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Conserved domains on  [gi|209881947|ref|XP_002142411|]
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U5 small nuclear ribonucleoprotein subunit [Cryptosporidium muris RN66]

Protein Classification

116 kDa U5 small nuclear ribonucleoprotein component( domain architecture ID 20749967)

116 kDa U5 small nuclear ribonucleoprotein component is required for pre-mRNA splicing as component of the spliceosome; belongs to the classic translation factor GTPase family, EF-G/EF-2 subfamily

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13351 super family cl46912
elongation factor G-like protein;
131-1032 0e+00

elongation factor G-like protein;


The actual alignment was detected with superfamily member PTZ00416:

Pssm-ID: 481252 [Multi-domain]  Cd Length: 836  Bit Score: 683.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  131 ITFSYDYMKDMMKQPKLIRNIAIVGDLHHGKTSLIDMLVR----ITHKFSKLKteklnRYTDSRIDEQEREISIKATPIS 206
Cdd:PTZ00416    2 VNFTVDQIREIMDNPDQIRNMSVIAHVDHGKSTLTDSLVCkagiISSKNAGDA-----RFTDTRADEQERGITIKSTGIS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  207 LILPNSIN-----KSYLLNIIDTPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDR 281
Cdd:PTZ00416   77 LYYEHDLEdgddkQPFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  282 LILELRIPPNDAYCKIGYIINEANEVVKSFyslyraDKNEIDRLIFSPEKGNVGFASGKFGFCFTLQSFARMYLKESYTT 361
Cdd:PTZ00416  157 AILELQLDPEEIYQNFVKTIENVNVIIATY------NDELMGDVQVYPEKGTVAFGSGLQGWAFTLTTFARIYAKKFGVE 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  362 TSELMQNidsfcnnLWGDLYYSKSLGKFLRSSNESTYKFC--SFVQFILEPLYKIFIYSLSEQPKVLSTLLPSIGVYLSR 439
Cdd:PTZ00416  231 ESKMMER-------LWGDNFFDAKTKKWIKDETNAQGKKLkrAFCQFILDPICQLFDAVMNEDKEKYDKMLKSLNISLTG 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  440 SELKKSPTSILDTICKRFFGGANAFTDLIVNNISNPLEASPIRTFNEYTGPQNDLLAQRIRNLSYDSPAVAFVTKHYHTS 519
Cdd:PTZ00416  304 EDKELTGKPLLKAVMQKWLPAADTLLEMIVDHLPSPKEAQKYRVENLYEGPMDDEAANAIRNCDPNGPLMMYISKMVPTS 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  520 SMDSFYSLCRVYCGILRKGDVVKVLGESYTAEDPEDMSICTIQNIWIFQARYKVEINEVPAGNWTLISGLNNSVIKTATI 599
Cdd:PTZ00416  384 DKGRFYAFGRVFSGTVATGQKVRIQGPNYVPGKKEDLFEKNIQRTVLMMGRYVEQIEDVPCGNTVGLVGVDQYLVKSGTI 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  600 icdTTrsnkynnnkpykevdelscknikdeiliedqrnqyltqqNDDLHILRPLKFPTNNVIRLACEPVNPSELPKMLEG 679
Cdd:PTZ00416  464 ---TT---------------------------------------SETAHNIRDMKYSVSPVVRVAVEPKNPKDLPKLVEG 501
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  680 LKSLDKAYPILKTKVEESGEHVIFGTGELQLDCIMHDLRRLYGNLDVKVSDPSVQLCETVLDTSVVKSFGDSSNKQNRIY 759
Cdd:PTZ00416  502 LKRLAKSDPLVVCTTEESGEHIVAGCGELHVEICLKDLEDDYANIDIIVSDPVVSYRETVTEESSQTCLSKSPNKHNRLY 581
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  760 IIAEPLEKGLAEDIENGIVkfydcIDNESTKYHQQILKDKYNWDHLALRSLWAFGPTFEGANVLIDDTlssiTDKKSLYE 839
Cdd:PTZ00416  582 MKAEPLTEELAEAIEEGKV-----GPEDDPKERANFLADKYEWDKNDARKIWCFGPENKGPNVLVDVT----KGVQYMNE 652
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  840 IKENIIQGFQWATREGPLLEENVRNVKFKILDVSLASNKASRGTGQIIPAARRACYTAMLMASPRLMEPICLVEIVCPSE 919
Cdd:PTZ00416  653 IKDSCVSAFQWATKEGVLCDENMRGIRFNILDVTLHADAIHRGAGQIIPTARRVFYACELTASPRLLEPMFLVDITAPED 732
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  920 SHNAIANVLLRRRGHCGKENPIPGTPLVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWALVPGNPLDRNiilrpl 999
Cdd:PTZ00416  733 AMGGIYSVLNRRRGVVIGEEQRPGTPLSNIKAYLPVAESFGFTAALRAATSGQAFPQCVFDHWQVVPGDPLEPG------ 806
                         890       900       910
                  ....*....|....*....|....*....|....
gi 209881947 1000 epapipHLAREFLLKTRRRKGLSEDV-SVQNFID 1032
Cdd:PTZ00416  807 ------SKANEIVLSIRKRKGLKPEIpDLDNYLD 834
EFTUD2 pfam16004
116 kDa U5 small nuclear ribonucleoprotein component N-terminus;
5-126 1.66e-25

116 kDa U5 small nuclear ribonucleoprotein component N-terminus;


:

Pssm-ID: 464968  Cd Length: 76  Bit Score: 100.69  E-value: 1.66e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947     5 EIYDEFGNYIGTEsesnldleisLDEDEDQSsdsqknpthdptevddvkminginrivdgmdiemdneAIILHEHKEYYE 84
Cdd:pfam16004    1 DLYDEFGNYIGPE----------LDSDDESN-------------------------------------AVVLHEDKQYYP 33
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 209881947    85 DADKIFGKDVEILFEDEDMHHIDTPTIVPLKDNKFDLVEGDI 126
Cdd:pfam16004   34 SAEEVYGPDVETLVQEEDAQPLTEPIIAPVKQKKFAVEEKDL 75
 
Name Accession Description Interval E-value
PTZ00416 PTZ00416
elongation factor 2; Provisional
131-1032 0e+00

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 683.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  131 ITFSYDYMKDMMKQPKLIRNIAIVGDLHHGKTSLIDMLVR----ITHKFSKLKteklnRYTDSRIDEQEREISIKATPIS 206
Cdd:PTZ00416    2 VNFTVDQIREIMDNPDQIRNMSVIAHVDHGKSTLTDSLVCkagiISSKNAGDA-----RFTDTRADEQERGITIKSTGIS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  207 LILPNSIN-----KSYLLNIIDTPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDR 281
Cdd:PTZ00416   77 LYYEHDLEdgddkQPFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  282 LILELRIPPNDAYCKIGYIINEANEVVKSFyslyraDKNEIDRLIFSPEKGNVGFASGKFGFCFTLQSFARMYLKESYTT 361
Cdd:PTZ00416  157 AILELQLDPEEIYQNFVKTIENVNVIIATY------NDELMGDVQVYPEKGTVAFGSGLQGWAFTLTTFARIYAKKFGVE 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  362 TSELMQNidsfcnnLWGDLYYSKSLGKFLRSSNESTYKFC--SFVQFILEPLYKIFIYSLSEQPKVLSTLLPSIGVYLSR 439
Cdd:PTZ00416  231 ESKMMER-------LWGDNFFDAKTKKWIKDETNAQGKKLkrAFCQFILDPICQLFDAVMNEDKEKYDKMLKSLNISLTG 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  440 SELKKSPTSILDTICKRFFGGANAFTDLIVNNISNPLEASPIRTFNEYTGPQNDLLAQRIRNLSYDSPAVAFVTKHYHTS 519
Cdd:PTZ00416  304 EDKELTGKPLLKAVMQKWLPAADTLLEMIVDHLPSPKEAQKYRVENLYEGPMDDEAANAIRNCDPNGPLMMYISKMVPTS 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  520 SMDSFYSLCRVYCGILRKGDVVKVLGESYTAEDPEDMSICTIQNIWIFQARYKVEINEVPAGNWTLISGLNNSVIKTATI 599
Cdd:PTZ00416  384 DKGRFYAFGRVFSGTVATGQKVRIQGPNYVPGKKEDLFEKNIQRTVLMMGRYVEQIEDVPCGNTVGLVGVDQYLVKSGTI 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  600 icdTTrsnkynnnkpykevdelscknikdeiliedqrnqyltqqNDDLHILRPLKFPTNNVIRLACEPVNPSELPKMLEG 679
Cdd:PTZ00416  464 ---TT---------------------------------------SETAHNIRDMKYSVSPVVRVAVEPKNPKDLPKLVEG 501
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  680 LKSLDKAYPILKTKVEESGEHVIFGTGELQLDCIMHDLRRLYGNLDVKVSDPSVQLCETVLDTSVVKSFGDSSNKQNRIY 759
Cdd:PTZ00416  502 LKRLAKSDPLVVCTTEESGEHIVAGCGELHVEICLKDLEDDYANIDIIVSDPVVSYRETVTEESSQTCLSKSPNKHNRLY 581
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  760 IIAEPLEKGLAEDIENGIVkfydcIDNESTKYHQQILKDKYNWDHLALRSLWAFGPTFEGANVLIDDTlssiTDKKSLYE 839
Cdd:PTZ00416  582 MKAEPLTEELAEAIEEGKV-----GPEDDPKERANFLADKYEWDKNDARKIWCFGPENKGPNVLVDVT----KGVQYMNE 652
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  840 IKENIIQGFQWATREGPLLEENVRNVKFKILDVSLASNKASRGTGQIIPAARRACYTAMLMASPRLMEPICLVEIVCPSE 919
Cdd:PTZ00416  653 IKDSCVSAFQWATKEGVLCDENMRGIRFNILDVTLHADAIHRGAGQIIPTARRVFYACELTASPRLLEPMFLVDITAPED 732
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  920 SHNAIANVLLRRRGHCGKENPIPGTPLVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWALVPGNPLDRNiilrpl 999
Cdd:PTZ00416  733 AMGGIYSVLNRRRGVVIGEEQRPGTPLSNIKAYLPVAESFGFTAALRAATSGQAFPQCVFDHWQVVPGDPLEPG------ 806
                         890       900       910
                  ....*....|....*....|....*....|....
gi 209881947 1000 epapipHLAREFLLKTRRRKGLSEDV-SVQNFID 1032
Cdd:PTZ00416  807 ------SKANEIVLSIRKRKGLKPEIpDLDNYLD 834
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
136-1022 3.52e-98

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: 326.47  E-value: 3.52e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   136 DYMKDMMKQPKLIRNIAIVGDLHHGKTSLIDMLVRITHKFSK-LKTEKLnrYTDSRIDEQEREISIKATPISLILPNSIN 214
Cdd:TIGR00490    7 DKIKELMWKPKFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEeLAGQQL--YLDFDEQEQERGITINAANVSMVHEYEGN 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   215 KsYLLNIIDTPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDRLILELRIPPNDAY 294
Cdd:TIGR00490   85 E-YLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRLINELKLTPQELQ 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   295 CKIGYIINEANEVVKSFYSLYRADKNEIDrlifsPEKGNVGFASGKFGFCFTLQSfarmyLKESYTTTSELmqnidsfcn 374
Cdd:TIGR00490  164 ERFIKIITEVNKLIKAMAPEEFRDKWKVR-----VEDGSVAFGSAYYNWAISVPS-----MKKTGIGFKDI--------- 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   375 nlwgdlyyskslgkflrssnestYKFCSfvqfileplykifiyslSEQPKVLSTLLPSIGVYLsrselkksptsildtic 454
Cdd:TIGR00490  225 -----------------------YKYCK-----------------EDKQKELAKKSPLHQVVL----------------- 247
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   455 krffgganaftDLIVNNISNPLEASPIRTFNEYTGPQNDLLAQRIRNLSYDSPAVAFVTK---HYHTSSMdsfySLCRVY 531
Cdd:TIGR00490  248 -----------DMVIRHLPSPIEAQKYRIPVIWKGDLNSEVGKAMLNCDPKGPLALMITKivvDKHAGEV----AVGRLY 312
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   532 CGILRKGDVVKVLGESYTAEdpedmsictIQNIWIFQARYKVEINEVPAGNWTLISGLNNSVikTATIICDTTRsnkynN 611
Cdd:TIGR00490  313 SGTIRPGMEVYIVDRKAKAR---------IQQVGVYMGPERVEVDEIPAGNIVAVIGLKDAV--AGETICTTVE-----N 376
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   612 NKPYKEVDelscknikdeiliedqrnqyltqqnddlHILRPlkfptnnVIRLACEPVNPSELPKMLEGLKSLDKAYPILK 691
Cdd:TIGR00490  377 ITPFESIK----------------------------HISEP-------VVTVAIEAKNTKDLPKLIEVLRQVAKEDPTVH 421
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   692 TKV-EESGEHVIFGTGELQLDCIMHDLRRLYGnLDVKVSDPSVQLCETVLDTSVVKSfGDSSNKQNRIYIIAEPLEKGLA 770
Cdd:TIGR00490  422 VEInEETGEHLISGMGELHLEIIVEKIREDYG-LDVETSPPIVVYRETVTGTSPVVE-GKSPNKHNRFYIVVEPLEESVI 499
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   771 EDIENGIVKFYDCIDNESTKYHQQILKDKYNwdhlaLRSLWAFgptFEGaNVLIDDTLSSitdkKSLYEIKENIIQGFQW 850
Cdd:TIGR00490  500 QAFKEGKIVDMKMKKKERRRLLIEAGMDSEE-----AARVEEY---YEG-NLFINMTRGI----QYLDETKELILEGFRE 566
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   851 ATREGPLLEENVRNVKFKILDVSLASNKASRGTGQIIPAARRACYTAMLMASPRLMEPICLVEIVCPSESHNAIANVLLR 930
Cdd:TIGR00490  567 AMRNGPIAREKCMGVKVKLMDAKLHEDAVHRGPAQVIPAVRSGIFAAMMQAKPVLLEPYQKVFINVPQDMMGAATREIQN 646
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   931 RRGHCgkENPIPGTPLVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWALVPGNpldrniilrplepapiphLARE 1010
Cdd:TIGR00490  647 RRGQI--LEMKQEGDMVTIIAKAPVAEMFGFAGAIRGATSGRCLWSTEHAGFELVPQN------------------LQQE 706
                          890
                   ....*....|..
gi 209881947  1011 FLLKTRRRKGLS 1022
Cdd:TIGR00490  707 FVMEVRKRKGLK 718
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
149-354 1.86e-95

