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Conserved domains on  [gi|1034588516|ref|XP_016877250|]
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ribosome quality control complex subunit NEMF isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RqcH_arch super family cl49222
ribosome rescue protein RqcH, archaeal type; This HMM (built with support from arCOG01695) ...
40-415 8.78e-75

ribosome rescue protein RqcH, archaeal type; This HMM (built with support from arCOG01695) describes archaeal homologs of the RqcH (Ribosome-associated Quality Control H), involved in release of defective mRNAs that lack a stop codons and so are stuck on ribosomes. Conservation of a role in ribosome rescue for this archaeal family is supported by presence in a conserved gene neighborhood with homologs of Pelota/Dom34 and ABCE1/Rli1 homologs, proteins involved in splitting the ribosome into large and small subunits.


The actual alignment was detected with superfamily member NF041120:

Pssm-ID: 469043 [Multi-domain]  Cd Length: 642  Bit Score: 256.75  E-value: 8.78e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516  40 TYEEFHPFLFSQHSqCPYIEFESFDKAVDEFYSKIEGQKIdlkalqQEKQALKKLDNVRKDHENRLEALQQA-----QEI 114
Cdd:NF041120  239 EPVDVLPIPLKEYE-YEKKEFDSFNEALDEYFSELELEEE------KEEEESEEEKEEIEKLERRIEQQEEAieefeKEA 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 115 DKL--KGELIEMNLQIVDRAIQVVRSAlanqidWTEIGLIVKEAqAQGDPVASAIKELKLQTNHVTMLLrnpyllseeed 192
Cdd:NF041120  312 EELreKAELIYANYQEVEEILNTLRKA------REKIKKILKEA-EEGIPAAKRVIEVDPAKGTVTLDL----------- 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 193 ddvdgdvnvekNETEppkgkkkkqknkqlqkpqknkpllVDVDLSLSAYANAKKYYDH-KRYAAKK--TQKTVEAAEKAF 269
Cdd:NF041120  374 -----------DGEE------------------------VELDIRKSVEENASRYYEKaKKLKRKIegALEAIEETKKEL 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 270 KSAEKKTKQTLKEVQTVtsiqkARKVYWFEKFLWFISSENYLIIGGRDQQQNEIIVKRYLTPGDIYVHADLHGATSCVIK 349
Cdd:NF041120  419 EKLEKKREEKKEEARRV-----RRKKEWYERFRWFITSDGFLVIGGRDADQNEELVKKYLEDNDIFFHADIHGAPAVVIK 493
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034588516 350 NpTGEPIPPRTLTEAGTMALCYSAAW-DARVITSAWWVYHHQVSKTAPTGEYLTTGSFMIRGKKNFL 415
Cdd:NF041120  494 T-GGESVPEEDLREAAQFAASYSKAWkAGLGSGDVYWVYPDQVSKTPPSGEYLAKGSFMIRGKRNYI 559
NFACT-C pfam11923
NFACT protein C-terminal domain; This is the C-terminal domain of the NFACT (NEMF, FbpA, ...
746-837 7.88e-40

NFACT protein C-terminal domain; This is the C-terminal domain of the NFACT (NEMF, FbpA, Caliban, and Tae2) proteins involved in the ribosomal quality control pathway. This context is conserved in archaea and eukaryotes, but NFACT proteins in bacteria lack the NFACT-C domain.


:

Pssm-ID: 432191  Cd Length: 104  Bit Score: 142.27  E-value: 7.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 746 NEENLFDSLTGQPHPEDVLLFAIPICAPYTTMTNYKYKVKLTPGVQKKGKAAKTALNSFMH---------SKEATAREKD 816
Cdd:pfam11923   3 NYLTLLDSLTGTPLPDDELLEAIPVCAPWAALQKYKYKVKLQPGTTKKGKAVKEILEYFLKrkvdessrdKERDWPREKE 82
                          90       100
                  ....*....|....*....|..
gi 1034588516 817 LFRSVKDTDLSRNIP-GKVKVS 837
Cdd:pfam11923  83 LIKALKDEELVNVIPvGKVKVS 104
COG5137 super family cl47089
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics] ...
429-547 6.81e-03

Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics];


The actual alignment was detected with superfamily member COG5137:

Pssm-ID: 227466 [Multi-domain]  Cd Length: 279  Bit Score: 39.21  E-value: 6.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 429 KVDESCVWRHQGERKVRVQDEDMETLASCTSELISEEMEQLDGGDTSSDEDKEEHETPVEVELMTQVDQEditlqsGRDE 508
Cdd:COG5137   134 KVDEEDVEREILAEKPRVTRFNIVWDNDEDNDEAPPAQPDVDNEEEERLEESDGREEEEDEEVGSDSYGE------GNRE 207
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1034588516 509 LNEELIQEES----SEDEGEYEEVRKDqDSVGEMKDEGEETLN 547
Cdd:COG5137   208 LNEEEEEEAEgsddGEDVVDYEGERID-KKQGEEEEMEEEVIN 249
 
Name Accession Description Interval E-value
RqcH_arch NF041120
ribosome rescue protein RqcH, archaeal type; This HMM (built with support from arCOG01695) ...
40-415 8.78e-75

ribosome rescue protein RqcH, archaeal type; This HMM (built with support from arCOG01695) describes archaeal homologs of the RqcH (Ribosome-associated Quality Control H), involved in release of defective mRNAs that lack a stop codons and so are stuck on ribosomes. Conservation of a role in ribosome rescue for this archaeal family is supported by presence in a conserved gene neighborhood with homologs of Pelota/Dom34 and ABCE1/Rli1 homologs, proteins involved in splitting the ribosome into large and small subunits.


Pssm-ID: 469043 [Multi-domain]  Cd Length: 642  Bit Score: 256.75  E-value: 8.78e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516  40 TYEEFHPFLFSQHSqCPYIEFESFDKAVDEFYSKIEGQKIdlkalqQEKQALKKLDNVRKDHENRLEALQQA-----QEI 114
Cdd:NF041120  239 EPVDVLPIPLKEYE-YEKKEFDSFNEALDEYFSELELEEE------KEEEESEEEKEEIEKLERRIEQQEEAieefeKEA 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 115 DKL--KGELIEMNLQIVDRAIQVVRSAlanqidWTEIGLIVKEAqAQGDPVASAIKELKLQTNHVTMLLrnpyllseeed 192
Cdd:NF041120  312 EELreKAELIYANYQEVEEILNTLRKA------REKIKKILKEA-EEGIPAAKRVIEVDPAKGTVTLDL----------- 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 193 ddvdgdvnvekNETEppkgkkkkqknkqlqkpqknkpllVDVDLSLSAYANAKKYYDH-KRYAAKK--TQKTVEAAEKAF 269
Cdd:NF041120  374 -----------DGEE------------------------VELDIRKSVEENASRYYEKaKKLKRKIegALEAIEETKKEL 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 270 KSAEKKTKQTLKEVQTVtsiqkARKVYWFEKFLWFISSENYLIIGGRDQQQNEIIVKRYLTPGDIYVHADLHGATSCVIK 349
Cdd:NF041120  419 EKLEKKREEKKEEARRV-----RRKKEWYERFRWFITSDGFLVIGGRDADQNEELVKKYLEDNDIFFHADIHGAPAVVIK 493
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034588516 350 NpTGEPIPPRTLTEAGTMALCYSAAW-DARVITSAWWVYHHQVSKTAPTGEYLTTGSFMIRGKKNFL 415
Cdd:NF041120  494 T-GGESVPEEDLREAAQFAASYSKAWkAGLGSGDVYWVYPDQVSKTPPSGEYLAKGSFMIRGKRNYI 559
NFACT-R_1 pfam05670
NFACT protein RNA binding domain; This domain occurs in proteins that have been annotated as ...
300-410 9.82e-51

NFACT protein RNA binding domain; This domain occurs in proteins that have been annotated as Fibronectin/fibrinogen binding protein by similarity. This annotation comes from Swiss:O34693 where the N-terminal region is involved in this activity. It is an RNA binding domain of the NFACT (NEMF, FbpA, Caliban, and Tae2) proteins. This NFACT-R family is found in two eukaryotic gene contexts: fused to the NFACT-N and NFACT-C domains in the NFACT protein involved in the ribosomal quality control pathway which contributes to CAT-tailing and as a standalone domain. Additionally this domain contains a conserved motif D/E-X-W/Y-X-H that may be functionally important.


