NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488946855|ref|WP_002857930|]
View 

MULTISPECIES: selenocysteine-specific translation elongation factor [Campylobacter]

Protein Classification

selenocysteine-specific translation elongation factor( domain architecture ID 11461714)

selenocysteine-specific translation elongation factor binds GTP and GDP and transfers selenocysteinyl-tRNA to the ribosome

Graphical summary

 Zoom to residue level

show extra options Â»

Show site features     Horizontal zoom: Ã—

List of domain hits

Name Accession Description Interval E-value
SelB super family cl34578
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
4-586 1.27e-127

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


The actual alignment was detected with superfamily member COG3276:

Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 388.89  E-value: 1.27e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   4 VIIGTAGHIDHGKTSLIKALNGFEGDSLKEEQERQITINLSFSNLKLKD-KNISFIDVPGHKDLVKTMVSGAFGFSVCLF 82
Cdd:COG3276    1 MIIGTAGHIDHGKTTLVKALTGIDTDRLKEEKKRGITIDLGFAYLPLPDgRRLGFVDVPGHEKFIKNMLAGAGGIDLVLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  83 VVDINEGLKEQSLEHLEILKILDIKNIILVLSKCDLC--ENIEQKSVEILEELKNLDYPILKVFHTSIKNNQGIEELKNY 160
Cdd:COG3276   81 VVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLVdeEWLELVEEEIRELLAGTFLEDAPIVPVSAVTGEGIDELRAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 161 LYTI--ENKENDEELIFHYYIDRVFSLKGIGTVVTGSLNEGSITLNEKIICLDTQKELIVKNIQNHDTNLEQIKACNRVA 238
Cdd:COG3276  161 LDALaaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 239 LSL-NCDYKELKKGYLLSKKGYFKAFKECDALVK-----AKNL-QNSKMIFCVGSRQIECKINILKKLE---NDEFFVHF 308
Cdd:COG3276  241 LNLaGVEKEEIERGDVLAAPGALRPTDRIDVRLRllpsaPRPLkHWQRVHLHHGTAEVLARVVLLDREElapGEEALAQL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 309 SFDKNVFLSFDEAFIL--LQNNRVIGGGKVLNPLSEPLKK--EQKNKFLMFLKNKDFKAAFSFLKDAHKYGFGLLSSYQR 384
Cdd:COG3276  321 RLEEPLVAARGDRFILrdYSPRRTIGGGRVLDPNPPKRKRrsPERLAWLEALAKGDPAELLAALLALAPGGLSLAELARL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 385 FKLSHQKALKLAKELNQVFV--DEKNLNVYHLQSLEEIKNFIKFIL----EKNPYAM-LSAHSLALRIT-WASENFCELG 456
Cdd:COG3276  401 TGLSEEELAALLEELGARVVvlGGGDRLLVSAAALEALKERLLAALaefhEKNPLRPgLSREELRRRLLpRLPEKLFDAL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 457 LKEMSN----LLDFQNGIYFKKGIDFEKLQEKNNNQMYEILKKQGIKPEAPYNLYDFLELDRKSGDNILKKLTQKGLVVR 532
Cdd:COG3276  481 LEELLAegelVLTGGWLHLPGHKVTLSAEEEALWQRLLPLLAAGGFPPPWLRELAAELGLEEEAVRELLRLLLRLGELVK 560
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488946855 533 LSHNLFIEKQALEKLMQECLNLLK-NQSLDVQSMKEYFNLSRKYAIAYLEYLDKF 586
Cdd:COG3276  561 VVDDLFYLAAALAALAALLAALLAeTGAAAAADRRDLLGGRRKLLLLLLEFFDRR 615
 
Name Accession Description Interval E-value
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
4-586 1.27e-127

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 388.89  E-value: 1.27e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   4 VIIGTAGHIDHGKTSLIKALNGFEGDSLKEEQERQITINLSFSNLKLKD-KNISFIDVPGHKDLVKTMVSGAFGFSVCLF 82
Cdd:COG3276    1 MIIGTAGHIDHGKTTLVKALTGIDTDRLKEEKKRGITIDLGFAYLPLPDgRRLGFVDVPGHEKFIKNMLAGAGGIDLVLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  83 VVDINEGLKEQSLEHLEILKILDIKNIILVLSKCDLC--ENIEQKSVEILEELKNLDYPILKVFHTSIKNNQGIEELKNY 160
Cdd:COG3276   81 VVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLVdeEWLELVEEEIRELLAGTFLEDAPIVPVSAVTGEGIDELRAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 161 LYTI--ENKENDEELIFHYYIDRVFSLKGIGTVVTGSLNEGSITLNEKIICLDTQKELIVKNIQNHDTNLEQIKACNRVA 238
Cdd:COG3276  161 LDALaaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 239 LSL-NCDYKELKKGYLLSKKGYFKAFKECDALVK-----AKNL-QNSKMIFCVGSRQIECKINILKKLE---NDEFFVHF 308
Cdd:COG3276  241 LNLaGVEKEEIERGDVLAAPGALRPTDRIDVRLRllpsaPRPLkHWQRVHLHHGTAEVLARVVLLDREElapGEEALAQL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 309 SFDKNVFLSFDEAFIL--LQNNRVIGGGKVLNPLSEPLKK--EQKNKFLMFLKNKDFKAAFSFLKDAHKYGFGLLSSYQR 384
Cdd:COG3276  321 RLEEPLVAARGDRFILrdYSPRRTIGGGRVLDPNPPKRKRrsPERLAWLEALAKGDPAELLAALLALAPGGLSLAELARL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 385 FKLSHQKALKLAKELNQVFV--DEKNLNVYHLQSLEEIKNFIKFIL----EKNPYAM-LSAHSLALRIT-WASENFCELG 456
Cdd:COG3276  401 TGLSEEELAALLEELGARVVvlGGGDRLLVSAAALEALKERLLAALaefhEKNPLRPgLSREELRRRLLpRLPEKLFDAL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 457 LKEMSN----LLDFQNGIYFKKGIDFEKLQEKNNNQMYEILKKQGIKPEAPYNLYDFLELDRKSGDNILKKLTQKGLVVR 532
Cdd:COG3276  481 LEELLAegelVLTGGWLHLPGHKVTLSAEEEALWQRLLPLLAAGGFPPPWLRELAAELGLEEEAVRELLRLLLRLGELVK 560
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488946855 533 LSHNLFIEKQALEKLMQECLNLLK-NQSLDVQSMKEYFNLSRKYAIAYLEYLDKF 586
Cdd:COG3276  561 VVDDLFYLAAALAALAALLAALLAeTGAAAAADRRDLLGGRRKLLLLLLEFFDRR 615
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
5-171 1.37e-87

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: 269.09  E-value: 1.37e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   5 IIGTAGHIDHGKTSLIKALNGFEGDSLKEEQERQITINLSFSNLKLKD-KNISFIDVPGHKDLVKTMVSGAFGFSVCLFV 83
Cdd:cd04171    1 IIGTAGHIDHGKTTLIKALTGIETDRLPEEKKRGITIDLGFAYLDLPDgKRLGFIDVPGHEKFVKNMLAGAGGIDAVLLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  84 VDINEGLKEQSLEHLEILKILDIKNIILVLSKCDLCEN--IEQKSVEILEELKNLDYPILKVFHTSIKNNQGIEELKNYL 161
Cdd:cd04171   81 VAADEGIMPQTREHLEILELLGIKKGLVVLTKADLVDEdrLELVEEEILELLAGTFLADAPIFPVSSVTGEGIEELKNYL 160
                        170
                 ....*....|
gi 488946855 162 YTIENKENDE 171
Cdd:cd04171  161 DELAEPQSKD 170
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
4-598 4.06e-66

selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 226.29  E-value: 4.06e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855    4 VIIGTAGHIDHGKTSLIKALNGFEGDSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKDLVKTMVSGAFGFSVCLFV 83
Cdd:TIGR00475   1 MIIATAGHVDHGKTTLLKALTGIAADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAIAGGGGIDAALLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   84 VDINEGLKEQSLEHLEILKILDIKNIILVLSKCD-----LCENIEQKSVEILEELKNLDYpiLKVFHTSIKNNQGIEELK 158
Cdd:TIGR00475  81 VDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADrvneeEIKRTEMFMKQILNSYIFLKN--AKIFKTSAKTGQGIGELK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  159 NYLYTIENKENDEEL--IFHYYIDRVFSLKGIGTVVTGSLNEGSITLNEKIICLDTQKELIVKNIQNHDTNLEQIKACNR 236
Cdd:TIGR00475 159 KELKNLLESLDIKRIqkPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  237 VALSLN-CDYKELKKGYLLSKKGYFKAFKECDALVKAKNLQNSKMIFCVGSRQIECKINILkklenDEFFVHFSFDKNVF 315
Cdd:TIGR00475 239 IALNLMdVEPESLKRGLLILTPEDPKLRVVVKFIAEVPLLELQPYHIAHGMSVTTGKISLL-----DKGIALLTLDAPLI 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  316 LSFDEAFILLQNNR-VIGGGKVLnplsEPLKKEQKNKFLMflknkdfkaafsflkdahKYGFGLLSSYQRFKLSHQKA-- 392
Cdd:TIGR00475 314 LAKGDKLVLRDSSGnFLAGARVL----EPPVRVKRKAFIA------------------ELIKAGDSCYCIFLLLERGAvd 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  393 --LKLAKELNQVFVDEKNLNVYHLQS---------LEEIKNFIKFILEKNPYAMLSAHSLAL-RITWASENFCELGLKEM 460
Cdd:TIGR00475 372 lgLEWFKQLTGILIMRLLLPPTTIRIcgfgenidfGEVEVKKILVKLGTEQHDVKGVDKERLeRMASLNEELLKTAIEKL 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  461 SNLLDFQNGIYfkkgIDFEKLQEKNNNQMYEILKkqGIKPEAPYNLYDFLE---LDRKSGDNILKKLTQKGLVVRLSHNL 537
Cdd:TIGR00475 452 IGTYKIGGWLH----IPDHKSDFEKEEDIWQKIK--GTFGTKGAWVREFAEevnGDEKVMLKRVRKAGHRGGETLIVKDR 525
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488946855  538 FIeKQALEKLMQEClnllknQSLDVQSMKEYFNLSRKYAIAYLEYLDKFPQVSKEAEKRFL 598
Cdd:TIGR00475 526 LL-KKYINELKEEG------GTFNVQQARDKLGLGRKLLIQLLEYFDRLGFTRREGNDHRL 579
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
5-244 1.08e-42