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: 301.49  E-value: 1.86e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  149 RNIAIVGDLHHGKTSLIDMLVRITHKFSKL--KTEKLNRYTDSRIDEQEREISIKATPISLILPNSINKSYLLNIIDTPG 226
Cdd:cd04167     1 RNVCIAGHLHHGKTSLLDMLIEQTHKRTPSvkLGWKPLRYTDTRKDEQERGISIKSNPISLVLEDSKGKSYLINIIDTPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  227 HVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDRLILELRIPPNDAYCKIGYIINEANE 306
Cdd:cd04167    81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDRLILELKLPPTDAYYKLRHTIDEINN 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 209881947  307 VVKSFYSLYradkneidRLIFSPEKGNVGFASGKFGFCFTLQSFARMY 354
Cdd:cd04167   161 YIASFSTTE--------GFLVSPELGNVLFASSKFGFCFTLESFAKKY 200
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
146-346 5.99e-38

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: 140.35  E-value: 5.99e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   146 KLIRNIAIVGDLHHGKTSLIDMLVRITHKFSKLKTEKL--NRYTDSRIDEQEREISIKATPISLIlpnsiNKSYLLNIID 223
Cdd:pfam00009    1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGegEAGLDNLPEERERGITIKSAAVSFE-----TKDYLINLID 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   224 TPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDRLilelrippndayckigyIINE 303
Cdd:pfam00009   76 TPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRV-----------------DGAE 138
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 209881947   304 ANEVVKSFYSLYradkneIDRLIFSPEKGNVGFASGKFGFCFT 346
Cdd:pfam00009  139 LEEVVEEVSREL------LEKYGEDGEFVPVVPGSALKGEGVQ 175
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
142-988 6.60e-36

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: 145.96  E-value: 6.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  142 MKQPKL--IRNIAIVGdlHH--GKTSLIDMLVRITHKFSKL-KTEKLNRYTDSRIDEQEREISI--KATPISlilpnsiN 214
Cdd:COG0480     1 MAEYPLekIRNIGIVA--HIdaGKTTLTERILFYTGAIHRIgEVHDGNTVMDWMPEEQERGITItsAATTCE-------W 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  215 KSYLLNIIDTPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYClrEKHDI--VLLINKIDR-------LILE 285
Cdd:COG0480    72 KGHKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQA--DKYGVprIVFVNKMDRegadfdrVLEQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  286 LR-----------IPpndayckIGyiineANEVVKSFYSL--YRAdkneidrLIFSPEKGNVgfasgkfgfcFT------ 346
Cdd:COG0480   150 LKerlganpvplqLP-------IG-----AEDDFKGVIDLvtMKA-------YVYDDELGAK----------YEeeeipa 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  347 -LQSFA---RMYLKESYTTTSE-LMQnidsfcnnlwgdlyyskslgKFLrsSNEStykfcsfvqfileplykifiyslse 421
Cdd:COG0480   201 eLKEEAeeaREELIEAVAETDDeLME--------------------KYL--EGEE------------------------- 233
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  422 qpkvlstllpsigvyLSRSELKKSPTS--ILDTICKRFFG------GANAFTDLIVNNISNPLEASPIRTFNEYTGpqnd 493
Cdd:COG0480   234 ---------------LTEEEIKAGLRKatLAGKIVPVLCGsafknkGVQPLLDAVVDYLPSPLDVPAIKGVDPDTG---- 294
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  494 llAQRIRNLSYDSPAVAFVTKHYHtssmDSF---YSLCRVYCGILRKGDVVkvlgesY--TAEDPEDMSictiqNIWIFQ 568
Cdd:COG0480   295 --EEVERKPDDDEPFSALVFKTMT----DPFvgkLSFFRVYSGTLKSGSTV------YnsTKGKKERIG-----RLLRMH 357
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  569 ARYKVEINEVPAGNWTLISGLNNsvIKTATIICDTtrsnkynnNKPYkevdelscknikdeiliedqrnqyltqqnddlh 648
Cdd:COG0480   358 GNKREEVDEAGAGDIVAVVKLKD--TTTGDTLCDE--------DHPI--------------------------------- 394
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  649 ILRPLKFPtNNVIRLACEPVNPSELPKMLEGLKSLDKAYPILKTKV-EESGEHVIFGTGELQLDCIMHDLRRLYGnLDVK 727
Cdd:COG0480   395 VLEPIEFP-EPVISVAIEPKTKADEDKLSTALAKLAEEDPTFRVETdEETGQTIISGMGELHLEIIVDRLKREFG-VEVN 472
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  728 VSDPSVQLCETVldTSVVKS-------------FGDssnkqnrIYIIAEPLEKGlaEDIEngivkFYDCIdnestkyhqq 794
Cdd:COG0480   473 VGKPQVAYRETI--RKKAEAegkhkkqsgghgqYGD-------VWIEIEPLPRG--EGFE-----FVDKI---------- 526
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  795 ilkdkynwdhlalrslwaFGptfeGAnvlIDdtlssitdkkslyeiKENI---IQGFQWATREGPLLEENVRNVKFKILD 871
Cdd:COG0480   527 ------------------VG----GV---IP---------------KEYIpavEKGIREAMEKGVLAGYPVVDVKVTLYD 566
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  872 VS--------LASnkasrgtgQIipAARRACYTAMLMASPRLMEPICLVEIVCPSEshnAIANV---LLRRRGHcgkenp 940
Cdd:COG0480   567 GSyhpvdsseMAF--------KI--AASMAFKEAAKKAKPVLLEPIMKVEVTVPEE---YMGDVmgdLNSRRGR------ 627
                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|..
gi 209881947  941 IPGT----PLVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWALVPGN 988
Cdd:COG0480   628 ILGMesrgGAQVIKAEVPLAEMFGYATDLRSLTQGRGSFTMEFSHYEEVPAN 679
EFG_IV smart00889
Elongation factor G, domain IV; Translation elongation factors are responsible for two main ...
788-902 5.80e-26

Elongation factor G, domain IV; Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution. Elongation factor EF2 (EF-G) is a G-protein. It brings about the translocation of peptidyl-tRNA and mRNA through a ratchet-like mechanism: the binding of GTP-EF2 to the ribosome causes a counter-clockwise rotation in the small ribosomal subunit; the hydrolysis of GTP to GDP by EF2 and the subsequent release of EF2 causes a clockwise rotation of the small subunit back to the starting position. This twisting action destabilises tRNA-ribosome interactions, freeing the tRNA to translocate along the ribosome upon GTP-hydrolysis by EF2. EF2 binding also affects the entry and exit channel openings for the mRNA, widening it when bound to enable the mRNA to translocate along the ribosome. EF2 has five domains. This entry represents domain IV found in EF2 (or EF-G) of both prokaryotes and eukaryotes. The EF2-GTP-ribosome complex undergoes extensive structural rearrangement for tRNA-mRNA movement to occur. Domain IV, which extends from the 'body' of the EF2 molecule much like a lever arm, appears to be essential for the structural transition to take place.


Pssm-ID: 214887 [Multi-domain]  Cd Length: 120  Bit Score: 103.39  E-value: 5.80e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947    788 STKYHQQILKDKYNWDHLALRSLWAFGPTFEGANVLIDDTlssITDKKSLYEIKENIIQGFQWATREGPLLEENVRNVKF 867
Cdd:smart00889   11 PVKEAEGKHKKQSGGDGQYARVILEVEPLERGSGFEFDDT---IVGGVIPKEYIPAVEKGFREALEEGPLAGYPVVDVKV 87
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 209881947    868 KILDVSLASnKASRGTGqIIPAARRACYTAMLMAS 902
Cdd:smart00889   88 TLLDGSYHE-VDSSEMA-FKPAARRAFKEALLKAG 120
EFTUD2 pfam16004
116 kDa U5 small nuclear ribonucleoprotein component N-terminus;
5-126 1.66e-25

116 kDa U5 small nuclear ribonucleoprotein component N-terminus;


Pssm-ID: 464968  Cd Length: 76  Bit Score: 100.69  E-value: 1.66e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947     5 EIYDEFGNYIGTEsesnldleisLDEDEDQSsdsqknpthdptevddvkminginrivdgmdiemdneAIILHEHKEYYE 84
Cdd:pfam16004    1 DLYDEFGNYIGPE----------LDSDDESN-------------------------------------AVVLHEDKQYYP 33
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 209881947    85 DADKIFGKDVEILFEDEDMHHIDTPTIVPLKDNKFDLVEGDI 126
Cdd:pfam16004   34 SAEEVYGPDVETLVQEEDAQPLTEPIIAPVKQKKFAVEEKDL 75
 
Name Accession Description Interval E-value
PTZ00416 PTZ00416
elongation factor 2; Provisional
131-1032 0e+00

