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Conserved domains on  [gi|929654105|dbj|BAA34461|]
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KIAA0741 protein [Homo sapiens]

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
627-1202 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: 556.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  627 EKLRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGH 706
Cdd:PRK04004    2 KKLRQPIVVVLGHVDHGKTTLLDKIRGTAVAAKEAGGITQHIGATEVPIDVIEKIAGPLKKPLPIKLKIPGLLFIDTPGH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  707 ESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLYDWKKSPDSDVAATLKKQKKNTKDE 786
Cdd:PRK04004   82 EAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDRIPGWKSTEDAPFLESIEKQSQRVQQE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  787 FEERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEE--LRAQVMEVK 864
Cdd:PRK04004  162 LEEKLYELIGQLSELGFSADRFDRVKDFTKTVAIVPVSAKTGEGIPDLLMVLAGLAQRYLEERLKIDVEgpGKGTVLEVK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  865 ALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELR-VKNQYEKHKEVEAAQGVKILGKDLEKTLA 943
Cdd:PRK04004  242 EERGLGTTIDVILYDGTLRKGDTIVVGGKDGPIVTKVRALLKPRPLDEMRdPEDKFKPVDEVVAAAGVKISAPDLEDALA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  944 GLPLLVAyKEDEIPVLKDELIHELKQtlNAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASV 1023
Cdd:PRK04004  322 GSPLRVV-RDEDVEEVKEEVEEEIEE--IRIETDEEGVVVKADTLGSLEALVNELREEGIPIRKADVGDISKRDVIEAST 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105 1024 MLEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYK-KQKQEEFKHIaVFPCKIKILPQYIF 1102
Cdd:PRK04004  399 VAEKDPLYGVILAFNVKVLPDAEEEAEKSDVKIFTGDVIYQLIEDYEKWVKEQKeAEKEKILEKI-VRPAKIRILPGYVF 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105 1103 NSRDPIVMGVTVEAGQVKQGTPmcVPSKNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEpipgesPKMFGRHFEATDIL 1182
Cdd:PRK04004  478 RQSDPAIVGVEVLGGTIKPGVP--LIKEDGKRVGTIKQIQDQGENVKEAKAGMEVAISID------GPTVGRQIKEGDIL 549
                         570       580
                  ....*....|....*....|
gi 929654105 1183 VSKISRQSIDALKDWFRDEM 1202
Cdd:PRK04004  550 YVDIPEEHAKILEQELKDEL 569
 
Name Accession Description Interval E-value
PRK04004 PRK04004
translation initiation factor IF-2; Validated
627-1202 0e+00

translation initiation factor IF-2; Validated


Pssm-ID: 235195 [Multi-domain]  Cd Length: 586  Bit Score: 556.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  627 EKLRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGH 706
Cdd:PRK04004    2 KKLRQPIVVVLGHVDHGKTTLLDKIRGTAVAAKEAGGITQHIGATEVPIDVIEKIAGPLKKPLPIKLKIPGLLFIDTPGH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  707 ESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLYDWKKSPDSDVAATLKKQKKNTKDE 786
Cdd:PRK04004   82 EAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDRIPGWKSTEDAPFLESIEKQSQRVQQE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  787 FEERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEE--LRAQVMEVK 864
Cdd:PRK04004  162 LEEKLYELIGQLSELGFSADRFDRVKDFTKTVAIVPVSAKTGEGIPDLLMVLAGLAQRYLEERLKIDVEgpGKGTVLEVK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  865 ALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELR-VKNQYEKHKEVEAAQGVKILGKDLEKTLA 943
Cdd:PRK04004  242 EERGLGTTIDVILYDGTLRKGDTIVVGGKDGPIVTKVRALLKPRPLDEMRdPEDKFKPVDEVVAAAGVKISAPDLEDALA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  944 GLPLLVAyKEDEIPVLKDELIHELKQtlNAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASV 1023
Cdd:PRK04004  322 GSPLRVV-RDEDVEEVKEEVEEEIEE--IRIETDEEGVVVKADTLGSLEALVNELREEGIPIRKADVGDISKRDVIEAST 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105 1024 MLEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYK-KQKQEEFKHIaVFPCKIKILPQYIF 1102
Cdd:PRK04004  399 VAEKDPLYGVILAFNVKVLPDAEEEAEKSDVKIFTGDVIYQLIEDYEKWVKEQKeAEKEKILEKI-VRPAKIRILPGYVF 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105 1103 NSRDPIVMGVTVEAGQVKQGTPmcVPSKNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEpipgesPKMFGRHFEATDIL 1182
Cdd:PRK04004  478 RQSDPAIVGVEVLGGTIKPGVP--LIKEDGKRVGTIKQIQDQGENVKEAKAGMEVAISID------GPTVGRQIKEGDIL 549
                         570       580
                  ....*....|....*....|
gi 929654105 1183 VSKISRQSIDALKDWFRDEM 1202
Cdd:PRK04004  550 YVDIPEEHAKILEQELKDEL 569
aIF-2 TIGR00491
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ...
628-1215 8.41e-137

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: 429.24  E-value: 8.41e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   628 KLRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGHE 707
Cdd:TIGR00491    1 RLRQPIVVVLGHVDHGKTTLLDKIRGTAVVKKEAGGITQHIGASEVPTDVIEKICGDLLKSFKIKLKIPGLLFIDTPGHE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   708 SFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLYDWKKSPDSDVAATLKKQKKNTKDEF 787
Cdd:TIGR00491   81 AFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDRIPGWKSHEGYPFLESINKQEQRVRQNL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   788 EERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEE--LRAQVMEVKA 865
Cdd:TIGR00491  161 DKQVYNLVIQLAEQGFNAERFDRIRDFTKTVAIIPVSAKTGEGIPELLAILAGLAQNYLENKLKLAIEgpAKGTILEVKE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   866 LPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRV-KNQYEKHKEVEAAQGVKILGKDLEKTLAG 944
Cdd:TIGR00491  241 EQGLGYTIDAVIYDGILRKGDIIVLAGIDDVIVTRVRAILKPRPLQEMRLaRKKFAQVDEVYAAAGVKVAAPNLDTVLAG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   945 LPlLVAYKEDEIPVLKDELIHELKQTlnAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASVM 1024
Cdd:TIGR00491  321 SP-IVVENNEEIEKYKEEIQKEVEEI--KIYTDEEGIVVKADTLGSLEALVNELRRRGIPIKKADIGDVSKRDVVEAEIV 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  1025 LEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYKKQKQEEFKHIAVFPCKIKILPQYIFNS 1104
Cdd:TIGR00491  398 KQEAKEYGAIAAFNVKPLPGAEIEAEKYDIKLFSDNIIYQLMENFEKWIEDIEESEKRKTLEAIIKPGKIKIIPGYVFRR 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  1105 RDPIVMGVTVEAGQVKQGTPMCVPSKNFVdiGIVTSIEINHKQVDVAKKGQEVCVKIEPIpgespkMFGRHFEATDIL-- 1182
Cdd:TIGR00491  478 SDPAIVGVEVLGGIIRPGYPLIKKDGRRV--GEVRQIQDNGKNVKRASAGMEVAIAIEDV------VIGRQLEEGDELyv 549
                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 929654105  1183 ------VSKISRQSIDALKDWFRDEMQKsdwqlIVELKK 1215
Cdd:TIGR00491  550 dvperhAKVLERDLLDSLDEEEKRAFKE-----FLEIKR 583
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
632-845 9.83e-78

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: 253.16  E-value: 9.83e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  632 PIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLeaineqtkmiknfdreNVRIPGMLIIDTPGHESFSN 711
Cdd:cd01887     1 PVVTVMGHVDHGKTTLLDKIRKTNVAAGEAGGITQHIGAYQVPI----------------DVKIPGITFIDTPGHEAFTN 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  712 LRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLYDwkkspdsdvaatlkkqkkntKDEFEERA 791
Cdd:cd01887    65 MRARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYG--------------------TEADPERV 124
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 929654105  792 KAIIVEFAQQGLnaalfyenkDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTM 845
Cdd:cd01887   125 KNELSELGLVGE---------EWGGDVSIVPISAKTGEGIDDLLEAILLLAEVL 169
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
630-1067 6.22e-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: 199.86  E-value: 6.22e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  630 RAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEaineqTKMIknfdrenvripgmLIIDTPGHESF 709
Cdd:COG0532     3 RPPVVTVMGHVDHGKTSLLDAIRKTNVAAGEAGGITQHIGAYQVETN-----GGKI-------------TFLDTPGHEAF 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  710 SNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRlydwkksPDSDVaatlkkqkkntkdefeE 789
Cdd:COG0532    65 TAMRARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDK-------PGANP----------------D 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  790 RAKAiivEFAQQGLNA------ALFyenkdprtfvslVPTSAHTGDGMGSL---IYLLVELtqtmlskrlahcEELRAQ- 859
Cdd:COG0532   122 RVKQ---ELAEHGLVPeewggdTIF------------VPVSAKTGEGIDELlemILLQAEV------------LELKANp 174
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  860 -------VMEVKALPGMGTTIDVILINGRLKEGDTIIVpgveGPIVTQIRGLLlpppmkelrvkNqyEKHKEVEAA---Q 929
Cdd:COG0532   175 drpargtVIEAKLDKGRGPVATVLVQNGTLKVGDIVVA----GTAYGRVRAMF-----------D--DRGKRVKEAgpsT 237
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  930 GVKILGkdlektLAGLPllvaykE--DEIPVLKDE-------------LIHELKQTLNAIKLE------------EKGVY 982
Cdd:COG0532   238 PVEILG------LSGVP------QagDEFVVVEDEkkareiaekrqqkAREKKLARQKRVSLEdlfsqikegevkELNLI 305
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  983 VQASTLGSLEAL---LEFLKTSEVpyaGINI-----GPVHKKDVM--KASvmlehdpqYAVILAFDVRIERDAQEMADSL 1052
Cdd:COG0532   306 LKADVQGSVEALkdsLEKLSTDEV---KVNIihsgvGAITESDVNlaAAS--------NAIIIGFNVRPDAKARKLAERE 374
                         490
                  ....*....|....*
gi 929654105 1053 GVRIFSAEIIYHLFD 1067
Cdd:COG0532   375 GVDIRYYSIIYDLID 389
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
630-844 2.62e-42

