnlRN--RGSSLCDIAILVVDIMHGLEPQT-----IESINILKSkkcpFIVALNKIDrLYDWKkspdsd 767
Cdd:TIGR02034   83 IVADTPGHEQYT--RNmaTGASTADLAVLLVDARKGVLEQTrrhsyIASLLGIRH----VVLAVNKMD-LVDYD------ 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   768 vavtlkkqkkntkdefEERAKAIIVEFAQqglnaalFYENKDPRTfVSLVPTSAHTGDGMGSLIYL--------LVELTQ 839
Cdd:TIGR02034  150 ----------------EEVFENIKKDYLA-------FAEQLGFRD-VTFIPLSALKGDNVVSRSESmpwysgptLLEILE 205
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 158635983   840 TMLSKRLAHCEELRAQVMEVKAlPGM------GTtidviLINGRLKEGDTIIV 886
Cdd:TIGR02034  206 TVEVERDAQDLPLRFPVQYVNR-PNLdfrgyaGT-----IASGSVHVGDEVVV 252
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
630-757 5.97e-07

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: 51.85  E-value: 5.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  630 ICVLGHVDTGKTKILDKLRHTHvqdgeagGITQQIGAT--------NVPLE---AINEQTKMIKnFDRENVRIPgmlIID 698
Cdd:cd04168     2 IGILAHVDAGKTTLTESLLYTS-------GAIRELGSVdkgttrtdSMELErqrGITIFSAVAS-FQWEDTKVN---IID 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 158635983  699 TPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRL 757
Cdd:cd04168    71 TPGHMDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRA 129
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
696-760 1.42e-06

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: 52.01  E-value: 1.42e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158635983  696 IIDTPGHESFsnLRN--RGSSLCDIAILVVDIMHGLEPQT-----IESinILKSKKcpFIVALNKIDrLYDW 760
Cdd:COG2895    99 IADTPGHEQY--TRNmvTGASTADLAILLIDARKGVLEQTrrhsyIAS--LLGIRH--VVVAVNKMD-LVDY 163
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
694-753 2.21e-06

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 47.61  E-value: 2.21e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158635983   694 MLIIDTPGH-ESFSNLRNRGSSL-----CDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNK 753
Cdd:pfam01926   48 IILVDTPGLiEGASEGEGLGRAFlaiieADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
697-759 2.34e-06

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 49.00  E-value: 2.34e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158635983  697 IDTPG-HESFSNLRNR-----GSSL--CDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLYD 759
Cdd:cd04163    56 VDTPGiHKPKKKLGERmvkaaWSALkdVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLVKD 126
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
696-755 4.10e-06

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 50.68  E-value: 4.10e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158635983  696 IIDTPGHESFSnlRN--RGSSLCDIAILVVDIMHGLEPQT-----IESINILKSkkcpFIVALNKID 755
Cdd:PRK05124  111 IADTPGHEQYT--RNmaTGASTCDLAILLIDARKGVLDQTrrhsfIATLLGIKH----LVVAVNKMD 171
PRK10218 PRK10218
translational GTPase TypA;
623-756 4.27e-06

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 50.86  E-value: 4.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  623 EKLRApiICVLGHVDTGKTKILDKLRHthvQDG--EAGGITQQIGATNVPLEAINEQTKMIKN--FDRENVRIPgmlIID 698
Cdd:PRK10218    3 EKLRN--IAIIAHVDHGKTTLVDKLLQ---QSGtfDSRAETQERVMDSNDLEKERGITILAKNtaIKWNDYRIN---IVD 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 158635983  699 TPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDR 756
Cdd:PRK10218   75 TPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDR 132
prfC TIGR00503
peptide chain release factor 3; This translation releasing factor, RF-3 (prfC) was originally ...
632-756 4.66e-06

peptide chain release factor 3; This translation releasing factor, RF-3 (prfC) was originally described as stop codon-independent, in contrast to peptide chain release factor 1 (RF-1, prfA) and RF-2 (prfB). RF-1 and RF-2 are closely related to each other, while RF-3 is similar to elongation factors EF-Tu and EF-G; RF-1 is active at UAA and UAG and RF-2 is active at UAA and UGA. More recently, RF-3 was shown to be active primarily at UGA stop codons in E. coli. All bacteria and organelles have RF-1. The Mycoplasmas and organelles, which translate UGA as Trp rather than as a stop codon, lack RF-2. RF-3, in contrast, seems to be rare among bacteria and is found so far only in Escherichia coli and some other gamma subdivision Proteobacteria, in Synechocystis PCC6803, and in Staphylococcus aureus. [Protein synthesis, Translation factors]


