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Conserved domains on  [gi|1386806265|ref|NP_001349948|]
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MYND-type zinc finger-containing chromatin reader ZMYND8 isoform 8 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF3544 pfam12064
Protein kinase C-binding protein 1; This is a domain found predominantly in eukaryotes and ...
 111-311 5.90e-77

Protein kinase C-binding protein 1; This is a domain found predominantly in eukaryotes and associated with pfam00628 pfam01753 pfam00439 pfam00855. Family members include protein kinase C-binding protein 1 (also known as ZMYND8) which acts as a transcriptional corepressor of the H3K4 demethylase JARID1D. ZMYND8 (zinc finger and MYND [myeloid, Nervy, and DEAF-1] domain containing 8) binds acetylated damaged chromatin, including actively transcribed regions, as a means of recruiting the nucleosome remodeling and histone deacetylation (NuRD) chromatin remodeling complex for transcriptional repression and DNA double-strand break (DSB) repair by homologous recombination (HR).


:

Pssm-ID: 463452  Cd Length: 195  Bit Score: 248.67  E-value: 5.90e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806265 111 RRISLSDMPRSPTSTNSSVHTGSDVEQDP----EKKAPSSHFSASEESMDFldksTASPASTKtgqAGSLSGSPKPFSPQ 186
Cdd:pfam12064   1 RRISLTDMPRSPMSTNSSAHTGSDGEQDTaekgQAKAPSSHYSTGEESMDC----TASPASPK---AGSSLDSPKPFHSQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806265 187 APTPimTKPDKTSTstTGSILNLNLDRSKAEMDLKELSESVQQ-QSAPVPLISPKRQIRSRFQLNLDKTIESCKAQLGIN 265
Cdd:pfam12064  74 APGT--PKQEKTPT--TGSILNLNLDRSKAEMDLKELSETVQQqQGATVVLTSPKRQIRSRFQLNLDKTIESCKAQLGID 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1386806265 266 EISEDVYTAVEHSDSEDSEKSESSDSEYVSDEEQKPKNEPEDPEDK 311
Cdd:pfam12064 150 EISVDVYKGVEHSDSEDSDKSDSSDSEYASDEEQKPKNSQDDASDK 195
PWWP super family cl02554
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 3-51 4.97e-21

PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids and is composed of a five-stranded antiparallel beta-barrel followed by a helical region. It is found in numerous proteins that are involved in cell division, growth, and differentiation. Most PWWP-domain proteins seem to be nuclear, often DNA-binding, proteins that function as transcription factors regulating a variety of developmental processes. PWWP domains specifically recognize DNA and histone methylated lysines at the level of the nucleosome. Based on the fact that other regions of PWWP-domain proteins are responsible for nuclear localization and DNA-binding, is likely that the PWWP domain acts as a site for protein-protein binding interactions, influencing chromatin remodeling and thereby regulating transcriptional processes. Some PWWP-domain proteins have been linked to cancer or other diseases; some are known to function as growth factors.


The actual alignment was detected with superfamily member cd20160:

Pssm-ID: 470613  Cd Length: 91  Bit Score: 88.39  E-value: 4.97e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1386806265   3 AWVPVNNCYLMSKEIPFSVKKTKSIFNSAMQEMEVYVENIRRKFGVFNY 51
Cdd:cd20160    43 AWVPVKDCYLYSKEPPTSVKKKKSGLDEAMEELEIHIEKLREKFGKFNY 91
zf-MYND pfam01753
MYND finger;
729-763 9.24e-09

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 51.65  E-value: 9.24e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1386806265 729 CANCKKEA--IFYC--CWNTSYCDYPCQQAHWPEHMKSC 763
Cdd:pfam01753   1 CAVCGKEAlkLLRCsrCKSVYYCSKECQKADWPYHKKEC 39
AtpF super family cl34015
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 658-725 9.20e-05

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


The actual alignment was detected with superfamily member COG0711:

Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 43.62  E-value: 9.20e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386806265 658 IAEIRRLRIEIEKLQWLHQQELAEMKH-----------NLELTMAEMRQSLEQERDRLIAEVKKQLELEKQQAVDETKK 725
Cdd:COG0711    40 LAEAERAKEEAEAALAEYEEKLAEARAeaaeiiaearkEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRA 118
PHA03264 super family cl42984
envelope glycoprotein D; Provisional
 350-454 7.93e-03

envelope glycoprotein D; Provisional


The actual alignment was detected with superfamily member PHA03264:

Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 39.60  E-value: 7.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806265 350 DPTPAKDKASPEPEKDFVEKAKPSPHPTKDKLKGKDETDSPTVHLGLDSDSESElvidlGEdPSGREGRKNkKDPKVPS- 428
Cdd:PHA03264  265 EPPPAPSGGSPAPPGDDRPEAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAG-----GE-PKPGPPRPA-PDADRPEg 337

                          90       100
                  ....*....|....*....|....*..
gi 1386806265 429 -PKQDAIGKPPPSSTSAGnqSPPETPV 454
Cdd:PHA03264  338 wPSLEAITFPPPTPATPA--VPRARPV 362
 
Name Accession Description Interval E-value
DUF3544 pfam12064
Protein kinase C-binding protein 1; This is a domain found predominantly in eukaryotes and ...
 111-311 5.90e-77

Protein kinase C-binding protein 1; This is a domain found predominantly in eukaryotes and associated with pfam00628 pfam01753 pfam00439 pfam00855. Family members include protein kinase C-binding protein 1 (also known as ZMYND8) which acts as a transcriptional corepressor of the H3K4 demethylase JARID1D. ZMYND8 (zinc finger and MYND [myeloid, Nervy, and DEAF-1] domain containing 8) binds acetylated damaged chromatin, including actively transcribed regions, as a means of recruiting the nucleosome remodeling and histone deacetylation (NuRD) chromatin remodeling complex for transcriptional repression and DNA double-strand break (DSB) repair by homologous recombination (HR).


Pssm-ID: 463452  Cd Length: 195  Bit Score: 248.67  E-value: 5.90e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806265 111 RRISLSDMPRSPTSTNSSVHTGSDVEQDP----EKKAPSSHFSASEESMDFldksTASPASTKtgqAGSLSGSPKPFSPQ 186
Cdd:pfam12064   1 RRISLTDMPRSPMSTNSSAHTGSDGEQDTaekgQAKAPSSHYSTGEESMDC----TASPASPK---AGSSLDSPKPFHSQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806265 187 APTPimTKPDKTSTstTGSILNLNLDRSKAEMDLKELSESVQQ-QSAPVPLISPKRQIRSRFQLNLDKTIESCKAQLGIN 265
Cdd:pfam12064  74 APGT--PKQEKTPT--TGSILNLNLDRSKAEMDLKELSETVQQqQGATVVLTSPKRQIRSRFQLNLDKTIESCKAQLGID 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1386806265 266 EISEDVYTAVEHSDSEDSEKSESSDSEYVSDEEQKPKNEPEDPEDK 311
Cdd:pfam12064 150 EISVDVYKGVEHSDSEDSDKSDSSDSEYASDEEQKPKNSQDDASDK 195
PWWP_PRKCBP1 cd20160
PWWP domain found in protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; ...
 3-51 4.97e-21

PWWP domain found in protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; PRKCBP1, also called cutaneous T-cell lymphoma-associated antigen se14-3 (CTCL-associated antigen se14-3), Rack7, or zinc finger MYND domain-containing protein 8 (ZMYND8), is a novel receptor for activated C-kinase (RACK)-like protein that may play an important role in the activation and regulation of PKC-beta I, and the PKC signaling cascade. It also has been identified as a formin homology-2-domain containing protein 1 (FHOD1)-binding protein that may be involved in FHOD1-regulated actin polymerization and transcription. Moreover, PRKCBP1 may function as a REST co-repressor 2 (RCOR2) interacting factor. They form a RCOR2/ZMYND8 complex which might be involved in the regulation of neural differentiation. PRKCBP1 contains a plant homeodomain (PHD) finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438988  Cd Length: 91  Bit Score: 88.39  E-value: 4.97e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1386806265   3 AWVPVNNCYLMSKEIPFSVKKTKSIFNSAMQEMEVYVENIRRKFGVFNY 51
Cdd:cd20160    43 AWVPVKDCYLYSKEPPTSVKKKKSGLDEAMEELEIHIEKLREKFGKFNY 91
zf-MYND pfam01753
MYND finger;
729-763 9.24e-09

