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Conserved domains on  [gi|28872803|ref|NP_005178|]
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protein CBFA2T3 isoform 1 [Homo sapiens]

Protein Classification

TAFH and NHR2 domain-containing protein( domain architecture ID 11167161)

protein containing domains TAFH, NHR2, ATP-synt_Fo_b, and zf-MYND

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TAFH pfam07531
NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the ...
173-262 3.84e-43

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: 149.72  E-value: 3.84e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872803   173 QLSKLKRFLTTLQQFGSDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCAR 252
Cdd:pfam07531   1 NVKKCKNFLSTLIKLAGEQSPETGENVKELVQGLLNGKIEPEEFTSKLQEELNSSPQPYLVPFLKKSLPALRQELLNSAR 80
                          90
                  ....*....|
gi 28872803   253 LAKQTPAQYL 262
Cdd:pfam07531  81 FIQQCPPQYL 90
NHR2 pfam08788
NHR2 domain like; The NHR2 (Nervy homology 2) domain is found in the ETO protein where it ...
379-445 4.93e-34

NHR2 domain like; The NHR2 (Nervy homology 2) domain is found in the ETO protein where it mediates oligomerization and protein-protein interactions. It forms an alpha-helical tetramer.


:

Pssm-ID: 430219  Cd Length: 67  Bit Score: 123.88  E-value: 4.93e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28872803   379 QEEVIDHKLTEREWAEEWKHLNNLLNCIMDMVEKTRRSLTVLRRCQEADREELNHWARRYSDAEDTK 445
Cdd:pfam08788   1 REEYIDTRLTDREWADEWRHLDHLLNCIMDMVEKTRRSLTVLRRCQEADREELNYWIRRYSDAEELK 67
zf-MYND pfam01753
MYND finger;
556-592 5.60e-12

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 60.51  E-value: 5.60e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 28872803   556 CWNCGRKASET--CSGCNAARYCGSFCQHRDWEKHHHVC 592
Cdd:pfam01753   1 CAVCGKEALKLlrCSRCKSVYYCSKECQKADWPYHKKEC 39
vATP-synt_E super family cl23750
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as ...
482-553 1.47e-04

ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as well as the archaebacterial ATP synthase E subunit.


The actual alignment was detected with superfamily member PRK02292:

Pssm-ID: 419987 [Multi-domain]  Cd Length: 188  Bit Score: 43.06  E-value: 1.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28872803  482 VPEDIWRKAEEAVNEVKRQAMSELQKAVSDAERKAHELItterakmERALAEAKRQASEdaltvINQQEDSS 553
Cdd:PRK02292   6 VVEDIRDEARARASEIRAEADEEAEEIIAEAEADAEEIL-------EDREAEAEREIEQ-----LREQELSS 65
 
Name Accession Description Interval E-value
TAFH pfam07531
NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the ...
173-262 3.84e-43

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: 149.72  E-value: 3.84e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872803   173 QLSKLKRFLTTLQQFGSDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCAR 252
Cdd:pfam07531   1 NVKKCKNFLSTLIKLAGEQSPETGENVKELVQGLLNGKIEPEEFTSKLQEELNSSPQPYLVPFLKKSLPALRQELLNSAR 80
                          90
                  ....*....|
gi 28872803   253 LAKQTPAQYL 262
Cdd:pfam07531  81 FIQQCPPQYL 90
TAFH smart00549
TAF homology; Domain in Drosophila nervy, CBFA2T1, human TAF105, human TAF130, and Drosophila ...
173-263 1.57e-39

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: 139.90  E-value: 1.57e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872803    173 QLSKLKRFLTTLQQFGSDIS-PEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCA 251
Cdd:smart00549   1 NVSKCKRFLTTLIQLSNDISqPEVAERVRTLVLGLVNGTITAEEFTSRLQEALNSPLQPYLIPFLKNSLPLLRRELLHCA 80
                           90
                   ....*....|..
gi 28872803    252 RLAKQTPAQYLA 263
Cdd:smart00549  81 RLIEQSPPQPLA 92
NHR2 pfam08788
NHR2 domain like; The NHR2 (Nervy homology 2) domain is found in the ETO protein where it ...
379-445 4.93e-34

NHR2 domain like; The NHR2 (Nervy homology 2) domain is found in the ETO protein where it mediates oligomerization and protein-protein interactions. It forms an alpha-helical tetramer.


Pssm-ID: 430219  Cd Length: 67  Bit Score: 123.88  E-value: 4.93e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28872803   379 QEEVIDHKLTEREWAEEWKHLNNLLNCIMDMVEKTRRSLTVLRRCQEADREELNHWARRYSDAEDTK 445
Cdd:pfam08788   1 REEYIDTRLTDREWADEWRHLDHLLNCIMDMVEKTRRSLTVLRRCQEADREELNYWIRRYSDAEELK 67
zf-MYND pfam01753
MYND finger;
556-592 5.60e-12

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 60.51  E-value: 5.60e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 28872803   556 CWNCGRKASET--CSGCNAARYCGSFCQHRDWEKHHHVC 592
Cdd:pfam01753   1 CAVCGKEALKLlrCSRCKSVYYCSKECQKADWPYHKKEC 39
PRK02292 PRK02292
V-type ATP synthase subunit E; Provisional
482-553 1.47e-04

V-type ATP synthase subunit E; Provisional


Pssm-ID: 235026 [Multi-domain]  Cd Length: 188  Bit Score: 43.06  E-value: 1.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28872803  482 VPEDIWRKAEEAVNEVKRQAMSELQKAVSDAERKAHELItterakmERALAEAKRQASEdaltvINQQEDSS 553
Cdd:PRK02292   6 VVEDIRDEARARASEIRAEADEEAEEIIAEAEADAEEIL-------EDREAEAEREIEQ-----LREQELSS 65
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
484-538 2.47e-04