Pssm-ID: 129594 [Multi-domain]  Cd Length: 527  Bit Score: 50.67  E-value: 4.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   632 VLGHVDTGKTKILDKLRHTHVQDGEAGGIT---QQIGATNVPLEAINEQ----TKMIKNFDRENVRIPgmlIIDTPGHES 704
Cdd:TIGR00503   16 IISHPDAGKTTITEKVLLYGGAIQTAGAVKgrgSQRHAKSDWMEMEKQRgisiTTSVMQFPYRDCLVN---LLDTPGHED 92
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 158635983   705 FSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDR 756
Cdd:TIGR00503   93 FSEDTYRTLTAVDNCLMVIDAAKGVETRTRKLMEVTRLRDTPIFTFMNKLDR 144
era PRK00089
GTPase Era; Reviewed
697-762 5.15e-06

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 49.66  E-value: 5.15e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158635983  697 IDTPG-HESFSNLrNRG------SSL--CDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLYDWKK 762
Cdd:PRK00089   58 VDTPGiHKPKRAL-NRAmnkaawSSLkdVDLVLFVVDADEKIGPGDEFILEKLKKVKTPVILVLNKIDLVKDKEE 131
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
692-838 5.25e-06

YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 47.89  E-value: 5.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  692 PGMLIIDTPG----------HESFSN-----LRNRgSSLCdIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDR 756
Cdd:cd01876    45 DKFRLVDLPGygyakvskevREKWGKlieeyLENR-ENLK-GVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADK 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  757 LydwKKSPdsdvavtLKKQKKNTKDEFEERAkaiivefaqqglnaalfyenkdprTFVSLVPTSAHTGDGMGSLIYLLVE 836
Cdd:cd01876   123 L---KKSE-------LAKVLKKIKEELNLFN------------------------ILPPVILFSSKKGTGIDELRALIAE 168

                  ..
gi 158635983  837 LT 838
Cdd:cd01876   169 WL 170
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
708-837 5.87e-06

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 48.14  E-value: 5.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  708 LRNRgSSLCdIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLydwKKSPdsdvavtLKKQKKNTKDEFEERA 787
Cdd:COG0218   100 LEGR-ENLK-GVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKL---KKSE-------LAKQLKAIKKALGKDP 167
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 158635983  788 KAiivefaqqglnaalfyenkdprtfVSLVPTSAHTGDGMGSLIYLLVEL 837
Cdd:COG0218   168 AA------------------------PEVILFSSLKKEGIDELRAAIEEW 193
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
696-891 8.61e-06

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: 49.55  E-value: 8.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  696 IIDTPGHESFsnLRN--RGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCP-FIVALNKIDRL-YDWKKspdsdvavt 771
Cdd:COG5256    89 IIDAPGHRDF--VKNmiTGASQADAAILVVSAKDGVMGQTREHAFLARTLGINqLIVAVNKMDAVnYSEKR--------- 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  772 lkkqkkntkdeFEErAKAIIVEFAQQglnaaLFYENKDprtfVSLVPTSAHTGDGmgsliylLVELTQTM-------LSK 844
Cdd:COG5256   158 -----------YEE-VKEEVSKLLKM-----VGYKVDK----IPFIPVSAWKGDN-------VVKKSDNMpwyngptLLE 209
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 158635983  845 RLAHCEE--------LRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIV--PGVEG 891
Cdd:COG5256   210 ALDNLKEpekpvdkpLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFmpAGVVG 266
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
694-837 2.74e-05