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 162.14  E-value: 1.08e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   5 IIGTAGHIDHGKTSLIKALNGFEGDSLKEEQERQITINLSFSNLKLKD-KNISFIDVPGHKDLVKTMVSGAFGFSVCLFV 83
Cdd:PRK10512   2 IIATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYAYWPQPDgRVLGFIDVPGHEKFLSNMLAGVGGIDHALLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  84 VDINEGLKEQSLEHLEILKILDIKNIILVLSKCDLCEN--IEQKSVEILEELKNLDYPILKVFHTSIKNNQGIEELKNYL 161
Cdd:PRK10512  82 VACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEarIAEVRRQVKAVLREYGFAEAKLFVTAATEGRGIDALREHL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 162 YTIENKENDEELIFHYYIDRVFSLKGIGTVVTGSLNEGSITLNEKIICLDTQKELIVKNIQNHDTNLEQIKACNRVALSL 241
Cdd:PRK10512 162 LQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNI 241

                 ...
gi 488946855 242 NCD 244
Cdd:PRK10512 242 AGD 244
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
2-157 1.38e-30

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: 118.01  E-value: 1.38e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855    2 KSVIIGTAGHIDHGKTSL---------------IKALNGFEG-DSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKD 65
Cdd:pfam00009   2 RHRNIGIIGHVDHGKTTLtdrllyytgaiskrgEVKGEGEAGlDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   66 LVKTMVSGAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKnIILVLSKCDLC-----ENIEQKSVEILEELKNLDYPI 140
Cdd:pfam00009  82 FVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVdgaelEEVVEEVSRELLEKYGEDGEF 160
                         170
                  ....*....|....*..
gi 488946855  141 LKVFHTSIKNNQGIEEL 157
Cdd:pfam00009 161 VPVVPGSALKGEGVQTL 177
 
Name Accession Description Interval E-value
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
4-586 1.27e-127

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 388.89  E-value: 1.27e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   4 VIIGTAGHIDHGKTSLIKALNGFEGDSLKEEQERQITINLSFSNLKLKD-KNISFIDVPGHKDLVKTMVSGAFGFSVCLF 82
Cdd:COG3276    1 MIIGTAGHIDHGKTTLVKALTGIDTDRLKEEKKRGITIDLGFAYLPLPDgRRLGFVDVPGHEKFIKNMLAGAGGIDLVLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  83 VVDINEGLKEQSLEHLEILKILDIKNIILVLSKCDLC--ENIEQKSVEILEELKNLDYPILKVFHTSIKNNQGIEELKNY 160
Cdd:COG3276   81 VVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLVdeEWLELVEEEIRELLAGTFLEDAPIVPVSAVTGEGIDELRAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 161 LYTI--ENKENDEELIFHYYIDRVFSLKGIGTVVTGSLNEGSITLNEKIICLDTQKELIVKNIQNHDTNLEQIKACNRVA 238
Cdd:COG3276  161 LDALaaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRVRGIQVHGQPVEEAYAGQRVA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 239 LSL-NCDYKELKKGYLLSKKGYFKAFKECDALVK-----AKNL-QNSKMIFCVGSRQIECKINILKKLE---NDEFFVHF 308
Cdd:COG3276  241 LNLaGVEKEEIERGDVLAAPGALRPTDRIDVRLRllpsaPRPLkHWQRVHLHHGTAEVLARVVLLDREElapGEEALAQL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 309 SFDKNVFLSFDEAFIL--LQNNRVIGGGKVLNPLSEPLKK--EQKNKFLMFLKNKDFKAAFSFLKDAHKYGFGLLSSYQR 384
Cdd:COG3276  321 RLEEPLVAARGDRFILrdYSPRRTIGGGRVLDPNPPKRKRrsPERLAWLEALAKGDPAELLAALLALAPGGLSLAELARL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 385 FKLSHQKALKLAKELNQVFV--DEKNLNVYHLQSLEEIKNFIKFIL----EKNPYAM-LSAHSLALRIT-WASENFCELG 456
Cdd:COG3276  401 TGLSEEELAALLEELGARVVvlGGGDRLLVSAAALEALKERLLAALaefhEKNPLRPgLSREELRRRLLpRLPEKLFDAL 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 457 LKEMSN----LLDFQNGIYFKKGIDFEKLQEKNNNQMYEILKKQGIKPEAPYNLYDFLELDRKSGDNILKKLTQKGLVVR 532
Cdd:COG3276  481 LEELLAegelVLTGGWLHLPGHKVTLSAEEEALWQRLLPLLAAGGFPPPWLRELAAELGLEEEAVRELLRLLLRLGELVK 560
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488946855 533 LSHNLFIEKQALEKLMQECLNLLK-NQSLDVQSMKEYFNLSRKYAIAYLEYLDKF 586
Cdd:COG3276  561 VVDDLFYLAAALAALAALLAALLAeTGAAAAADRRDLLGGRRKLLLLLLEFFDRR 615
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
5-171 1.37e-87

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: 269.09  E-value: 1.37e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   5 IIGTAGHIDHGKTSLIKALNGFEGDSLKEEQERQITINLSFSNLKLKD-KNISFIDVPGHKDLVKTMVSGAFGFSVCLFV 83
Cdd:cd04171    1 IIGTAGHIDHGKTTLIKALTGIETDRLPEEKKRGITIDLGFAYLDLPDgKRLGFIDVPGHEKFVKNMLAGAGGIDAVLLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  84 VDINEGLKEQSLEHLEILKILDIKNIILVLSKCDLCEN--IEQKSVEILEELKNLDYPILKVFHTSIKNNQGIEELKNYL 161
Cdd:cd04171   81 VAADEGIMPQTREHLEILELLGIKKGLVVLTKADLVDEdrLELVEEEILELLAGTFLADAPIFPVSSVTGEGIEELKNYL 160
                        170
                 ....*....|
gi 488946855 162 YTIENKENDE 171
Cdd:cd04171  161 DELAEPQSKD 170
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
4-598 4.06e-66

selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 226.29  E-value: 4.06e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855    4 VIIGTAGHIDHGKTSLIKALNGFEGDSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKDLVKTMVSGAFGFSVCLFV 83
Cdd:TIGR00475   1 MIIATAGHVDHGKTTLLKALTGIAADRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNAIAGGGGIDAALLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   84 VDINEGLKEQSLEHLEILKILDIKNIILVLSKCD-----LCENIEQKSVEILEELKNLDYpiLKVFHTSIKNNQGIEELK 158
Cdd:TIGR00475  81 VDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADrvneeEIKRTEMFMKQILNSYIFLKN--AKIFKTSAKTGQGIGELK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  159 NYLYTIENKENDEEL--IFHYYIDRVFSLKGIGTVVTGSLNEGSITLNEKIICLDTQKELIVKNIQNHDTNLEQIKACNR 236
Cdd:TIGR00475 159 KELKNLLESLDIKRIqkPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPINHEVRVKAIQAQNQDVEIAYAGQR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  237 VALSLN-CDYKELKKGYLLSKKGYFKAFKECDALVKAKNLQNSKMIFCVGSRQIECKINILkklenDEFFVHFSFDKNVF 315
Cdd:TIGR00475 239 IALNLMdVEPESLKRGLLILTPEDPKLRVVVKFIAEVPLLELQPYHIAHGMSVTTGKISLL-----DKGIALLTLDAPLI 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  316 LSFDEAFILLQNNR-VIGGGKVLnplsEPLKKEQKNKFLMflknkdfkaafsflkdahKYGFGLLSSYQRFKLSHQKA-- 392
Cdd:TIGR00475 314 LAKGDKLVLRDSSGnFLAGARVL----EPPVRVKRKAFIA------------------ELIKAGDSCYCIFLLLERGAvd 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  393 --LKLAKELNQVFVDEKNLNVYHLQS---------LEEIKNFIKFILEKNPYAMLSAHSLAL-RITWASENFCELGLKEM 460
Cdd:TIGR00475 372 lgLEWFKQLTGILIMRLLLPPTTIRIcgfgenidfGEVEVKKILVKLGTEQHDVKGVDKERLeRMASLNEELLKTAIEKL 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  461 SNLLDFQNGIYfkkgIDFEKLQEKNNNQMYEILKkqGIKPEAPYNLYDFLE---LDRKSGDNILKKLTQKGLVVRLSHNL 537
Cdd:TIGR00475 452 IGTYKIGGWLH----IPDHKSDFEKEEDIWQKIK--GTFGTKGAWVREFAEevnGDEKVMLKRVRKAGHRGGETLIVKDR 525
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488946855  538 FIeKQALEKLMQEClnllknQSLDVQSMKEYFNLSRKYAIAYLEYLDKFPQVSKEAEKRFL 598
Cdd:TIGR00475 526 LL-KKYINELKEEG------GTFNVQQARDKLGLGRKLLIQLLEYFDRLGFTRREGNDHRL 579
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
5-244 1.08e-42

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 162.14  E-value: 1.08e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   5 IIGTAGHIDHGKTSLIKALNGFEGDSLKEEQERQITINLSFSNLKLKD-KNISFIDVPGHKDLVKTMVSGAFGFSVCLFV 83
Cdd:PRK10512   2 IIATAGHVDHGKTTLLQAITGVNADRLPEEKKRGMTIDLGYAYWPQPDgRVLGFIDVPGHEKFLSNMLAGVGGIDHALLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  84 VDINEGLKEQSLEHLEILKILDIKNIILVLSKCDLCEN--IEQKSVEILEELKNLDYPILKVFHTSIKNNQGIEELKNYL 161
Cdd:PRK10512  82 VACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEarIAEVRRQVKAVLREYGFAEAKLFVTAATEGRGIDALREHL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 162 YTIENKENDEELIFHYYIDRVFSLKGIGTVVTGSLNEGSITLNEKIICLDTQKELIVKNIQNHDTNLEQIKACNRVALSL 241
Cdd:PRK10512 162 LQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMRVRGLHAQNQPTEQAQAGQRIALNI 241

                 ...
gi 488946855 242 NCD 244
Cdd:PRK10512 242 AGD 244
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
5-165 5.45e-39

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: 141.28  E-value: 5.45e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   5 IIGTAGHIDHGKTSLIKALNGFEG-------------DSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKDLVKTMV 71
Cdd:cd00881    1 NVGVIGHVDHGKTTLTGSLLYQTGaidrrgtrketflDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  72 SGAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKnIILVLSKCDLC--ENIEQKSVEILEELKNLDYPILK-----VF 144
Cdd:cd00881   81 RGLAQADGALLVVDANEGVEPQTREHLNIALAGGLP-IIVAVNKIDRVgeEDFDEVLREIKELLKLIGFTFLKgkdvpII 159
                        170       180
                 ....*....|....*....|.
gi 488946855 145 HTSIKNNQGIEELKNYLYTIE 165
Cdd:cd00881  160 PISALTGEGIEELLDAIVEHL 180
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
2-157 1.38e-30

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: 118.01  E-value: 1.38e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855    2 KSVIIGTAGHIDHGKTSL---------------IKALNGFEG-DSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKD 65
Cdd:pfam00009   2 RHRNIGIIGHVDHGKTTLtdrllyytgaiskrgEVKGEGEAGlDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHVD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   66 LVKTMVSGAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKnIILVLSKCDLC-----ENIEQKSVEILEELKNLDYPI 140
Cdd:pfam00009  82 FVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVdgaelEEVVEEVSRELLEKYGEDGEF 160
                         170
                  ....*....|....*..
gi 488946855  141 LKVFHTSIKNNQGIEEL 157
Cdd:pfam00009 161 VPVVPGSALKGEGVQTL 177
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
175-256 2.09e-30

Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.