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 683.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  131 ITFSYDYMKDMMKQPKLIRNIAIVGDLHHGKTSLIDMLVR----ITHKFSKLKteklnRYTDSRIDEQEREISIKATPIS 206
Cdd:PTZ00416    2 VNFTVDQIREIMDNPDQIRNMSVIAHVDHGKSTLTDSLVCkagiISSKNAGDA-----RFTDTRADEQERGITIKSTGIS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  207 LILPNSIN-----KSYLLNIIDTPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDR 281
Cdd:PTZ00416   77 LYYEHDLEdgddkQPFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVEGVCVQTETVLRQALQERIRPVLFINKVDR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  282 LILELRIPPNDAYCKIGYIINEANEVVKSFyslyraDKNEIDRLIFSPEKGNVGFASGKFGFCFTLQSFARMYLKESYTT 361
Cdd:PTZ00416  157 AILELQLDPEEIYQNFVKTIENVNVIIATY------NDELMGDVQVYPEKGTVAFGSGLQGWAFTLTTFARIYAKKFGVE 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  362 TSELMQNidsfcnnLWGDLYYSKSLGKFLRSSNESTYKFC--SFVQFILEPLYKIFIYSLSEQPKVLSTLLPSIGVYLSR 439
Cdd:PTZ00416  231 ESKMMER-------LWGDNFFDAKTKKWIKDETNAQGKKLkrAFCQFILDPICQLFDAVMNEDKEKYDKMLKSLNISLTG 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  440 SELKKSPTSILDTICKRFFGGANAFTDLIVNNISNPLEASPIRTFNEYTGPQNDLLAQRIRNLSYDSPAVAFVTKHYHTS 519
Cdd:PTZ00416  304 EDKELTGKPLLKAVMQKWLPAADTLLEMIVDHLPSPKEAQKYRVENLYEGPMDDEAANAIRNCDPNGPLMMYISKMVPTS 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  520 SMDSFYSLCRVYCGILRKGDVVKVLGESYTAEDPEDMSICTIQNIWIFQARYKVEINEVPAGNWTLISGLNNSVIKTATI 599
Cdd:PTZ00416  384 DKGRFYAFGRVFSGTVATGQKVRIQGPNYVPGKKEDLFEKNIQRTVLMMGRYVEQIEDVPCGNTVGLVGVDQYLVKSGTI 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  600 icdTTrsnkynnnkpykevdelscknikdeiliedqrnqyltqqNDDLHILRPLKFPTNNVIRLACEPVNPSELPKMLEG 679
Cdd:PTZ00416  464 ---TT---------------------------------------SETAHNIRDMKYSVSPVVRVAVEPKNPKDLPKLVEG 501
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  680 LKSLDKAYPILKTKVEESGEHVIFGTGELQLDCIMHDLRRLYGNLDVKVSDPSVQLCETVLDTSVVKSFGDSSNKQNRIY 759
Cdd:PTZ00416  502 LKRLAKSDPLVVCTTEESGEHIVAGCGELHVEICLKDLEDDYANIDIIVSDPVVSYRETVTEESSQTCLSKSPNKHNRLY 581
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  760 IIAEPLEKGLAEDIENGIVkfydcIDNESTKYHQQILKDKYNWDHLALRSLWAFGPTFEGANVLIDDTlssiTDKKSLYE 839
Cdd:PTZ00416  582 MKAEPLTEELAEAIEEGKV-----GPEDDPKERANFLADKYEWDKNDARKIWCFGPENKGPNVLVDVT----KGVQYMNE 652
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  840 IKENIIQGFQWATREGPLLEENVRNVKFKILDVSLASNKASRGTGQIIPAARRACYTAMLMASPRLMEPICLVEIVCPSE 919
Cdd:PTZ00416  653 IKDSCVSAFQWATKEGVLCDENMRGIRFNILDVTLHADAIHRGAGQIIPTARRVFYACELTASPRLLEPMFLVDITAPED 732
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  920 SHNAIANVLLRRRGHCGKENPIPGTPLVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWALVPGNPLDRNiilrpl 999
Cdd:PTZ00416  733 AMGGIYSVLNRRRGVVIGEEQRPGTPLSNIKAYLPVAESFGFTAALRAATSGQAFPQCVFDHWQVVPGDPLEPG------ 806
                         890       900       910
                  ....*....|....*....|....*....|....
gi 209881947 1000 epapipHLAREFLLKTRRRKGLSEDV-SVQNFID 1032
Cdd:PTZ00416  807 ------SKANEIVLSIRKRKGLKPEIpDLDNYLD 834
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
133-1032 0e+00

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 629.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  133 FSYDYMKDMMKQPKLIRNIAIVGDLHHGKTSLIDMLVRITHKFSkLKTEKLNRYTDSRIDEQEREISIKATPISL----- 207
Cdd:PLN00116    4 FTAEELRRIMDKKHNIRNMSVIAHVDHGKSTLTDSLVAAAGIIA-QEVAGDVRMTDTRADEAERGITIKSTGISLyyemt 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  208 -----ILPNSIN-KSYLLNIIDTPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDR 281
Cdd:PLN00116   83 deslkDFKGERDgNEYLINLIDSPGHVDFSSEVTAALRITDGALVVVDCIEGVCVQTETVLRQALGERIRPVLTVNKMDR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  282 LILELRIPPNDAYCKIGYIINEANEVVKSFYSLYRADkneidrLIFSPEKGNVGFASGKFGFCFTLQSFARMYLKESYTT 361
Cdd:PLN00116  163 CFLELQVDGEEAYQTFSRVIENANVIMATYEDPLLGD------VQVYPEKGTVAFSAGLHGWAFTLTNFAKMYASKFGVD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  362 TSELMQNidsfcnnLWGDLYYSKSLGKFLRSSNESTYKFCSFVQFILEPLYKIFIYSLSEQPKVLSTLLPSIGVYLSRSE 441
Cdd:PLN00116  237 ESKMMER-------LWGENFFDPATKKWTTKNTGSPTCKRGFVQFCYEPIKQIINTCMNDQKDKLWPMLEKLGVTLKSDE 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  442 LKKSPTSILDTICKRFFGGANAFTDLIVNNISNPLEASPIRTFNEYTGPQNDLLAQRIRNLSYDSPAVAFVTKHYHTSSM 521
Cdd:PLN00116  310 KELMGKALMKRVMQTWLPASDALLEMIIFHLPSPAKAQRYRVENLYEGPLDDKYATAIRNCDPNGPLMLYVSKMIPASDK 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  522 DSFYSLCRVYCGILRKGDVVKVLGESYTAEDPEDMSICTIQNIWIFQARYKVEINEVPAGNWTLISGLNNSVIKTATIIc 601
Cdd:PLN00116  390 GRFFAFGRVFSGTVATGMKVRIMGPNYVPGEKKDLYVKSVQRTVIWMGKKQESVEDVPCGNTVAMVGLDQFITKNATLT- 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  602 dttrsnkynnnkpykevdelscknikdeiliedqrnqylTQQNDDLHILRPLKFPTNNVIRLACEPVNPSELPKMLEGLK 681
Cdd:PLN00116  469 ---------------------------------------NEKEVDAHPIKAMKFSVSPVVRVAVQCKNASDLPKLVEGLK 509
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  682 SLDKAYPILKTKVEESGEHVIFGTGELQLDCIMHDLRRLY-GNLDVKVSDPSVQLCETVLDTSVVKSFGDSSNKQNRIYI 760
Cdd:PLN00116  510 RLAKSDPMVQCTIEESGEHIIAGAGELHLEICLKDLQDDFmGGAEIKVSDPVVSFRETVLEKSCRTVMSKSPNKHNRLYM 589
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  761 IAEPLEKGLAEDIENGIVKFYDcidneSTKYHQQILKDKYNWDHLALRSLWAFGPTFEGANVLIDDTLSSitdkKSLYEI 840
Cdd:PLN00116  590 EARPLEEGLAEAIDDGRIGPRD-----DPKIRSKILAEEFGWDKDLAKKIWCFGPETTGPNMVVDMCKGV----QYLNEI 660
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  841 KENIIQGFQWATREGPLLEENVRNVKFKILDVSLASNKASRGTGQIIPAARRACYTAMLMASPRLMEPICLVEIVCPSES 920
Cdd:PLN00116  661 KDSVVAGFQWATKEGALAEENMRGICFEVCDVVLHADAIHRGGGQIIPTARRVIYASQLTAKPRLLEPVYLVEIQAPEQA 740
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  921 HNAIANVLLRRRGHCGKENPIPGTPLVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWALVPGNPLDRNiilrple 1000
Cdd:PLN00116  741 LGGIYSVLNQKRGHVFEEMQRPGTPLYNIKAYLPVIESFGFSGTLRAATSGQAFPQCVFDHWDMMSSDPLEAG------- 813
                         890       900       910
                  ....*....|....*....|....*....|...
gi 209881947 1001 papipHLAREFLLKTRRRKGLSEDV-SVQNFID 1032
Cdd:PLN00116  814 -----SQAAQLVADIRKRKGLKEQMpPLSEYED 841
PRK07560 PRK07560
elongation factor EF-2; Reviewed
139-1024 1.91e-126

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 401.93  E-value: 1.91e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  139 KDMMKQPKLIRNIAIVGDLHHGKTSLIDMLVRITHKFS-KLKTEKLnrYTDSRIDEQEREISIKATPISLILpNSINKSY 217
Cdd:PRK07560   11 LELMKNPEQIRNIGIIAHIDHGKTTLSDNLLAGAGMISeELAGEQL--ALDFDEEEQARGITIKAANVSMVH-EYEGKEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  218 LLNIIDTPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDRLILELRIPPNDAYCKI 297
Cdd:PRK07560   88 LINLIDTPGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQTETVLRQALRERVKPVLFINKVDRLIKELKLTPQEMQQRL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  298 GYIINEANEVVKSFyslyrADKNEIDRLIFSPEKGNVGFASGKFGFCFTLQsfarmYLKESYTTTSELMQnidsfcnnlw 377
Cdd:PRK07560  168 LKIIKDVNKLIKGM-----APEEFKEKWKVDVEDGTVAFGSALYNWAISVP-----MMQKTGIKFKDIID---------- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  378 gdlYYSKSLGKFLRSSNestykfcsfvqfilePLYKIfiyslseqpkvlstllpsigvylsrselkksptsILDTICKrf 457
Cdd:PRK07560  228 ---YYEKGKQKELAEKA---------------PLHEV----------------------------------VLDMVVK-- 253
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  458 fgganaftdlivnNISNPLEASPIRTFNEYTGPQNDLLAQRIRNLSYDSPAVAFVTKhyhtSSMD---SFYSLCRVYCGI 534
Cdd:PRK07560  254 -------------HLPNPIEAQKYRIPKIWKGDLNSEVGKAMLNCDPNGPLVMMVTD----IIVDphaGEVATGRVFSGT 316
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  535 LRKGDVVKVLGESYTAEdpedmsictIQNIWIFQARYKVEINEVPAGNWTLISGLNNSvIKTATIiCDTtrsnkyNNNKP 614
Cdd:PRK07560  317 LRKGQEVYLVGAKKKNR---------VQQVGIYMGPEREEVEEIPAGNIAAVTGLKDA-RAGETV-VSV------EDMTP 379
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  615 YKEVDelscknikdeiliedqrnqyltqqnddlHILRPlkfptnnVIRLACEPVNPSELPKMLEGLKSLDKAYPILKTKV 694
Cdd:PRK07560  380 FESLK----------------------------HISEP-------VVTVAIEAKNPKDLPKLIEVLRQLAKEDPTLVVKI 424
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  695 -EESGEHVIFGTGELQLDCIMHDLRRLYGnLDVKVSDPSVQLCETVLDTS-VVKsfGDSSNKQNRIYIIAEPLEKGLAED 772
Cdd:PRK07560  425 nEETGEHLLSGMGELHLEVITYRIKRDYG-IEVVTSEPIVVYRETVRGKSqVVE--GKSPNKHNRFYISVEPLEEEVIEA 501
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  773 IENGIvkfydcIDNESTKYHQQILKD---KYNWDHLALRSLWAFgptfEGANVLIDDTlSSItdkKSLYEIKENIIQGFQ 849
Cdd:PRK07560  502 IKEGE------ISEDMDKKEAKILREkliEAGMDKDEAKRVWAI----YNGNVFIDMT-KGI---QYLNEVMELIIEGFR 567
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  850 WATREGPLLEENVRNVKFKILDVSLASNKASRGTGQIIPAARRACYTAMLMASPRLMEPICLVEIVCPSESHNAIANVLL 929
Cdd:PRK07560  568 EAMKEGPLAAEPVRGVKVRLHDAKLHEDAIHRGPAQVIPAVRNAIFAAMLTAKPTLLEPIQKVDINVPQDYMGAVTREIQ 647
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  930 RRRGHCgkENPIPGTPLVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWALVPGNpldrniilrplepapiphLAR 1009
Cdd:PRK07560  648 GRRGKI--LDMEQEGDMAIIEAEAPVAEMFGFAGEIRSATEGRALWSTEFAGFEPVPDS------------------LQL 707
                         890
                  ....*....|....*
gi 209881947 1010 EFLLKTRRRKGLSED 1024
Cdd:PRK07560  708 DIVRQIRERKGLKPE 722
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
136-1022 3.52e-98