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: 153.06  E-value: 2.62e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   630 RAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGAT--NVPLEAINEQTKMIKN--FDRENVRIpgmLIIDTPG 705
Cdd:pfam00009    2 RHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEAGldNLPEERERGITIKSAAvsFETKDYLI---NLIDTPG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   706 HESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLYDwkkspdsdvaATLKKQKKNTKD 785
Cdd:pfam00009   79 HVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDG----------AELEEVVEEVSR 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 929654105   786 EFeerakaiIVEFAQQGLnaalfyenkdprtFVSLVPTSAHTGDGMGSLIYLLVELTQT 844
Cdd:pfam00009  149 EL-------LEKYGEDGE-------------FVPVVPGSALKGEGVQTLLDALDEYLPS 187
 
Name Accession Description Interval E-value
PRK04004 PRK04004
translation initiation factor IF-2; Validated
627-1202 0e+00

translation initiation factor IF-2; Validated


Pssm-ID: 235195 [Multi-domain]  Cd Length: 586  Bit Score: 556.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  627 EKLRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGH 706
Cdd:PRK04004    2 KKLRQPIVVVLGHVDHGKTTLLDKIRGTAVAAKEAGGITQHIGATEVPIDVIEKIAGPLKKPLPIKLKIPGLLFIDTPGH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  707 ESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLYDWKKSPDSDVAATLKKQKKNTKDE 786
Cdd:PRK04004   82 EAFTNLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVAANKIDRIPGWKSTEDAPFLESIEKQSQRVQQE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  787 FEERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEE--LRAQVMEVK 864
Cdd:PRK04004  162 LEEKLYELIGQLSELGFSADRFDRVKDFTKTVAIVPVSAKTGEGIPDLLMVLAGLAQRYLEERLKIDVEgpGKGTVLEVK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  865 ALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELR-VKNQYEKHKEVEAAQGVKILGKDLEKTLA 943
Cdd:PRK04004  242 EERGLGTTIDVILYDGTLRKGDTIVVGGKDGPIVTKVRALLKPRPLDEMRdPEDKFKPVDEVVAAAGVKISAPDLEDALA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  944 GLPLLVAyKEDEIPVLKDELIHELKQtlNAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASV 1023
Cdd:PRK04004  322 GSPLRVV-RDEDVEEVKEEVEEEIEE--IRIETDEEGVVVKADTLGSLEALVNELREEGIPIRKADVGDISKRDVIEAST 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105 1024 MLEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYK-KQKQEEFKHIaVFPCKIKILPQYIF 1102
Cdd:PRK04004  399 VAEKDPLYGVILAFNVKVLPDAEEEAEKSDVKIFTGDVIYQLIEDYEKWVKEQKeAEKEKILEKI-VRPAKIRILPGYVF 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105 1103 NSRDPIVMGVTVEAGQVKQGTPmcVPSKNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEpipgesPKMFGRHFEATDIL 1182
Cdd:PRK04004  478 RQSDPAIVGVEVLGGTIKPGVP--LIKEDGKRVGTIKQIQDQGENVKEAKAGMEVAISID------GPTVGRQIKEGDIL 549
                         570       580
                  ....*....|....*....|
gi 929654105 1183 VSKISRQSIDALKDWFRDEM 1202
Cdd:PRK04004  550 YVDIPEEHAKILEQELKDEL 569
aIF-2 TIGR00491
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ...
628-1215 8.41e-137

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: 429.24  E-value: 8.41e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   628 KLRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGHE 707
Cdd:TIGR00491    1 RLRQPIVVVLGHVDHGKTTLLDKIRGTAVVKKEAGGITQHIGASEVPTDVIEKICGDLLKSFKIKLKIPGLLFIDTPGHE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   708 SFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLYDWKKSPDSDVAATLKKQKKNTKDEF 787
Cdd:TIGR00491   81 AFTNLRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPFVVAANKIDRIPGWKSHEGYPFLESINKQEQRVRQNL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   788 EERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEE--LRAQVMEVKA 865
Cdd:TIGR00491  161 DKQVYNLVIQLAEQGFNAERFDRIRDFTKTVAIIPVSAKTGEGIPELLAILAGLAQNYLENKLKLAIEgpAKGTILEVKE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   866 LPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRV-KNQYEKHKEVEAAQGVKILGKDLEKTLAG 944
Cdd:TIGR00491  241 EQGLGYTIDAVIYDGILRKGDIIVLAGIDDVIVTRVRAILKPRPLQEMRLaRKKFAQVDEVYAAAGVKVAAPNLDTVLAG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   945 LPlLVAYKEDEIPVLKDELIHELKQTlnAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASVM 1024
Cdd:TIGR00491  321 SP-IVVENNEEIEKYKEEIQKEVEEI--KIYTDEEGIVVKADTLGSLEALVNELRRRGIPIKKADIGDVSKRDVVEAEIV 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  1025 LEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYKKQKQEEFKHIAVFPCKIKILPQYIFNS 1104
Cdd:TIGR00491  398 KQEAKEYGAIAAFNVKPLPGAEIEAEKYDIKLFSDNIIYQLMENFEKWIEDIEESEKRKTLEAIIKPGKIKIIPGYVFRR 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  1105 RDPIVMGVTVEAGQVKQGTPMCVPSKNFVdiGIVTSIEINHKQVDVAKKGQEVCVKIEPIpgespkMFGRHFEATDIL-- 1182
Cdd:TIGR00491  478 SDPAIVGVEVLGGIIRPGYPLIKKDGRRV--GEVRQIQDNGKNVKRASAGMEVAIAIEDV------VIGRQLEEGDELyv 549
                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 929654105  1183 ------VSKISRQSIDALKDWFRDEMQKsdwqlIVELKK 1215
Cdd:TIGR00491  550 dvperhAKVLERDLLDSLDEEEKRAFKE-----FLEIKR 583
PRK14845 PRK14845
translation initiation factor IF-2; Provisional
645-1216 3.45e-126

translation initiation factor IF-2; Provisional


Pssm-ID: 237833 [Multi-domain]  Cd Length: 1049  Bit Score: 414.67  E-value: 3.45e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  645 TKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGHESFSNLRNRGSSLCDIAI 724
Cdd:PRK14845  475 TTLLDKIRKTRVAKKEAGGITQHIGATEIPIDVIKKICGPLLKLLKAEIKIPGLLFIDTPGHEAFTSLRKRGGSLADLAV 554
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  725 LVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLYDWKKSPDSDVAATLKKQKKNTKDEFEERAKAIIVEFAQQGLN 804
Cdd:PRK14845  555 LVVDINEGFKPQTIEAINILRQYKTPFVVAANKIDLIPGWNISEDEPFLLNFNEQDQHALTELEIKLYELIGKLYELGFD 634
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  805 AALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEE--LRAQVMEVKALPGMGTTIDVILINGRL 882
Cdd:PRK14845  635 ADRFDRVQDFTRTVAIVPVSAKTGEGIPELLMMVAGLAQKYLEERLKLNVEgyAKGTILEVKEEKGLGTTIDAIIYDGTL 714
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  883 KEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRV-KNQYEKHKEVEAAQGVKILGKDLEKTLAGLPLLVAYKEDEIPVLKD 961
Cdd:PRK14845  715 RRGDTIVVGGPDDVIVTKVRALLKPKPLDEIRDpRDKFDPVDEVTAAAGVKIAAPGLEEVLAGSPIRIVPTKEKIEKAKE 794
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  962 ELIHELKQTlnAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASVMLEHDPQYAVILAFDVRI 1041
Cdd:PRK14845  795 EVMKEVEEA--KIETDKEGILIKADTLGSLEALANELRKAGIPIKKAEVGDITKKDVIEALSYKQENPLYGVILGFNVKV 872
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105 1042 ERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYK-KQKQEEFKHIaVFPCKIKILPQYIFNSRDPIVMGVTVEAGQVK 1120
Cdd:PRK14845  873 LPEAQEEAEKYGVKIFVDNIIYKLVEDYTEWVKEEEeKKKRELFEKL-IKPGIIRLLPDCIFRRSNPAIVGVEVLEGTLR 951
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105 1121 QGTPMCVPskNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEPIpgespkMFGRHFEATDILVSKISRQSIDALKDWFRD 1200
Cdd:PRK14845  952 VGVTLIKE--DGMKVGTVRSIKDRGENVKEAKAGKAVAIAIEGA------ILGRHVDEGETLYVDVPESHVRELYHKYMD 1023
                         570
                  ....*....|....*.
gi 929654105 1201 EMQKSDWQLIVELKKV 1216
Cdd:PRK14845 1024 RLRDDEKEALKMYMEL 1039
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
632-845 9.83e-78