Pssm-ID: 293897 [Multi-domain]  Cd Length: 83  Bit Score: 113.78  E-value: 2.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 175 FHYYIDRVFSLKGIGTVVTGSLNEGSITLNEKIICLDTQKELIVKNIQNHDTNLEQIKACNRVALSLNCDY-KELKKGYL 253
Cdd:cd03696    1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDaKELERGFV 80

                 ...
gi 488946855 254 LSK 256
Cdd:cd03696   81 LSE 83
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
4-270 2.60e-28

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


Pssm-ID: 129576 [Multi-domain]  Cd Length: 394  Bit Score: 117.19  E-value: 2.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855    4 VIIGTAGHIDHGKTSLIKALNGF-------------EGDSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKDLVKTM 70
Cdd:TIGR00485  13 VNVGTIGHVDHGKTTLTAAITTVlakeggaaaraydQIDNAPEEKARGITINTAHVEYETETRHYAHVDCPGHADYVKNM 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   71 VSGAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKNIILVLSKCD------LCENIEQKSVEILEE--LKNLDYPI-- 140
Cdd:TIGR00485  93 ITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDmvddeeLLELVEMEVRELLSQydFPGDDTPIir 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  141 ---LKVFHTSIKNNQGIEELKNYLYT-IENKENDEELIFHYYIDRVFSLKGIGTVVTGSLNEGSITLNEK--IICLDTQK 214
Cdd:TIGR00485 173 gsaLKALEGDAEWEAKILELMDAVDEyIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEveIVGLKDTR 252
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 488946855  215 ELIVKNIQNHDTNLEQIKACNRVALSL-NCDYKELKKGYLLSKKGYFKAFKECDALV 270
Cdd:TIGR00485 253 KTTVTGVEMFRKELDEGRAGDNVGLLLrGIKREEIERGMVLAKPGSIKPHTKFEAEV 309
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
4-135 3.04e-28

Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 111.98  E-value: 3.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   4 VIIGTAGHIDHGKTSLIKALNGFEGDSLKEEQERQITINLSFSNLKLKDK---------------------------NIS 56
Cdd:cd01888    1 INIGTIGHVAHGKTTLVKALSGVWTVRHKEELKRNITIKLGYANAKIYKCpncgcprpydtpececpgcggetklvrHVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  57 FIDVPGHKDLVKTMVSGAFGFSVCLFVVDINEGLKE-QSLEHLEILKILDIKNIILVLSKCDLCEniEQKSVEILEELKN 135
Cdd:cd01888   81 FVDCPGHEILMATMLSGAAVMDGALLLIAANEPCPQpQTSEHLAALEIMGLKHIIILQNKIDLVK--EEQALENYEQIKE 158
tufA CHL00071
elongation factor Tu
4-270 3.34e-27

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 114.28  E-value: 3.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   4 VIIGTAGHIDHGKTSL-------IKALNGFEG------DSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKDLVKTM 70
Cdd:CHL00071  13 VNIGTIGHVDHGKTTLtaaitmtLAAKGGAKAkkydeiDSAPEEKARGITINTAHVEYETENRHYAHVDCPGHADYVKNM 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  71 VSGAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKNIILVLSKCDLC---ENIEQKSVEILEELKNLDYP-------- 139
Cdd:CHL00071  93 ITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVddeELLELVELEVRELLSKYDFPgddipivs 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 140 --ILKVFHTSIKNN--------------QGIEELKNYlytIENKENDEELIFHYYIDRVFSLKGIGTVVTGSLNEGSITL 203
Cdd:CHL00071 173 gsALLALEALTENPkikrgenkwvdkiyNLMDAVDSY---IPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKV 249
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 204 NEK--IICLDTQKELIVKNIQNHDTNLEQIKACNRVALSL-NCDYKELKKGYLLSKKGYFKAFKECDALV 270
Cdd:CHL00071 250 GDTveIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLrGIQKEDIERGMVLAKPGTITPHTKFEAQV 319
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
6-143 3.38e-27

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: 108.61  E-value: 3.38e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   6 IGTAGHIDHGKTSLIKALNGFEG----DSLKEEQERQITINLSFSNLKLKDKN--------------ISFIDVPGHKDLV 67
Cdd:cd01889    3 VGLLGHVDSGKTSLAKALSEIAStaafDKNPQSQERGITLDLGFSSFEVDKPKhlednenpqienyqITLVDCPGHASLI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  68 KTMVSGAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKnIILVLSKCDL------CENIE---QKSVEILEELKNLDY 138
Cdd:cd01889   83 RTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKP-LIVVLNKIDLipeeerKRKIEkmkKRLQKTLEKTRLKDS 161

                 ....*
gi 488946855 139 PILKV 143
Cdd:cd01889  162 PIIPV 166
PRK12736 PRK12736
elongation factor Tu; Reviewed
4-258 5.56e-26

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 110.42  E-value: 5.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   4 VIIGTAGHIDHGKTSLIKA---------LNGFEG----DSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKDLVKTM 70
Cdd:PRK12736  13 VNIGTIGHVDHGKTTLTAAitkvlaergLNQAKDydsiDAAPEEKERGITINTAHVEYETEKRHYAHVDCPGHADYVKNM 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  71 VSGAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKNIILVLSKCDLC---ENIEQKSVEILEELKNLDYP-------- 139
Cdd:PRK12736  93 ITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVddeELLELVEMEVRELLSEYDFPgddipvir 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 140 --ILKVFHTSIKNNQGIEELKNYLYT-IENKENDEELIFHYYIDRVFSLKGIGTVVTGSLNEGSITLNE--KIICLDTQK 214
Cdd:PRK12736 173 gsALKALEGDPKWEDAIMELMDAVDEyIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDevEIVGIKETQ 252
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 488946855 215 ELIVKNIQNHDTNLEQIKACNRVALSL-NCDYKELKKGYLLSKKG 258
Cdd:PRK12736 253 KTVVTGVEMFRKLLDEGQAGDNVGVLLrGVDRDEVERGQVLAKPG 297
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
1-230 9.22e-26

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: 110.02  E-value: 9.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   1 MKSVIIGtagHIDHGKTSLI------------KALNGFEG----------------DSLKEEQERQITINLSFSNLKLKD 52
Cdd:COG5256    8 LNLVVIG---HVDHGKSTLVgrllyetgaideHIIEKYEEeaekkgkesfkfawvmDRLKEERERGVTIDLAHKKFETDK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  53 KNISFIDVPGHKDLVKTMVSGAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKNIILVLSKCDLCENIEQKSVEILEE 132
Cdd:COG5256   85 YYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNYSEKRYEEVKEE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 133 LKNL---------DYPIL--------KVFHTSIK----NNQGIEELKNYLyTIENKENDEELifHYYIDRVFSLKGIGTV 191
Cdd:COG5256  165 VSKLlkmvgykvdKIPFIpvsawkgdNVVKKSDNmpwyNGPTLLEALDNL-KEPEKPVDKPL--RIPIQDVYSISGIGTV 241
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 488946855 192 VTGSLNEGSITLNEKIICLDTQKELIVKNIQNHDTNLEQ 230
Cdd:COG5256  242 PVGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELEQ 280
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
4-207 2.05e-25

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 108.79  E-value: 2.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   4 VIIGTAGHIDHGKTSLIKALNGFEGDSLKEEQERQITINLSFSNLKLKD--------------------------KNISF 57
Cdd:PRK04000  10 VNIGMVGHVDHGKTTLVQALTGVWTDRHSEELKRGITIRLGYADATIRKcpdceepeayttepkcpncgsetellRRVSF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  58 IDVPGHKDLVKTMVSGAFGFSVCLFVVDINEGLKE-QSLEHLEILKILDIKNIILVLSKCDLCEniEQKSVEILEELKNL 136
Cdd:PRK04000  90 VDAPGHETLMATMLSGAALMDGAILVIAANEPCPQpQTKEHLMALDIIGIKNIVIVQNKIDLVS--KERALENYEQIKEF 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 137 -------DYPILKVfhtSIKNNQGIEELKNYLY-TIENKENDEELIFHYYIDRVFSLKGIGT--------VVTGSLNEGS 200
Cdd:PRK04000 168 vkgtvaeNAPIIPV---SALHKVNIDALIEAIEeEIPTPERDLDKPPRMYVARSFDVNKPGTppeklkggVIGGSLIQGV 244

                 ....*..
gi 488946855 201 ITLNEKI 207
Cdd:PRK04000 245 LKVGDEI 251
PLN03126 PLN03126
Elongation factor Tu; Provisional
4-270 8.13e-25

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 108.16  E-value: 8.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   4 VIIGTAGHIDHGKTSLIKALNGF-------------EGDSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKDLVKTM 70
Cdd:PLN03126  82 VNIGTIGHVDHGKTTLTAALTMAlasmggsapkkydEIDAAPEERARGITINTATVEYETENRHYAHVDCPGHADYVKNM 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  71 VSGAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKNIILVLSKCD------LCENIEQKSVEILE--ELKNLDYPILK 142
Cdd:PLN03126 162 ITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDqvddeeLLELVELEVRELLSsyEFPGDDIPIIS 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 143 ----------VFHTSIK--NNQGIEELKNYLYTIEN----KENDEELIFHYYIDRVFSLKGIGTVVTGSLNEGSITLNE- 205
Cdd:PLN03126 242 gsallalealMENPNIKrgDNKWVDKIYELMDAVDSyipiPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGEt 321
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488946855 206 -KIICLDTQKELIVKNIQNHDTNLEQIKACNRVALSLNCDYK-ELKKGYLLSKKGYFKAFKECDALV 270
Cdd:PLN03126 322 vDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKaDIQRGMVLAKPGSITPHTKFEAIV 388
PLN03127 PLN03127
Elongation factor Tu; Provisional
6-268 8.03e-23