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 47.29  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  694 MLIIDTPG-HESfSNLRNRG------SSL--CDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRLydwkksp 764
Cdd:COG1159    53 IVFVDTPGiHKP-KRKLGRRmnkaawSALedVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLV------- 124
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158635983  765 dsdvavtlkkqkknTKDEFEERAKAiivefaqqglnaalfYENKDPrtFVSLVPTSAHTGDGMGSLIYLLVEL 837
Cdd:COG1159   125 --------------KKEELLPLLAE---------------YSELLD--FAEIVPISALKGDNVDELLDEIAKL 166
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
629-900 5.15e-05

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 47.15  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  629 IICVLGHVDTGKTKILDKL------RHTHvqdgEAG-GITQQIGATNVPL------------------EAINEQTKMIKn 683
Cdd:PRK04000   11 NIGMVGHVDHGKTTLVQALtgvwtdRHSE----ELKrGITIRLGYADATIrkcpdceepeayttepkcPNCGSETELLR- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  684 fdrenvRIPgmlIIDTPGHESFSNLRNRGSSLCDIAILVVDI-MHGLEPQTIE---SINILKSKKcpFIVALNKIDrlyd 759
Cdd:PRK04000   86 ------RVS---FVDAPGHETLMATMLSGAALMDGAILVIAAnEPCPQPQTKEhlmALDIIGIKN--IVIVQNKID---- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  760 wkkspdsdvAVTLKKQKKNtkdeFEErakaiIVEFAqQGLNAalfyENkdprtfVSLVPTSAHTGDGMGSLIYLLVELTQ 839
Cdd:PRK04000  151 ---------LVSKERALEN----YEQ-----IKEFV-KGTVA----EN------APIIPVSALHKVNIDALIEAIEEEIP 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  840 TmlSKRlahceelraqvmEVKALPGM-----------GTTID-----VI---LINGRLKEGDTI-IVPGVEG-------- 891
Cdd:PRK04000  202 T--PER------------DLDKPPRMyvarsfdvnkpGTPPEklkggVIggsLIQGVLKVGDEIeIRPGIKVeeggktkw 267
                         330
                  ....*....|
gi 158635983  892 -PIVTQIRGL 900
Cdd:PRK04000  268 ePITTKIVSL 277
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
635-757 5.33e-05

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: 46.33  E-value: 5.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  635 HVDTGKT----KIL---DKLRHTH-VQDGEAG----------GITQQIGATNvpleaineqtkmiknFDRENVRIPgmlI 696
Cdd:cd01886     7 HIDAGKTttteRILyytGRIHKIGeVHGGGATmdwmeqererGITIQSAATT---------------CFWKDHRIN---I 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158635983  697 IDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDRL 757
Cdd:cd01886    69 IDTPGHVDFTIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRT 129
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
618-756 6.22e-05

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: 47.35  E-value: 6.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  618 KNVNTEKLRapIICVLGHVDTGKT----------KILDKLRHTHvqDGEA----------GGITqqIGATNVPLE----A 673
Cdd:COG0480     2 AEYPLEKIR--NIGIVAHIDAGKTtlterilfytGAIHRIGEVH--DGNTvmdwmpeeqeRGIT--ITSAATTCEwkghK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  674 INeqtkmiknfdrenvripgmlIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNK 753
Cdd:COG0480    76 IN--------------------IIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNK 135

                  ...
gi 158635983  754 IDR 756
Cdd:COG0480   136 MDR 138
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
852-943 7.25e-05

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: 42.25  E-value: 7.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  852 LRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIVPGVegPIVTQIRGLLLPppmkelrvknqYEKHKEVEAAQGVKILG 931
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPK--GITGRVTSIERF-----------HEEVDEAKAGDIVGIGI 67
                          90
                  ....*....|..
gi 158635983  932 KDLEKTLAGLPL 943
Cdd:cd01342    68 LGVKDILTGDTL 79
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
635-756 9.76e-05

Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 46.55  E-value: 9.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  635 HVDTGKTKILDK-LRHTHV-QDGEAG--------------GITqqIGATNVpleAINeqtkmiknfdRENVRIPgmlIID 698
Cdd:COG1217    14 HVDHGKTTLVDAlLKQSGTfRENQEVaervmdsndlererGIT--ILAKNT---AVR----------YKGVKIN---IVD 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158635983  699 TPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQT-------IEsinilksKKCPFIVALNKIDR 756
Cdd:COG1217    76 TPGHADFGGEVERVLSMVDGVLLLVDAFEGPMPQTrfvlkkaLE-------LGLKPIVVINKIDR 133
prfC PRK00741
peptide chain release factor 3; Provisional
696-756 1.62e-04

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 45.89  E-value: 1.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158635983  696 IIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDR 756
Cdd:PRK00741   83 LLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTPIFTFINKLDR 143
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
695-837 1.80e-04

EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first 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: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 43.19  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  695 LIIDTPGHESFSNL---RNRGSSL-----CDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDrlydwkkspds 766
Cdd:cd01894    48 ILIDTGGIEPDDEGiskEIREQAEiaieeADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKID----------- 116
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158635983  767 dvavtlkkqkkNTKDEFEerakaiIVEFAQQGLnaalfyenKDPrtfvslVPTSAHTGDGMGSLIYLLVEL 837
Cdd:cd01894   117 -----------NIKEEEE------AAEFYSLGF--------GEP------IPISAEHGRGIGDLLDAILEL 156
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
696-760 1.81e-04

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 45.69  E-value: 1.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158635983  696 IIDTPGHESFSnlRN--RGSSLCDIAILVVDIMHGLEPQTiesinilksKKCPFIVAL----------NKIDrLYDW 760
Cdd:PRK05506  108 VADTPGHEQYT--RNmvTGASTADLAIILVDARKGVLTQT---------RRHSFIASLlgirhvvlavNKMD-LVDY 172
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
696-756 1.88e-04

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 45.89  E-value: 1.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158635983  696 IIDTPGHESF-----SNLRnrgssLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDR 756
Cdd:PRK12740   64 LIDTPGHVDFtgeveRALR-----VLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDR 124
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
696-891 2.78e-04

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 44.92  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  696 IIDTPGHESFsnLRN--RGSSLCDIAILVV---DIMhGLEPQTIESINILKSKKCP-FIVALNKIDRL-YDWKKspdsdv 768
Cdd:PRK12317   88 IVDCPGHRDF--VKNmiTGASQADAAVLVVaadDAG-GVMPQTREHVFLARTLGINqLIVAINKMDAVnYDEKR------ 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  769 avtlkkqkkntkdeFEErakaiIVEFAQQGLNAALFYENKdprtfVSLVPTSAHTGDGmgsliylLVELTQTM------- 841
Cdd:PRK12317  159 --------------YEE-----VKEEVSKLLKMVGYKPDD-----IPFIPVSAFEGDN-------VVKKSENMpwyngpt 207
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  842 LSKRLAHCEE--------LRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIV--PGVEG 891
Cdd:PRK12317  208 LLEALDNLKPpekptdkpLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFmpAGVVG 267
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
630-793 3.91e-04

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: 44.89  E-value: 3.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   630 ICVLGHVDTGKTKILDKLRhthvqdGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRI------PGMLI--IDTPG 701
Cdd:TIGR00490   22 IGIVAHIDHGKTTLSDNLL------AGAGMISEELAGQQLYLDFDEQEQERGITINAANVSMvheyegNEYLInlIDTPG 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   702 HESFSNLRNRGSSLCDIAILVVDIMHGLEPQTiESI--NILKSKKCPfIVALNKIDRLYdwkkspdsdvavtlkKQKKNT 779
Cdd:TIGR00490   96 HVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQT-ETVlrQALKENVKP-VLFINKVDRLI---------------NELKLT 158
                          170
                   ....*....|....
gi 158635983   780 KDEFEERAKAIIVE 793
Cdd:TIGR00490  159 PQELQERFIKIITE 172
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
866-940 5.62e-04