Pssm-ID: 428576 [Multi-domain]  Cd Length: 111  Bit Score: 173.18  E-value: 9.82e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 300 KFLWFISSENYLIIGGRDQQQNEIIVKRYLTPGDIYVHADLHGATSCVIKNPTGEPIPPRTLTEAGTMALCYSAAWDARV 379
Cdd:pfam05670   1 KFYWFVSSEGYLVIGGRDKQENELLIKKYLEEGDLWFHADKHGSAHVYLKLPEGEDIPPETLEEAAQLAKANSIAWGNKQ 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1034588516 380 -ITSAWWVYHHQVSKTAPTGeYLTTGSFMIRG 410
Cdd:pfam05670  81 nNISVWYTPASQVSKTGPSG-YLDTGSFMFKG 111
RqcH COG1293
Ribosome quality control (RQC) protein RqcH, Rqc2/NEMF/Tae2 family, contains fibronectin-(FbpA) ...
4-415 7.14e-43

Ribosome quality control (RQC) protein RqcH, Rqc2/NEMF/Tae2 family, contains fibronectin-(FbpA) and RNA- (NFACT) binding domains [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440904 [Multi-domain]  Cd Length: 578  Bit Score: 165.01  E-value: 7.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516   4 RVMSKWMKNLK---LKGYIIQKREIKPsleadkpvediltyEEFHPFLFSQHSQCPYIEFESFDKAVDEFYSkiegQKID 80
Cdd:COG1293   235 EALQELLEELEngeFKPTIYYEEDGKP--------------VDFSPFPLTHYEGLEKESFDSFSEALDEYYS----EKAE 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516  81 LKALQQEKQAL-KKLDNVRKDHENRL----EALQQAQEIDKLK--GELIEMNLQIVDRAIqvvrsalanqidwteigliv 153
Cdd:COG1293   297 RDRVKQLAEDLrKKVENELEKLERKLekqeEELEEAEKAEKYRekGELLTANLYQVEKGM-------------------- 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 154 keaqaqgdpvasaiKELKLQtnhvtmllrNPYllseeedddvdgdvnvekneteppkgkkkkqknkqlqkpqknKPLLVD 233
Cdd:COG1293   357 --------------KEVTLP---------NYY------------------------------------------EEVTIP 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 234 VDLSLSAYANAKKYYdhKRYaaKKTQKTVEAAEKAFKSAEKK--------------TKQTLKEVQT---------VTSIQ 290
Cdd:COG1293   372 LDPRLSPSENAQRYY--KKY--KKLKRKKEGAEEQLEETEEEleylesvlaqleqaEDEDLEEIREelieqgylkKKKKK 447
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 291 KARKVYWFEKFLWFISSENYLIIGGRDQQQNEIIVKRYLTPGDIYVHADLHGATSCVIKNpTGEPIPPRTLTEAGTMALC 370
Cdd:COG1293   448 KKKKKKWYEKPRWFISSDGFLILVGRNNRQNDELTKKYARKNDIWFHAKDIPGSHVIIKT-EGKEPPEETLEEAAQLAAY 526
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1034588516 371 YSAAWDARVITsAWWVYHHQVSKtaPTGEyltTGSFMIRGKKNFL 415
Cdd:COG1293   527 YSKARKSGSVP-VDYTEPKQVSK--PKGA---KPGFVIYGNRKTL 565
NFACT-C pfam11923
NFACT protein C-terminal domain; This is the C-terminal domain of the NFACT (NEMF, FbpA, ...
746-837 7.88e-40

NFACT protein C-terminal domain; This is the C-terminal domain of the NFACT (NEMF, FbpA, Caliban, and Tae2) proteins involved in the ribosomal quality control pathway. This context is conserved in archaea and eukaryotes, but NFACT proteins in bacteria lack the NFACT-C domain.