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 101.44  E-value: 8.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   6 IGTAGHIDHGKTSLIKALN------------GFEG-DSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKDLVKTMVS 72
Cdd:PLN03127  64 VGTIGHVDHGKTTLTAAITkvlaeegkakavAFDEiDKAPEEKARGITIATAHVEYETAKRHYAHVDCPGHADYVKNMIT 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  73 GAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKNIILVLSKCDLCENIEQksVEILE-ELKNL---------DYPI-- 140
Cdd:PLN03127 144 GAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEEL--LELVEmELRELlsfykfpgdEIPIir 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 141 ------LKVFHTSIKNNQGIEELKNYLYTIENKENDEELIFHYYIDRVFSLKGIGTVVTGSLNEGSITLNE--KIICLDT 212
Cdd:PLN03127 222 gsalsaLQGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEevEIVGLRP 301
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488946855 213 QKEL--IVKNIQNHDTNLEQIKACNRVALSLNCDYKE-LKKGYLLSKKGYFKAFKECDA 268
Cdd:PLN03127 302 GGPLktTVTGVEMFKKILDQGQAGDNVGLLLRGLKREdVQRGQVICKPGSIKTYKKFEA 360
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
4-230 4.94e-22

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 98.84  E-value: 4.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   4 VIIGtagHIDHGKTSLI------------------------KALNGFE----GDSLKEEQERQITINLSFSNLKLKDKNI 55
Cdd:PRK12317  10 AVIG---HVDHGKSTLVgrllyetgaidehiieelreeakeKGKESFKfawvMDRLKEERERGVTIDLAHKKFETDKYYF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  56 SFIDVPGHKDLVKTMVSGAFGFSVCLFVVDINE--GLKEQSLEHLEILKILDIKNIILVLSKCDLCENIEQKSVEILEEL 133
Cdd:PRK12317  87 TIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNYDEKRYEEVKEEV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 134 KNL---------DYPILKV--FH----------TSIKNNQGIEELKNYLyTIENKENDEELifHYYIDRVFSLKGIGTVV 192
Cdd:PRK12317 167 SKLlkmvgykpdDIPFIPVsaFEgdnvvkksenMPWYNGPTLLEALDNL-KPPEKPTDKPL--RIPIQDVYSISGVGTVP 243
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 488946855 193 TGSLNEGSITLNEKIICLDTQKELIVKNIQNHDTNLEQ 230
Cdd:PRK12317 244 VGRVETGVLKVGDKVVFMPAGVVGEVKSIEMHHEELPQ 281
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
4-139 2.04e-21

Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.


Pssm-ID: 206671 [Multi-domain]  Cd Length: 195  Bit Score: 92.26  E-value: 2.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   4 VIIGTAGHIDHGKTSLI-------------KALNGFEGDSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKDLVKTM 70
Cdd:cd01884    3 VNVGTIGHVDHGKTTLTaaitkvlakkggaKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIKNM 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488946855  71 VSGAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKNIILVLSKCDLC---ENIEQKSVEILEELKNLDYP 139
Cdd:cd01884   83 ITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVddeELLELVEMEVRELLSKYGFD 154
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
6-214 4.84e-21

Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 439820 [Multi-domain]  Cd Length: 396  Bit Score: 95.60  E-value: 4.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   6 IGTAGHIDHGKTSLIKALN------------GFEG-DSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKDLVKTMVS 72
Cdd:COG0050   15 IGTIGHVDHGKTTLTAAITkvlakkggakakAYDQiDKAPEEKERGITINTSHVEYETEKRHYAHVDCPGHADYVKNMIT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  73 GAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKNIILVLSKCDLC---ENIEQKSVEILEELKNLDY-----PILKVF 144
Cdd:COG0050   95 GAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVddeELLELVEMEVRELLSKYGFpgddtPIIRGS 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 145 -------HTSIKNNQGIEELKNYLYT-IENKENDEELIFHYYIDRVFSLKGIGTVVTGSLNEGSITLNEK--IICL-DTQ 213
Cdd:COG0050  175 alkalegDPDPEWEKKILELMDAVDSyIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEveIVGIrDTQ 254

                 .
gi 488946855 214 K 214
Cdd:COG0050  255 K 255
PRK00049 PRK00049
elongation factor Tu; Reviewed
4-214 3.65e-20

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 92.94  E-value: 3.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   4 VIIGTAGHIDHGKTSLIKALN------------GFEG-DSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKDLVKTM 70
Cdd:PRK00049  13 VNVGTIGHVDHGKTTLTAAITkvlakkggaeakAYDQiDKAPEEKARGITINTAHVEYETEKRHYAHVDCPGHADYVKNM 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  71 VSGAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKNIILVLSKCDLC---ENIEQKSVEILEELKNLDYP-------- 139
Cdd:PRK00049  93 ITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVddeELLELVEMEVRELLSKYDFPgddtpiir 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 140 --ILKVFHTSIKNN--QGIEELKNYLYT-IENKENDEELIFHYYIDRVFSLKGIGTVVTGSLNEGSITLNEK--IICL-D 211
Cdd:PRK00049 173 gsALKALEGDDDEEweKKILELMDAVDSyIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEveIVGIrD 252

                 ...
gi 488946855 212 TQK 214
Cdd:PRK00049 253 TQK 255
PRK12735 PRK12735
elongation factor Tu; Reviewed
4-214 1.39e-19

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 91.05  E-value: 1.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   4 VIIGTAGHIDHGKTSLIKALN------------GFEG-DSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKDLVKTM 70
Cdd:PRK12735  13 VNVGTIGHVDHGKTTLTAAITkvlakkgggeakAYDQiDNAPEEKARGITINTSHVEYETANRHYAHVDCPGHADYVKNM 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  71 VSGAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKNIILVLSKCDLC---ENIEQKSVEILEELKNLDYP-------- 139
Cdd:PRK12735  93 ITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVddeELLELVEMEVRELLSKYDFPgddtpiir 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 140 --ILKVFH--TSIKNNQGIEELKNYLYT-IENKENDEELIFHYYIDRVFSLKGIGTVVTGSLNEGSITLNEK--IICL-D 211
Cdd:PRK12735 173 gsALKALEgdDDEEWEAKILELMDAVDSyIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEveIVGIkE 252

                 ...
gi 488946855 212 TQK 214
Cdd:PRK12735 253 TQK 255
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
6-135 1.78e-17

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 85.44  E-value: 1.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   6 IGTAGHIDHGKTSLIKALNGFEGDSLKEEQERQITINLSFSNLK----------------------------------LK 51
Cdd:PTZ00327  37 IGTIGHVAHGKSTVVKALSGVKTVRFKREKVRNITIKLGYANAKiykcpkcprptcyqsygsskpdnppcpgcghkmtLK 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  52 dKNISFIDVPGHKDLVKTMVSGAFGFSVCLFVVDINEGLKE-QSLEHLEILKILDIKNIILVLSKCDLCEniEQKSVEIL 130
Cdd:PTZ00327 117 -RHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANESCPQpQTSEHLAAVEIMKLKHIIILQNKIDLVK--EAQAQDQY 193

                 ....*
gi 488946855 131 EELKN 135
Cdd:PTZ00327 194 EEIRN 198
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
4-255 3.54e-16

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 81.33  E-value: 3.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   4 VIIGtagHIDHGKTS----LIKALNG--------FEG----------------DSLKEEQERQITINLSFSNLKLKDKNI 55
Cdd:PTZ00141  11 VVIG---HVDSGKSTttghLIYKCGGidkrtiekFEKeaaemgkgsfkyawvlDKLKAERERGITIDIALWKFETPKYYF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  56 SFIDVPGHKDLVKTMVSGAFGFSVCLFVVDINEGLKE-------QSLEHLEILKILDIKNIILVLSKCDL--CENIEQKS 126
Cdd:PTZ00141  88 TIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDktVNYSQERY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 127 VEILEE----LKNLDYPILKVFHTSIKNNQG---IEELKNY-----------LYTIENKENDEELIFHYYIDRVFSLKGI 188
Cdd:PTZ00141 168 DEIKKEvsayLKKVGYNPEKVPFIPISGWQGdnmIEKSDNMpwykgptlleaLDTLEPPKRPVDKPLRLPLQDVYKIGGI 247
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488946855 189 GTVVTGSLNEGSITLNEKIICLDTQKELIVKNIQNHDTNLEQIKACNRVALSL-NCDYKELKKGYLLS 255
Cdd:PTZ00141 248 GTVPVGRVETGILKPGMVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVkNVSVKDIKRGYVAS 315
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
4-161 4.69e-16

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: 75.96  E-value: 4.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   4 VIIGTAGHidhGKTSLIKALngFEGDSLKEEQERQITINLSFSNLKLKDK--NISFIDVPGHKD--------LVKTMVSG 73
Cdd:cd00882    1 VVVGRGGV---GKSSLLNAL--LGGEVGEVSDVPGTTRDPDVYVKELDKGkvKLVLVDTPGLDEfgglgreeLARLLLRG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  74 AfgfSVCLFVVDINEGLKEQSLEHLEILKILDI-KNIILVLSKCDLCENIEQKSVEILEELKNLdyPILKVFHTSIKNNQ 152
Cdd:cd00882   76 A---DLILLVVDSTDRESEEDAKLLILRRLRKEgIPIILVGNKIDLLEEREVEELLRLEELAKI--LGVPVFEVSAKTGE 150

                 ....*....
gi 488946855 153 GIEELKNYL 161
Cdd:cd00882  151 GVDELFEKL 159
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
10-157 7.31e-16

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: 75.59  E-value: 7.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  10 GHIDHGKTSLIKALngfEGDSLKEEQERQIT--INLSFSNLKLKDKNISFIDVPGHKdlvktmvsgAF------GFSVC- 80
Cdd:cd01887    7 GHVDHGKTTLLDKI---RKTNVAAGEAGGITqhIGAYQVPIDVKIPGITFIDTPGHE---------AFtnmrarGASVTd 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  81 --LFVVDINEGLKEQSLEHLEILKILDIKnIILVLSKCDLCENIE---QKSVEILEELKNL------DYPILKVfhtSIK 149
Cdd:cd01887   75 iaILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDKPYGTEadpERVKNELSELGLVgeewggDVSIVPI---SAK 150

                 ....*...
gi 488946855 150 NNQGIEEL 157
Cdd:cd01887  151 TGEGIDDL 158
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
8-136 1.10e-15

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: 76.07  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   8 TAGHIDHGKTSLI-------------------------KALNGFE----GDSLKEEQERQITINLS---FSNLKLKdkni 55
Cdd:cd04166    4 TCGSVDDGKSTLIgrllydsksifedqlaalerskssgTQGEKLDlallVDGLQAEREQGITIDVAyryFSTPKRK---- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  56 sFI--DVPGHKDLVKTMVSGAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKNIILVLSKCDLCENIEQKSVEILEEL 133
Cdd:cd04166   80 -FIiaDTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVFEEIKADY 158

