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Conserved domains on  [gi|1333608568|ref|XP_001491025|]
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LOW QUALITY PROTEIN: transcription initiation factor TFIID subunit 4 [Equus caballus]

Protein Classification

TAFH and TAF4 domain-containing protein( domain architecture ID 11167152)

TAFH and TAF4 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TAF4 pfam05236
Transcription initiation factor TFIID component TAF4 family; This region of similarity is ...
 797-1045 9.59e-120

Transcription initiation factor TFIID component TAF4 family; This region of similarity is found in Transcription initiation factor TFIID component TAF4.


:

Pssm-ID: 461598 [Multi-domain]  Cd Length: 264  Bit Score: 367.75  E-value: 9.59e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  797 INDVASMAGVNLSEESARIL-----ATNSELVGTLTRSCKDETFLLPAPLQRRILEIGKKHGITELHPDVVSYVSHATQQ 871
Cdd:pfam05236    1 LNDVLAMAGVNLREEEERLLssqeaSTNSEAVGTVVRSCKDEPFLNPYPLQRKILEIAKKNGLKEIDPDVLELLSHACEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  872 RLQSLVEKISETAQQKNFSYKDDDRYEQASDVRAQLKFFEQLDQIEKQRKDEQEREILMRAAKSRSRQEDPEQLRLKQKA 951
Cdd:pfam05236   81 RLRNLLEKLIVISRHRRDGEKTDHRYEQTSDVRKQLKFLAQKDKEEEERRVAEEREGLLKAAKSRSNQEDPEQLKLKQEA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  952 KEMQQQELAQMRQRDANLTALAAIGPRKKRKVD----SPGPGSGTEGAGPGSAVPGSSGVGTPRQFT------RQRITRV 1021
Cdd:pfam05236  161 KEMQKEEDEKMRHRAANLTALAAIGPRKKKYSWmsssASGSGGGGSGSSKPSSSSGSSSKGTSQTQSsaisreARRIKRV 240

                          250       260
                   ....*....|....*....|....
gi 1333608568 1022 NLRDLIFCLENERETSHSLLLYKA 1045
Cdd:pfam05236  241 TLRDLLFALEQEREGSRSALLYGY 264
TAFH pfam07531
NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the ...
 556-639 1.88e-41

NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the product of the nervy gene in Drosophila and the human mtg8b protein, which is hypothesized to be a transcription factor.


:

Pssm-ID: 462195  Cd Length: 90  Bit Score: 146.64  E-value: 1.88e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  556 NVKKCKNFLSTLIKLAssGKQSTETAANVKELVQNLLDGKIEAEDFTSRLYRELNSSPQPYLVPFLKRSLPALRQLTPDS 635
Cdd:pfam07531    1 NVKKCKNFLSTLIKLA--GEQSPETGENVKELVQGLLNGKIEPEEFTSKLQEELNSSPQPYLVPFLKKSLPALRQELLNS 78


                   ....
gi 1333608568  636 AAFI 639
Cdd:pfam07531   79 ARFI 82
 
Name Accession Description Interval E-value
TAF4 pfam05236
Transcription initiation factor TFIID component TAF4 family; This region of similarity is ...
 797-1045 9.59e-120

Transcription initiation factor TFIID component TAF4 family; This region of similarity is found in Transcription initiation factor TFIID component TAF4.


Pssm-ID: 461598 [Multi-domain]  Cd Length: 264  Bit Score: 367.75  E-value: 9.59e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  797 INDVASMAGVNLSEESARIL-----ATNSELVGTLTRSCKDETFLLPAPLQRRILEIGKKHGITELHPDVVSYVSHATQQ 871
Cdd:pfam05236    1 LNDVLAMAGVNLREEEERLLssqeaSTNSEAVGTVVRSCKDEPFLNPYPLQRKILEIAKKNGLKEIDPDVLELLSHACEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  872 RLQSLVEKISETAQQKNFSYKDDDRYEQASDVRAQLKFFEQLDQIEKQRKDEQEREILMRAAKSRSRQEDPEQLRLKQKA 951
Cdd:pfam05236   81 RLRNLLEKLIVISRHRRDGEKTDHRYEQTSDVRKQLKFLAQKDKEEEERRVAEEREGLLKAAKSRSNQEDPEQLKLKQEA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  952 KEMQQQELAQMRQRDANLTALAAIGPRKKRKVD----SPGPGSGTEGAGPGSAVPGSSGVGTPRQFT------RQRITRV 1021
Cdd:pfam05236  161 KEMQKEEDEKMRHRAANLTALAAIGPRKKKYSWmsssASGSGGGGSGSSKPSSSSGSSSKGTSQTQSsaisreARRIKRV 240

