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Conserved domains on  [gi|2038301173|ref|XP_041431412|]
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protein CBFA2T2 isoform X1 [Xenopus laevis]

Protein Classification

zinc finger MYND domain-containing protein; PWWP and zinc finger MYND domain-containing protein( domain architecture ID 13727748)

MYND (myeloid-Nervy-DEAF-1) domain-containing protein, defined by a C6HC zinc-chelating motif, does not bind DNA, but instead mediates interactions with other proteins; PWWP and zinc finger MYND domain-containing protein

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 ...
 120-209 6.27e-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: 148.57  E-value: 6.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038301173 120 QLSKLKRFLTTLQQFGNDISPEIGEKVRTLVLALVNSTVTIEEFHCKLQEATNFPLRPFVIPFLKANLPLLQRELLHCAR 199
Cdd:pfam07531   1 NVKKCKNFLSTLIKLAGEQSPETGENVKELVQGLLNGKIEPEEFTSKLQEELNSSPQPYLVPFLKKSLPALRQELLNSAR 80

                          90
                  ....*....|
gi 2038301173 200 AAKQTPSQYL 209
Cdd:pfam07531  81 FIQQCPPQYL 90
NHR2 pfam08788
NHR2 domain like; The NHR2 (Nervy homology 2) domain is found in the ETO protein where it ...
 338-404 3.28e-30

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: 113.10  E-value: 3.28e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038301173 338 QEELVDHRLTEREWAEEWKHLDHALNCIMEMVEKTRRSMAVLRRCQEVDRDELNYWKRRFNESNEIR 404
Cdd:pfam08788   1 REEYIDTRLTDREWADEWRHLDHLLNCIMDMVEKTRRSLTVLRRCQEADREELNYWIRRYSDAEELK 67
zf-MYND pfam01753
MYND finger;
513-549 3.11e-12

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 61.28  E-value: 3.11e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2038301173 513 CWNCGRKASET--CSGCNIARYCGSFCQHKDWEKHHRIC 549
Cdd:pfam01753   1 CAVCGKEALKLlrCSRCKSVYYCSKECQKADWPYHKKEC 39
NtpE super family cl34249
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 439-501 2.13e-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


The actual alignment was detected with superfamily member COG1390:

Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 42.62  E-value: 2.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038301173 439 VTDEIWRKAEEAVNEVKRQAMSEVQKAVSEAEQKAFEMIASERARMEQTIVDAKRRAAEDAVL 501
Cdd:COG1390     7 IIEEILEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAEL 69
 
Name Accession Description Interval E-value
TAFH pfam07531
NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the ...
 120-209 6.27e-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: 148.57  E-value: 6.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038301173 120 QLSKLKRFLTTLQQFGNDISPEIGEKVRTLVLALVNSTVTIEEFHCKLQEATNFPLRPFVIPFLKANLPLLQRELLHCAR 199
Cdd:pfam07531   1 NVKKCKNFLSTLIKLAGEQSPETGENVKELVQGLLNGKIEPEEFTSKLQEELNSSPQPYLVPFLKKSLPALRQELLNSAR 80

                          90
                  ....*....|
gi 2038301173 200 AAKQTPSQYL 209
Cdd:pfam07531  81 FIQQCPPQYL 90
TAFH smart00549
TAF homology; Domain in Drosophila nervy, CBFA2T1, human TAF105, human TAF130, and Drosophila ...
 120-210 1.18e-37

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: 134.51  E-value: 1.18e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038301173  120 QLSKLKRFLTTLQQFGNDIS-PEIGEKVRTLVLALVNSTVTIEEFHCKLQEATNFPLRPFVIPFLKANLPLLQRELLHCA 198
Cdd:smart00549   1 NVSKCKRFLTTLIQLSNDISqPEVAERVRTLVLGLVNGTITAEEFTSRLQEALNSPLQPYLIPFLKNSLPLLRRELLHCA 80

                           90
                   ....*....|..
gi 2038301173  199 RAAKQTPSQYLA 210
Cdd:smart00549  81 RLIEQSPPQPLA 92
NHR2 pfam08788
NHR2 domain like; The NHR2 (Nervy homology 2) domain is found in the ETO protein where it ...
 338-404 3.28e-30

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: 113.10  E-value: 3.28e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038301173 338 QEELVDHRLTEREWAEEWKHLDHALNCIMEMVEKTRRSMAVLRRCQEVDRDELNYWKRRFNESNEIR 404
Cdd:pfam08788   1 REEYIDTRLTDREWADEWRHLDHLLNCIMDMVEKTRRSLTVLRRCQEADREELNYWIRRYSDAEELK 67
zf-MYND pfam01753
MYND finger;
513-549 3.11e-12

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 61.28  E-value: 3.11e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2038301173 513 CWNCGRKASET--CSGCNIARYCGSFCQHKDWEKHHRIC 549
Cdd:pfam01753   1 CAVCGKEALKLlrCSRCKSVYYCSKECQKADWPYHKKEC 39
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 439-501 2.13e-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: 2.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038301173 439 VTDEIWRKAEEAVNEVKRQAMSEVQKAVSEAEQKAFEMIASERARMEQTIVDAKRRAAEDAVL 501
Cdd:COG1390     7 IIEEILEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAEL 69
PRK02292 PRK02292
V-type ATP synthase subunit E; Provisional
 439-494 1.70e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 235026 [Multi-domain]  Cd Length: 188  Bit Score: 39.98  E-value: 1.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2038301173 439 VTDEIWRKAEEAVNEVKRQAMSEVQKAVSEAEQKAFEMIASERARMEQTIvDAKRR 494
Cdd:PRK02292    6 VVEDIRDEARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAEREI-EQLRE 60
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 445-503 7.73e-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: 37.03  E-value: 7.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038301173 445 RKAEEAVNEVKRQAMSEVQKAVSEAEQKAFEMIASERARMEQ----TIVDAKRRAAEDAVLVV 503
Cdd:cd06503    65 AEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIEQekekALAELRKEVADLAVEAA 127
 