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: 253.16  E-value: 9.83e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  632 PIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLeaineqtkmiknfdreNVRIPGMLIIDTPGHESFSN 711
Cdd:cd01887     1 PVVTVMGHVDHGKTTLLDKIRKTNVAAGEAGGITQHIGAYQVPI----------------DVKIPGITFIDTPGHEAFTN 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  712 LRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLYDwkkspdsdvaatlkkqkkntKDEFEERA 791
Cdd:cd01887    65 MRARGASVTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYG--------------------TEADPERV 124
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 929654105  792 KAIIVEFAQQGLnaalfyenkDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTM 845
Cdd:cd01887   125 KNELSELGLVGE---------EWGGDVSIVPISAKTGEGIDDLLEAILLLAEVL 169
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
630-1067 6.22e-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: 199.86  E-value: 6.22e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  630 RAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEaineqTKMIknfdrenvripgmLIIDTPGHESF 709
Cdd:COG0532     3 RPPVVTVMGHVDHGKTSLLDAIRKTNVAAGEAGGITQHIGAYQVETN-----GGKI-------------TFLDTPGHEAF 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  710 SNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRlydwkksPDSDVaatlkkqkkntkdefeE 789
Cdd:COG0532    65 TAMRARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVPIIVAINKIDK-------PGANP----------------D 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  790 RAKAiivEFAQQGLNA------ALFyenkdprtfvslVPTSAHTGDGMGSL---IYLLVELtqtmlskrlahcEELRAQ- 859
Cdd:COG0532   122 RVKQ---ELAEHGLVPeewggdTIF------------VPVSAKTGEGIDELlemILLQAEV------------LELKANp 174
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  860 -------VMEVKALPGMGTTIDVILINGRLKEGDTIIVpgveGPIVTQIRGLLlpppmkelrvkNqyEKHKEVEAA---Q 929
Cdd:COG0532   175 drpargtVIEAKLDKGRGPVATVLVQNGTLKVGDIVVA----GTAYGRVRAMF-----------D--DRGKRVKEAgpsT 237
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  930 GVKILGkdlektLAGLPllvaykE--DEIPVLKDE-------------LIHELKQTLNAIKLE------------EKGVY 982
Cdd:COG0532   238 PVEILG------LSGVP------QagDEFVVVEDEkkareiaekrqqkAREKKLARQKRVSLEdlfsqikegevkELNLI 305
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  983 VQASTLGSLEAL---LEFLKTSEVpyaGINI-----GPVHKKDVM--KASvmlehdpqYAVILAFDVRIERDAQEMADSL 1052
Cdd:COG0532   306 LKADVQGSVEALkdsLEKLSTDEV---KVNIihsgvGAITESDVNlaAAS--------NAIIIGFNVRPDAKARKLAERE 374
                         490
                  ....*....|....*
gi 929654105 1053 GVRIFSAEIIYHLFD 1067
Cdd:COG0532   375 GVDIRYYSIIYDLID 389
aeIF5B_II cd03703
Domain II of archaeal and eukaryotic Initiation Factor 5; This family represents domain II of ...
855-965 8.32e-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: 171.57  E-value: 8.32e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  855 ELRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRVKNQYEKHKEVEAAQGVKIL 934
Cdd:cd03703     1 PGKGTVLEVKEEEGLGTTIDVILYDGTLREGDTIVVGGLNGPIVTKVRALLKPKPLKEMRVKSRFIHVKEVVAAAGVKIA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 929654105  935 GKDLEKTLAGLPLLVAYKEDEIPVLKDELIH 965
Cdd:cd03703    81 APDLEKAIAGSPLRVVGNEDEIEELIEEVME 111
IF2_IF5B_II cd03701
Domain II of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; ...
855-950 8.18e-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: 153.98  E-value: 8.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  855 ELRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRVKNQYEKHKEVEAAQGVKIL 934
Cdd:cd03701     1 EPRGVILEVKLDKGAGITIDMLVQEGTLRVGDTIVAGESKDVIYTRIRALLDPDPLEEMESRKKGNKRKEVGAASGVKIL 80
                          90
                  ....*....|....*.
gi 929654105  935 GKDLEKTLAGLPLLVA 950
Cdd:cd03701    81 GFGQELPHAGDPLEVV 96
IF-2 TIGR00487
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ...
630-1067 1.53e-42

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: 165.33  E-value: 1.53e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   630 RAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVpleaINEQTKMIKnfdrenvripgmlIIDTPGHESF 709
Cdd:TIGR00487   86 RPPVVTIMGHVDHGKTSLLDSIRKTKVAQGEAGGITQHIGAYHV----ENEDGKMIT-------------FLDTPGHEAF 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   710 SNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRlydwkksPDSDvaatlkkqkkntkdefee 789
Cdd:TIGR00487  149 TSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVPIIVAINKIDK-------PEAN------------------ 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   790 rAKAIIVEFAQQGLNAALFYENkdprtfVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHcEELRAQVMEVKALPGM 869
Cdd:TIGR00487  204 -PDRVKQELSEYGLVPEDWGGD------TIFVPVSALTGDGIDELLDMILLQSEVEELKANPN-GQASGVVIEAQLDKGR 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   870 GTTIDVILINGRLKEGDTIIVpgveGPIVTQIRGLllpppmkelrVKNQYEKHKEVEAAQGVKILGKDlEKTLAGLPLLV 949
Cdd:TIGR00487  276 GPVATVLVQSGTLRVGDIVVV----GAAYGRVRAM----------IDENGKSVKEAGPSKPVEILGLS-DVPAAGDEFIV 340
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   950 AYKEDEIPVLKDELIHELKQTLNA-------------IK---LEEKGVYVQASTLGSLEAL---LEFLKTSEVPYAGIN- 1009
Cdd:TIGR00487  341 FKDEKDARLVAEKRAGKLRQKALSrsvkvtldnlfeqIKegeLKELNIILKADVQGSLEAIknsLEKLNNEEVKVKVIHs 420
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 929654105  1010 -IGPVHKKDVMKASVmlehdpQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFD 1067
Cdd:TIGR00487  421 gVGGITETDISLASA------SNAIIIGFNVRPDATAKNVAEAENVDIRYYSVIYKLID 473
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
630-844 2.62e-42

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: 153.06  E-value: 2.62e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   630 RAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGAT--NVPLEAINEQTKMIKN--FDRENVRIpgmLIIDTPG 705
Cdd:pfam00009    2 RHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEAGldNLPEERERGITIKSAAvsFETKDYLI---NLIDTPG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   706 HESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLYDwkkspdsdvaATLKKQKKNTKD 785
Cdd:pfam00009   79 HVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRVDG----------AELEEVVEEVSR 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 929654105   786 EFeerakaiIVEFAQQGLnaalfyenkdprtFVSLVPTSAHTGDGMGSLIYLLVELTQT 844
Cdd:pfam00009  149 EL-------LEKYGEDGE-------------FVPVVPGSALKGEGVQTLLDALDEYLPS 187
infB CHL00189
translation initiation factor 2; Provisional
623-1156 9.78e-39