                          250       260
                   ....*....|....*....|....
gi 1333608568 1022 NLRDLIFCLENERETSHSLLLYKA 1045
Cdd:pfam05236  241 TLRDLLFALEQEREGSRSALLYGY 264
TAFH pfam07531
NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the ...
 556-639 1.88e-41

NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the product of the nervy gene in Drosophila and the human mtg8b protein, which is hypothesized to be a transcription factor.


Pssm-ID: 462195  Cd Length: 90  Bit Score: 146.64  E-value: 1.88e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  556 NVKKCKNFLSTLIKLAssGKQSTETAANVKELVQNLLDGKIEAEDFTSRLYRELNSSPQPYLVPFLKRSLPALRQLTPDS 635
Cdd:pfam07531    1 NVKKCKNFLSTLIKLA--GEQSPETGENVKELVQGLLNGKIEPEEFTSKLQEELNSSPQPYLVPFLKKSLPALRQELLNS 78


                   ....
gi 1333608568  636 AAFI 639
Cdd:pfam07531   79 ARFI 82
HFD_TAF4 cd08045
histone-fold domain found in transcription initiation factor TFIID subunit 4 (TAF4) and ...
 832-931 1.41e-37

histone-fold domain found in transcription initiation factor TFIID subunit 4 (TAF4) and similar proteins; TAF4, also called TATA Binding Protein (TBP) associated factor 4, RNA polymerase II TBP-associated factor subunit C, TBP-associated factor 4, transcription initiation factor TFIID 130 kDa subunit (TAF(II)130, TAFII-130, TAFII130), or transcription initiation factor TFIID 135 kDa subunit (TAF(II)135, TAFII-135, TAFII135), is a component of the TFIID complex that is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). TFIID is one of the general transcription factors required for accurate and regulated initiation by RNA polymerase II. It plays a central role in mediating promoter responses to various activators and repressors. TAF4 potentiates transcriptional activation by the AF-2S of retinoic acid, vitamin D3 and thyroid hormone. TAF4 also acts as a component of the TFTC-HAT complex and some MLL1/MLL complexes. TAF4 interacts with ATF7 and the interaction inhibits ATF7-mediated transactivation.


Pssm-ID: 467027 [Multi-domain]  Cd Length: 100  Bit Score: 135.82  E-value: 1.41e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  832 DETFLLPAPLQRRILEIGKKHGITELHPDVVSYVSHATQQRLQSLVEKISETAQQKNFSYKDDDRYEQASDVRAQLKFFE 911
Cdd:cd08045      1 EESFLNPPPLQKKIQKIAKKHGLKEVSPDVLSLLSLAVQERLRDLLEKLIVASKHRVDSEKPDYRYEVTSDVRRQLKALE 80

                           90       100
                   ....*....|....*....|
gi 1333608568  912 QLDQIEKQRKDEQEREILMR 931
Cdd:cd08045     81 RLEREEEERRREEERERLLR 100
TAFH smart00549
TAF homology; Domain in Drosophila nervy, CBFA2T1, human TAF105, human TAF130, and Drosophila ...
 556-639 2.50e-33

TAF homology; Domain in Drosophila nervy, CBFA2T1, human TAF105, human TAF130, and Drosophila TAF110. Also known as nervy homology region 1 (NHR1).