                 ...
gi 488946855 134 KNL 136
Cdd:cd04166  159 LAF 161
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
4-136 7.87e-15

Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 206670 [Multi-domain]  Cd Length: 219  Bit Score: 73.68  E-value: 7.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   4 VIIGtagHIDHGKTSLI------------KALNGFEG----------------DSLKEEQERQITINLSFSNLKLKDKNI 55
Cdd:cd01883    3 VVIG---HVDAGKSTLTghllyklggvdkRTIEKYEKeakemgkesfkyawvlDKLKEERERGVTIDVGLAKFETEKYRF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  56 SFIDVPGHKDLVKTMVSGAFGFSVCLFVVDINEGLKE-------QSLEHLEILKILDIKNIILVLSKCDLCE-NIEQKSV 127
Cdd:cd01883   80 TIIDAPGHRDFVKNMITGASQADVAVLVVSARKGEFEagfekggQTREHALLARTLGVKQLIVAVNKMDDVTvNWSQERY 159
                        170
                 ....*....|
gi 488946855 128 -EILEELKNL 136
Cdd:cd01883  160 dEIKKKVSPF 169
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
4-173 1.39e-13

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 69.24  E-value: 1.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   4 VIIGTAGHidhGKTSLIKAlngFEGDSLKEEQErQIT--INLSFSNLKLKDKNISF--IDVPGH---KDLVKTMVSGAFG 76
Cdd:COG1100    7 VVVGTGGV---GKTSLVNR---LVGDIFSLEKY-LSTngVTIDKKELKLDGLDVDLviWDTPGQdefRETRQFYARQLTG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  77 FSVCLFVVD--INEGLKEQSLEHLEILKILDIKNIILVLSKCDLCENIEQKSVEILEELKNlDYPILKVFHTSIKNNQGI 154
Cdd:COG1100   80 ASLYLFVVDgtREETLQSLYELLESLRRLGKKSPIILVLNKIDLYDEEEIEDEERLKEALS-EDNIVEVVATSAKTGEGV 158
                        170
                 ....*....|....*....
gi 488946855 155 EELKNYLYTIENKENDEEL 173
Cdd:COG1100  159 EELFAALAEILRGEGDSLD 177
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
11-157 7.24e-13

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: 67.17  E-value: 7.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  11 HIDHGKTSL----IKALNGFEG--------DSLKEEQERQITINLSFSNLKLKDKN-----ISFIDVPGHKDlvktmvsg 73
Cdd:cd01890    8 HIDHGKSTLadrlLELTGTVSEremkeqvlDSMDLERERGITIKAQAVRLFYKAKDgeeylLNLIDTPGHVD-------- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  74 aFGFSV------C---LFVVDINEGLKEQSLEHLEILKILDIKnIILVLSKCDL-CENIEqksvEILEELKN-LDYPILK 142
Cdd:cd01890   80 -FSYEVsrslaaCegaLLVVDATQGVEAQTLANFYLALENNLE-IIPVINKIDLpAADPD----RVKQEIEDvLGLDASE 153
                        170
                 ....*....|....*
gi 488946855 143 VFHTSIKNNQGIEEL 157
Cdd:cd01890  154 AILVSAKTGLGVEDL 168
lepA TIGR01393
elongation factor 4; LepA (GUF1 in Saccaromyces), now called elongation factor 4, is a ...
11-221 3.02e-12

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: 69.27  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   11 HIDHGKTSL----IKALNGFEG--------DSLKEEQERQITINLSFSNLKLKDKN-----ISFIDVPGHKDLVKTmVSG 73
Cdd:TIGR01393  11 HIDHGKSTLadrlLEYTGAISEremreqvlDSMDLERERGITIKAQAVRLNYKAKDgetyvLNLIDTPGHVDFSYE-VSR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   74 AfgFSVC---LFVVDINEGLKEQSLEHLeilkILDIKN---IILVLSKCDL-CENIEQKSVEIlEELKNLDYPIlkVFHT 146
Cdd:TIGR01393  90 S--LAACegaLLLVDAAQGIEAQTLANV----YLALENdleIIPVINKIDLpSADPERVKKEI-EEVIGLDASE--AILA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  147 SIKNNQGIEELknyLYTIENK----ENDEE-----LIFHYYIDrvfSLKGIgtVVTGSLNEGSITLNEKIICLDTQKELI 217
Cdd:TIGR01393 161 SAKTGIGIEEI---LEAIVKRvpppKGDPDaplkaLIFDSHYD---NYRGV--VALVRVFEGTIKPGDKIRFMSTGKEYE 232

                  ....
gi 488946855  218 VKNI 221
Cdd:TIGR01393 233 VDEV 236
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
10-255 1.76e-11

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 66.65  E-value: 1.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  10 GHIDHGKTS----LIKALNGFEG------------------------DSLKEEQERQITINLSFSNLKLKDKNISFIDVP 61
Cdd:PLN00043  14 GHVDSGKSTttghLIYKLGGIDKrvierfekeaaemnkrsfkyawvlDKLKAERERGITIDIALWKFETTKYYCTVIDAP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  62 GHKDLVKTMVSGAFGFSVCLFVVDINEGLKE-------QSLEHLEILKILDIKNIILVLSKCDLCE------NIEQKSVE 128
Cdd:PLN00043  94 GHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTpkyskaRYDEIVKE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 129 ILEELKNLDYPILKVFHTSIKNNQG---IEELKNY-----------LYTIENKENDEELIFHYYIDRVFSLKGIGTVVTG 194
Cdd:PLN00043 174 VSSYLKKVGYNPDKIPFVPISGFEGdnmIERSTNLdwykgptlleaLDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVG 253
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488946855 195 SLNEGSITLNEKIICLDTQKELIVKNIQNHDTNLEQIKACNRVALSL-NCDYKELKKGYLLS 255
Cdd:PLN00043 254 RVETGVIKPGMVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVkNVAVKDLKRGYVAS 315
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
11-141 4.18e-11

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: 62.23  E-value: 4.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  11 HIDHGKTSLIKAL---------NGFEG----DSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKDL------VKTMV 71
Cdd:cd01891   10 HVDHGKTTLVDALlkqsgtfreNEEVGervmDSNDLERERGITILAKNTAITYKDTKINIIDTPGHADFggeverVLSMV 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488946855  72 SGafgfsvCLFVVDINEGLKEQSLEHLEilKILDIK-NIILVLSKCDL----CENIEQKSVEILEEL----KNLDYPIL 141
Cdd:cd01891   90 DG------VLLLVDASEGPMPQTRFVLK--KALEAGlKPIVVINKIDRpdarPEEVVDEVFDLFLELnatdEQLDFPIV 160
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
8-118 6.29e-11

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: 64.72  E-value: 6.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   8 TAGHIDHGKTSLI-------KAL--------------NGFEG-------DSLKEEQERQITINLS---FSNLKLKdknis 56
Cdd:COG2895   22 TCGSVDDGKSTLIgrllydtKSIfedqlaalerdskkRGTQEidlalltDGLQAEREQGITIDVAyryFSTPKRK----- 96
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488946855  57 FI--DVPGHKDLVKTMVSGAfgfSVC---LFVVDINEGLKEQSLEHLEILKILDIKNIILVLSKCDL 118
Cdd:COG2895   97 FIiaDTPGHEQYTRNMVTGA---STAdlaILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDL 160
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
15-164 1.82e-10

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 59.57  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  15 GKTSLIKALNGfegdslkeeQERQITINL--------SFSNLKLKDKNISFIDVPG-------HKDLVKTMVSGAFGFSV 79
Cdd:cd00880    9 GKSSLLNALLG---------QNVGIVSPIpgttrdpvRKEWELLPLGPVVLIDTPGldeegglGRERVEEARQVADRADL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  80 CLFVVDINEGLKEQSLEHLEILKILdiKNIILVLSKCDLCENIEQKsvEILEELKNLDYPILKVFHTSIKNNQGIEELKN 159
Cdd:cd00880   80 VLLVVDSDLTPVEEEAKLGLLRERG--KPVLLVLNKIDLVPESEEE--ELLRERKLELLPDLPVIAVSALPGEGIDELRK 155

                 ....*
gi 488946855 160 YLYTI 164
Cdd:cd00880  156 KIAEL 160
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
6-117 2.68e-10

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: 60.36  E-value: 2.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   6 IGTAGHIDHGKTSLIKALNGFEG----------------DSLKEEQERQITINLS-----FSNLKLKDKNISFIDVPGHK 64
Cdd:cd04167    3 VCIAGHLHHGKTSLLDMLIEQTHkrtpsvklgwkplrytDTRKDEQERGISIKSNpislvLEDSKGKSYLINIIDTPGHV 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488946855  65 DLVKTMVSGAFGFSVCLFVVDINEGLKEQSlEHLEILKILDIKNIILVLSKCD 117
Cdd:cd04167   83 NFMDEVAAALRLCDGVVLVVDVVEGLTSVT-ERLIRHAIQEGLPMVLVINKID 134
SelB-wing_3 pfam09107
Elongation factor SelB, winged helix; Members of this family adopt a winged-helix fold, with ...
554-598 3.21e-10

Elongation factor SelB, winged helix; Members of this family adopt a winged-helix fold, with an alpha/beta structure consisting of three alpha-helices and a twisted three-stranded antiparallel beta-sheet, with an alpha-beta-alpha-alpha-beta-beta connectivity. They are involved in both DNA and RNA binding.