Name Accession Description Interval E-value
TAFH pfam07531
NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the ...
 120-209 6.27e-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: 148.57  E-value: 6.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038301173 120 QLSKLKRFLTTLQQFGNDISPEIGEKVRTLVLALVNSTVTIEEFHCKLQEATNFPLRPFVIPFLKANLPLLQRELLHCAR 199
Cdd:pfam07531   1 NVKKCKNFLSTLIKLAGEQSPETGENVKELVQGLLNGKIEPEEFTSKLQEELNSSPQPYLVPFLKKSLPALRQELLNSAR 80

                          90
                  ....*....|
gi 2038301173 200 AAKQTPSQYL 209
Cdd:pfam07531  81 FIQQCPPQYL 90
TAFH smart00549
TAF homology; Domain in Drosophila nervy, CBFA2T1, human TAF105, human TAF130, and Drosophila ...
 120-210 1.18e-37

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: 134.51  E-value: 1.18e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038301173  120 QLSKLKRFLTTLQQFGNDIS-PEIGEKVRTLVLALVNSTVTIEEFHCKLQEATNFPLRPFVIPFLKANLPLLQRELLHCA 198
Cdd:smart00549   1 NVSKCKRFLTTLIQLSNDISqPEVAERVRTLVLGLVNGTITAEEFTSRLQEALNSPLQPYLIPFLKNSLPLLRRELLHCA 80

                           90
                   ....*....|..
gi 2038301173  199 RAAKQTPSQYLA 210
Cdd:smart00549  81 RLIEQSPPQPLA 92
NHR2 pfam08788
NHR2 domain like; The NHR2 (Nervy homology 2) domain is found in the ETO protein where it ...
 338-404 3.28e-30

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: 113.10  E-value: 3.28e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038301173 338 QEELVDHRLTEREWAEEWKHLDHALNCIMEMVEKTRRSMAVLRRCQEVDRDELNYWKRRFNESNEIR 404
Cdd:pfam08788   1 REEYIDTRLTDREWADEWRHLDHLLNCIMDMVEKTRRSLTVLRRCQEADREELNYWIRRYSDAEELK 67
zf-MYND pfam01753
MYND finger;
513-549 3.11e-12

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 61.28  E-value: 3.11e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2038301173 513 CWNCGRKASET--CSGCNIARYCGSFCQHKDWEKHHRIC 549
Cdd:pfam01753   1 CAVCGKEALKLlrCSRCKSVYYCSKECQKADWPYHKKEC 39
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 439-501 2.13e-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: 2.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038301173 439 VTDEIWRKAEEAVNEVKRQAMSEVQKAVSEAEQKAFEMIASERARMEQTIVDAKRRAAEDAVL 501
Cdd:COG1390     7 IIEEILEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAEL 69
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
444-511 2.79e-04

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 43.87  E-value: 2.79e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038301173 444 WRKAEEAVNEVKRQAMSEVQKAVSEAEQKAFEMIASERARmEQTIVDAKRRAAEDAVLVVNEQEESTE 511
Cdd:COG3064    79 LAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAE-KEKAEEAKRKAEEEAKRKAEEERKAAE 145
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 447-494 1.53e-03

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: 38.68  E-value: 1.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2038301173 447 AEEAVNEVKRQAMSEVQKAVSEAEQKAFEMI--ASERAR-MEQTIVDAKRR 494
Cdd:COG3599    74 AQETAEEVKENAEKEAELIIKEAELEAEKIIeeAQEKARkIVREIEELKRQ 124
PRK02292 PRK02292
V-type ATP synthase subunit E; Provisional
 439-494 1.70e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 235026 [Multi-domain]  Cd Length: 188  Bit Score: 39.98  E-value: 1.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2038301173 439 VTDEIWRKAEEAVNEVKRQAMSEVQKAVSEAEQKAFEMIASERARMEQTIvDAKRR 494
Cdd:PRK02292    6 VVEDIRDEARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAEREI-EQLRE 60
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 445-503 3.61e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 38.23  E-value: 3.61e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038301173 445 RKAEEAVNEVKRQAMSEVQKAVSEAEQKAFEMIASERARMEQTIVDA----KRRAAEDAVLVV 503
Cdd:COG0711    66 AEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKAlaelRAEVADLAVAIA 128
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 446-499 5.21e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 37.84  E-value: 5.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2038301173 446 KAEEAVNEVKrQAMSEVQKAVSEAEQKAFEMIASERARMEQTIVDAKRRAAEDA 499
Cdd:COG0711    42 EAERAKEEAE-AALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEA 94
PRK02292 PRK02292
V-type ATP synthase subunit E; Provisional
 448-499 5.47e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 235026 [Multi-domain]  Cd Length: 188  Bit Score: 38.44  E-value: 5.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2038301173 448 EEAVNEVKRQAMSEVQKAVSEAEQKAFEMIASERARMEQTIVDAKRRAAEDA 499
Cdd:PRK02292    4 ETVVEDIRDEARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAEREI 55
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 445-503 7.73e-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: 37.03  E-value: 7.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038301173 445 RKAEEAVNEVKRQAMSEVQKAVSEAEQKAFEMIASERARMEQ----TIVDAKRRAAEDAVLVV 503
Cdd:cd06503    65 AEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIEQekekALAELRKEVADLAVEAA 127
 
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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