Pssm-ID: 197785 [Multi-domain]  Cd Length: 92  Bit Score: 123.73  E-value: 2.50e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568   556 NVKKCKNFLSTLIKLASSGKQsTETAANVKELVQNLLDGKIEAEDFTSRLYRELNSSPQPYLVPFLKRSLPALRQLTPDS 635
Cdd:smart00549    1 NVSKCKRFLTTLIQLSNDISQ-PEVAERVRTLVLGLVNGTITAEEFTSRLQEALNSPLQPYLIPFLKNSLPLLRRELLHC 79


                    ....
gi 1333608568   636 AAFI 639
Cdd:smart00549   80 ARLI 83
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 870-974 2.48e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 2.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  870 QQRLQSLVEKISETAQQKNFsYKDDDRYEQASDVRAQlkffEQLDQiEKQRKDEQEREILMRAAKSRSRQEDPEQLRLKQ 949
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQI-LRERLANLERQLEELE----AQLEE-LESKLDELAEELAELEEKLEELKEELESLEAEL 360

                           90       100
                   ....*....|....*....|....*.
gi 1333608568  950 KAKEMQQQEL-AQMRQRDANLTALAA 974
Cdd:TIGR02168  361 EELEAELEELeSRLEELEEQLETLRS 386
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 867-974 1.50e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  867 HATQQRLQSLVEKISETAQQKNFsykDDDRYEQASDVRAQLKffEQLDQIEKQRKDEQEREIlmrAAKSRSRQEDPEQLR 946
Cdd:COG1196    284 EEAQAEEYELLAELARLEQDIAR---LEERRRELEERLEELE--EELAELEEELEELEEELE---ELEEELEEAEEELEE 355

                           90       100
                   ....*....|....*....|....*...
gi 1333608568  947 LKQKAKEMQQQELAQMRQRDANLTALAA 974
Cdd:COG1196    356 AEAELAEAEEALLEAEAELAEAEEELEE 383
 
Name Accession Description Interval E-value
TAF4 pfam05236
Transcription initiation factor TFIID component TAF4 family; This region of similarity is ...
 797-1045 9.59e-120

Transcription initiation factor TFIID component TAF4 family; This region of similarity is found in Transcription initiation factor TFIID component TAF4.


Pssm-ID: 461598 [Multi-domain]  Cd Length: 264  Bit Score: 367.75  E-value: 9.59e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  797 INDVASMAGVNLSEESARIL-----ATNSELVGTLTRSCKDETFLLPAPLQRRILEIGKKHGITELHPDVVSYVSHATQQ 871
Cdd:pfam05236    1 LNDVLAMAGVNLREEEERLLssqeaSTNSEAVGTVVRSCKDEPFLNPYPLQRKILEIAKKNGLKEIDPDVLELLSHACEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  872 RLQSLVEKISETAQQKNFSYKDDDRYEQASDVRAQLKFFEQLDQIEKQRKDEQEREILMRAAKSRSRQEDPEQLRLKQKA 951
Cdd:pfam05236   81 RLRNLLEKLIVISRHRRDGEKTDHRYEQTSDVRKQLKFLAQKDKEEEERRVAEEREGLLKAAKSRSNQEDPEQLKLKQEA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  952 KEMQQQELAQMRQRDANLTALAAIGPRKKRKVD----SPGPGSGTEGAGPGSAVPGSSGVGTPRQFT------RQRITRV 1021
Cdd:pfam05236  161 KEMQKEEDEKMRHRAANLTALAAIGPRKKKYSWmsssASGSGGGGSGSSKPSSSSGSSSKGTSQTQSsaisreARRIKRV 240

                          250       260
                   ....*....|....*....|....
gi 1333608568 1022 NLRDLIFCLENERETSHSLLLYKA 1045
Cdd:pfam05236  241 TLRDLLFALEQEREGSRSALLYGY 264
TAFH pfam07531
NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the ...
 556-639 1.88e-41

NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the product of the nervy gene in Drosophila and the human mtg8b protein, which is hypothesized to be a transcription factor.