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: 326.47  E-value: 3.52e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   136 DYMKDMMKQPKLIRNIAIVGDLHHGKTSLIDMLVRITHKFSK-LKTEKLnrYTDSRIDEQEREISIKATPISLILPNSIN 214
Cdd:TIGR00490    7 DKIKELMWKPKFIRNIGIVAHIDHGKTTLSDNLLAGAGMISEeLAGQQL--YLDFDEQEQERGITINAANVSMVHEYEGN 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   215 KsYLLNIIDTPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDRLILELRIPPNDAY 294
Cdd:TIGR00490   85 E-YLINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQTETVLRQALKENVKPVLFINKVDRLINELKLTPQELQ 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   295 CKIGYIINEANEVVKSFYSLYRADKNEIDrlifsPEKGNVGFASGKFGFCFTLQSfarmyLKESYTTTSELmqnidsfcn 374
Cdd:TIGR00490  164 ERFIKIITEVNKLIKAMAPEEFRDKWKVR-----VEDGSVAFGSAYYNWAISVPS-----MKKTGIGFKDI--------- 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   375 nlwgdlyyskslgkflrssnestYKFCSfvqfileplykifiyslSEQPKVLSTLLPSIGVYLsrselkksptsildtic 454
Cdd:TIGR00490  225 -----------------------YKYCK-----------------EDKQKELAKKSPLHQVVL----------------- 247
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   455 krffgganaftDLIVNNISNPLEASPIRTFNEYTGPQNDLLAQRIRNLSYDSPAVAFVTK---HYHTSSMdsfySLCRVY 531
Cdd:TIGR00490  248 -----------DMVIRHLPSPIEAQKYRIPVIWKGDLNSEVGKAMLNCDPKGPLALMITKivvDKHAGEV----AVGRLY 312
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   532 CGILRKGDVVKVLGESYTAEdpedmsictIQNIWIFQARYKVEINEVPAGNWTLISGLNNSVikTATIICDTTRsnkynN 611
Cdd:TIGR00490  313 SGTIRPGMEVYIVDRKAKAR---------IQQVGVYMGPERVEVDEIPAGNIVAVIGLKDAV--AGETICTTVE-----N 376
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   612 NKPYKEVDelscknikdeiliedqrnqyltqqnddlHILRPlkfptnnVIRLACEPVNPSELPKMLEGLKSLDKAYPILK 691
Cdd:TIGR00490  377 ITPFESIK----------------------------HISEP-------VVTVAIEAKNTKDLPKLIEVLRQVAKEDPTVH 421
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   692 TKV-EESGEHVIFGTGELQLDCIMHDLRRLYGnLDVKVSDPSVQLCETVLDTSVVKSfGDSSNKQNRIYIIAEPLEKGLA 770
Cdd:TIGR00490  422 VEInEETGEHLISGMGELHLEIIVEKIREDYG-LDVETSPPIVVYRETVTGTSPVVE-GKSPNKHNRFYIVVEPLEESVI 499
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   771 EDIENGIVKFYDCIDNESTKYHQQILKDKYNwdhlaLRSLWAFgptFEGaNVLIDDTLSSitdkKSLYEIKENIIQGFQW 850
Cdd:TIGR00490  500 QAFKEGKIVDMKMKKKERRRLLIEAGMDSEE-----AARVEEY---YEG-NLFINMTRGI----QYLDETKELILEGFRE 566
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   851 ATREGPLLEENVRNVKFKILDVSLASNKASRGTGQIIPAARRACYTAMLMASPRLMEPICLVEIVCPSESHNAIANVLLR 930
Cdd:TIGR00490  567 AMRNGPIAREKCMGVKVKLMDAKLHEDAVHRGPAQVIPAVRSGIFAAMMQAKPVLLEPYQKVFINVPQDMMGAATREIQN 646
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   931 RRGHCgkENPIPGTPLVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWALVPGNpldrniilrplepapiphLARE 1010
Cdd:TIGR00490  647 RRGQI--LEMKQEGDMVTIIAKAPVAEMFGFAGAIRGATSGRCLWSTEHAGFELVPQN------------------LQQE 706
                          890
                   ....*....|..
gi 209881947  1011 FLLKTRRRKGLS 1022
Cdd:TIGR00490  707 FVMEVRKRKGLK 718
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
149-354 1.86e-95

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: 301.49  E-value: 1.86e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  149 RNIAIVGDLHHGKTSLIDMLVRITHKFSKL--KTEKLNRYTDSRIDEQEREISIKATPISLILPNSINKSYLLNIIDTPG 226
Cdd:cd04167     1 RNVCIAGHLHHGKTSLLDMLIEQTHKRTPSvkLGWKPLRYTDTRKDEQERGISIKSNPISLVLEDSKGKSYLINIIDTPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  227 HVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDRLILELRIPPNDAYCKIGYIINEANE 306
Cdd:cd04167    81 HVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLVINKIDRLILELKLPPTDAYYKLRHTIDEINN 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 209881947  307 VVKSFYSLYradkneidRLIFSPEKGNVGFASGKFGFCFTLQSFARMY 354
Cdd:cd04167   161 YIASFSTTE--------GFLVSPELGNVLFASSKFGFCFTLESFAKKY 200
EF2_IV_snRNP cd01683
EF-2_domain IV_snRNP domain is a part of 116kD U5-specific protein of the U5 small ...
730-912 1.46e-85

EF-2_domain IV_snRNP domain is a part of 116kD U5-specific protein of the U5 small nucleoprotein (snRNP) particle, essential component of the spliceosome. The protein is structurally closely related to the eukaryotic translational elongation factor EF2. This domain has been also identified in 114kD U5-specific protein of Saccharomyces cerevisiae and may play an important role either in splicing process itself or the recycling of spliceosomal snRNP.


Pssm-ID: 238840 [Multi-domain]  Cd Length: 178  Bit Score: 273.40  E-value: 1.46e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  730 DPSVQLCETVLDTSVVKSFGDSSNKQNRIYIIAEPLEKGLAEDIENGIVKFydcidNESTKYHQQILKDKYNWDHLALRS 809
Cdd:cd01683     1 DPVVTFCETVVETSSAKCFAETPNKKNKITMIAEPLDKGLAEDIENGQLKL-----SWNRKKLGKFLRTKYGWDALAARS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  810 LWAFGPTFEGANVLIDDTLSSITDKKSLYEIKENIIQGFQWATREGPLLEENVRNVKFKILDVSLASNKASRGTGQIIPA 889
Cdd:cd01683    76 IWAFGPDTKGPNVLIDDTLPEEVDKNLLNSVKESIVQGFQWAVREGPLCEEPIRNVKFKLLDADIASEPIDRGGGQIIPT 155
                         170       180
                  ....*....|....*....|...
gi 209881947  890 ARRACYTAMLMASPRLMEPICLV 912
Cdd:cd01683   156 ARRACYSAFLLATPRLMEPIYEV 178
aeEF2_snRNP_like_IV cd01681
This family represents domain IV of archaeal and eukaryotic elongation factor 2 (aeEF-2) and ...
730-909 8.74e-78

This family represents domain IV of archaeal and eukaryotic elongation factor 2 (aeEF-2) and of an evolutionarily conserved U5 snRNP-specific protein. U5 snRNP is a GTP-binding factor closely related to the ribosomal translocase EF-2. In complex with GTP, EF-2 promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site of the small subunit of ribosome and the mRNA is shifted one codon relative to the ribosome. It has been shown that EF-2_IV domain mimics the shape of anticodon arm of the tRNA in the structurally homologous ternary complex of Phe-tRNA, EF-1 (another transcriptional elongation factor) and GTP analog. The tip portion of this domain is found in a position that overlaps the anticodon arm of the A-site tRNA, implying that EF-2 displaces the A-site tRNA to the P-site by physical interaction with the anticodon arm.


Pssm-ID: 238839 [Multi-domain]  Cd Length: 177  Bit Score: 252.11  E-value: 8.74e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  730 DPSVQLCETVLDTSVVKSFGDSSNKQNRIYIIAEPLEKGLAEDIENGIVKfydcIDNESTKYHQqILKDKYNWDHLALRS 809
Cdd:cd01681     1 DPVVSFRETVVETSSGTCLAKSPNKHNRLYMRAEPLPEELIEDIEKGKIT----LKDDKKKRAR-ILLDKYGWDKLAARK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  810 LWAFGPTFEGANVLIDDTLSSITDKKSLYEIKENIIQGFQWATREGPLLEENVRNVKFKILDVSLASNKASRGTGQIIPA 889
Cdd:cd01681    76 IWAFGPDRTGPNILVDDTKGVQYDKSLLNEIKDSIVAGFQWATKEGPLCEEPMRGVKFKLEDATLHADAIHRGGGQIIPA 155
                         170       180
                  ....*....|....*....|
gi 209881947  890 ARRACYTAMLMASPRLMEPI 909
Cdd:cd01681   156 ARRACYAAFLLASPRLMEPM 175
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
149-354 2.09e-59

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: 202.85  E-value: 2.09e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  149 RNIAIVGDLHHGKTSLIDMLVrithKFSKLKTEKLN---RYTDSRIDEQEREISIKATPISL----ILPNSINKSYLLNI 221
Cdd:cd01885     1 RNICIIAHVDHGKTTLSDSLL----ASAGIISEKLAgkaRYLDTREDEQERGITIKSSAISLyfeyEEEKMDGNDYLINL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  222 IDTPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDRLILELRIPPNDAYCKIGYII 301
Cdd:cd01885    77 IDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQTETVLRQALEERVKPVLVINKIDRLILELKLSPEEAYQRLLRIV 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 209881947  302 NEANEVVKSFYSlyraDKNEIDRLIFSPEKGNVGFASGKFGFCFTLQSFARMY 354
Cdd:cd01885   157 EDVNAIIETYAP----EEFKQEKWKFSPQKGNVAFGSALDGWGFTIIKFADIY 205
EF2_II_snRNP cd04090
Domain II of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; This ...
509-600 4.68e-44

Domain II of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; This subfamily includes domain II of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and its yeast counterpart Snu114p. This domain is homologous to domain II of the eukaryotic translational elongation factor EF-2. U5-116 kD is a GTPase which is a component of the spliceosome complex which processes precursor mRNAs to produce mature mRNAs.


Pssm-ID: 293907 [Multi-domain]  Cd Length: 94  Bit Score: 154.32  E-value: 4.68e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  509 VAFVTKHYHTSSMDSFYSLCRVYCGILRKGDVVKVLGESYTAEDPEDMSICTIQNIWIFQARYKVEINEVPAGNWTLISG 588
Cdd:cd04090     2 VVHVTKLYSSSDGGSFWALGRIYSGTLRKGQKVKVLGENYSLEDEEDMTVCTVGRLWILGARYKYEVNSAPAGNWVLIKG 81
                          90
                  ....*....|..
gi 209881947  589 LNNSVIKTATII 600
Cdd:cd04090    82 IDQSIVKTATIT 93
eEF2_C_snRNP cd04098
eEF2_C_snRNP: This family includes a C-terminal portion of the spliceosomal human 116kD U5 ...
907-986 2.09e-41

eEF2_C_snRNP: This family includes a C-terminal portion of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and, its yeast counterpart Snu114p. This domain is homologous to the C-terminal domain of the eukaryotic translational elongation factor EF-2. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. In complex with GTP, EF-2 promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site, the uncharged tRNA from the P site to the E-site and, the mRNA is shifted one codon relative to the ribosome.


Pssm-ID: 239765 [Multi-domain]  Cd Length: 80  Bit Score: 146.24  E-value: 2.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  907 EPICLVEIVCPSESHNAIANVLLRRRGHCGKENPIPGTPLVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWALVP 986
Cdd:cd04098     1 EPIYEVEITCPADAVSAVYEVLSRRRGHVIYDTPIPGTPLYEVKAFIPVIESFGFETDLRVHTQGQAFCQSVFDHWQIVP 80
PRK13351 PRK13351
elongation factor G-like protein;
141-992 2.73e-40

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 159.35  E-value: 2.73e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  141 MMKQPKLIRNIAIVGDLHHGKTSLIDMLVRITHKFSKLKT-EKLNRYTDSRIDEQEREISIKATPISLILPNsinksYLL 219
Cdd:PRK13351    1 AEMPLMQIRNIGILAHIDAGKTTLTERILFYTGKIHKMGEvEDGTTVTDWMPQEQERGITIESAATSCDWDN-----HRI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  220 NIIDTPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDRLilelrippndayckigy 299
Cdd:PRK13351   76 NLIDTPGHIDFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIPRLIFINKMDRV----------------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  300 iineanevvksfyslyradKNEIDRLIFSPEKgnvgfasgKFGF-CFTLQsfarmylkesYTTTSElmqnidsfcNNLWG 378
Cdd:PRK13351  139 -------------------GADLFKVLEDIEE--------RFGKrPLPLQ----------LPIGSE---------DGFEG 172
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  379 --DLYYSKSLGkFLRSSNESTYKFCSFVQFILEPL---YKIFIYSLSEQ-PKVLSTLL--PSIGVYLSRSELKKSPTSil 450
Cdd:PRK13351  173 vvDLITEPELH-FSEGDGGSTVEEGPIPEELLEEVeeaREKLIEALAEFdDELLELYLegEELSAEQLRAPLREGTRS-- 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  451 DTICKRFFGGA--NA----FTDLIVNNISNPLEASPIRTFNEYTGPqndllaqRIRNLSYDSPAVAFVTKHYHTSSMDSF 524
Cdd:PRK13351  250 GHLVPVLFGSAlkNIgiepLLDAVVDYLPSPLEVPPPRGSKDNGKP-------VKVDPDPEKPLLALVFKVQYDPYAGKL 322
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  525 YSLcRVYCGILRKGDvvKVLgeSYTAEDPEdmsicTIQNIWIFQARYKVEINEVPAGNWTLISGLNNsvIKTATIICDTT 604
Cdd:PRK13351  323 TYL-RVYSGTLRAGS--QLY--NGTGGKRE-----KVGRLFRLQGNKREEVDRAKAGDIVAVAGLKE--LETGDTLHDSA 390
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  605 rsnkynnnkpykevdelscknikdeiliedqrnqyltqQNDDLHilrPLKFPTnNVIRLACEPVNPSELPKMLEGLKSLD 684
Cdd:PRK13351  391 --------------------------------------DPVLLE---LLTFPE-PVVSLAVEPERRGDEQKLAEALEKLV 428
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  685 KAYPILKTKV-EESGEHVIFGTGELQLDCIMHDLRRLYgNLDVKVSDPSVQLCETVLDTS-----VVKSFGDSsnKQN-R 757
Cdd:PRK13351  429 WEDPSLRVEEdEETGQTILSGMGELHLEVALERLRREF-KLEVNTGKPQVAYRETIRKMAegvyrHKKQFGGK--GQFgE 505
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  758 IYIIAEPLEKGLAEdiengivKFYDCIdnestkyhqqilkdkynwdhlalrslwaFGPTFEGanvliddtlssitdkksl 837
Cdd:PRK13351  506 VHLRVEPLERGAGF-------IFVSKV----------------------------VGGAIPE------------------ 532
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  838 yEIKENIIQGFQWATREGPLLEENVRNVKFKILDVSLASNKASRGTgqIIPAARRACYTAMLMASPRLMEPICLVEIVCP 917
Cdd:PRK13351  533 -ELIPAVEKGIREALASGPLAGYPVTDLRVTVLDGKYHPVDSSESA--FKAAARKAFLEAFRKANPVLLEPIMELEITVP 609
                         810       820       830       840       850       860       870
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209881947  918 SESHNAIANVLLRRRGH-CGKENpiPGTPLVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWALVPGNPLDR 992
Cdd:PRK13351  610 TEHVGDVLGDLSQRRGRiEGTEP--RGDGEVLVKAEAPLAELFGYATRLRSMTKGRGSFTMEFSHFDPVPPAVQKK 683
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
146-346 5.99e-38