Pssm-ID: 430413 [Multi-domain]  Cd Length: 46  Bit Score: 55.51  E-value: 3.21e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 488946855  554 LLKNQSLDVQSMKEYFNLSRKYAIAYLEYLDKFPQVSKEAEKRFL 598
Cdd:pfam09107   2 LKENGEITVAEFRDLLGTSRKYAIPLLEYLDRIGITRRVGDKRVL 46
PRK07560 PRK07560
elongation factor EF-2; Reviewed
6-93 3.03e-09

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 59.88  E-value: 3.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   6 IGTAGHIDHGKTSLIKALNGFEG-------------DSLKEEQERQITINLsfSNLKL----KDKN--ISFIDVPGHKD- 65
Cdd:PRK07560  23 IGIIAHIDHGKTTLSDNLLAGAGmiseelageqlalDFDEEEQARGITIKA--ANVSMvheyEGKEylINLIDTPGHVDf 100
                         90       100       110
                 ....*....|....*....|....*....|...
gi 488946855  66 ---LVKTM--VSGAfgfsvcLFVVDINEGLKEQ 93
Cdd:PRK07560 101 ggdVTRAMraVDGA------IVVVDAVEGVMPQ 127
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
57-162 3.61e-09

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


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 56.32  E-value: 3.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  57 FIDVPG----HKDLVKTMVSGAF----GFSVCLFVVDINEGLKEQSLEHLEILKILDIKnIILVLSKCDLCENiEQKSVE 128
Cdd:cd04163   55 FVDTPGihkpKKKLGERMVKAAWsalkDVDLVLFVVDASEWIGEGDEFILELLKKSKTP-VILVLNKIDLVKD-KEDLLP 132
                         90       100       110
                 ....*....|....*....|....*....|....
gi 488946855 129 ILEELKNLdYPILKVFHTSIKNNQGIEELKNYLY 162
Cdd:cd04163  133 LLEKLKEL-HPFAEIFPISALKGENVDELLEYIV 165
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
79-164 5.02e-09

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 55.58  E-value: 5.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  79 VCLFVVDINEGLKEqslEHLEILKILDIKNIILVLSKCDLCENIEQKSVEileelknldyPILKVFHTSIKNNQGIEELK 158
Cdd:cd04164   85 LVLLVVDASEGLDE---EDLEILELPAKKPVIVVLNKSDLLSDAEGISEL----------NGKPIIAISAKTGEGIDELK 151

                 ....*.
gi 488946855 159 NYLYTI 164
Cdd:cd04164  152 EALLEL 157
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
6-221 6.67e-09

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: 56.47  E-value: 6.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   6 IGTAGHIDHGKTSLIKAL---NGFEG----------DSLKEEQERQIT-----INLSFSNLKLKDKN----ISFIDVPGH 63
Cdd:cd01885    3 ICIIAHVDHGKTTLSDSLlasAGIISeklagkarylDTREDEQERGITikssaISLYFEYEEEKMDGndylINLIDSPGH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  64 KDL---VKT---MVSGAfgfsvcLFVVDINEGLKEQS---LEH--LEILKildiknIILVLSKCDLCenIEQKSVEILEE 132
Cdd:cd01885   83 VDFsseVTAalrLTDGA------LVVVDAVEGVCVQTetvLRQalEERVK------PVLVINKIDRL--ILELKLSPEEA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 133 LKNLdypilkvfhtsiknNQGIEELKNYLYTIENKENDEELIFhYYIDRvfslkgiGTVVTGSLNEG-SITLNeKIICLD 211
Cdd:cd01885  149 YQRL--------------LRIVEDVNAIIETYAPEEFKQEKWK-FSPQK-------GNVAFGSALDGwGFTII-KFADIY 205
                        250
                 ....*....|
gi 488946855 212 TQKELIVKNI 221
Cdd:cd01885  206 AVLEMVVKHL 215
PRK13351 PRK13351
elongation factor G-like protein;
6-65 7.92e-09

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 58.42  E-value: 7.92e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488946855   6 IGTAGHIDHGKTSLIKAL--------------NG-FEGDSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKD 65
Cdd:PRK13351  11 IGILAHIDAGKTTLTERIlfytgkihkmgeveDGtTVTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHID 85
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
6-65 8.33e-09

Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440248 [Multi-domain]  Cd Length: 693  Bit Score: 58.52  E-value: 8.33e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488946855   6 IGTAGHIDHGKTSLIKAL-----------NGFEG----DSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKD 65
Cdd:COG0480   12 IGIVAHIDAGKTTLTERIlfytgaihrigEVHDGntvmDWMPEEQERGITITSAATTCEWKGHKINIIDTPGHVD 86
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
10-117 1.13e-08

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 58.21  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  10 GHIDHGKTSLIKALNGFEG---------------DSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKDLVKTMVSGA 74
Cdd:PRK12740   2 GHSGAGKTTLTEAILFYTGaihrigevedgtttmDFMPEERERGISITSAATTCEWKGHKINLIDTPGHVDFTGEVERAL 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488946855  75 FGFSVCLFVVDINEGLKEQSLEHLEILKILDIKNIIlVLSKCD 117
Cdd:PRK12740  82 RVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVPRII-FVNKMD 123
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
110-161 2.25e-08

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 54.71  E-value: 2.25e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488946855 110 ILVLSKCDLCENIEQKsvEILEELKNLDYPilkVFHTSIKNNQGIEELKNYL 161
Cdd:cd01854   37 VIVLNKADLVDDEELE--ELLEIYEKLGYP---VLAVSAKTGEGLDELRELL 83
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
81-174 5.25e-08

tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 55.45  E-value: 5.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  81 LFVVDINEGLKEqslEHLEILKILDIKNIILVLSKCDLceniEQKSVEILEELKNLDypilkVFHTSIKNNQGIEELKNY 160
Cdd:COG0486  297 LLLLDASEPLTE---EDEEILEKLKDKPVIVVLNKIDL----PSEADGELKSLPGEP-----VIAISAKTGEGIDELKEA 364
                         90
                 ....*....|....*.
gi 488946855 161 LYTI--ENKENDEELI 174
Cdd:COG0486  365 ILELvgEGALEGEGVL 380
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
85-161 1.28e-07

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 51.77  E-value: 1.28e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488946855   85 DINEGLKEQSLEHLEILKIldikNIILVLSKCDLCENiEQKSVEILEELKNLDYPILKVfhtSIKNNQGIEELKNYL 161
Cdd:pfam03193  36 DFNLNLLDRFLVLAEASGI----EPVIVLNKIDLLDE-EEELEELLKIYRAIGYPVLFV---SAKTGEGIEALKELL 104
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
6-140 2.14e-07

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: 52.60  E-value: 2.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   6 IGTAGHIDHGKTSLIKAL-------NGFE--------GDSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKDLVKTM 70
Cdd:cd04170    2 IALVGHSGSGKTTLAEALlyatgaiDRLGrvedgntvSDYDPEEKKRKMSIETSVAPLEWNGHKINLIDTPGYADFVGET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  71 VSGAFGFSVCLFVVDINEGLK---EQSLEHLEILKIldikNIILVLSKCDLcENIEQKsvEILEELKN--------LDYP 139
Cdd:cd04170   82 LSALRAVDAALIVVEAQSGVEvgtEKVWEFLDDAKL----PRIIFINKMDR-ARADFD--KTLAALREafgrpvvpIQLP 154

                 .
gi 488946855 140 I 140
Cdd:cd04170  155 I 155
era PRK00089
GTPase Era; Reviewed
57-162 3.34e-07

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 52.36  E-value: 3.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  57 FIDVPG-HKD-------LVKTMVSGAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKnIILVLSKCDLCENIEQKsVE 128
Cdd:PRK00089  57 FVDTPGiHKPkralnraMNKAAWSSLKDVDLVLFVVDADEKIGPGDEFILEKLKKVKTP-VILVLNKIDLVKDKEEL-LP 134
                         90       100       110
                 ....*....|....*....|....*....|....
gi 488946855 129 ILEELKNLdYPILKVFHTSIKNNQGIEELKNYLY 162
Cdd:PRK00089 135 LLEELSEL-MDFAEIVPISALKGDNVDELLDVIA 167
PRK04004 PRK04004
translation initiation factor IF-2; Validated
10-102 3.36e-07

translation initiation factor IF-2; Validated


Pssm-ID: 235195 [Multi-domain]  Cd Length: 586  Bit Score: 53.26  E-value: 3.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  10 GHIDHGKTSLikaLNGFEGDSLKEEQERQIT--INLSF----------------SNLKLKDKNISFIDVPGHKdlvktmv 71
Cdd:PRK04004  13 GHVDHGKTTL---LDKIRGTAVAAKEAGGITqhIGATEvpidviekiagplkkpLPIKLKIPGLLFIDTPGHE------- 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488946855  72 sgAF------GFSVC---LFVVDINEGLKEQSLEHLEILK 102
Cdd:PRK04004  83 --AFtnlrkrGGALAdiaILVVDINEGFQPQTIEAINILK 120
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
52-143 3.94e-07

GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.


Pssm-ID: 206728 [Multi-domain]  Cd Length: 224  Bit Score: 51.14  E-value: 3.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  52 DKNISFIDVPGHKDLVKTMVSGAFGFSV--CLFVVDINEGLKEQSLEHLEILKILDIKnIILVLSKCDLCenieqkSVEI 129
Cdd:cd04165   83 SKVVTFIDLAGHERYLKTTVFGMTGYAPdyAMLVVGANAGIIGMTKEHLGLALALKVP-VFVVVTKIDMT------PANV 155
                         90
                 ....*....|....
gi 488946855 130 LEELKNLDYPILKV 143
Cdd:cd04165  156 LQETLKDLKRLLKS 169
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
8-118 4.01e-07

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 53.01  E-value: 4.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   8 TAGHIDHGKTSLI-------KA-----LNGFEGDS------------------LKEEQERQITINLS---FSNLKLKdkn 54
Cdd:PRK05506  29 TCGSVDDGKSTLIgrllydsKMifedqLAALERDSkkvgtqgdeidlallvdgLAAEREQGITIDVAyryFATPKRK--- 105
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488946855  55 isFI--DVPGHKDLVKTMVSGAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKNIILVLSKCDL 118
Cdd:PRK05506 106 --FIvaDTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDL 169
IF-2 TIGR00487
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ...
5-209 9.09e-07

translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]


Pssm-ID: 273102 [Multi-domain]  Cd Length: 587  Bit Score: 51.69  E-value: 9.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855    5 IIGTAGHIDHGKTSLIkalngfegDSLKEEQERQ-----ITINLSFSNLKLKD-KNISFIDVPGHKDLVKTMVSGAFGFS 78
Cdd:TIGR00487  89 VVTIMGHVDHGKTSLL--------DSIRKTKVAQgeaggITQHIGAYHVENEDgKMITFLDTPGHEAFTSMRARGAKVTD 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   79 VCLFVVDINEGLKEQSLEHLEILKILDIKnIILVLSKCDLCENIEQKsveILEELKNLDYPILK-----VF-HTSIKNNQ 152
Cdd:TIGR00487 161 IVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKIDKPEANPDR---VKQELSEYGLVPEDwggdtIFvPVSALTGD 236
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488946855  153 GIEELknyLYTI-------ENKENDEELIFHYYIDrVFSLKGIGTVVTGSLNEGSITLNEKIIC 209
Cdd:TIGR00487 237 GIDEL---LDMIllqseveELKANPNGQASGVVIE-AQLDKGRGPVATVLVQSGTLRVGDIVVV 296
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
57-161 2.34e-06

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 49.60  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  57 FIDVPG--------HKDLVKTMVSGAFGFSVCLFVVDINEGLKEQSLEHLEILKILDIKnIILVLSKCDLCEniEQKSVE 128
Cdd:COG1159   55 FVDTPGihkpkrklGRRMNKAAWSALEDVDVILFVVDATEKIGEGDEFILELLKKLKTP-VILVINKIDLVK--KEELLP 131
                         90       100       110
                 ....*....|....*....|....*....|...
gi 488946855 129 ILEELKNLdYPILKVFHTSIKNNQGIEELKNYL 161
Cdd:COG1159  132 LLAEYSEL-LDFAEIVPISALKGDNVDELLDEI 163
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
78-161 2.48e-06

Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in eukaryotes ranging from trypanosomes to humans. NOG1 is functionally linked to ribosome biogenesis and found in association with the nuclear pore complexes and identified in many preribosomal complexes. Thus, defects in NOG1 can lead to defects in 60S biogenesis. The S. cerevisiae NOG1 gene is essential for cell viability, and mutations in the predicted G motifs abrogate function. It is a member of the ODN family of GTP-binding proteins that also includes the bacterial Obg and DRG proteins.