Pssm-ID: 462195  Cd Length: 90  Bit Score: 146.64  E-value: 1.88e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  556 NVKKCKNFLSTLIKLAssGKQSTETAANVKELVQNLLDGKIEAEDFTSRLYRELNSSPQPYLVPFLKRSLPALRQLTPDS 635
Cdd:pfam07531    1 NVKKCKNFLSTLIKLA--GEQSPETGENVKELVQGLLNGKIEPEEFTSKLQEELNSSPQPYLVPFLKKSLPALRQELLNS 78


                   ....
gi 1333608568  636 AAFI 639
Cdd:pfam07531   79 ARFI 82
HFD_TAF4 cd08045
histone-fold domain found in transcription initiation factor TFIID subunit 4 (TAF4) and ...
 832-931 1.41e-37

histone-fold domain found in transcription initiation factor TFIID subunit 4 (TAF4) and similar proteins; TAF4, also called TATA Binding Protein (TBP) associated factor 4, RNA polymerase II TBP-associated factor subunit C, TBP-associated factor 4, transcription initiation factor TFIID 130 kDa subunit (TAF(II)130, TAFII-130, TAFII130), or transcription initiation factor TFIID 135 kDa subunit (TAF(II)135, TAFII-135, TAFII135), is a component of the TFIID complex that is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). TFIID is one of the general transcription factors required for accurate and regulated initiation by RNA polymerase II. It plays a central role in mediating promoter responses to various activators and repressors. TAF4 potentiates transcriptional activation by the AF-2S of retinoic acid, vitamin D3 and thyroid hormone. TAF4 also acts as a component of the TFTC-HAT complex and some MLL1/MLL complexes. TAF4 interacts with ATF7 and the interaction inhibits ATF7-mediated transactivation.


Pssm-ID: 467027 [Multi-domain]  Cd Length: 100  Bit Score: 135.82  E-value: 1.41e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  832 DETFLLPAPLQRRILEIGKKHGITELHPDVVSYVSHATQQRLQSLVEKISETAQQKNFSYKDDDRYEQASDVRAQLKFFE 911
Cdd:cd08045      1 EESFLNPPPLQKKIQKIAKKHGLKEVSPDVLSLLSLAVQERLRDLLEKLIVASKHRVDSEKPDYRYEVTSDVRRQLKALE 80

                           90       100
                   ....*....|....*....|
gi 1333608568  912 QLDQIEKQRKDEQEREILMR 931
Cdd:cd08045     81 RLEREEEERRREEERERLLR 100
TAFH smart00549
TAF homology; Domain in Drosophila nervy, CBFA2T1, human TAF105, human TAF130, and Drosophila ...
 556-639 2.50e-33

TAF homology; Domain in Drosophila nervy, CBFA2T1, human TAF105, human TAF130, and Drosophila TAF110. Also known as nervy homology region 1 (NHR1).


Pssm-ID: 197785 [Multi-domain]  Cd Length: 92  Bit Score: 123.73  E-value: 2.50e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568   556 NVKKCKNFLSTLIKLASSGKQsTETAANVKELVQNLLDGKIEAEDFTSRLYRELNSSPQPYLVPFLKRSLPALRQLTPDS 635
Cdd:smart00549    1 NVSKCKRFLTTLIQLSNDISQ-PEVAERVRTLVLGLVNGTITAEEFTSRLQEALNSPLQPYLIPFLKNSLPLLRRELLHC 79


                    ....
gi 1333608568   636 AAFI 639
Cdd:smart00549   80 ARLI 83
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 870-965 9.45e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.68  E-value: 9.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  870 QQRLQSLVEKISETAQQKnfsykdDDRYEqasdVRAQLkFFEQLDQIEKQR-KDEQEREILMRAAKSRSRQEdpeQLRLK 948
Cdd:pfam13868  183 EREIARLRAQQEKAQDEK------AERDE----LRAKL-YQEEQERKERQKeREEAEKKARQRQELQQAREE---QIELK 248

                           90
                   ....*....|....*..
gi 1333608568  949 QKAKEMQQQELAQMRQR 965
Cdd:pfam13868  249 ERRLAEEAEREEEEFER 265
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 870-974 2.48e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 2.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  870 QQRLQSLVEKISETAQQKNFsYKDDDRYEQASDVRAQlkffEQLDQiEKQRKDEQEREILMRAAKSRSRQEDPEQLRLKQ 949
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQI-LRERLANLERQLEELE----AQLEE-LESKLDELAEELAELEEKLEELKEELESLEAEL 360