Pssm-ID: 432191  Cd Length: 104  Bit Score: 142.27  E-value: 7.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 746 NEENLFDSLTGQPHPEDVLLFAIPICAPYTTMTNYKYKVKLTPGVQKKGKAAKTALNSFMH---------SKEATAREKD 816
Cdd:pfam11923   3 NYLTLLDSLTGTPLPDDELLEAIPVCAPWAALQKYKYKVKLQPGTTKKGKAVKEILEYFLKrkvdessrdKERDWPREKE 82
                          90       100
                  ....*....|....*....|..
gi 1034588516 817 LFRSVKDTDLSRNIP-GKVKVS 837
Cdd:pfam11923  83 LIKALKDEELVNVIPvGKVKVS 104
COG5137 COG5137
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics] ...
429-547 6.81e-03

Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics];


Pssm-ID: 227466 [Multi-domain]  Cd Length: 279  Bit Score: 39.21  E-value: 6.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 429 KVDESCVWRHQGERKVRVQDEDMETLASCTSELISEEMEQLDGGDTSSDEDKEEHETPVEVELMTQVDQEditlqsGRDE 508
Cdd:COG5137   134 KVDEEDVEREILAEKPRVTRFNIVWDNDEDNDEAPPAQPDVDNEEEERLEESDGREEEEDEEVGSDSYGE------GNRE 207
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1034588516 509 LNEELIQEES----SEDEGEYEEVRKDqDSVGEMKDEGEETLN 547
Cdd:COG5137   208 LNEEEEEEAEgsddGEDVVDYEGERID-KKQGEEEEMEEEVIN 249
 
Name Accession Description Interval E-value
RqcH_arch NF041120
ribosome rescue protein RqcH, archaeal type; This HMM (built with support from arCOG01695) ...
40-415 8.78e-75

ribosome rescue protein RqcH, archaeal type; This HMM (built with support from arCOG01695) describes archaeal homologs of the RqcH (Ribosome-associated Quality Control H), involved in release of defective mRNAs that lack a stop codons and so are stuck on ribosomes. Conservation of a role in ribosome rescue for this archaeal family is supported by presence in a conserved gene neighborhood with homologs of Pelota/Dom34 and ABCE1/Rli1 homologs, proteins involved in splitting the ribosome into large and small subunits.


Pssm-ID: 469043 [Multi-domain]  Cd Length: 642  Bit Score: 256.75  E-value: 8.78e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516  40 TYEEFHPFLFSQHSqCPYIEFESFDKAVDEFYSKIEGQKIdlkalqQEKQALKKLDNVRKDHENRLEALQQA-----QEI 114
Cdd:NF041120  239 EPVDVLPIPLKEYE-YEKKEFDSFNEALDEYFSELELEEE------KEEEESEEEKEEIEKLERRIEQQEEAieefeKEA 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 115 DKL--KGELIEMNLQIVDRAIQVVRSAlanqidWTEIGLIVKEAqAQGDPVASAIKELKLQTNHVTMLLrnpyllseeed 192
Cdd:NF041120  312 EELreKAELIYANYQEVEEILNTLRKA------REKIKKILKEA-EEGIPAAKRVIEVDPAKGTVTLDL----------- 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 193 ddvdgdvnvekNETEppkgkkkkqknkqlqkpqknkpllVDVDLSLSAYANAKKYYDH-KRYAAKK--TQKTVEAAEKAF 269
Cdd:NF041120  374 -----------DGEE------------------------VELDIRKSVEENASRYYEKaKKLKRKIegALEAIEETKKEL 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 270 KSAEKKTKQTLKEVQTVtsiqkARKVYWFEKFLWFISSENYLIIGGRDQQQNEIIVKRYLTPGDIYVHADLHGATSCVIK 349
Cdd:NF041120  419 EKLEKKREEKKEEARRV-----RRKKEWYERFRWFITSDGFLVIGGRDADQNEELVKKYLEDNDIFFHADIHGAPAVVIK 493
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034588516 350 NpTGEPIPPRTLTEAGTMALCYSAAW-DARVITSAWWVYHHQVSKTAPTGEYLTTGSFMIRGKKNFL 415
Cdd:NF041120  494 T-GGESVPEEDLREAAQFAASYSKAWkAGLGSGDVYWVYPDQVSKTPPSGEYLAKGSFMIRGKRNYI 559
NFACT-R_1 pfam05670
NFACT protein RNA binding domain; This domain occurs in proteins that have been annotated as ...
300-410 9.82e-51