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: 39.56  E-value: 5.62e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158635983   866 GTTIDVILINGRLKEGDTIIVPGV---EGPIVTQIRGLLlpPPMKELRVknqyekhKEVEAAQGVKILGKDLEKTLAG 940
Cdd:pfam03144    1 GTVATGRVESGTLKKGDKVRILPNgtgKKKIVTRVTSLL--MFHAPLRE-------AVAGDNAGLILAGVGLEDIRVG 69
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
630-837 6.30e-04

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: 42.66  E-value: 6.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  630 ICVLGHVDTGKTKILDKL-----------------RHTH-VQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRI 691
Cdd:cd04165     2 VAVVGNVDAGKSTLLGVLtqgeldngrgkarlnlfRHKHeVESGRTSSVSNDILGFDSDGEVVNYPDNHLGELDVEICEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  692 PGMLI--IDTPGHESF--SNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDrlydwkKSPDSD 767
Cdd:cd04165    82 SSKVVtfIDLAGHERYlkTTVFGMTGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVVVTKID------MTPANV 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158635983  768 VAVTLKKQKKNTKDEFeERAKAIIVEFAQQGLNAALFYenkdprTFVSLVP---TSAHTGDGMGSLIYLLVEL 837
Cdd:cd04165   156 LQETLKDLKRLLKSPG-VRKLPVPVKSKDDVVLSASNL------SSGRVVPifqVSNVTGEGLDLLRRFLNLL 221
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
630-755 8.60e-04

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 40.18  E-value: 8.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983   630 ICVLGHVDTGKTKILDKLRHTHVQDGEaggiTQQIGATNVpleaineqTKMIKNFDRENVRIpgMLII-DTPGHESFSNL 708
Cdd:pfam08477    2 VVLLGDSGVGKTSLLKRFVDDTFDPKY----KSTIGVDFK--------TKTVLENDDNGKKI--KLNIwDTAGQERFRSL 67
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 158635983   709 RN---RGSSlcdIAILVVDImhglepQTIES----INILK--SKKCPFIVALNKID 755
Cdd:pfam08477   68 HPfyyRGAA---AALLVYDS------RTFSNlkywLRELKkyAGNSPVILVGNKID 114
YeeP COG3596
Predicted GTPase [General function prediction only];
678-856 1.42e-03

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 42.45  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  678 TKMIKNFDRENVRIPGMLIIDTPGHESfSNLRNRG-------SSLCDIAILVVDIM---HGLEPQTIESInILKSKKCPF 747
Cdd:COG3596    74 TREIQRYRLESDGLPGLVLLDTPGLGE-VNERDREyrelrelLPEADLILWVVKADdraLATDEEFLQAL-RAQYPDPPV 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  748 IVALNKIDRLY---DWKKSPDSdvavTLKKQKKNTKDEFEERAKaiivefaqqglnaaLFYENKDPrtfvsLVPTSA--- 821
Cdd:COG3596   152 LVVLTQVDRLEperEWDPPYNW----PSPPKEQNIRRALEAIAE--------------QLGVPIDR-----VIPVSAaed 208
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 158635983  822 HTGDGMGSLIYLLVELTQTMLSKRLAHCeeLRAQV 856
Cdd:COG3596   209 RTGYGLEELVDALAEALPEAKRSRLARL--LRAKA 241
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
630-756 2.35e-03

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: 41.42  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  630 ICVLGHVDTGKTKILDKLRHThvqdgeAGGITQQ--IGATNVPLEAINEQTKM-------IKNFDRENVRIPgmlIIDTP 700
Cdd:cd04170     2 IALVGHSGSGKTTLAEALLYA------TGAIDRLgrVEDGNTVSDYDPEEKKRkmsietsVAPLEWNGHKIN---LIDTP 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158635983  701 G-----HESFSNLRnrgssLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDR 756
Cdd:cd04170    73 GyadfvGETLSALR-----AVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDR 128
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
695-757 3.34e-03