                           90       100
                   ....*....|....*....|....*.
gi 1333608568  950 KAKEMQQQEL-AQMRQRDANLTALAA 974
Cdd:TIGR02168  361 EELEAELEELeSRLEELEEQLETLRS 386
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 867-974 1.50e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  867 HATQQRLQSLVEKISETAQQKNFsykDDDRYEQASDVRAQLKffEQLDQIEKQRKDEQEREIlmrAAKSRSRQEDPEQLR 946
Cdd:COG1196    284 EEAQAEEYELLAELARLEQDIAR---LEERRRELEERLEELE--EELAELEEELEELEEELE---ELEEELEEAEEELEE 355

                           90       100
                   ....*....|....*....|....*...
gi 1333608568  947 LKQKAKEMQQQELAQMRQRDANLTALAA 974
Cdd:COG1196    356 AEAELAEAEEALLEAEAELAEAEEELEE 383
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 870-965 1.74e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  870 QQRLQSLVEKISETAQ--QKNFSYKDDDRYEQASDVRAQLKFFEQLDQIEKQRKD------EQEREILMRAA-----KSR 936
Cdd:pfam13868   87 QKRQEEYEEKLQEREQmdEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEwkelekEEEREEDERILeylkeKAE 166

                           90       100
                   ....*....|....*....|....*....
gi 1333608568  937 SRQEDPEQLRLKQKAKEMQQQELAQMRQR 965
Cdd:pfam13868  167 REEEREAEREEIEEEKEREIARLRAQQEK 195
RRP36 pfam06102
rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.
 872-956 1.89e-03

rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.


Pssm-ID: 461829 [Multi-domain]  Cd Length: 158  Bit Score: 40.23  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  872 RLQSLVEKISETAQQKNFSYKDDDRYEQASDVRAQLKffeqldqiekQRKDEQEREILMRA-------AKSRSRQEDPEQ 944
Cdd:pfam06102   34 RFDSLSGEFDEDKFRKNYGFLDEYRKKEIEELKKQLK----------KTKDPEEKEELKRTlqsmesrLKAKKRKDRERE 103

                           90
                   ....*....|..
gi 1333608568  945 LRLKQKAKEMQQ 956
Cdd:pfam06102  104 VLKEHKKEEKEK 115
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 867-965 4.90e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 4.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  867 HATQQRLQSLVEKISEtaQQKNFSYKDDDRyEQASDVRAqLKFFEQLDQIEKQRKDEQEREILMRA----------AKSR 936
Cdd:pfam13868  122 LEKQRQLREEIDEFNE--EQAEWKELEKEE-EREEDERI-LEYLKEKAEREEEREAEREEIEEEKEreiarlraqqEKAQ 197

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1333608568  937 SRQEDPEQLRLK----QKAKEMQQQELAQMRQR 965
Cdd:pfam13868  198 DEKAERDELRAKlyqeEQERKERQKEREEAEKK 230
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 870-965 6.26e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 6.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  870 QQRLQSLVEKisETAQQKnfsYKDDDRyEQASDVRAQLKFFEQLDQIEKQRKDEQE----REILM-----RAAKSRSRQE 940
Cdd:pfam13868  239 QAREEQIELK--ERRLAE---EAEREE-EEFERMLRKQAEDEEIEQEEAEKRRMKRlehrRELEKqieerEEQRAAEREE 312

                           90       100
                   ....*....|....*....|....*
gi 1333608568  941 DPEQLRLKQKAKEMQQQELAQMRQR 965
Cdd:pfam13868  313 ELEEGERLREEEAERRERIEEERQK 337
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
835-974 7.70e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 7.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  835 FLLPAPLQRRILEIGKKHG----------------ITELHPDVVSYvsHATQQRLQSLVEKISETAQQKNFSYKDDDRYE 898
Cdd:COG4717     45 AMLLERLEKEADELFKPQGrkpelnlkelkeleeeLKEAEEKEEEY--AELQEELEELEEELEELEAELEELREELEKLE 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333608568  899 QASDVRAQLKFFEQL--------DQIEKQRKDEQEREILMRAAKSRSRQEDPEQLRLKQKAKEMQQQELAQMRQRDANLT 970
Cdd:COG4717    123 KLLQLLPLYQELEALeaelaelpERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202


                   ....
gi 1333608568  971 ALAA 974
Cdd:COG4717    203 ELQQ 206
 
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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