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 42.62  E-value: 2.47e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28872803 484 EDIWRKAEEAVNEVKRQAMSELQKAVSDAERKAHELITTERAKMERALAEAKRQA 538
Cdd:COG1390   9 EEILEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRI 63
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
488-545 3.38e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.19  E-value: 3.38e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28872803 488 RKAEEAVNEVKRQAMSELQKAVSDAERKAHELIttERAKME------RALAEAKRQASEDALTV 545
Cdd:cd06503  65 AEAQEIIEEARKEAEKIKEEILAEAKEEAERIL--EQAKAEieqekeKALAELRKEVADLAVEA 126
 
Name Accession Description Interval E-value
TAFH pfam07531
NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the ...
173-262 3.84e-43

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: 149.72  E-value: 3.84e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872803   173 QLSKLKRFLTTLQQFGSDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCAR 252
Cdd:pfam07531   1 NVKKCKNFLSTLIKLAGEQSPETGENVKELVQGLLNGKIEPEEFTSKLQEELNSSPQPYLVPFLKKSLPALRQELLNSAR 80
                          90
                  ....*....|
gi 28872803   253 LAKQTPAQYL 262
Cdd:pfam07531  81 FIQQCPPQYL 90
TAFH smart00549
TAF homology; Domain in Drosophila nervy, CBFA2T1, human TAF105, human TAF130, and Drosophila ...
173-263 1.57e-39

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: 139.90  E-value: 1.57e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28872803    173 QLSKLKRFLTTLQQFGSDIS-PEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCA 251
Cdd:smart00549   1 NVSKCKRFLTTLIQLSNDISqPEVAERVRTLVLGLVNGTITAEEFTSRLQEALNSPLQPYLIPFLKNSLPLLRRELLHCA 80
                           90
                   ....*....|..
gi 28872803    252 RLAKQTPAQYLA 263
Cdd:smart00549  81 RLIEQSPPQPLA 92
NHR2 pfam08788
NHR2 domain like; The NHR2 (Nervy homology 2) domain is found in the ETO protein where it ...
379-445 4.93e-34

NHR2 domain like; The NHR2 (Nervy homology 2) domain is found in the ETO protein where it mediates oligomerization and protein-protein interactions. It forms an alpha-helical tetramer.


Pssm-ID: 430219  Cd Length: 67  Bit Score: 123.88  E-value: 4.93e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28872803   379 QEEVIDHKLTEREWAEEWKHLNNLLNCIMDMVEKTRRSLTVLRRCQEADREELNHWARRYSDAEDTK 445
Cdd:pfam08788   1 REEYIDTRLTDREWADEWRHLDHLLNCIMDMVEKTRRSLTVLRRCQEADREELNYWIRRYSDAEELK 67
zf-MYND pfam01753
MYND finger;
556-592 5.60e-12

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 60.51  E-value: 5.60e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 28872803   556 CWNCGRKASET--CSGCNAARYCGSFCQHRDWEKHHHVC 592
Cdd:pfam01753   1 CAVCGKEALKLlrCSRCKSVYYCSKECQKADWPYHKKEC 39
PRK02292 PRK02292
V-type ATP synthase subunit E; Provisional
482-553 1.47e-04

V-type ATP synthase subunit E; Provisional


Pssm-ID: 235026 [Multi-domain]  Cd Length: 188  Bit Score: 43.06  E-value: 1.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28872803  482 VPEDIWRKAEEAVNEVKRQAMSELQKAVSDAERKAHELItterakmERALAEAKRQASEdaltvINQQEDSS 553
Cdd:PRK02292   6 VVEDIRDEARARASEIRAEADEEAEEIIAEAEADAEEIL-------EDREAEAEREIEQ-----LREQELSS 65
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
484-538 2.47e-04

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 42.62  E-value: 2.47e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 28872803 484 EDIWRKAEEAVNEVKRQAMSELQKAVSDAERKAHELITTERAKMERALAEAKRQA 538
Cdd:COG1390   9 EEILEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRI 63
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
490-537 3.21e-04

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 40.99  E-value: 3.21e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 28872803 490 AEEAVNEVKRQAMSELQKAVSDAERKAHELI---TTERAKMERALAEAKRQ 537
Cdd:COG3599  74 AQETAEEVKENAEKEAELIIKEAELEAEKIIeeaQEKARKIVREIEELKRQ 124
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
488-545 3.38e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.19  E-value: 3.38e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28872803 488 RKAEEAVNEVKRQAMSELQKAVSDAERKAHELIttERAKME------RALAEAKRQASEDALTV 545
Cdd:cd06503  65 AEAQEIIEEARKEAEKIKEEILAEAKEEAERIL--EQAKAEieqekeKALAELRKEVADLAVEA 126
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
487-542 4.35e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.02  E-value: 4.35e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 28872803 487 WRKAEEAVNEVKRQAMSELQKAVSDAERKAHELITTERAKmERALAEAKRQASEDA 542
Cdd:COG3064  79 LAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAE-KEKAEEAKRKAEEEA 133
NtpH COG2811
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ...
488-550 4.73e-03

Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit H is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 442060 [Multi-domain]  Cd Length: 108  Bit Score: 37.20  E-value: 4.73e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28872803 488 RKAEEAVNEVKRQAMSELQKAVSDAERKAHELITTERAKME----RALAEAKRQASEDALTVINQQE 550
Cdd:COG2811  11 KEAEEEADEIIEEAKEEREERIAEAREEAEEIIEQAEEEAEeeaqERLEEAREEAEAEAEEIIEEGE 77
 
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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