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: 140.35  E-value: 5.99e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   146 KLIRNIAIVGDLHHGKTSLIDMLVRITHKFSKLKTEKL--NRYTDSRIDEQEREISIKATPISLIlpnsiNKSYLLNIID 223
Cdd:pfam00009    1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGegEAGLDNLPEERERGITIKSAAVSFE-----TKDYLINLID 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   224 TPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDRLilelrippndayckigyIINE 303
Cdd:pfam00009   76 TPGHVDFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVPIIVFINKMDRV-----------------DGAE 138
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 209881947   304 ANEVVKSFYSLYradkneIDRLIFSPEKGNVGFASGKFGFCFT 346
Cdd:pfam00009  139 LEEVVEEVSREL------LEKYGEDGEFVPVVPGSALKGEGVQ 175
eEF2_snRNP_like_C cd04096
eEF2_snRNP_like_C: this family represents a C-terminal domain of eukaryotic elongation factor ...
907-986 3.21e-37

eEF2_snRNP_like_C: this family represents a C-terminal domain of eukaryotic elongation factor 2 (eEF-2) and a homologous domain of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and, its yeast counterpart Snu114p. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. In complex with GTP, EF-2 promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site, the uncharged tRNA from the P site to the E-site and, the mRNA is shifted one codon relative to the ribosome.


Pssm-ID: 239763 [Multi-domain]  Cd Length: 80  Bit Score: 134.21  E-value: 3.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  907 EPICLVEIVCPSESHNAIANVLLRRRGHCGKENPIPGTPLVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWALVP 986
Cdd:cd04096     1 EPIYLVEIQCPEDALGKVYSVLSKRRGHVLSEEPKEGTPLFEIKAYLPVIESFGFETDLRSATSGQAFPQLVFSHWEIVP 80
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
142-988 6.60e-36

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: 145.96  E-value: 6.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  142 MKQPKL--IRNIAIVGdlHH--GKTSLIDMLVRITHKFSKL-KTEKLNRYTDSRIDEQEREISI--KATPISlilpnsiN 214
Cdd:COG0480     1 MAEYPLekIRNIGIVA--HIdaGKTTLTERILFYTGAIHRIgEVHDGNTVMDWMPEEQERGITItsAATTCE-------W 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  215 KSYLLNIIDTPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYClrEKHDI--VLLINKIDR-------LILE 285
Cdd:COG0480    72 KGHKINIIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQTETVWRQA--DKYGVprIVFVNKMDRegadfdrVLEQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  286 LR-----------IPpndayckIGyiineANEVVKSFYSL--YRAdkneidrLIFSPEKGNVgfasgkfgfcFT------ 346
Cdd:COG0480   150 LKerlganpvplqLP-------IG-----AEDDFKGVIDLvtMKA-------YVYDDELGAK----------YEeeeipa 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  347 -LQSFA---RMYLKESYTTTSE-LMQnidsfcnnlwgdlyyskslgKFLrsSNEStykfcsfvqfileplykifiyslse 421
Cdd:COG0480   201 eLKEEAeeaREELIEAVAETDDeLME--------------------KYL--EGEE------------------------- 233
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  422 qpkvlstllpsigvyLSRSELKKSPTS--ILDTICKRFFG------GANAFTDLIVNNISNPLEASPIRTFNEYTGpqnd 493
Cdd:COG0480   234 ---------------LTEEEIKAGLRKatLAGKIVPVLCGsafknkGVQPLLDAVVDYLPSPLDVPAIKGVDPDTG---- 294
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  494 llAQRIRNLSYDSPAVAFVTKHYHtssmDSF---YSLCRVYCGILRKGDVVkvlgesY--TAEDPEDMSictiqNIWIFQ 568
Cdd:COG0480   295 --EEVERKPDDDEPFSALVFKTMT----DPFvgkLSFFRVYSGTLKSGSTV------YnsTKGKKERIG-----RLLRMH 357
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  569 ARYKVEINEVPAGNWTLISGLNNsvIKTATIICDTtrsnkynnNKPYkevdelscknikdeiliedqrnqyltqqnddlh 648
Cdd:COG0480   358 GNKREEVDEAGAGDIVAVVKLKD--TTTGDTLCDE--------DHPI--------------------------------- 394
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  649 ILRPLKFPtNNVIRLACEPVNPSELPKMLEGLKSLDKAYPILKTKV-EESGEHVIFGTGELQLDCIMHDLRRLYGnLDVK 727
Cdd:COG0480   395 VLEPIEFP-EPVISVAIEPKTKADEDKLSTALAKLAEEDPTFRVETdEETGQTIISGMGELHLEIIVDRLKREFG-VEVN 472
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  728 VSDPSVQLCETVldTSVVKS-------------FGDssnkqnrIYIIAEPLEKGlaEDIEngivkFYDCIdnestkyhqq 794
Cdd:COG0480   473 VGKPQVAYRETI--RKKAEAegkhkkqsgghgqYGD-------VWIEIEPLPRG--EGFE-----FVDKI---------- 526
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  795 ilkdkynwdhlalrslwaFGptfeGAnvlIDdtlssitdkkslyeiKENI---IQGFQWATREGPLLEENVRNVKFKILD 871
Cdd:COG0480   527 ------------------VG----GV---IP---------------KEYIpavEKGIREAMEKGVLAGYPVVDVKVTLYD 566
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  872 VS--------LASnkasrgtgQIipAARRACYTAMLMASPRLMEPICLVEIVCPSEshnAIANV---LLRRRGHcgkenp 940
Cdd:COG0480   567 GSyhpvdsseMAF--------KI--AASMAFKEAAKKAKPVLLEPIMKVEVTVPEE---YMGDVmgdLNSRRGR------ 627
                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|..
gi 209881947  941 IPGT----PLVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWALVPGN 988
Cdd:COG0480   628 ILGMesrgGAQVIKAEVPLAEMFGYATDLRSLTQGRGSFTMEFSHYEEVPAN 679
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
150-346 9.11e-34

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: 128.18  E-value: 9.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  150 NIAIVGDLHHGKTSLIDMLVRITHKFSKLKTEKLnRYTDSRIDEQEREISIKATPISLILPnsinkSYLLNIIDTPGHVN 229
Cdd:cd00881     1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKE-TFLDTLKEERERGITIKTGVVEFEWP-----KRRINFIDTPGHED 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  230 FMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDrlilelRIPPNDAYckigyiineanEVVK 309
Cdd:cd00881    75 FSKETVRGLAQADGALLVVDANEGVEPQTREHLNIALAGGLPIIVAVNKID------RVGEEDFD-----------EVLR 137
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 209881947  310 SfyslYRADKNEIDRLIFSPEKGNVGFASGKFGFCFT 346
Cdd:cd00881   138 E----IKELLKLIGFTFLKGKDVPIIPISALTGEGIE 170
snRNP_III cd16264
Domain III of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; ...
660-730 9.20e-30

Domain III of the spliceosomal 116kD U5 small nuclear ribonucleoprotein (snRNP) component; Domain III of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and its yeast counterpart Snu114p is homologous to domain III of the eukaryotic translational elongation factor EF-2. U5-116 kD is a GTPase component of the spliceosome complex which functions in the processing of precursor mRNAs to produce mature mRNAs.


Pssm-ID: 293921 [Multi-domain]  Cd Length: 72  Bit Score: 112.59  E-value: 9.20e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209881947  660 VIRLACEPVNPSELPKMLEGLKSLDKAYPILKTKVEESGEHVIFGTGELQLDCIMHDLRRLYGNLDVKVSD 730
Cdd:cd16264     2 VFKIAVEPLNPSELPKMLDGLRKVNKSYPLLITKVEESGEHVILGTGELYMDCVMHDLRKMYSEIEIKVAD 72
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
160-988 1.62e-29

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 126.01  E-value: 1.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  160 GKTSLIDMLVRITHKFSKL-KTEKLNRYTDSRIDEQEREISIKATPISLILPNsinksYLLNIIDTPGHVNFMDEFCASI 238
Cdd:PRK12740    7 GKTTLTEAILFYTGAIHRIgEVEDGTTTMDFMPEERERGISITSAATTCEWKG-----HKINLIDTPGHVDFTGEVERAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  239 RLCDGAVIVVDAILGISKHTERMIYYClrEKHDI--VLLINKIDRLilelrippndayckigyiineanevvksfyslyR 316
Cdd:PRK12740   82 RVLDGAVVVVCAVGGVEPQTETVWRQA--EKYGVprIIFVNKMDRA---------------------------------G 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  317 ADkneidrlifspekgnvgfasgkfgfcftlqsFARMY--LKESYTTTSELMQ-NIDSfcnnlwGDlyyskslgkflrss 393
Cdd:PRK12740  127 AD-------------------------------FFRVLaqLQEKLGAPVVPLQlPIGE------GD-------------- 155
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  394 nestyKFCSFVQFILEplyKIFIYSLSEQPKVL--------------STLLPSI-------------GVYLSRSELKKSP 446
Cdd:PRK12740  156 -----DFTGVVDLLSM---KAYRYDEGGPSEEIeipaelldraeearEELLEALaefddelmekyleGEELSEEEIKAGL 227
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  447 TSIL--DTICKRFFGGanAFT--------DLIVNNISNPLEASPIrtfneytgPQNDLLAQRIRNLSYDSPAVAFVTKhy 516
Cdd:PRK12740  228 RKATlaGEIVPVFCGS--ALKnkgvqrllDAVVDYLPSPLEVPPV--------DGEDGEEGAELAPDPDGPLVALVFK-- 295
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  517 htSSMDSF---YSLCRVYCGILRKGDVVKVLGesytAEDPEDMSictiqNIWIFQARYKVEINEVPAGNWTLISGLNNsv 593
Cdd:PRK12740  296 --TMDDPFvgkLSLVRVYSGTLKKGDTLYNSG----TGKKERVG-----RLYRMHGKQREEVDEAVAGDIVAVAKLKD-- 362
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  594 IKTATIICDTtrsnkynnnkpykevdelsckniKDEILIEdqrnqyltqqnddlhilrPLKFPTnNVIRLACEPVNPSEL 673
Cdd:PRK12740  363 AATGDTLCDK-----------------------GDPILLE------------------PMEFPE-PVISLAIEPKDKGDE 400
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  674 PKMLEGLKSLDKAYPILKTKV-EESGEHVIFGTGELQLDCIMHDLRRLYGnLDVKVSDPSVQLCETVldTSVVKS----- 747
Cdd:PRK12740  401 EKLSEALGKLAEEDPTLRVERdEETGQTILSGMGELHLDVALERLKREYG-VEVETGPPQVPYRETI--RKKAEGhgrhk 477
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  748 --------FGDssnkqnrIYIIAEPLEKGlaEDIEngivkFYDCIdnestkyhqqilkdkynwdhlalrslwaFGptfeG 819
Cdd:PRK12740  478 kqsgghgqFGD-------VWLEVEPLPRG--EGFE-----FVDKV----------------------------VG----G 511
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  820 AnvliddtlssitdkkslyeIKENII----QGFQWATREGPLLEENVRNVKFKILDVS---LASNKASRgtgQIipAARR 892
Cdd:PRK12740  512 A-------------------VPRQYIpaveKGVREALEKGVLAGYPVVDVKVTLTDGSyhsVDSSEMAF---KI--AARL 567
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  893 ACYTAMLMASPRLMEPICLVEIVCPSESHNAIANVLLRRRGHcgkenpIPGT----PLVTIYGFIPAIESFGFETDLRVH 968
Cdd:PRK12740  568 AFREALPKAKPVLLEPIMKVEVSVPEEFVGDVIGDLSSRRGR------ILGMesrgGGDVVRAEVPLAEMFGYATDLRSL 641
                         890       900
                  ....*....|....*....|
gi 209881947  969 TSGQAFCSTCFDHWALVPGN 988
Cdd:PRK12740  642 TQGRGSFSMEFSHYEEVPGN 661
EF-G TIGR00484
translation elongation factor EF-G; After peptide bond formation, this elongation factor of ...
148-988 6.00e-29

translation elongation factor EF-G; After peptide bond formation, this elongation factor of bacteria and organelles catalyzes the translocation of the tRNA-mRNA complex, with its attached nascent polypeptide chain, from the A-site to the P-site of the ribosome. Every completed bacterial genome has at least one copy, but some species have additional EF-G-like proteins. The closest homolog to canonical (e.g. E. coli) EF-G in the spirochetes clusters as if it is derived from mitochondrial forms, while a more distant second copy is also present. Synechocystis PCC6803 has a few proteins more closely related to EF-G than to any other characterized protein. Two of these resemble E. coli EF-G more closely than does the best match from the spirochetes; it may be that both function as authentic EF-G. [Protein synthesis, Translation factors]