NFACT protein RNA binding domain; This domain occurs in proteins that have been annotated as Fibronectin/fibrinogen binding protein by similarity. This annotation comes from Swiss:O34693 where the N-terminal region is involved in this activity. It is an RNA binding domain of the NFACT (NEMF, FbpA, Caliban, and Tae2) proteins. This NFACT-R family is found in two eukaryotic gene contexts: fused to the NFACT-N and NFACT-C domains in the NFACT protein involved in the ribosomal quality control pathway which contributes to CAT-tailing and as a standalone domain. Additionally this domain contains a conserved motif D/E-X-W/Y-X-H that may be functionally important.


Pssm-ID: 428576 [Multi-domain]  Cd Length: 111  Bit Score: 173.18  E-value: 9.82e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 300 KFLWFISSENYLIIGGRDQQQNEIIVKRYLTPGDIYVHADLHGATSCVIKNPTGEPIPPRTLTEAGTMALCYSAAWDARV 379
Cdd:pfam05670   1 KFYWFVSSEGYLVIGGRDKQENELLIKKYLEEGDLWFHADKHGSAHVYLKLPEGEDIPPETLEEAAQLAKANSIAWGNKQ 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1034588516 380 -ITSAWWVYHHQVSKTAPTGeYLTTGSFMIRG 410
Cdd:pfam05670  81 nNISVWYTPASQVSKTGPSG-YLDTGSFMFKG 111
RqcH COG1293
Ribosome quality control (RQC) protein RqcH, Rqc2/NEMF/Tae2 family, contains fibronectin-(FbpA) ...
4-415 7.14e-43

Ribosome quality control (RQC) protein RqcH, Rqc2/NEMF/Tae2 family, contains fibronectin-(FbpA) and RNA- (NFACT) binding domains [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440904 [Multi-domain]  Cd Length: 578  Bit Score: 165.01  E-value: 7.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516   4 RVMSKWMKNLK---LKGYIIQKREIKPsleadkpvediltyEEFHPFLFSQHSQCPYIEFESFDKAVDEFYSkiegQKID 80
Cdd:COG1293   235 EALQELLEELEngeFKPTIYYEEDGKP--------------VDFSPFPLTHYEGLEKESFDSFSEALDEYYS----EKAE 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516  81 LKALQQEKQAL-KKLDNVRKDHENRL----EALQQAQEIDKLK--GELIEMNLQIVDRAIqvvrsalanqidwteigliv 153
Cdd:COG1293   297 RDRVKQLAEDLrKKVENELEKLERKLekqeEELEEAEKAEKYRekGELLTANLYQVEKGM-------------------- 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 154 keaqaqgdpvasaiKELKLQtnhvtmllrNPYllseeedddvdgdvnvekneteppkgkkkkqknkqlqkpqknKPLLVD 233
Cdd:COG1293   357 --------------KEVTLP---------NYY------------------------------------------EEVTIP 371
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 234 VDLSLSAYANAKKYYdhKRYaaKKTQKTVEAAEKAFKSAEKK--------------TKQTLKEVQT---------VTSIQ 290
Cdd:COG1293   372 LDPRLSPSENAQRYY--KKY--KKLKRKKEGAEEQLEETEEEleylesvlaqleqaEDEDLEEIREelieqgylkKKKKK 447
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 291 KARKVYWFEKFLWFISSENYLIIGGRDQQQNEIIVKRYLTPGDIYVHADLHGATSCVIKNpTGEPIPPRTLTEAGTMALC 370
Cdd:COG1293   448 KKKKKKWYEKPRWFISSDGFLILVGRNNRQNDELTKKYARKNDIWFHAKDIPGSHVIIKT-EGKEPPEETLEEAAQLAAY 526
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1034588516 371 YSAAWDARVITsAWWVYHHQVSKtaPTGEyltTGSFMIRGKKNFL 415
Cdd:COG1293   527 YSKARKSGSVP-VDYTEPKQVSK--PKGA---KPGFVIYGNRKTL 565
NFACT-C pfam11923
NFACT protein C-terminal domain; This is the C-terminal domain of the NFACT (NEMF, FbpA, ...
746-837 7.88e-40