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 155.76  E-value: 9.78e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  623 NVNTEKlRAPIICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIknfdrenvripgmlIID 702
Cdd:CHL00189  237 TENSIN-RPPIVTILGHVDHGKTTLLDKIRKTQIAQKEAGGITQKIGAYEVEFEYKDENQKIV--------------FLD 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  703 TPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDrlydwkkspdsdvaatlkKQKKN 782
Cdd:CHL00189  302 TPGHEAFSSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKID------------------KANAN 363
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  783 TkdefeERAKaiivefaQQGLNAALFYENKDPRTfvSLVPTSAHTGDGMGSLIYLLVELTQtMLSKRLAHCEELRAQVME 862
Cdd:CHL00189  364 T-----ERIK-------QQLAKYNLIPEKWGGDT--PMIPISASQGTNIDKLLETILLLAE-IEDLKADPTQLAQGIILE 428
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  863 VKALPGMGTTIDVILINGRLKEGDTIivpgVEGPIVTQIRGLllpppmkelrVKNQYEKHKEVEAAQGVKILGkdLEKTL 942
Cdd:CHL00189  429 AHLDKTKGPVATILVQNGTLHIGDII----VIGTSYAKIRGM----------INSLGNKINLATPSSVVEIWG--LSSVP 492
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  943 A-GLPLLVAYKEDE-IPVLKDELIHELKQTLNAIKLEEKGVY------------VQASTLGSLEALLEFLKTSEVPYAGI 1008
Cdd:CHL00189  493 AtGEHFQVFNSEKEaKLKIIKNKENNKKDTTKRITLSTTKTInkkdnkkqinliIKTDTQGSIEAIINSISQIPQKKVQL 572
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105 1009 NI-----GPVHKKDVMKASVmlehdpQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYkkqKQEE 1083
Cdd:CHL00189  573 NIlyaslGEVTETDVEFAST------TNAEILAFNTNLAPGAKKAARKLNIIIKEYQVIYDLLEYIEALMEDL---LDPE 643
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 929654105 1084 FKHIAVFPCKIkilpQYIFNSRDPIVMGVTVEAGQVKQGTPMCVPSKN-FVDIGIVTSIEINHKQVDVAKKGQE 1156
Cdd:CHL00189  644 YKKVPIGEAEV----KTVFPLAKRFVAGCRVTEGKITKNALIKVIRENkLIYEGKITSLKRVKEDVEEAQEGNE 713
IF2_aeIF5B_IV cd16266
Domain IV of prokaryotic Initiation Factor 2 and archaeal and eukaryotic Initiation Factor 5; ...
1092-1186 1.97e-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: 135.37  E-value: 1.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105 1092 CKIKILPQYIFNSRDPIVMGVTVEAGQVKQGTPMCVPskNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEPIPgespkm 1171
Cdd:cd16266     1 AKIRILPGCVFRQSKPAIVGVEVLEGTLKPGVPLIVP--DGKDVGRVKSIQDNGENVKEAKKGQEVAVSIEGPT------ 72
                          90
                  ....*....|....*
gi 929654105 1172 FGRHFEATDILVSKI 1186
Cdd:cd16266    73 VGRHIEEGDILYVDI 87
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
633-841 9.21e-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: 9.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  633 IICVLGHVDTGKTKILDKLRH---------------THVQDGE-AGGITQQIGATNVPLEaineqtkmiknfdreNVRIp 696
Cdd:cd00881     1 NVGVIGHVDHGKTTLTGSLLYqtgaidrrgtrketfLDTLKEErERGITIKTGVVEFEWP---------------KRRI- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  697 gmLIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLydwkksPDSDVAATL 776
Cdd:cd00881    65 --NFIDTPGHEDFSKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKIDRV------GEEDFDEVL 136
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 929654105  777 KkqkkntkdEFEERAKAIIVEFaqqglnaalfyenkDPRTFVSLVPTSAHTGDGMGSLIYLLVEL 841
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 ...
966-1067 2.87e-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: 87.49  E-value: 2.87e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   966 ELKQTLNAIKLEEK--GVYVQASTLGSLEALLEFLKTSEVPYAGINI-----GPVHKKDVMKASvmlehdPQYAVILAFD 1038
Cdd:pfam11987   11 SLEDLFSQIKEEVKelNLIIKADVQGSLEALKESLEKLSNDEVKVNIihsgvGAITESDVMLAS------ASNAIIIGFN 84
                           90       100
                   ....*....|....*....|....*....
gi 929654105  1039 VRIERDAQEMADSLGVRIFSAEIIYHLFD 1067
Cdd:pfam11987   85 VRPDAKARKLAEKEGVDIRYYNIIYDLID 113
GTP_EFTU_D4 pfam14578
Elongation factor Tu domain 4; Elongation factor Tu consists of several structural domains, ...
1091-1182 1.29e-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: 78.83  E-value: 1.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  1091 PCKIKILPQYIFNSRDPIVMGVTVEAGQVKQGTPMCVPSKNfvDIGIVTSIEINHKQVDVAKKGQEVCVKIepipgESPK 1170
Cdd:pfam14578    1 PGKIRILPGYVFRRSDPAIVGVEVLGGIIKPGYPLIREDGR--EVGEIMQIQDNGKSLDEAKAGQEVAISI-----EGKI 73
                           90
                   ....*....|..
gi 929654105  1171 MFGRHFEATDIL 1182
Cdd:pfam14578   74 MVGRQIKEGDIL 85
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
633-897 3.28e-14

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: 77.22  E-value: 3.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   633 IICVLGHVDTGKTKILDKLRHT---HVQDGEAGGITQQIGATNVPLEAineqtkmiknfdrenvRIPGmlIIDTPGHESF 709
Cdd:TIGR00475    2 IIATAGHVDHGKTTLLKALTGIaadRLPEEKKRGMTIDLGFAYFPLPD----------------YRLG--FIDVPGHEKF 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   710 snLRNRGSSLCDI--AILVVDIMHGLEPQTIESINLLKSKKCPF-IVALNKIDRLYdwkkspdsdvaatlkkqkkntkde 786
Cdd:TIGR00475   64 --ISNAIAGGGGIdaALLVVDADEGVMTQTGEHLAVLDLLGIPHtIVVITKADRVN------------------------ 117
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   787 fEERAKaIIVEFAQQGLNAALFYENKDprtfvsLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHceELRAQVMEVKAL 866
Cdd:TIGR00475  118 -EEEIK-RTEMFMKQILNSYIFLKNAK------IFKTSAKTGQGIGELKKELKNLLESLDIKRIQK--PLRMAIDRAFKV 187
                          250       260       270
                   ....*....|....*....|....*....|.
gi 929654105   867 PGMGTTIDVILINGRLKEGDTIIVPGVEGPI 897
Cdd:TIGR00475  188 KGAGTVVTGTAFSGEVKVGDNLRLLPINHEV 218
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
633-929 2.02e-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: 74.57  E-value: 2.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  633 IICVLGHVDTGKT---KIL-----DKL-----RhthvqdgeagGITQQIGATNVPLEaineqtkmiknfdreNVRIPGml 699
Cdd:COG3276     2 IIGTAGHIDHGKTtlvKALtgidtDRLkeekkR----------GITIDLGFAYLPLP---------------DGRRLG-- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  700 IIDTPGHESFsnLRN--RGSSLCDIAILVVD----IMhglePQTIES---INLLKSKKCpfIVALNKIDRlydwkkspds 770
Cdd:COG3276    55 FVDVPGHEKF--IKNmlAGAGGIDLVLLVVAadegVM----PQTREHlaiLDLLGIKRG--IVVLTKADL---------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  771 dVAatlkkqkkntkDEFEERAKAIIVEFaqqgLnAALFYENKDprtfvsLVPTSAHTGDGMGSLIYLLVELTQTMLSKRL 850
Cdd:COG3276   117 -VD-----------EEWLELVEEEIREL----L-AGTFLEDAP------IVPVSAVTGEGIDELRAALDALAAAVPARDA 173
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  851 AHCeeLRAQVMEVKALPGMGTtidVI---LINGRLKEGDTiivpgvegpivtqirgLLLPPPMKELRVKN---QYEKHKE 924
Cdd:COG3276   174 DGP--FRLPIDRVFSIKGFGT---VVtgtLLSGTVRVGDE----------------LELLPSGKPVRVRGiqvHGQPVEE 232

                  ....*
gi 929654105  925 VEAAQ 929
Cdd:COG3276   233 AYAGQ 237
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
634-788 2.24e-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 eukaryotic SelBs and some from archaea.


Pssm-ID: 206676 [Multi-domain]  Cd Length: 192  Bit Score: 67.01  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  634 ICVLGHVDTGKTKI------------LDKLRHTHVQdgeagGITQQIG--ATNVPLEAINEQTKmikNFDRENVRIpgmL 699
Cdd:cd01889     3 VGLLGHVDSGKTSLakalseiastaaFDKNPQSQER-----GITLDLGfsSFEVDKPKHLEDNE---NPQIENYQI---T 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  700 IIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLydwkksPDSDVAATLKKQ 779
Cdd:cd01889    72 LVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKIDLI------PEEERKRKIEKM 145