Pssm-ID: 129575 [Multi-domain]  Cd Length: 689  Bit Score: 124.15  E-value: 6.00e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   148 IRNIAIVGDLHHGKTSLIDMLVRITHKFSKLKTEKLNRYT-DSRIDEQEREISIK--ATPISLilpnsinKSYLLNIIDT 224
Cdd:TIGR00484   10 FRNIGISAHIDAGKTTTTERILFYTGRIHKIGEVHDGAATmDWMEQEKERGITITsaATTVFW-------KGHRINIIDT 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   225 PGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDrlilelrippndaycKIGyiineA 304
Cdd:TIGR00484   83 PGHVDFTVEVERSLRVLDGAVAVLDAVGGVQPQSETVWRQANRYEVPRIAFVNKMD---------------KTG-----A 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   305 N--EVVKSFYSlyRADKNEIdrlifsPEKGNVGfasgkfgfcftlqsfarmyLKESYTTTSELMQNIDSFCNNLWGDLYY 382
Cdd:TIGR00484  143 NflRVVNQIKQ--RLGANAV------PIQLPIG-------------------AEDNFIGVIDLVEMKAYFFNGDKGTKAI 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   383 SKSLGKFLRSSNEStykfcsfvqfilepLYKIFIYSLSEQPKVLSTLLPSiGVYLSRSELKKS------PTSILDTICKR 456
Cdd:TIGR00484  196 EKEIPSDLLEQAKE--------------LRENLVEAVAEFDEELMEKYLE-GEELTIEEIKNAirkgvlNCEFFPVLCGS 260
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   457 FF--GGANAFTDLIVNNISNPLEASPIRTFNEYTGPQNDllaqriRNLSYDSPAVAFVTKhyhtSSMDSF---YSLCRVY 531
Cdd:TIGR00484  261 AFknKGVQLLLDAVVDYLPSPTDVPAIKGIDPDTEKEIE------RKASDDEPFSALAFK----VATDPFvgqLTFVRVY 330
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   532 CGILRKGDVVKvlgeSYTAEDPEDMSictiqNIWIFQARYKVEINEVPAGNWTLISGLNNSVikTATIICDttrsnkynn 611
Cdd:TIGR00484  331 SGVLKSGSYVK----NSRKNKKERVG-----RLVKMHANNREEIKEVRAGDICAAIGLKDTT--TGDTLCD--------- 390
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   612 nkpykevdelscknikdeiliedqrnqyltqqNDDLHILRPLKFPtNNVIRLACEPVNPSELPKMLEGLKSLDKAYPILK 691
Cdd:TIGR00484  391 --------------------------------PKIDVILERMEFP-EPVISLAVEPKTKADQEKMGIALGKLAEEDPTFR 437
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   692 TKV-EESGEHVIFGTGELQLDCIMHDLRRLYgNLDVKVSDPSVQLCETVLDTSVVKSfgdSSNKQN-------RIYIIAE 763
Cdd:TIGR00484  438 TFTdPETGQTIIAGMGELHLDIIVDRMKREF-KVEANVGAPQVAYRETIRSKVEVEG---KHAKQSggrgqygHVKIRFE 513
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   764 PLEKGLAE---DIENGIVkfydcidnestkyhqqilkdkynwdhlalrslwafgPTfeganvliddtlssitdkkslyEI 840
Cdd:TIGR00484  514 PLEPKGYEfvnEIKGGVI------------------------------------PR----------------------EY 535
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   841 KENIIQGFQWATREGPLLEENVRNVKFKILDVSLASNKASRGTGQIipAARRACYTAMLMASPRLMEPICLVEIVCPSES 920
Cdd:TIGR00484  536 IPAVDKGLQEAMESGPLAGYPVVDIKATLFDGSYHDVDSSEMAFKL--AASLAFKEAGKKANPVLLEPIMKVEVEVPEEY 613
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209881947   921 HNAIANVLLRRRGHcgkenpIPGTP----LVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWALVPGN 988
Cdd:TIGR00484  614 MGDVMGDLSSRRGI------IEGMEargnVQKIKAEVPLSEMFGYATDLRSFTQGRGTYSMEFLHYGEVPSS 679
EF2_snRNP_III cd16261
Domain III of Elongation Factor 2 (EF2); This model represents domain III of Elongation factor ...
660-730 1.07e-26

Domain III of Elongation Factor 2 (EF2); This model represents domain III of Elongation factor 2 (EF2) found in eukaryotes and archaea, and the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and its yeast counterpart Snu114p. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. This translocation step is catalyzed by EF-2_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis are important for the function of the U5-116 kD/Snu114p.


Pssm-ID: 293918 [Multi-domain]  Cd Length: 72  Bit Score: 103.81  E-value: 1.07e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209881947  660 VIRLACEPVNPSELPKMLEGLKSLDKAYPILKTKVEESGEHVIFGTGELQLDCIMHDLRRLYGNLDVKVSD 730
Cdd:cd16261     2 VVRVAVEPKNPSDLPKLVEGLKKLAKSDPTVQVKIEEEGEHLIAGAGELHLEICLKDLKEDFAGIEIKVSD 72
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
149-280 1.30e-26

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: 107.62  E-value: 1.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  149 RNIAIVGDLHHGKTSLIDMLVRITHKFSKlkTEKLNRYTDSRIDEQEREISIKATPISLILPNSINKSYLLNIIDTPGHV 228
Cdd:cd01890     1 RNFSIIAHIDHGKSTLADRLLELTGTVSE--REMKEQVLDSMDLERERGITIKAQAVRLFYKAKDGEEYLLNLIDTPGHV 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 209881947  229 NFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKID 280
Cdd:cd01890    79 DFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLEIIPVINKID 130
EFG_IV smart00889
Elongation factor G, domain IV; Translation elongation factors are responsible for two main ...
788-902 5.80e-26

Elongation factor G, domain IV; Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution. Elongation factor EF2 (EF-G) is a G-protein. It brings about the translocation of peptidyl-tRNA and mRNA through a ratchet-like mechanism: the binding of GTP-EF2 to the ribosome causes a counter-clockwise rotation in the small ribosomal subunit; the hydrolysis of GTP to GDP by EF2 and the subsequent release of EF2 causes a clockwise rotation of the small subunit back to the starting position. This twisting action destabilises tRNA-ribosome interactions, freeing the tRNA to translocate along the ribosome upon GTP-hydrolysis by EF2. EF2 binding also affects the entry and exit channel openings for the mRNA, widening it when bound to enable the mRNA to translocate along the ribosome. EF2 has five domains. This entry represents domain IV found in EF2 (or EF-G) of both prokaryotes and eukaryotes. The EF2-GTP-ribosome complex undergoes extensive structural rearrangement for tRNA-mRNA movement to occur. Domain IV, which extends from the 'body' of the EF2 molecule much like a lever arm, appears to be essential for the structural transition to take place.


Pssm-ID: 214887 [Multi-domain]  Cd Length: 120  Bit Score: 103.39  E-value: 5.80e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947    788 STKYHQQILKDKYNWDHLALRSLWAFGPTFEGANVLIDDTlssITDKKSLYEIKENIIQGFQWATREGPLLEENVRNVKF 867
Cdd:smart00889   11 PVKEAEGKHKKQSGGDGQYARVILEVEPLERGSGFEFDDT---IVGGVIPKEYIPAVEKGFREALEEGPLAGYPVVDVKV 87
                            90       100       110
                    ....*....|....*....|....*....|....*
gi 209881947    868 KILDVSLASnKASRGTGqIIPAARRACYTAMLMAS 902
Cdd:smart00889   88 TLLDGSYHE-VDSSEMA-FKPAARRAFKEALLKAG 120
EFTUD2 pfam16004
116 kDa U5 small nuclear ribonucleoprotein component N-terminus;
5-126 1.66e-25

116 kDa U5 small nuclear ribonucleoprotein component N-terminus;


Pssm-ID: 464968  Cd Length: 76  Bit Score: 100.69  E-value: 1.66e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947     5 EIYDEFGNYIGTEsesnldleisLDEDEDQSsdsqknpthdptevddvkminginrivdgmdiemdneAIILHEHKEYYE 84
Cdd:pfam16004    1 DLYDEFGNYIGPE----------LDSDDESN-------------------------------------AVVLHEDKQYYP 33
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 209881947    85 DADKIFGKDVEILFEDEDMHHIDTPTIVPLKDNKFDLVEGDI 126
Cdd:pfam16004   34 SAEEVYGPDVETLVQEEDAQPLTEPIIAPVKQKKFAVEEKDL 75
EFG_C pfam00679
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
904-992 1.37e-24

Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.


Pssm-ID: 425814 [Multi-domain]  Cd Length: 88  Bit Score: 98.39  E-value: 1.37e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   904 RLMEPICLVEIVCPSESHNAIANVLLRRRGHCGKENPIPGTpLVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWA 983
Cdd:pfam00679    1 VLLEPIEKVTIDVPEEYVGDVISDLNSRRGEILDMDPDDGG-RVVIEAEVPLAELFGFATELRSLTKGRGSFSMEFSGYQ 79

                   ....*....
gi 209881947   984 LVPGNPLDR 992
Cdd:pfam00679   80 PVPGDILDR 88
lepA TIGR01393
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ...
146-280 4.12e-24

elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a GTP-binding membrane protein related to EF-G and EF-Tu. Two types of phylogenetic tree, rooted by other GTP-binding proteins, suggest that eukaryotic homologs (including GUF1 of yeast) originated within the bacterial LepA family. The function is unknown. [Unknown function, General]


Pssm-ID: 130460 [Multi-domain]  Cd Length: 595  Bit Score: 108.18  E-value: 4.12e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   146 KLIRNIAIVGDLHHGKTSLIDMLVRITHKFSKlkTEKLNRYTDSRIDEQEREISIKATPISLILPNSINKSYLLNIIDTP 225
Cdd:TIGR01393    1 KNIRNFSIIAHIDHGKSTLADRLLEYTGAISE--REMREQVLDSMDLERERGITIKAQAVRLNYKAKDGETYVLNLIDTP 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 209881947   226 GHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKID 280
Cdd:TIGR01393   79 GHVDFSYEVSRSLAACEGALLLVDAAQGIEAQTLANVYLALENDLEIIPVINKID 133
Elongation_Factor_C cd01514
Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of ...
907-986 1.44e-22

Elongation factor G C-terminus. This domain includes the carboxyl terminal regions of elongation factors (EFs) bacterial EF-G, eukaryotic and archeal EF-2 and eukaryotic mitochondrial mtEFG1s and mtEFG2s. This group also includes proteins similar to the ribosomal protection proteins Tet(M) and Tet(O), BipA, LepA and, spliceosomal proteins: human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and yeast counterpart Snu114p. This domain adopts a ferredoxin-like fold consisting of an alpha-beta sandwich with anti-parallel beta-sheets, resembling the topology of domain III found in the elongation factors EF-G and eukaryotic EF-2, with which it forms the C-terminal block. The two domains however are not superimposable and domain III lacks some of the characteristics of this domain. EF-2/EF-G in complex with GTP, promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site, the uncharged tRNA from the P site to the E-site and, the mRNA is shifted one codon relative to the ribosome. Tet(M) and Tet(O) mediate Tc resistance. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner. BipA is a highly conserved protein with global regulatory properties in Escherichia coli. Yeast Snu114p is essential for cell viability and for splicing in vivo. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. The function of LepA proteins is unknown.