NFACT protein C-terminal domain; This is the C-terminal domain of the NFACT (NEMF, FbpA, Caliban, and Tae2) proteins involved in the ribosomal quality control pathway. This context is conserved in archaea and eukaryotes, but NFACT proteins in bacteria lack the NFACT-C domain.


Pssm-ID: 432191  Cd Length: 104  Bit Score: 142.27  E-value: 7.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 746 NEENLFDSLTGQPHPEDVLLFAIPICAPYTTMTNYKYKVKLTPGVQKKGKAAKTALNSFMH---------SKEATAREKD 816
Cdd:pfam11923   3 NYLTLLDSLTGTPLPDDELLEAIPVCAPWAALQKYKYKVKLQPGTTKKGKAVKEILEYFLKrkvdessrdKERDWPREKE 82
                          90       100
                  ....*....|....*....|..
gi 1034588516 817 LFRSVKDTDLSRNIP-GKVKVS 837
Cdd:pfam11923  83 LIKALKDEELVNVIPvGKVKVS 104
NFACT_N pfam05833
NFACT N-terminal and middle domains; This family contains the N-terminal and middle domains of ...
42-131 1.52e-05

NFACT N-terminal and middle domains; This family contains the N-terminal and middle domains of NFACT (NEMF, FbpA, Caliban, and Tae2) proteins from eukaryotes, archaea and bacteria. Many members of this family act in ribosome quality control (RQC), including RqcH, which are involved in the addition of a poly-Ala tail to defective translated proteins to tag them for degradation. This process is analogous to the ssrA/tmRNA bacterial system. However, some other NFACT family members, such as bacterial proteins FbpA in Listeria or PavA in Streptococcus, are exported (despite lack of a classical signal peptide) and behave as fibronectin-binding adhesins associated with virulence.


Pssm-ID: 428644 [Multi-domain]  Cd Length: 451  Bit Score: 48.39  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516  42 EEFHPFLFSqHSQCPYIEFESFDKAVDEFYS-KIEGQKIDLKA--LQQE-KQALKKLDNVRKDHENRLEALQQAQEIdKL 117
Cdd:pfam05833 256 KDFSVLPLS-HLGLEKETFDSLSELLDEYYAeKAERDRVKQKRsdLEKVvQNELEKLEKKLKKLEKELEEAENADEY-RL 333
                          90
                  ....*....|....
gi 1034588516 118 KGELIEMNLQIVDR 131
Cdd:pfam05833 334 YGELLTANLYQIKK 347
COG5137 COG5137
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics] ...
429-547 6.81e-03

Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics];


Pssm-ID: 227466 [Multi-domain]  Cd Length: 279  Bit Score: 39.21  E-value: 6.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034588516 429 KVDESCVWRHQGERKVRVQDEDMETLASCTSELISEEMEQLDGGDTSSDEDKEEHETPVEVELMTQVDQEditlqsGRDE 508
Cdd:COG5137   134 KVDEEDVEREILAEKPRVTRFNIVWDNDEDNDEAPPAQPDVDNEEEERLEESDGREEEEDEEVGSDSYGE------GNRE 207
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1034588516 509 LNEELIQEES----SEDEGEYEEVRKDqDSVGEMKDEGEETLN 547
Cdd:COG5137   208 LNEEEEEEAEgsddGEDVVDYEGERID-KKQGEEEEMEEEVIN 249
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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