                  ....*....
gi 929654105  780 KKNTKDEFE 788
Cdd:cd01889   146 KKRLQKTLE 154
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
634-839 4.69e-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: 65.47  E-value: 4.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   634 ICVLGHVDTGKTKILDKLRHTHVQDGEAG-GITQQIGATnvpLEAINEQTKMIKnfdrenvripgmlIIDTPGHESFSNL 712
Cdd:TIGR00231    4 IVIVGHPNVGKSTLLNSLLGNKGSITEYYpGTTRNYVTT---VIEEDGKTYKFN-------------LLDTAGQEDYDAI 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   713 R-------NRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKcPFIVALNKIDRlydwkksPDSDVaatlkkqKKNTKD 785
Cdd:TIGR00231   68 RrlyypqvERSLRVFDIVILVLDVEEILEKQTKEIIHHADSGV-PIILVGNKIDL-------KDADL-------KTHVAS 132
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 929654105   786 EFEERAKAIIvefaqqglnaalfyenkdprtfvslVPTSAHTGDGMGSLIYLLV 839
Cdd:TIGR00231  133 EFAKLNGEPI-------------------------IPLSAETGKNIDSAFKIVE 161
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
633-841 6.85e-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: 64.93  E-value: 6.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  633 IICVLGHVDTGKTKILDKLRHT---HVQDGEAGGITQQIGATNVPLEaineqtkmiknfdreNVRIPGmlIIDTPGHESF 709
Cdd:cd04171     1 IIGTAGHIDHGKTTLIKALTGIetdRLPEEKKRGITIDLGFAYLDLP---------------DGKRLG--FIDVPGHEKF 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  710 snLRNRGSSLC--DIAILVVDIMHGLEPQTIESI---NLLKSKKCpfIVALNKIDRLydwkkspDSDVAATLKKQkkntk 784
Cdd:cd04171    64 --VKNMLAGAGgiDAVLLVVAADEGIMPQTREHLeilELLGIKKG--LVVLTKADLV-------DEDRLELVEEE----- 127
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 929654105  785 defeerakaiIVEFAqqglnAALFYENkdprtfVSLVPTSAHTGDGMGSLIYLLVEL 841
Cdd:cd04171   128 ----------ILELL-----AGTFLAD------APIFPVSSVTGEGIEELKNYLDEL 163
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
1092-1183 1.09e-10

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: 58.82  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105 1092 CKIKIlpQYIFNSR-DPIVMGVTVEAGQVKQGTPMCVPSKNfvDIGIVTSIEINHKQVDVAKKGQEVCVKIEPIpgespk 1170
Cdd:cd01342     1 LVMQV--FKVFYIPgRGRVAGGRVESGTLKVGDEIRILPKG--ITGRVTSIERFHEEVDEAKAGDIVGIGILGV------ 70
                          90
                  ....*....|...
gi 929654105 1171 mfgRHFEATDILV 1183
Cdd:cd01342    71 ---KDILTGDTLT 80
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
634-761 1.35e-10

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: 62.63  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  634 ICVLGHVDTGKTKILD---------------KLRHT-HVQDGEAGGITqqIGATNVPLEAINEQTKMIKNfdrenvripG 697
Cdd:cd01885     3 ICIIAHVDHGKTTLSDsllasagiiseklagKARYLdTREDEQERGIT--IKSSAISLYFEYEEEKMDGN---------D 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 929654105  698 MLI--IDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQT--------IESInllksKKCPFIvalNKIDRL 761
Cdd:cd01885    72 YLInlIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTetvlrqalEERV-----KPVLVI---NKIDRL 137
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
634-840 7.37e-10

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 59.22  E-value: 7.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  634 ICVLGHVDTGKTKILDKLRHTHVQDGEAGGItqqIGATnvpleaineQTKMIKNFDRENVRIpgmLIIDTPG-------H 706
Cdd:COG1100     6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLST---NGVT---------IDKKELKLDGLDVDL---VIWDTPGqdefretR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  707 ESF-SNLRNRgsslcDIAILVVDimhGLEPQTIESINLL------KSKKCPFIVALNKIDRLYDWKKSPDSDVAATLKKQ 779
Cdd:COG1100    71 QFYaRQLTGA-----SLYLFVVD---GTREETLQSLYELleslrrLGKKSPIILVLNKIDLYDEEEIEDEERLKEALSED 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 929654105  780 KkntkdefeerakaiivefaqqglnaalfyenkdprtFVSLVPTSAHTGDGMGSLIYLLVE 840
Cdd:COG1100   143 N------------------------------------IVEVVATSAKTGEGVEELFAALAE 167
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
634-760 1.36e-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: 59.14  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  634 ICVLGHVDTGKTKILDK-LRHTHVQDgEAGGITQQIGATNvPLEAINEQTKMIKN--FDRENVRIPgmlIIDTPGHESFS 710
Cdd:cd01891     5 IAIIAHVDHGKTTLVDAlLKQSGTFR-ENEEVGERVMDSN-DLERERGITILAKNtaITYKDTKIN---IIDTPGHADFG 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 929654105  711 NLRNRGSSLCDIAILVVDIMHGLEPQTieSINLLKS--KKCPFIVALNKIDR 760
Cdd:cd01891    80 GEVERVLSMVDGVLLLVDASEGPMPQT--RFVLKKAleAGLKPIVVINKIDR 129
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
634-761 1.62e-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: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  634 ICVLGHVDTGKTKILDKLRH-THVQDGEAGGITQQIGATN--------------VPLEAINEQTKmiknfDRENVripgM 698
Cdd:cd04167     3 VCIAGHLHHGKTSLLDMLIEqTHKRTPSVKLGWKPLRYTDtrkdeqergisiksNPISLVLEDSK-----GKSYL----I 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 929654105  699 LIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRL 761
Cdd:cd04167    74 NIIDTPGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDRL 136
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
633-940 5.09e-09

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 60.45  E-value: 5.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  633 IICVLGHVDTGKTKILDKL---RHTHVQDGEAGGITQQIGATNVPleaineqtkmiknfdRENVRIPGMliIDTPGHESF 709
Cdd:PRK10512    2 IIATAGHVDHGKTTLLQAItgvNADRLPEEKKRGMTIDLGYAYWP---------------QPDGRVLGF--IDVPGHEKF 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  710 snLRN--RGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFI-VALNKIDRLydwkkspDSDVAATLKKQkkntkde 786
Cdd:PRK10512   65 --LSNmlAGVGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLtVALTKADRV-------DEARIAEVRRQ------- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  787 feerakaIIVEFAQQGLNAAlfyenkdprtfvSLVPTSAHTGDGMGSLIYLLVELTQT--MLSKRlahceeLRAQVMEVK 864
Cdd:PRK10512  129 -------VKAVLREYGFAEA------------KLFVTAATEGRGIDALREHLLQLPERehAAQHR------FRLAIDRAF 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  865 ALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIvtQIRGlllpppmkeLRVKNQyekhkEVEAAQ-GVKI---LGKDLEK 940
Cdd:PRK10512  184 TVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPM--RVRG---------LHAQNQ-----PTEQAQaGQRIalnIAGDAEK 247
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
700-766 7.68e-09

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: 57.19  E-value: 7.68e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 929654105  700 IIDTPGHESFsnLRN--RGSSLCDIAILVVDIMHGLEPQT-----IESinLLKSKKcpFIVALNKIDrLYDWKK 766
Cdd:cd04166    82 IADTPGHEQY--TRNmvTGASTADLAILLVDARKGVLEQTrrhsyIAS--LLGIRH--VVVAVNKMD-LVDYDE 148
PRK13351 PRK13351
elongation factor G-like protein;
634-760 9.83e-09

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 59.58  E-value: 9.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  634 ICVLGHVDTGKTKILDKLRH----TH----VQDGEA----------GGITQQIGATNVpleaineqtkmiknfDRENVRI 695
Cdd:PRK13351   11 IGILAHIDAGKTTLTERILFytgkIHkmgeVEDGTTvtdwmpqeqeRGITIESAATSC---------------DWDNHRI 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 929654105  696 PgmlIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDR 760
Cdd:PRK13351   76 N---LIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDR 137
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
635-761 1.30e-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: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  635 CVLGHVDTGKTKILDKLrhthvqdgeaggitqqIGATNVPLEAINEQTKMIknfDRENVRIP----GMLIIDTPGHESFS 710
Cdd:cd00882     1 VVVGRGGVGKSSLLNAL----------------LGGEVGEVSDVPGTTRDP---DVYVKELDkgkvKLVLVDTPGLDEFG 61
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 929654105  711 NLRNRGSSL-----CDIAILVVDIMHG--LEPQTIESINLLKSKKCPFIVALNKIDRL 761
Cdd:cd00882    62 GLGREELARlllrgADLILLVVDSTDResEEDAKLLILRRLRKEGIPIILVGNKIDLL 119
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
635-759 1.63e-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: 55.62  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  635 CVLGHVDTGKTKILDK-LRHTHVQDGEAG--------------GITqqIGATNVPLeaineqtkMIKNFDRENVRIPgml 699
Cdd:cd01890     4 SIIAHIDHGKSTLADRlLELTGTVSEREMkeqvldsmdlererGIT--IKAQAVRL--------FYKAKDGEEYLLN--- 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  700 IIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKID 759
Cdd:cd01890    71 LIDTPGHVDFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKID 130
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
700-760 2.74e-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: 56.45  E-value: 2.74e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 929654105  700 IIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDR 760
Cdd:cd04169    75 LLDTPGHEDFSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIPIITFINKLDR 135
TypA_BipA TIGR01394
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ...
634-760 5.37e-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: 57.31  E-value: 5.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   634 ICVLGHVDTGKTKILDK-LRHTHVQDgEAGGITQQIGATNvPLEAINEQTKMIKN--FDRENVRIPgmlIIDTPGHESFS 710
Cdd:TIGR01394    4 IAIIAHVDHGKTTLVDAlLKQSGTFR-ANEAVAERVMDSN-DLERERGITILAKNtaIRYNGTKIN---IVDTPGHADFG 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 929654105   711 NLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDR 760
Cdd:TIGR01394   79 GEVERVLGMVDGVLLLVDASEGPMPQTRFVLKKALELGLKPIVVINKIDR 128
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
700-829 9.87e-08