Pssm-ID: 206684 [Multi-domain]  Cd Length: 167  Bit Score: 47.94  E-value: 2.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  78 SVCLFVVDINE----GLKEQslEHL--EILKILDiKNIILVLSKCDLCENIEQKSVEILEELKnldypILKVFHTSIKNN 151
Cdd:cd01897   81 AAVLFFIDPSEtcgySIEEQ--LSLfkEIKPLFN-KPVIVVLNKIDLLTEEDLSEIEKELEKE-----GEEVIKISTLTE 152
                         90
                 ....*....|
gi 488946855 152 QGIEELKNYL 161
Cdd:cd01897  153 EGVDELKNKA 162
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
6-161 2.53e-06

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: 47.75  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855    6 IGTAGHIDHGKTSLikaLNGFEGDSLKEEqERQITINLSFSNLKLKDKNISF----IDVPGHKDL-------VKTMVSGA 74
Cdd:TIGR00231   4 IVIVGHPNVGKSTL---LNSLLGNKGSIT-EYYPGTTRNYVTTVIEEDGKTYkfnlLDTAGQEDYdairrlyYPQVERSL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   75 FGFSVCLFVVDINEGLkeqsLEHLEILKILDIKN--IILVLSKCDL-CENIEQKSVEILEELKNLDYpilkvFHTSIKNN 151
Cdd:TIGR00231  80 RVFDIVILVLDVEEIL----EKQTKEIIHHADSGvpIILVGNKIDLkDADLKTHVASEFAKLNGEPI-----IPLSAETG 150
                         170
                  ....*....|
gi 488946855  152 QGIEELKNYL 161
Cdd:TIGR00231 151 KNIDSAFKIV 160
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
6-65 2.75e-06

Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.


Pssm-ID: 206673 [Multi-domain]  Cd Length: 270  Bit Score: 49.03  E-value: 2.75e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488946855   6 IGTAGHIDHGKTSL---IKALNGF--------EG----DSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKD 65
Cdd:cd01886    2 IGIIAHIDAGKTTTterILYYTGRihkigevhGGgatmDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVD 76
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
175-255 3.67e-06

Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.


Pssm-ID: 293895 [Multi-domain]  Cd Length: 87  Bit Score: 45.29  E-value: 3.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 175 FHYYIDRVFSLKGIGTVVTGSLNEGSITLNEKIICLDTQ----KELIVKNIQNHDTNLEQIKACNRVALSLN-CDYKELK 249
Cdd:cd03694    1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDAdgkfRPVTVKSIHRNRQPVDRARAGQSASFALKkIKRESLR 80

                 ....*.
gi 488946855 250 KGYLLS 255
Cdd:cd03694   81 KGMVLV 86
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
179-258 4.01e-06

Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.


Pssm-ID: 293898 [Multi-domain]  Cd Length: 87  Bit Score: 45.20  E-value: 4.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 179 IDRVFSLKGIGTVVTGSLNEGSITLNEK--IICLDTQKELIVKNIQNHDTNLEQIKACNRVALSL-NCDYKELKKGYLLS 255
Cdd:cd03697    5 IEDVFSIPGRGTVVTGRIERGVIKVGDEveIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLrGVKKEDVERGMVLA 84

                 ...
gi 488946855 256 KKG 258
Cdd:cd03697   85 KPG 87
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
15-115 4.15e-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: 46.07  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   15 GKTSLIKALngFEGDSLKEEQErQITINLSFSNLKLKDKNISFIDVPG--HKDLVKTMVSGAF----GFSVCLFVVDINE 88
Cdd:pfam01926  11 GKSTLINAL--TGAKAIVSDYP-GTTRDPNEGRLELKGKQIILVDTPGliEGASEGEGLGRAFlaiiEADLILFVVDSEE 87
                          90       100
                  ....*....|....*....|....*..
gi 488946855   89 GLKEQSLEHLEILKILDiKNIILVLSK 115
Cdd:pfam01926  88 GITPLDEELLELLRENK-KPIILVLNK 113
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
1-161 7.61e-06

Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.


Pssm-ID: 206640 [Multi-domain]  Cd Length: 159  Bit Score: 46.30  E-value: 7.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   1 MKSVIIGTAGHidhGKTSLikaLNGFEGDSLKEEQERQITINLSFSNLKLKDKNIS--FIDVPGhKDLVKTMVS----GA 74
Cdd:cd00154    1 FKIVLIGDSGV---GKTSL---LLRFVDNKFSENYKSTIGVDFKSKTIEVDGKKVKlqIWDTAG-QERFRSITSsyyrGA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  75 fgfSVCLFVVDINeglKEQSLEHLEILkILDIKN-------IILVLSKCDLcenIEQKSVEIlEELKNL-DYPILKVFHT 146
Cdd:cd00154   74 ---HGAILVYDVT---NRESFENLDKW-LNELKEyappnipIILVGNKSDL---EDERQVST-EEAQQFaKENGLLFFET 142
                        170
                 ....*....|....*
gi 488946855 147 SIKNNQGIEELKNYL 161
Cdd:cd00154  143 SAKTGENVDEAFESL 157
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
80-162 1.01e-05

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


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 45.96  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  80 CLFVVDINEGLKEQSLEHLEILKILDIkNIILVLSKCD-LCENIEQKSVEILEELKNLDYPILKVFHTSIKNNQGIEELK 158
Cdd:cd01876   85 VVLLIDARHGPTPIDLEMLEFLEELGI-PFLIVLTKADkLKKSELAKVLKKIKEELNLFNILPPVILFSSKKGTGIDELR 163

                 ....
gi 488946855 159 NYLY 162
Cdd:cd01876  164 ALIA 167
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
11-89 1.36e-05

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 48.09  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  11 HIDHGKTSLIKAL---------NGFEG----DSLKEEQERQITI---NLSfsnLKLKDKNISFIDVPGHKDL------VK 68
Cdd:COG1217   14 HVDHGKTTLVDALlkqsgtfreNQEVAervmDSNDLERERGITIlakNTA---VRYKGVKINIVDTPGHADFggeverVL 90
                         90       100
                 ....*....|....*....|.
gi 488946855  69 TMVSGAfgfsvcLFVVDINEG 89
Cdd:COG1217   91 SMVDGV------LLLVDAFEG 105
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
79-157 1.38e-05

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 47.74  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  79 VCLFVVDINEGLKEQSlehleiLKILDI-----KNIILVLSKCDLCENIEQKSVE--ILEELKNLDY-PILKVfhtSIKN 150
Cdd:PRK00093 258 VVLLVIDATEGITEQD------LRIAGLaleagRALVIVVNKWDLVDEKTMEEFKkeLRRRLPFLDYaPIVFI---SALT 328

                 ....*..
gi 488946855 151 NQGIEEL 157
Cdd:PRK00093 329 GQGVDKL 335
LepA COG0481
Translation elongation factor EF-4, membrane-bound GTPase [Translation, ribosomal structure ...
11-221 1.99e-05

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


Pssm-ID: 440249 [Multi-domain]  Cd Length: 598  Bit Score: 47.71  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  11 HIDHGKTSL----IKALNGFEGDSLKE--------EQERQITINLSFSNLKLKDKN-----ISFIDVPGHKDlvktmvsg 73
Cdd:COG0481   14 HIDHGKSTLadrlLELTGTLSEREMKEqvldsmdlERERGITIKAQAVRLNYKAKDgetyqLNLIDTPGHVD-------- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  74 aFGFSV------C---LFVVDINEGLKEQSL-------EH-LEilkildiknIILVLSKCDL-CENIEQKSVEIlEELKN 135
Cdd:COG0481   86 -FSYEVsrslaaCegaLLVVDASQGVEAQTLanvylalENdLE---------IIPVINKIDLpSADPERVKQEI-EDIIG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 136 LDYP-ILKVfhtSIKNNQGIEELknyLYTIENK----ENDEE-----LIF--HY--------YIdRVFslkgigtvvtgs 195
Cdd:COG0481  155 IDASdAILV---SAKTGIGIEEI---LEAIVERipppKGDPDaplqaLIFdsWYdsyrgvvvYV-RVF------------ 215
                        250       260
                 ....*....|....*....|....*.
gi 488946855 196 lnEGSITLNEKIICLDTQKELIVKNI 221
Cdd:COG0481  216 --DGTLKKGDKIKMMSTGKEYEVDEV 239
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
15-157 3.17e-05

Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 46.56  E-value: 3.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  15 GKTSLIKALngfegdsLKEEqeRQITINLS-------FSNLKLKDKNISFIDVPG-------HKDL-----VKTMvsGAF 75
Cdd:COG1160  187 GKSSLINAL-------LGEE--RVIVSDIAgttrdsiDTPFERDGKKYTLIDTAGirrkgkvDEGIekysvLRTL--RAI 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  76 GFS-VCLFVVDINEGLKEQSlehleiLKILDI-----KNIILVLSKCDLCEN----IEQKSVEILEELKNLDY-PIlkVF 144
Cdd:COG1160  256 ERAdVVLLVIDATEGITEQD------LKIAGLaleagKALVIVVNKWDLVEKdrktREELEKEIRRRLPFLDYaPI--VF 327
                        170
                 ....*....|...
gi 488946855 145 hTSIKNNQGIEEL 157
Cdd:COG1160  328 -ISALTGQGVDKL 339
PRK10218 PRK10218
translational GTPase TypA;
6-213 3.39e-05

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 47.01  E-value: 3.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   6 IGTAGHIDHGKTSLIKALNGFEG-------------DSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKDL------ 66
Cdd:PRK10218   8 IAIIAHVDHGKTTLVDKLLQQSGtfdsraetqervmDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFggever 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  67 VKTMVSGAfgfsvcLFVVDINEGLKEQSLEHLEILKILDIKNIIlVLSKCD--------LCENIEQKSVEILEELKNLDY 138
Cdd:PRK10218  88 VMSMVDSV------LLVVDAFDGPMPQTRFVTKKAFAYGLKPIV-VINKVDrpgarpdwVVDQVFDLFVNLDATDEQLDF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 139 PIlkVFHTSIKNNQGIEElknylytiENKENDEELIFHYYIDRV----FSLKG--------------IGTVVTGSLNEGS 200
Cdd:PRK10218 161 PI--VYASALNGIAGLDH--------EDMAEDMTPLYQAIVDHVpapdVDLDGpfqmqisqldynsyVGVIGIGRIKRGK 230
                        250
                 ....*....|...
gi 488946855 201 ITLNEKIICLDTQ 213
Cdd:PRK10218 231 VKPNQQVTIIDSE 243
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
179-258 3.51e-05

Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.