Pssm-ID: 238772 [Multi-domain]  Cd Length: 79  Bit Score: 92.55  E-value: 1.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  907 EPICLVEIVCPSESHNAIANVLLRRRGHCGKENPIpGTPLVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWALVP 986
Cdd:cd01514     1 EPIMKVEITVPEEYLGAVIGDLSKRRGEILGMEPR-GTGRVVIKAELPLAEMFGFATDLRSLTQGRASFSMEFSHYEPVP 79
EF2_snRNP_like_II cd03700
Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 ...
511-599 1.48e-21

Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein; This subfamily represents domain II of elongation factor (EF) EF-2 found in eukaryotes and archaea, and the C-terminal portion of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and its yeast counterpart Snu114p. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. This translocation step is catalyzed by EF-2_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of U5-116 kD/Snu114p.


Pssm-ID: 293901 [Multi-domain]  Cd Length: 95  Bit Score: 89.98  E-value: 1.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  511 FVTKHYHTSSMDSFYSLCRVYCGILRKGDVVKVLGESYTAEDPEDMSICTIQNIWIFQARYKVEINEVPAGNWTLISGLN 590
Cdd:cd03700     4 YSSKMVPTSDKGRFYAFGRVFAGTVHAGQKVRILGPNYTPGKKEDLRIKAIQRLWLMMGRYVEEINDVPAGNIVGLVGID 83

                  ....*....
gi 209881947  591 NSVIKTATI 599
Cdd:cd03700    84 QFLQKTGTT 92
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
148-281 1.39e-20

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: 90.73  E-value: 1.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  148 IRNIAIVGDLHHGKTSLIDMLVRITHKFSKlKTEKLNRYTDSRIDEQEREISIKATPISLILpnsinKSYLLNIIDTPGH 227
Cdd:cd01891     2 IRNIAIIAHVDHGKTTLVDALLKQSGTFRE-NEEVGERVMDSNDLERERGITILAKNTAITY-----KDTKINIIDTPGH 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 209881947  228 VNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDR 281
Cdd:cd01891    76 ADFGGEVERVLSMVDGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVVINKIDR 129
EFG_IV pfam03764
Elongation factor G, domain IV; This domain is found in elongation factor G, elongation factor ...
794-902 1.43e-19

Elongation factor G, domain IV; This domain is found in elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopts a ribosomal protein S5 domain 2-like fold.


Pssm-ID: 397710 [Multi-domain]  Cd Length: 121  Bit Score: 85.35  E-value: 1.43e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   794 QILKDKYNWDHLALRSLWAFGPTFEGA-NVLIDDTlssiTDKKSLYEIKENIIQGFQWATREGPLLEENVRNVKFKILDV 872
Cdd:pfam03764   18 YKHKKQSGGDGQYARVILRIEPLPPGSgNEFVDET----VGGQIPKEFIPAVEKGFQEAMKEGPLAGEPVTDVKVTLLDG 93
                           90       100       110
                   ....*....|....*....|....*....|
gi 209881947   873 SLASNKasRGTGQIIPAARRACYTAMLMAS 902
Cdd:pfam03764   94 SYHEVD--SSEAAFIPAARRAFREALLKAS 121
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
145-280 4.88e-19

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


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 92.39  E-value: 4.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  145 PKLIRNIAIVGDLHHGKTSLIDMLVRITHKFSKlkTEKLNRYTDSrID-EQEREISIKATPISLILPNSINKSYLLNIID 223
Cdd:COG0481     3 QKNIRNFSIIAHIDHGKSTLADRLLELTGTLSE--REMKEQVLDS-MDlERERGITIKAQAVRLNYKAKDGETYQLNLID 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 209881947  224 TPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKID 280
Cdd:COG0481    80 TPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVINKID 136
EF2_II cd16268
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ...
507-602 1.86e-18

Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 (EF-2) found in eukaryotes and archaea. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. This translocation step is catalyzed by EF-2_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site.


Pssm-ID: 293913 [Multi-domain]  Cd Length: 96  Bit Score: 81.11  E-value: 1.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  507 PAVAFVTKHYHTSSMDSFYSLCRVYCGILRKGDVVKVLGESYTAEDPEDMSICTIQNIWIFQARYKVEINEVPAGNWTLI 586
Cdd:cd16268     1 PLVMYVSKMVPTDKGAGFVAFGRVFSGTVRRGQEVYILGPKYVPGKKDDLKKKRIQQTYLMMGREREPVDEVPAGNIVGL 80
                          90
                  ....*....|....*.
gi 209881947  587 SGLNNSVIKTATIICD 602
Cdd:cd16268    81 VGLDDFLAKSGTTTSS 96
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
150-281 3.22e-18

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: 85.72  E-value: 3.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  150 NIAIVGDLHHGKTSLIDMLVRITHKFSKL-KTEKLNRYTDSRIDEQEREISIKATPISLilpnsinkSYL---LNIIDTP 225
Cdd:cd04170     1 NIALVGHSGSGKTTLAEALLYATGAIDRLgRVEDGNTVSDYDPEEKKRKMSIETSVAPL--------EWNghkINLIDTP 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 209881947  226 GHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDR 281
Cdd:cd04170    73 GYADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLPRIIFINKMDR 128
EFG_C smart00838
Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of ...
905-991 4.60e-17

Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.


Pssm-ID: 197906 [Multi-domain]  Cd Length: 85  Bit Score: 76.77  E-value: 4.60e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947    905 LMEPICLVEIVCPSESHNAIANVLLRRRGHCgkENPIPGTPLVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWAL 984
Cdd:smart00838    1 LLEPIMKVEVTVPEEYMGDVIGDLNSRRGKI--EGMEQRGGAQVIKAKVPLSEMFGYATDLRSATQGRATWSMEFSHYEE 78

                    ....*..
gi 209881947    985 VPGNPLD 991
Cdd:smart00838   79 VPKSIAE 85
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
150-282 2.75e-15

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: 76.51  E-value: 2.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  150 NIAIVGDLHHGKTSLIDMLVRITHKFSKL-KTEKLNRYTDSRIDEQEREISIKATPISLILPNSinksyLLNIIDTPGHV 228
Cdd:cd04168     1 NIGILAHVDAGKTTLTESLLYTSGAIRELgSVDKGTTRTDSMELERQRGITIFSAVASFQWEDT-----KVNIIDTPGHM 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 209881947  229 NFMDEFCASIRLCDGAVIVVDAILGISKHTeRMIYYCLReKHDI--VLLINKIDRL 282
Cdd:cd04168    76 DFIAEVERSLSVLDGAILVISAVEGVQAQT-RILFRLLR-KLNIptIIFVNKIDRA 129
PRK10218 PRK10218
translational GTPase TypA;
148-281 3.14e-13

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 73.59  E-value: 3.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  148 IRNIAIVGDLHHGKTSLIDMLVRITHKFSKlKTEKLNRYTDSRIDEQEREISIKATPISLILpnsinKSYLLNIIDTPGH 227
Cdd:PRK10218    5 LRNIAIIAHVDHGKTTLVDKLLQQSGTFDS-RAETQERVMDSNDLEKERGITILAKNTAIKW-----NDYRINIVDTPGH 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 209881947  228 VNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDR 281
Cdd:PRK10218   79 ADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDR 132
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
139-281 4.31e-13

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 73.13  E-value: 4.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  139 KDMMKqpklIRNIAIVGDLHHGKTSLIDMLVRITHKFSKlkteklNRYTDSRI---DEQERE--ISI--KATpislilpn 211
Cdd:COG1217     1 MMRED----IRNIAIIAHVDHGKTTLVDALLKQSGTFRE------NQEVAERVmdsNDLERErgITIlaKNT-------- 62
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209881947  212 SIN-KSYLLNIIDTPGHVNFMDEFCASIRLCDGAVIVVDAILG--------ISKhtermiyyCLREKHDIVLLINKIDR 281
Cdd:COG1217    63 AVRyKGVKINIVDTPGHADFGGEVERVLSMVDGVLLLVDAFEGpmpqtrfvLKK--------ALELGLKPIVVINKIDR 133
EFG_like_IV cd01680
Elongation Factor G-like domain IV. This family includes the translational elongation factor ...
793-902 1.27e-11

Elongation Factor G-like domain IV. This family includes the translational elongation factor termed EF-2 (for Archaea and Eukarya) and EF-G (for Bacteria), ribosomal protection proteins that mediate tetracycline resistance and, an evolutionarily conserved U5 snRNP-specific protein (U5-116kD). In complex with GTP, EF-G/EF-2 promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site of the small subunit of ribosome and the mRNA is shifted one codon relative to the ribosome. It has been shown that EF-G/EF-2_IV domain mimics the shape of anticodon arm of the tRNA in the structurally homologous ternary complex of Petra, EF-Tu (another transcriptional elongation factor) and GTP analog. The tip portion of this domain is found in a position that overlaps the anticodon arm of the A-site tRNA, implying that EF-G/EF-2 displaces the A-site tRNA to the P-site by physical interaction with the anticodon arm.


Pssm-ID: 238838 [Multi-domain]  Cd Length: 116  Bit Score: 62.65  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  793 QQILKDKYNWDHLALRslwaFGPTFEGANVLIDDtlsSITDKKSLYEIKENIIQGFQWATREGPLLEENVRNVKFKILDV 872
Cdd:cd01680    16 ERELGGKPQFGEVTLR----VEPLERGSGVRVVD---PVDEELLPAELKEAVEEGIRDACASGPLTGYPLTDVRVTVLDV 88
                          90       100       110
                  ....*....|....*....|....*....|
gi 209881947  873 SLASNKasRGTGQIIPAARRACYTAMLMAS 902
Cdd:cd01680    89 PYHEGV--STEAGFRAAAGRAFESAAQKAG 116
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
187-282 3.36e-10

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: 62.12  E-value: 3.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  187 TDSRIDEQEREISIKATPISLILpnsinKSYLLNIIDTPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMiyycL 266
Cdd:cd01886    39 MDWMEQERERGITIQSAATTCFW-----KDHRINIIDTPGHVDFTIEVERSLRVLDGAVAVFDAVAGVQPQTETV----W 109
                          90       100
                  ....*....|....*....|
gi 209881947  267 R--EKHDI--VLLINKIDRL 282
Cdd:cd01886   110 RqaDRYGVprIAFVNKMDRT 129
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
151-311 1.14e-09

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: 58.25  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  151 IAIVGDLHHGKTSLIDMLVRithkfsklkteklnrytdSRIDEQE-REI--SIKATPISLilPNSINKsylLNIIDTPGH 227
Cdd:cd01887     3 VTVMGHVDHGKTTLLDKIRK------------------TNVAAGEaGGItqHIGAYQVPI--DVKIPG---ITFIDTPGH 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  228 VNF--MDEFCASirLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDRLILELRIPPndaycKIGYIINEAN 305
Cdd:cd01887    60 EAFtnMRARGAS--VTDIAILVVAADDGVMPQTIEAINHAKAANVPIIVAINKIDKPYGTEADPE-----RVKNELSELG 132

                  ....*.
gi 209881947  306 EVVKSF 311
Cdd:cd01887   133 LVGEEW 138
EFG_mtEFG_C cd03713
EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational ...
907-986 4.73e-09

EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational elongation factor (EF) EF-G. Included in this group is the C-terminus of mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2) proteins. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homologue of mtEFG2, MEF2.


Pssm-ID: 239683 [Multi-domain]  Cd Length: 78  Bit Score: 54.07  E-value: 4.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  907 EPICLVEIVCPSESHNAIANVLLRRRGHCGKENPIPGTplVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWALVP 986
Cdd:cd03713     1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRGGW--KVIKAEVPLAEMFGYSTDLRSLTQGRGSFTMEFSHYEEVP 78
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
152-282 7.45e-09

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: 55.93  E-value: 7.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  152 AIVGDLHHGKTSLIdmlvrithkfsklkteklNRYTDSRIDEQEREISIKATPISLILPNSINKsYLLNIIDTPGHVNF- 230
Cdd:cd00882     1 VVVGRGGVGKSSLL------------------NALLGGEVGEVSDVPGTTRDPDVYVKELDKGK-VKLVLVDTPGLDEFg 61
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 209881947  231 ----MDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHD--IVLLINKIDRL 282
Cdd:cd00882    62 glgrEELARLLLRGADLILLVVDSTDRESEEDAKLLILRRLRKEGipIILVGNKIDLL 119
EFG_III pfam14492
Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a ...
660-728 2.29e-08

Elongation Factor G, domain III; This domain is found in Elongation Factor G. It shares a similar structure with domain V (pfam00679). Structural studies in drosophila indicate this is domain 3.