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: 55.86  E-value: 9.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  700 IIDTPGHESFsnLRN--RGSSLCDIAILVVDIMHGLEPQT-----IESinLLKSKKcpFIVALNKIDrLYDWkkspDSDV 772
Cdd:COG2895    99 IADTPGHEQY--TRNmvTGASTADLAILLIDARKGVLEQTrrhsyIAS--LLGIRH--VVVAVNKMD-LVDY----SEEV 167
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 929654105  773 aatlkkqkkntkdeFEErAKAIIVEFAQQ-GLNAALFyenkdprtfvslVPTSAHTGD 829
Cdd:COG2895   168 --------------FEE-IVADYRAFAAKlGLEDITF------------IPISALKGD 198
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
699-890 1.25e-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: 55.46  E-value: 1.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   699 LIIDTPGHESFSnlRN--RGSSLCDIAILVVDIMHGLEPQT-----IESinLLKSKKcpFIVALNKIDrLYDWKkspdsd 771
Cdd:TIGR02034   83 IVADTPGHEQYT--RNmaTGASTADLAVLLVDARKGVLEQTrrhsyIAS--LLGIRH--VVLAVNKMD-LVDYD------ 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   772 vaatlkkqkkntkdefEERAKAIIVEFAQqglnaalFYENKDPRTfVSLVPTSAHTGDGMGSLIYL--------LVELTQ 843
Cdd:TIGR02034  150 ----------------EEVFENIKKDYLA-------FAEQLGFRD-VTFIPLSALKGDNVVSRSESmpwysgptLLEILE 205
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 929654105   844 TMLSKRLAHCEELRAQVMEVKAlPGM------GTtidviLINGRLKEGDTIIV 890
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 ...
634-761 1.62e-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: 53.78  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  634 ICVLGHVDTGKTKILDKLRHTHvqdgeagGITQQIGAT--------NVPLE---AINEQTKMIKnFDRENVRIPgmlIID 702
Cdd:cd04168     2 IGILAHVDAGKTTLTESLLYTS-------GAIRELGSVdkgttrtdSMELErqrGITIFSAVAS-FQWEDTKVN---IID 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 929654105  703 TPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRL 761
Cdd:cd04168    71 TPGHMDFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIFVNKIDRA 129
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
701-789 1.07e-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: 49.77  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  701 IDTPG-HESFSNLRNR-----GSSL--CDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLydwkkSPDSDV 772
Cdd:cd04163    56 VDTPGiHKPKKKLGERmvkaaWSALkdVDLVLFVVDASEWIGEGDEFILELLKKSKTPVILVLNKIDLV-----KDKEDL 130
                          90
                  ....*....|....*..
gi 929654105  773 AATLKKQKKntKDEFEE 789
Cdd:cd04163   131 LPLLEKLKE--LHPFAE 145
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
700-759 1.45e-06

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 52.22  E-value: 1.45e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 929654105  700 IIDTPGHESFSnlRN--RGSSLCDIAILVVDIMHGLEPQT-----IESinLLKSKKcpFIVALNKID 759
Cdd:PRK05124  111 IADTPGHEQYT--RNmaTGASTCDLAILLIDARKGVLDQTrrhsfIAT--LLGIKH--LVVAVNKMD 171
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
700-895 2.11e-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: 51.47  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  700 IIDTPGHESFsnLRN--RGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCP-FIVALNKIDRL-YDwkkspdsdvaat 775
Cdd:COG5256    89 IIDAPGHRDF--VKNmiTGASQADAAILVVSAKDGVMGQTREHAFLARTLGINqLIVAVNKMDAVnYS------------ 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  776 lKKQKKNTKDEFEERAKAIivefaqqGlnaalfYENKDprtfVSLVPTSAHTGDGmgsliylLVELTQTM-------LSK 848
Cdd:COG5256   155 -EKRYEEVKEEVSKLLKMV-------G------YKVDK----IPFIPVSAWKGDN-------VVKKSDNMpwyngptLLE 209
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 929654105  849 RLAHCEE--------LRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIV--PGVEG 895
Cdd:COG5256   210 ALDNLKEpekpvdkpLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFmpAGVVG 266
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
698-757 3.30e-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: 47.23  E-value: 3.30e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 929654105   698 MLIIDTPGH-ESFSNLRNRGSSL-----CDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNK 757
Cdd:pfam01926   48 IILVDTPGLiEGASEGEGLGRAFlaiieADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
PRK10218 PRK10218
translational GTPase TypA;
627-760 3.46e-06

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 51.25  E-value: 3.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  627 EKLRApiICVLGHVDTGKTKILDKLRHthvQDG--EAGGITQQIGATNVPLEAINEQTKMIKN--FDRENVRIPgmlIID 702
Cdd:PRK10218    3 EKLRN--IAIIAHVDHGKTTLVDKLLQ---QSGtfDSRAETQERVMDSNDLEKERGITILAKNtaIKWNDYRIN---IVD 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 929654105  703 TPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDR 760
Cdd:PRK10218   75 TPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDR 132
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
712-841 3.76e-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: 48.91  E-value: 3.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  712 LRNRgSSLCdIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLydwKKSPdsdvaatLKKQKKNTKDEFEERA 791
Cdd:COG0218   100 LEGR-ENLK-GVVLLIDIRHPPKELDLEMLEWLDEAGIPFLIVLTKADKL---KKSE-------LAKQLKAIKKALGKDP 167
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 929654105  792 KAiivefaqqglnaalfyenkdprtfVSLVPTSAHTGDGMGSLIYLLVEL 841
Cdd:COG0218   168 AA------------------------PEVILFSSLKKEGIDELRAAIEEW 193
era PRK00089
GTPase Era; Reviewed
701-766 3.88e-06

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 50.05  E-value: 3.88e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 929654105  701 IDTPG-HESFSNLrNRG------SSL--CDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLYDWKK 766
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 ...
696-842 4.16e-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: 48.28  E-value: 4.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  696 PGMLIIDTPG----------HESFSN-----LRNRgSSLCdIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDR 760
Cdd:cd01876    45 DKFRLVDLPGygyakvskevREKWGKlieeyLENR-ENLK-GVVLLIDARHGPTPIDLEMLEFLEELGIPFLIVLTKADK 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  761 LydwKKSPdsdvaatLKKQKKNTKDEFEERAkaiivefaqqglnaalfyenkdprTFVSLVPTSAHTGDGMGSLIYLLVE 840
Cdd:cd01876   123 L---KKSE-------LAKVLKKIKEELNLFN------------------------ILPPVILFSSKKGTGIDELRALIAE 168

                  ..
gi 929654105  841 LT 842
Cdd:cd01876   169 WL 170
prfC TIGR00503
peptide chain release factor 3; This translation releasing factor, RF-3 (prfC) was originally ...
636-760 8.45e-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: 49.90  E-value: 8.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   636 VLGHVDTGKTKILDKLRHTHVQDGEAGGIT---QQIGATNVPLEAINEQ----TKMIKNFDRENVRIPgmlIIDTPGHES 708
Cdd:TIGR00503   16 IISHPDAGKTTITEKVLLYGGAIQTAGAVKgrgSQRHAKSDWMEMEKQRgisiTTSVMQFPYRDCLVN---LLDTPGHED 92
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 929654105   709 FSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDR 760
Cdd:TIGR00503   93 FSEDTYRTLTAVDNCLMVIDAAKGVETRTRKLMEVTRLRDTPIFTFMNKLDR 144
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
698-841 1.74e-05

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 48.06  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  698 MLIIDTPG-HESfSNLRNRG------SSL--CDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLydwkksp 768
Cdd:COG1159    53 IVFVDTPGiHKP-KRKLGRRmnkaawSALedVDVILFVVDATEKIGEGDEFILELLKKLKTPVILVINKIDLV------- 124
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 929654105  769 dsdvaatlkkqkknTKDEFEERAKAiivefaqqglnaalfYENKDPrtFVSLVPTSAHTGDGMGSLIYLLVEL 841
Cdd:COG1159   125 --------------KKEELLPLLAE---------------YSELLD--FAEIVPISALKGDNVDELLDEIAKL 166
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
639-761 3.04e-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: 47.10  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  639 HVDTGKT----KIL---DKLRHTH-VQDGEAG----------GITQQIGATNvpleaineqtkmiknFDRENVRIPgmlI 700
Cdd:cd01886     7 HIDAGKTttteRILyytGRIHKIGeVHGGGATmdwmeqererGITIQSAATT---------------CFWKDHRIN---I 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 929654105  701 IDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRL 761
Cdd:cd01886    69 IDTPGHVDFTIEVERSLRVLDGAVAVFDAVAGVQPQTETVWRQADRYGVPRIAFVNKMDRT 129
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
622-760 3.98e-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: 47.73  E-value: 3.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  622 KNVNTEKLRapIICVLGHVDTGKT----------KILDKLRHTHvqDGEA----------GGITqqIGATNVPLE----A 677
Cdd:COG0480     2 AEYPLEKIR--NIGIVAHIDAGKTtlterilfytGAIHRIGEVH--DGNTvmdwmpeeqeRGIT--ITSAATTCEwkghK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  678 INeqtkmiknfdrenvripgmlIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNK 757
Cdd:COG0480    76 IN--------------------IIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQADKYGVPRIVFVNK 135

                  ...
gi 929654105  758 IDR 760
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 ...
856-947 6.16e-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: 42.64  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  856 LRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIVPGVegPIVTQIRGLLLPppmkelrvknqYEKHKEVEAAQGVKILG 935
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPK--GITGRVTSIERF-----------HEEVDEAKAGDIVGIGI 67
                          90
                  ....*....|..
gi 929654105  936 KDLEKTLAGLPL 947
Cdd:cd01342    68 LGVKDILTGDTL 79
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
700-895 6.26e-05

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 46.84  E-value: 6.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  700 IIDTPGHESFsnLRN--RGSSLCDIAILVV---DIMhGLEPQTIESINLLKSKKCP-FIVALNKIDRL-YDWKKspdsdv 772
Cdd:PRK12317   88 IVDCPGHRDF--VKNmiTGASQADAAVLVVaadDAG-GVMPQTREHVFLARTLGINqLIVAINKMDAVnYDEKR------ 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  773 aatlkkqkkntkdeFEErakaiIVEFAQQGLNAALFYENKdprtfVSLVPTSAHTGDGmgsliylLVELTQTM------- 845
Cdd:PRK12317  159 --------------YEE-----VKEEVSKLLKMVGYKPDD-----IPFIPVSAFEGDN-------VVKKSENMpwyngpt 207
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  846 LSKRLAHCEE--------LRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIV--PGVEG 895
Cdd:PRK12317  208 LLEALDNLKPpekptdkpLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVFmpAGVVG 267
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
639-760 7.78e-05

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 46.94  E-value: 7.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  639 HVDTGKTKILDK-LRHTHV-QDGEAG--------------GITqqIGATNVpleAINeqtkmiknfdRENVRIPgmlIID 702
Cdd:COG1217    14 HVDHGKTTLVDAlLKQSGTfRENQEVaervmdsndlererGIT--ILAKNT---AVR----------YKGVKIN---IVD 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 929654105  703 TPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQT-------IEsINLlkskkcPFIVALNKIDR 760
Cdd:COG1217    76 TPGHADFGGEVERVLSMVDGVLLLVDAFEGPMPQTrfvlkkaLE-LGL------KPIVVINKIDR 133
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
700-764 9.98e-05

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 46.46  E-value: 9.98e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 929654105  700 IIDTPGHESFSnlRN--RGSSLCDIAILVVDIMHGLEPQT-----IESinLLKSKKcpFIVALNKIDrLYDW 764
Cdd:PRK05506  108 VADTPGHEQYT--RNmvTGASTADLAIILVDARKGVLTQTrrhsfIAS--LLGIRH--VVLAVNKMD-LVDY 172
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
700-760 1.38e-04

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 46.27  E-value: 1.38e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 929654105  700 IIDTPGHESF-----SNLRnrgssLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDR 760
Cdd:PRK12740   64 LIDTPGHVDFtgeveRALR-----VLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRIIFVNKMDR 124
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
634-841 1.62e-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: 44.59  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  634 ICVLGHVDTGKTKILDKL-----------------RHTH-VQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRI 695
Cdd:cd04165     2 VAVVGNVDAGKSTLLGVLtqgeldngrgkarlnlfRHKHeVESGRTSSVSNDILGFDSDGEVVNYPDNHLGELDVEICEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  696 PGMLI--IDTPGHESF--SNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDrlydwkKSPDSD 771
Cdd:cd04165    82 SSKVVtfIDLAGHERYlkTTVFGMTGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVVVTKID------MTPANV 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 929654105  772 VAATLKKQKKNTKDEFeERAKAIIVEFAQQGLNAALFYenkdprTFVSLVP---TSAHTGDGMGSLIYLLVEL 841
Cdd:cd04165   156 LQETLKDLKRLLKSPG-VRKLPVPVKSKDDVVLSASNL------SSGRVVPifqVSNVTGEGLDLLRRFLNLL 221
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
699-841 2.08e-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: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  699 LIIDTPGHESFSNL---RNRGSSL-----CDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDrlydwkkSPDS 770
Cdd:cd01894    48 ILIDTGGIEPDDEGiskEIREQAEiaieeADVILFVVDGREGLTPADEEIAKYLRKSKKPVILVVNKID-------NIKE 120
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 929654105  771 DVAATlkkqkkntkdefeerakaiivEFAQQGLnaalfyenKDPrtfvslVPTSAHTGDGMGSLIYLLVEL 841
Cdd:cd01894   121 EEEAA---------------------EFYSLGF--------GEP------IPISAEHGRGIGDLLDAILEL 156
prfC PRK00741
peptide chain release factor 3; Provisional
700-760 4.02e-04

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 44.35  E-value: 4.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 929654105  700 IIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDR 760
Cdd:PRK00741   83 LLDTPGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTPIFTFINKLDR 143
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
870-944 4.50e-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: 39.94  E-value: 4.50e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 929654105   870 GTTIDVILINGRLKEGDTIIVPGV---EGPIVTQIRGLLlpPPMKELRVknqyekhKEVEAAQGVKILGKDLEKTLAG 944
Cdd:pfam03144    1 GTVATGRVESGTLKKGDKVRILPNgtgKKKIVTRVTSLL--MFHAPLRE-------AVAGDNAGLILAGVGLEDIRVG 69
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
634-797 5.10e-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: 44.50  E-value: 5.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   634 ICVLGHVDTGKTKILDKLRhthvqdGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRI------PGMLI--IDTPG 705
Cdd:TIGR00490   22 IGIVAHIDHGKTTLSDNLL------AGAGMISEELAGQQLYLDFDEQEQERGITINAANVSMvheyegNEYLInlIDTPG 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   706 HESFSNLRNRGSSLCDIAILVVDIMHGLEPQTiESI--NLLKSKKCPfIVALNKIDRLYdwkkspdsdvaatlkKQKKNT 783
Cdd:TIGR00490   96 HVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQT-ETVlrQALKENVKP-VLFINKVDRLI---------------NELKLT 158
                          170
                   ....*....|....
gi 929654105   784 KDEFEERAKAIIVE 797
Cdd:TIGR00490  159 PQELQERFIKIITE 172
YeeP COG3596
Predicted GTPase [General function prediction only];
682-860 5.18e-04

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 43.60  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  682 TKMIKNFDRENVRIPGMLIIDTPGHESfSNLRNRG-------SSLCDIAILVVDIM---HGLEPQTIESInLLKSKKCPF 751
Cdd:COG3596    74 TREIQRYRLESDGLPGLVLLDTPGLGE-VNERDREyrelrelLPEADLILWVVKADdraLATDEEFLQAL-RAQYPDPPV 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  752 IVALNKIDRLY---DWKKSPDSDVAAtlkkQKKNTKDEFEERAKaiivefaqqglnaaLFYENKDPrtfvsLVPTSA--- 825
Cdd:COG3596   152 LVVLTQVDRLEperEWDPPYNWPSPP----KEQNIRRALEAIAE--------------QLGVPIDR-----VIPVSAaed 208
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 929654105  826 HTGDGMGSLIYLLVELTQTMLSKRLAHCeeLRAQV 860
Cdd:COG3596   209 RTGYGLEELVDALAEALPEAKRSRLARL--LRAKA 241
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
699-781 6.82e-04

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: 41.46  E-value: 6.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  699 LIIDTPG-HESFSNLRNRGSSL------CDIAILVVDIMHGLEPQTIESINLLKSKKcPFIVALNKIDRLydwkksPDSD 771
Cdd:cd00880    49 VLIDTPGlDEEGGLGRERVEEArqvadrADLVLLVVDSDLTPVEEEAKLGLLRERGK-PVLLVLNKIDLV------PESE 121
                          90
                  ....*....|
gi 929654105  772 VAATLKKQKK 781
Cdd:cd00880   122 EEELLRERKL 131
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
634-760 7.15e-04

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: 42.97  E-value: 7.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  634 ICVLGHVDTGKTKILDKLRHThvqdgeAGGITQQ--IGATNVPLEAINEQTKM-------IKNFDRENVRIpgmLIIDTP 704
Cdd:cd04170     2 IALVGHSGSGKTTLAEALLYA------TGAIDRLgrVEDGNTVSDYDPEEKKRkmsietsVAPLEWNGHKI---NLIDTP 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 929654105  705 G-----HESFSNLRnrgssLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDR 760
Cdd:cd04170    73 GyadfvGETLSALR-----AVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDR 128
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
688-841 9.95e-04

EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 41.26  E-value: 9.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  688 FDRENVRipgMLIIDTPG----------HESFSNLRNRGS-SLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALN 756
Cdd:cd01895    45 FEYDGQK---YTLIDTAGirkkgkvtegIEKYSVLRTLKAiERADVVLLVLDASEGITEQDLRIAGLILEEGKALIIVVN 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  757 KIDrlydwkkspdsdvaatLKKQKKNTKDEFEERakaiivefaqqgLNAALFYENkdprtFVSLVPTSAHTGDGMGSLIY 836
Cdd:cd01895   122 KWD----------------LVEKDEKTMKEFEKE------------LRRKLPFLD-----YAPIVFISALTGQGVDKLFD 168

                  ....*
gi 929654105  837 LLVEL 841
Cdd:cd01895   169 AIKEV 173
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
634-759 1.59e-03

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: 39.41  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   634 ICVLGHVDTGKTKILDKLRHTHVQDGEaggiTQQIGATNVpleaineqTKMIKNFDRENVRIpgMLII-DTPGHESFSNL 712
Cdd:pfam08477    2 VVLLGDSGVGKTSLLKRFVDDTFDPKY----KSTIGVDFK--------TKTVLENDDNGKKI--KLNIwDTAGQERFRSL 67
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 929654105   713 RN---RGSSlcdIAILVVDImhglepQTIES----INLLK--SKKCPFIVALNKID 759
Cdd:pfam08477   68 HPfyyRGAA---AALLVYDS------RTFSNlkywLRELKkyAGNSPVILVGNKID 114
PLN03126 PLN03126
Elongation factor Tu; Provisional
634-763 1.61e-03

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 42.68  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  634 ICVLGHVDTGKTKILDKLrhTHVQDGEAGGITQQIGATNVPLE------AINEQTKMIKNFDRENVRIpgmliiDTPGHE 707
Cdd:PLN03126   84 IGTIGHVDHGKTTLTAAL--TMALASMGGSAPKKYDEIDAAPEerargiTINTATVEYETENRHYAHV------DCPGHA 155
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 929654105  708 SFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCP-FIVALNKIDRLYD 763
Cdd:PLN03126  156 DYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPnMVVFLNKQDQVDD 212
PRK13768 PRK13768
GTPase; Provisional
696-856 1.76e-03

GTPase; Provisional


Pssm-ID: 237498 [Multi-domain]  Cd Length: 253  Bit Score: 41.39  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  696 PGMLIIDTPGH-ESFSnLRNRGSSLCD--------IAILVVDIMHGLEPQTIESINLLKSK-----KCPFIVALNKID-- 759
Cdd:PRK13768   97 ADYVLVDTPGQmELFA-FRESGRKLVErlsgssksVVVFLIDAVLAKTPSDFVSLLLLALSvqlrlGLPQIPVLNKADll 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  760 ------RLYDWKKSPDSdVAATLKKQKKNTKDEFEERAKAIivefaqqgLNAALFYEnkdprtfvsLVPTSAHTGDGMGS 833
Cdd:PRK13768  176 seeeleRILKWLEDPEY-LLEELKLEKGLQGLLSLELLRAL--------EETGLPVR---------VIPVSAKTGEGFDE 237
                         170       180
                  ....*....|....*....|...
gi 929654105  834 LIYLLVELtqtmlskrLAHCEEL 856
Cdd:PRK13768  238 LYAAIQEV--------FCGGEDL 252
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
700-831 2.13e-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: 40.94  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  700 IIDTPGHESF-SNLRNrGSSLCDIAILVVDIMHG-------LEPQTIESINLLKS---KKcpFIVALNKIDR-LYDWKks 767
Cdd:cd01883    81 IIDAPGHRDFvKNMIT-GASQADVAVLVVSARKGefeagfeKGGQTREHALLARTlgvKQ--LIVAVNKMDDvTVNWS-- 155
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 929654105  768 pdsdvaatlkkqkkntKDEFEErAKAIIVEFAQQglnaaLFYENKDprtfVSLVPTSAHTGDGM 831
Cdd:cd01883   156 ----------------QERYDE-IKKKVSPFLKK-----VGYNPKD----VPFIPISGFTGDNL 193
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
701-763 2.44e-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: 40.64  E-value: 2.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 929654105  701 IDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCP-FIVALNKIDRLYD 763
Cdd:cd01884    70 VDCPGHADYIKNMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPyIVVFLNKADMVDD 133
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
633-904 2.51e-03

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 41.76  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  633 IICVLGHVDTGKTKILDKL------RHTHvqdgEAG-GITQQIGATNVPL------------------EAINEQTKMIKn 687
Cdd:PRK04000   11 NIGMVGHVDHGKTTLVQALtgvwtdRHSE----ELKrGITIRLGYADATIrkcpdceepeayttepkcPNCGSETELLR- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  688 fdrenvRIPgmlIIDTPGHESFSNLRNRGSSLCDIAILVVDI-MHGLEPQTIE---SINLLKSKKcpFIVALNKIDrLYD 763
Cdd:PRK04000   86 ------RVS---FVDAPGHETLMATMLSGAALMDGAILVIAAnEPCPQPQTKEhlmALDIIGIKN--IVIVQNKID-LVS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  764 wkkspdsdvaatlkkqKKNTKDEFEErakaiIVEFAqQGLNAalfyENkdprtfVSLVPTSAHTGDGMGSLIYLLVELTQ 843
Cdd:PRK04000  154 ----------------KERALENYEQ-----IKEFV-KGTVA----EN------APIIPVSALHKVNIDALIEAIEEEIP 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  844 TmlSKRlahceelraqvmEVKALPGM-----------GTTID-----VI---LINGRLKEGDTI-IVPGVEG-------- 895
Cdd:PRK04000  202 T--PER------------DLDKPPRMyvarsfdvnkpGTPPEklkggVIggsLIQGVLKVGDEIeIRPGIKVeeggktkw 267
                         330
                  ....*....|
gi 929654105  896 -PIVTQIRGL 904
Cdd:PRK04000  268 ePITTKIVSL 277
tufA CHL00071
elongation factor Tu
701-763 2.64e-03

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 41.48  E-value: 2.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 929654105  701 IDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCP-FIVALNKIDRLYD 763
Cdd:CHL00071   80 VDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPnIVVFLNKEDQVDD 143
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
701-759 3.48e-03

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


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 41.54  E-value: 3.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 929654105  701 IDTPGHESFSNLRNRgsSL--CDIAILVVDIMHGLEPQTIESINL-----LKskkcpFIVALNKID 759
Cdd:COG0481    78 IDTPGHVDFSYEVSR--SLaaCEGALLVVDASQGVEAQTLANVYLalendLE-----IIPVINKID 136
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
634-760 5.46e-03

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 40.86  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  634 ICVLGHVDTGKTKILDKL---------------RHTHVQDGEAG-GITqqIGATNVPL--EAINEQTKMIKNFDRENvri 695
Cdd:PLN00116   22 MSVIAHVDHGKSTLTDSLvaaagiiaqevagdvRMTDTRADEAErGIT--IKSTGISLyyEMTDESLKDFKGERDGN--- 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 929654105  696 pGMLI--IDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDR 760
Cdd:PLN00116   97 -EYLInlIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDR 162
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
634-763 6.05e-03

translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]


Pssm-ID: 129576 [Multi-domain]  Cd Length: 394  Bit Score: 40.53  E-value: 6.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105   634 ICVLGHVDTGKTKILDKLRHTHVQDGEAGGIT-QQIgaTNVPLE---AINEQTKMIKnFDRENVRIPGmliIDTPGHESF 709
Cdd:TIGR00485   15 VGTIGHVDHGKTTLTAAITTVLAKEGGAAARAyDQI--DNAPEEkarGITINTAHVE-YETETRHYAH---VDCPGHADY 88
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 929654105   710 SNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVA-LNKIDRLYD 763
Cdd:TIGR00485   89 VKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVfLNKCDMVDD 143
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
688-835 9.19e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 40.03  E-value: 9.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  688 FDRENVRIpgmLIIDTPG-------HES---FSNLRnrgsSL-----CDIAILVVDIMHGLEPQ--TIesINLLKSKKCP 750
Cdd:PRK00093  216 FERDGQKY---TLIDTAGirrkgkvTEGvekYSVIR----TLkaierADVVLLVIDATEGITEQdlRI--AGLALEAGRA 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654105  751 FIVALNKIDRLydwkkspdsdvaatlkkqKKNTKDEFEERAKAiivEFAQqgLNaalfyenkdprtFVSLVPTSAHTGDG 830
Cdd:PRK00093  287 LVIVVNKWDLV------------------DEKTMEEFKKELRR---RLPF--LD------------YAPIVFISALTGQG 331

                  ....*
gi 929654105  831 MGSLI 835
Cdd:PRK00093  332 VDKLL 336
 
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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