Pssm-ID: 293894 [Multi-domain]  Cd Length: 91  Bit Score: 42.56  E-value: 3.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855 179 IDRVFSLKGIGTVVTGSLNEGSITLNEKIICLDTQKELIVKNIQNHDTNLEQIKACNRVALSL-NCDYKELKKGYLLSKK 257
Cdd:cd03693    9 IQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVkGVSVKDIKRGDVAGDS 88

                 .
gi 488946855 258 G 258
Cdd:cd03693   89 K 89
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
81-164 8.38e-05

Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.


Pssm-ID: 206685 [Multi-domain]  Cd Length: 170  Bit Score: 43.57  E-value: 8.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  81 LFVVDINEglKEQSLEHLEILK--------ILDIKNIILVLSKCDLC--ENIEQKSVEILEELKNldypiLKVFHTSIKN 150
Cdd:cd01898   83 LHVIDLSG--EDDPVEDYETIRneleaynpGLAEKPRIVVLNKIDLLdaEERFEKLKELLKELKG-----KKVFPISALT 155
                         90
                 ....*....|....
gi 488946855 151 NQGIEELKNYLYTI 164
Cdd:cd01898  156 GEGLDELLKKLAKL 169
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
6-94 1.04e-04

translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]


Pssm-ID: 129581 [Multi-domain]  Cd Length: 720  Bit Score: 45.27  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855    6 IGTAGHIDHGKTSLIKAL--------NGFEGDSL-----KEEQERQITINLsfSNLKL------KDKNISFIDVPGHKDL 66
Cdd:TIGR00490  22 IGIVAHIDHGKTTLSDNLlagagmisEELAGQQLyldfdEQEQERGITINA--ANVSMvheyegNEYLINLIDTPGHVDF 99
                          90       100
                  ....*....|....*....|....*...
gi 488946855   67 VKTMVSGAFGFSVCLFVVDINEGLKEQS 94
Cdd:TIGR00490 100 GGDVTRAMRAVDGAIVVVCAVEGVMPQT 127
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
178-255 1.15e-04

Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 40.71  E-value: 1.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488946855 178 YIDRVFSLKGIGTVVTGSLNEGSITLNEKIICLDTQKELIVKNIQNHDTNLEQIKACNRVALSLNcDYKELKKGYLLS 255
Cdd:cd01342    4 QVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGIL-GVKDILTGDTLT 80
infB CHL00189
translation initiation factor 2; Provisional
5-201 1.58e-04

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 44.82  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   5 IIGTAGHIDHGKTSLIkalngfegDSLKEEQERQ-----ITINLSF--SNLKLKDKN--ISFIDVPGHKDLVKTMVSGAF 75
Cdd:CHL00189 246 IVTILGHVDHGKTTLL--------DKIRKTQIAQkeaggITQKIGAyeVEFEYKDENqkIVFLDTPGHEAFSSMRSRGAN 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  76 GFSVCLFVVDINEGLKEQSLEHLEILKILDIKnIILVLSKCDL----CENIEQKSVE---ILEELKNlDYPILKVfhtSI 148
Cdd:CHL00189 318 VTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKananTERIKQQLAKynlIPEKWGG-DTPMIPI---SA 392
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488946855 149 KNNQGIEELKN---YLYTIENKENDEE-----LIFHYYIDRVfslKGIGT---VVTGSLNEGSI 201
Cdd:CHL00189 393 SQGTNIDKLLEtilLLAEIEDLKADPTqlaqgIILEAHLDKT---KGPVAtilVQNGTLHIGDI 453
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
79-157 2.39e-04

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


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 42.03  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  79 VCLFVVDINEGLKEQSlehleiLKILDI-----KNIILVLSKCDLCEN----IEQKSVEILEELKNLDY-PIlkVFhTSI 148
Cdd:cd01895   87 VVLLVLDASEGITEQD------LRIAGLileegKALIIVVNKWDLVEKdektMKEFEKELRRKLPFLDYaPI--VF-ISA 157

                 ....*....
gi 488946855 149 KNNQGIEEL 157
Cdd:cd01895  158 LTGQGVDKL 166
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
6-117 3.63e-04

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: 42.61  E-value: 3.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   6 IGTAGHIDHGKTSLIKAL----------------NGFEgDSLKEEQERQITINLSFSNLKLKDKNISFIDVPGHKDLVK- 68
Cdd:cd04168    2 IGILAHVDAGKTTLTESLlytsgairelgsvdkgTTRT-DSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAe 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488946855  69 -----TMVSGAfgfsvcLFVVDINEGLKEQSLEHLEILKILDIKNIILVlSKCD 117
Cdd:cd04168   81 verslSVLDGA------ILVISAVEGVQAQTRILFRLLRKLNIPTIIFV-NKID 127
obgE PRK12299
GTPase CgtA; Reviewed
81-172 6.51e-04

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 42.36  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  81 LFVVDINEglkEQSLEHLEIL--------KILDIKNIILVLSKCDLCENIEQKSVEILEELKNLDYPILKVfhtSIKNNQ 152
Cdd:PRK12299 241 LHLVDIEA---VDPVEDYKTIrnelekysPELADKPRILVLNKIDLLDEEEEREKRAALELAALGGPVFLI---SAVTGE 314
                         90       100
                 ....*....|....*....|
gi 488946855 153 GIEELKNYLYTIENKENDEE 172
Cdd:PRK12299 315 GLDELLRALWELLEEARREE 334
PRK14845 PRK14845
translation initiation factor IF-2; Provisional
47-102 9.35e-04

translation initiation factor IF-2; Provisional


Pssm-ID: 237833 [Multi-domain]  Cd Length: 1049  Bit Score: 42.18  E-value: 9.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 488946855   47 NLKLKDKNISFIDVPGHKDLVKTMVSGAFGFSVCLFVVDINEGLKEQSLEHLEILK 102
Cdd:PRK14845  520 KAEIKIPGLLFIDTPGHEAFTSLRKRGGSLADLAVLVVDINEGFKPQTIEAINILR 575
PRK00098 PRK00098
GTPase RsgA; Reviewed
105-161 1.15e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 41.34  E-value: 1.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488946855 105 DIKNIIlVLSKCDLCENIEQKSvEILEELKNLDYPilkVFHTSIKNNQGIEELKNYL 161
Cdd:PRK00098 111 GIKPII-VLNKIDLLDDLEEAR-ELLALYRAIGYD---VLELSAKEGEGLDELKPLL 162
PTZ00416 PTZ00416
elongation factor 2; Provisional
3-89 1.20e-03

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 41.96  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   3 SVIigtaGHIDHGKTSLIKALNGFEG-------------DSLKEEQERQITI-----NLSFSNlKLKDKN------ISFI 58
Cdd:PTZ00416  23 SVI----AHVDHGKSTLTDSLVCKAGiissknagdarftDTRADEQERGITIkstgiSLYYEH-DLEDGDdkqpflINLI 97
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488946855  59 DVPGHKDLVKTMVS------GAfgfsvcLFVVDINEG 89
Cdd:PTZ00416  98 DSPGHVDFSSEVTAalrvtdGA------LVVVDCVEG 128
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
3-89 1.69e-03

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 41.63  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855   3 SVIigtaGHIDHGKTSLIKALNGFEG-------------DSLKEEQERQITIN-------LSFSNLKLKDKN-------- 54
Cdd:PLN00116  23 SVI----AHVDHGKSTLTDSLVAAAGiiaqevagdvrmtDTRADEAERGITIKstgislyYEMTDESLKDFKgerdgney 98
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488946855  55 -ISFIDVPGHKDLvKTMVSGAFGFS-VCLFVVDINEG 89
Cdd:PLN00116  99 lINLIDSPGHVDF-SSEVTAALRITdGALVVVDCIEG 134
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
81-164 2.50e-03

HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 39.36  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  81 LFVVDI-NEGLKEQSLEHLEILKILDIKNI--ILVLSKCDLCEnieqkSVEILEELKNLDYPILKVfhtSIKNNQGIEEL 157
Cdd:cd01878  125 LHVVDAsDPDREEQIETVEEVLKELGADDIpiILVLNKIDLLD-----DEELEERLRAGRPDAVFI---SAKTGEGLDLL 196

                 ....*..
gi 488946855 158 KNYLYTI 164
Cdd:cd01878  197 KEAIEEL 203
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
189-255 2.92e-03

Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 293899 [Multi-domain]  Cd Length: 84  Bit Score: 37.10  E-value: 2.92e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488946855 189 GTVVTGSLNEGSITLNEKIICLDTQKELIVKNIQ-NHDTNLEQIKACNRVALSLNCDYKE-LKKGYLLS 255
Cdd:cd03698   15 GTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIrNSDEETDWAIAGDTVTLRLRGIEVEdIQPGDILS 83
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
10-163 4.62e-03

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 38.30  E-value: 4.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  10 GHIDHGKTSLIKALngfegdsLKEE--QERQI--TINLSFSNLKLKdKNISFIDVPG-------HKDLVKTMVSGAFGFs 78
Cdd:cd09912    7 GEFSAGKSTLLNAL-------LGEEvlPTGVTptTAVITVLRYGLL-KGVVLVDTPGlnstiehHTEITESFLPRADAV- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946855  79 vcLFVVDINEGLKEQSLEHLEILKILDIKNIILVLSKCDL-----CENIEQKSVEILEELKNLDYPIlKVFHTSIKN--- 150
Cdd:cd09912   78 --IFVLSADQPLTESEREFLKEILKWSGKKIFFVLNKIDLlseeeLEEVLEYSREELGVLELGGGEP-RIFPVSAKEale 154
                        170       180
                 ....*....|....*....|....
gi 488946855 151 -----------NQGIEELKNYLYT 163
Cdd:cd09912  155 arlqgdeelleQSGFEELEEHLEE 178
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH
HHS Vulnerability Disclosure