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: 39.54  E-value: 3.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  695 LIIDTPG-HESFSNLRNRGSSL------CDIAILVVDIMHGLEPQTIESINILKSKKcPFIVALNKIDRL 757
Cdd:cd00880    49 VLIDTPGlDEEGGLGRERVEEArqvadrADLVLLVVDSDLTPVEEEAKLGLLRERGK-PVLLVLNKIDLV 117
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
684-831 3.40e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 41.19  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  684 FDRENVRIpgmLIIDTPG-------HES---FSNLRnrgsSL-----CDIAILVVDIMHGLEPQ--TIESInILKSKKcP 746
Cdd:PRK00093  216 FERDGQKY---TLIDTAGirrkgkvTEGvekYSVIR----TLkaierADVVLLVIDATEGITEQdlRIAGL-ALEAGR-A 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  747 FIVALNKIDRLydwkkspdsdvavtlkkqKKNTKDEFEERAKAiivEFAQqgLNaalfyenkdprtFVSLVPTSAHTGDG 826
Cdd:PRK00093  287 LVIVVNKWDLV------------------DEKTMEEFKKELRR---RLPF--LD------------YAPIVFISALTGQG 331

                  ....*
gi 158635983  827 MGSLI 831
Cdd:PRK00093  332 VDKLL 336
PLN03126 PLN03126
Elongation factor Tu; Provisional
630-759 4.58e-03

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 41.14  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  630 ICVLGHVDTGKTKILDKLrhTHVQDGEAGGITQQIGATNVPLE------AINEQTKMIKNFDRENVRIpgmliiDTPGHE 703
Cdd:PLN03126   84 IGTIGHVDHGKTTLTAAL--TMALASMGGSAPKKYDEIDAAPEerargiTINTATVEYETENRHYAHV------DCPGHA 155
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 158635983  704 SFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCP-FIVALNKIDRLYD 759
Cdd:PLN03126  156 DYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPnMVVFLNKQDQVDD 212
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
630-756 5.44e-03

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 40.86  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  630 ICVLGHVDTGKTKILDKL---------------RHTHVQDGEAG-GITqqIGATNVPL--EAINEQTKMIKNFDRENvri 691
Cdd:PLN00116   22 MSVIAHVDHGKSTLTDSLvaaagiiaqevagdvRMTDTRADEAErGIT--IKSTGISLyyEMTDESLKDFKGERDGN--- 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158635983  692 pGMLI--IDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCPFIVALNKIDR 756
Cdd:PLN00116   97 -EYLInlIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDR 162
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
696-827 5.99e-03

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: 39.78  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158635983  696 IIDTPGHESF-SNLRNrGSSLCDIAILVVDIMHG-------LEPQTIESINILKS---KKcpFIVALNKIDR-LYDWKks 763
Cdd:cd01883    81 IIDAPGHRDFvKNMIT-GASQADVAVLVVSARKGefeagfeKGGQTREHALLARTlgvKQ--LIVAVNKMDDvTVNWS-- 155
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158635983  764 pdsdvavtlkkqkkntKDEFEErAKAIIVEFAQQglnaaLFYENKDprtfVSLVPTSAHTGDGM 827
Cdd:cd01883   156 ----------------QERYDE-IKKKVSPFLKK-----VGYNPKD----VPFIPISGFTGDNL 193
tufA CHL00071
elongation factor Tu
697-759 6.86e-03

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 40.33  E-value: 6.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158635983  697 IDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCP-FIVALNKIDRLYD 759
Cdd:CHL00071   80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPnIVVFLNKEDQVDD 143
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
697-759 8.05e-03

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: 39.10  E-value: 8.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158635983  697 IDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINILKSKKCP-FIVALNKIDRLYD 759
Cdd:cd01884    70 VDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPyIVVFLNKADMVDD 133
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
697-755 9.83e-03

Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 40.00  E-value: 9.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158635983  697 IDTPGHESFSNLRNRgsSL--CDIAILVVDIMHGLEPQTIESINI-----LKskkcpFIVALNKID 755
Cdd:COG0481    78 IDTPGHVDFSYEVSR--SLaaCEGALLVVDASQGVEAQTLANVYLalendLE-----IIPVINKID 136
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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