Pssm-ID: 464188 [Multi-domain]  Cd Length: 75  Bit Score: 51.71  E-value: 2.29e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   660 VIRLACEPVNPSELPKMLEGLKSLDKAYPILKTKV-EESGEHVIFGTGELQLDCIMHDLRRLYGnLDVKV 728
Cdd:pfam14492    5 VISVAIEPKTKGDEDKLSKALNRLLEEDPTLRVERdEETGETILSGMGELHLEIVVDRLKRKYG-VEVEL 73
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
150-280 5.77e-08

CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.


Pssm-ID: 206729 [Multi-domain]  Cd Length: 209  Bit Score: 54.50  E-value: 5.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  150 NIAIVGDLHHGKTSLIDMLVRITH-----KFSKLKTEKLNRYTDSRID--------EQERE--ISIK------ATPisli 208
Cdd:cd04166     1 RFITCGSVDDGKSTLIGRLLYDSKsifedQLAALERSKSSGTQGEKLDlallvdglQAEREqgITIDvayryfSTP---- 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209881947  209 lpnsiNKSYLlnIIDTPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYC--LREKHdIVLLINKID 280
Cdd:cd04166    77 -----KRKFI--IADTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIAslLGIRH-VVVAVNKMD 142
EFG_III cd16262
Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial ...
660-731 1.46e-07

Domain III of Elongation Factor G (EFG); This model represents domain III of bacterial Elongation factor G (EF-G), and mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2), which play an important role during peptide synthesis and tRNA site changes. In bacteria, this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. mtEFG1 and mtEFG2 show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects, and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants of the yeast homolog of mtEFG2, MEF2.


Pssm-ID: 293919 [Multi-domain]  Cd Length: 76  Bit Score: 49.76  E-value: 1.46e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209881947  660 VIRLACEPVNPSELPKMLEGLKSLDKAYPILKTKV-EESGEHVIFGTGELQLDCIMHDLRRLYGnLDVKVSDP 731
Cdd:cd16262     4 VISLAIEPKTKADEDKLSKALARLAEEDPTLRVSRdEETGQTILSGMGELHLEIIVERLKREYG-VEVEVGKP 75
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
148-280 2.18e-07

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: 51.60  E-value: 2.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   148 IRNIAIVGDLHHGKTSLIDMLVRiTHKFsklKTEKLNRYTDSRIDEQEREISIKatpislilpnsinksYLLNIIDTPGH 227
Cdd:TIGR00231    1 DIKIVIVGHPNVGKSTLLNSLLG-NKGS---ITEYYPGTTRNYVTTVIEEDGKT---------------YKFNLLDTAGQ 61
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   228 VNF-------MDEFCASIRLCDGAVIVVDAILGISKHTERMIYYClREKHDIVLLINKID 280
Cdd:TIGR00231   62 EDYdairrlyYPQVERSLRVFDIVILVLDVEEILEKQTKEIIHHA-DSGVPIILVGNKID 120
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
524-599 4.46e-07

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: 48.03  E-value: 4.46e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209881947   524 FYSLCRVYCGILRKGDVVKVLGeSYTAEDPEdmsICTIQNIWIFQARYKVEINEVPAGNWTLISGLNNsVIKTATI 599
Cdd:pfam03144    2 TVATGRVESGTLKKGDKVRILP-NGTGKKKI---VTRVTSLLMFHAPLREAVAGDNAGLILAGVGLED-IRVGDTL 72
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
151-281 3.21e-06

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: 48.37  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  151 IAIVGDLHHGKTSLIDMLVRIThkfsklkteklnryTDSRIDEQEREISIKATPISLILPNSINksylLNIIDTPGHVNF 230
Cdd:cd04171     2 IGTAGHIDHGKTTLIKALTGIE--------------TDRLPEEKKRGITIDLGFAYLDLPDGKR----LGFIDVPGHEKF 63
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 209881947  231 MDEFCASIRLCDGAVIVVDAILGISKHTERMIYYC--LREKHdIVLLINKIDR 281
Cdd:cd04171    64 VKNMLAGAGGIDAVLLVVAADEGIMPQTREHLEILelLGIKK-GLVVLTKADL 115
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
150-280 5.50e-06

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: 48.13  E-value: 5.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  150 NIAIVGDLHHGKTSLIDMLVRI--THKFSKLKteklnrytdsriDEQEREISI---------KATPISLILPNSINKSYL 218
Cdd:cd01889     2 NVGLLGHVDSGKTSLAKALSEIasTAAFDKNP------------QSQERGITLdlgfssfevDKPKHLEDNENPQIENYQ 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 209881947  219 LNIIDTPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKID 280
Cdd:cd01889    70 ITLVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVVLNKID 131
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
150-278 8.95e-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: 45.69  E-value: 8.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947   150 NIAIVGDLHHGKTSLIDMLVRithkfSKLKTEKLNRYTdsrIDEQEREISIKATPIslilpnsinksyllNIIDTPGHVN 229
Cdd:pfam01926    1 RVALVGRPNVGKSTLINALTG-----AKAIVSDYPGTT---RDPNEGRLELKGKQI--------------ILVDTPGLIE 58
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 209881947   230 -------FMDEFCASIRlCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINK 278
Cdd:pfam01926   59 gasegegLGRAFLAIIE-ADLILFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
151-298 1.07e-05

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 46.90  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  151 IAIVGDLHHGKTSLIDMLVRIthKFSKLKTEKLNrytdsRIDEQEREISIKATPISlilpnsinksylLNIIDTPGHVNF 230
Cdd:COG1100     6 IVVVGTGGVGKTSLVNRLVGD--IFSLEKYLSTN-----GVTIDKKELKLDGLDVD------------LVIWDTPGQDEF 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209881947  231 MDE---FCASIRLCDGAVIVVDAILGISKHTERMIYYCLRE---KHDIVLLINKIDRLILELRIPPNDAYCKIG 298
Cdd:COG1100    67 RETrqfYARQLTGASLYLFVVDGTREETLQSLYELLESLRRlgkKSPIILVLNKIDLYDEEEIEDEERLKEALS 140
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
141-280 2.33e-05

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: 48.01  E-value: 2.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  141 MMKQ-PKLirNIAIVGDLHHGKTSLIDMLVRIT-----HKFSKLK--TEKLNRYT-------DSRIDEQEREISIKATPI 205
Cdd:COG5256     1 MASEkPHL--NLVVIGHVDHGKSTLVGRLLYETgaideHIIEKYEeeAEKKGKESfkfawvmDRLKEERERGVTIDLAHK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  206 SLILPNsinksYLLNIIDTPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTermiyyclREkH----------DIVLL 275
Cdd:COG5256    79 KFETDK-----YYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQT--------RE-HaflartlginQLIVA 144

                  ....*
gi 209881947  276 INKID 280
Cdd:COG5256   145 VNKMD 149
mtEFG1_C cd04097
mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in ...
907-986 4.61e-05

mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in eukaryotes. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s) mtEFG2s are not present in this group.


Pssm-ID: 239764 [Multi-domain]  Cd Length: 78  Bit Score: 42.69  E-value: 4.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  907 EPICLVEIVCPSESHNAIANVLLRRRGhcgkenPIPGTPL----VTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHW 982
Cdd:cd04097     1 EPIMKVEVTAPTEFQGNVIGLLNKRKG------TIVDTDTgedeFTLEAEVPLNDMFGYSTELRSMTQGKGEFSMEFSRY 74

                  ....
gi 209881947  983 ALVP 986
Cdd:cd04097    75 APVP 78
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
150-280 1.40e-04

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: 45.46  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  150 NIAIVGDLHHGKTSLI---------------DMLVRITHKFSKLKTEkLNRYTDSRIDEQEREISIK------ATPisli 208
Cdd:COG2895    19 RFITCGSVDDGKSTLIgrllydtksifedqlAALERDSKKRGTQEID-LALLTDGLQAEREQGITIDvayryfSTP---- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  209 lpnsiNKSYLlnIIDTPGHVnfmdEFC------ASirLCDGAVIVVDAILGISKHTERMIYYC--LREKHdIVLLINKID 280
Cdd:COG2895    94 -----KRKFI--IADTPGHE----QYTrnmvtgAS--TADLAILLIDARKGVLEQTRRHSYIAslLGIRH-VVVAVNKMD 159
infB CHL00189
translation initiation factor 2; Provisional
151-281 2.64e-04

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 45.21  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  151 IAIVGDLHHGKTSLIDmlvrithkfsKLKTEKLNRYTDSRIDEqereiSIKATPISLILPNSINKsylLNIIDTPGHVNF 230
Cdd:CHL00189  247 VTILGHVDHGKTTLLD----------KIRKTQIAQKEAGGITQ-----KIGAYEVEFEYKDENQK---IVFLDTPGHEAF 308
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 209881947  231 MDEFCASIRLCDGAVIVVDAILGISKHTERMIYYCLREKHDIVLLINKIDR 281
Cdd:CHL00189  309 SSMRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDK 359
Tet_C cd03711
Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology ...
907-986 5.03e-04

Tet_C: C-terminus of ribosomal protection proteins Tet(M) and Tet(O). This domain has homology to the C terminal domains of the elongation factors EF-G and EF-2. Tet(M) and Tet(O) catalyze the release of tetracycline (Tc) from the ribosome in a GTP-dependent manner thereby mediating Tc resistance. Tcs are broad-spectrum antibiotics. Typical Tcs bind to the ribosome and inhibit the elongation phase of protein synthesis, by inhibiting the occupation of site A by aminoacyl-tRNA.


Pssm-ID: 239682 [Multi-domain]  Cd Length: 78  Bit Score: 39.53  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  907 EPICLVEIVCPSESHNAIANVLLRRRGHCgkENPIPGTPLVTIYGFIPAIESFGFETDLRVHTSGQAFCSTCFDHWALVP 986
Cdd:cd03711     1 EPYLRFELEVPQDALGRAMSDLAKMGATF--EDPQIKGDEVTLEGTIPVATSQDYQSELPSYTHGEGVLETEFKGYRPCH 78
PLN03126 PLN03126
Elongation factor Tu; Provisional
143-286 1.37e-03

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 42.29  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  143 KQPKLirNIAIVGDLHHGKTSLIDMLvriTHKFSKLKTEKLNRY--TDSRIDEQEREISIKATPISLilpNSINKSYLLn 220
Cdd:PLN03126   78 KKPHV--NIGTIGHVDHGKTTLTAAL---TMALASMGGSAPKKYdeIDAAPEERARGITINTATVEY---ETENRHYAH- 148
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 209881947  221 iIDTPGHVNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIyycLREKH----DIVLLINKIDRL----ILEL 286
Cdd:PLN03126  149 -VDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHI---LLAKQvgvpNMVVFLNKQDQVddeeLLEL 218
tufA CHL00071
elongation factor Tu
150-286 1.67e-03

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 41.87  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  150 NIAIVGDLHHGKTSLIdmlVRITHKFSKLKTEKLNRYT--DSRIDEQEREISIKATPISLilpNSINKSYLLniIDTPGH 227
Cdd:CHL00071   14 NIGTIGHVDHGKTTLT---AAITMTLAAKGGAKAKKYDeiDSAPEEKARGITINTAHVEY---ETENRHYAH--VDCPGH 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209881947  228 VNFMDEFCASIRLCDGAVIVVDAILGISKHTERMIyycLREKH----DIVLLINKIDRL----ILEL 286
Cdd:CHL00071   86 ADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHI---LLAKQvgvpNIVVFLNKEDQVddeeLLEL 149
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
142-280 1.85e-03

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 42.04  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  142 MKQPKLIRNIAIVGDLHHGKTSLIDMLV--------RITHKFSKLKTE------KLNRYTDSRIDEQEREISIKatpISL 207
Cdd:PTZ00141    1 MGKEKTHINLVVIGHVDSGKSTTTGHLIykcggidkRTIEKFEKEAAEmgkgsfKYAWVLDKLKAERERGITID---IAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  208 ILPNSinKSYLLNIIDTPGHVNFMDEFCASIRLCDGAVIVVDAILG-----ISKHTER----MIYYCLREKHDIVlLINK 278
Cdd:PTZ00141   78 WKFET--PKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGefeagISKDGQTrehaLLAFTLGVKQMIV-CINK 154

                  ..
gi 209881947  279 ID 280
Cdd:PTZ00141  155 MD 156
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
142-253 7.12e-03

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 40.07  E-value: 7.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209881947  142 MKQPKLIRNIAIVGDLHHGKTSLIDMLV--------RITHKFSKLKTEKLNR------YTDSRIDEQEREISIkatpiSL 207
Cdd:PLN00043    1 MGKEKVHINIVVIGHVDSGKSTTTGHLIyklggidkRVIERFEKEAAEMNKRsfkyawVLDKLKAERERGITI-----DI 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 209881947  208 ILPNSINKSYLLNIIDTPGHVNFMDEFCASIRLCDGAVIVVDAILG 253
Cdd:PLN00043   76 ALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTG 121
 
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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