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 51.65  E-value: 9.24e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1386806265 729 CANCKKEA--IFYC--CWNTSYCDYPCQQAHWPEHMKSC 763
Cdd:pfam01753   1 CAVCGKEAlkLLRCsrCKSVYYCSKECQKADWPYHKKEC 39
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 658-725 9.20e-05

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: 43.62  E-value: 9.20e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386806265 658 IAEIRRLRIEIEKLQWLHQQELAEMKH-----------NLELTMAEMRQSLEQERDRLIAEVKKQLELEKQQAVDETKK 725
Cdd:COG0711    40 LAEAERAKEEAEAALAEYEEKLAEARAeaaeiiaearkEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRA 118
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 656-725 4.81e-04

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: 40.88  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806265 656 STIAEIRRLRIEIEKLQWLHQQELAE-----------MKHNLELTMAEMRQSLEQERDRLIAEVKKQLELEKQQAVDETK 724
Cdd:cd06503    37 ESLEEAEKAKEEAEELLAEYEEKLAEaraeaqeiieeARKEAEKIKEEILAEAKEEAERILEQAKAEIEQEKEKALAELR 116


                  .
gi 1386806265 725 K 725
Cdd:cd06503   117 K 117
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 657-726 1.09e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 40.53  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806265 657 TIAEIRRLRIEIEKLQWLHQQELAEMKH-----------NLELTMAEMRQSLEQERDRLIAEVKKQLELEKQQAVDETKK 725
Cdd:PRK05759   43 GLAAAERAKKELELAQAKYEAQLAEARAeaaeiieqakkRAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRK 122


                  .
gi 1386806265 726 K 726
Cdd:PRK05759  123 Q 123
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 350-454 7.93e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 39.60  E-value: 7.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806265 350 DPTPAKDKASPEPEKDFVEKAKPSPHPTKDKLKGKDETDSPTVHLGLDSDSESElvidlGEdPSGREGRKNkKDPKVPS- 428
Cdd:PHA03264  265 EPPPAPSGGSPAPPGDDRPEAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAG-----GE-PKPGPPRPA-PDADRPEg 337

                          90       100
                  ....*....|....*....|....*..
gi 1386806265 429 -PKQDAIGKPPPSSTSAGnqSPPETPV 454
Cdd:PHA03264  338 wPSLEAITFPPPTPATPA--VPRARPV 362
 
Name Accession Description Interval E-value
DUF3544 pfam12064
Protein kinase C-binding protein 1; This is a domain found predominantly in eukaryotes and ...
 111-311 5.90e-77

Protein kinase C-binding protein 1; This is a domain found predominantly in eukaryotes and associated with pfam00628 pfam01753 pfam00439 pfam00855. Family members include protein kinase C-binding protein 1 (also known as ZMYND8) which acts as a transcriptional corepressor of the H3K4 demethylase JARID1D. ZMYND8 (zinc finger and MYND [myeloid, Nervy, and DEAF-1] domain containing 8) binds acetylated damaged chromatin, including actively transcribed regions, as a means of recruiting the nucleosome remodeling and histone deacetylation (NuRD) chromatin remodeling complex for transcriptional repression and DNA double-strand break (DSB) repair by homologous recombination (HR).


Pssm-ID: 463452  Cd Length: 195  Bit Score: 248.67  E-value: 5.90e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806265 111 RRISLSDMPRSPTSTNSSVHTGSDVEQDP----EKKAPSSHFSASEESMDFldksTASPASTKtgqAGSLSGSPKPFSPQ 186
Cdd:pfam12064   1 RRISLTDMPRSPMSTNSSAHTGSDGEQDTaekgQAKAPSSHYSTGEESMDC----TASPASPK---AGSSLDSPKPFHSQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806265 187 APTPimTKPDKTSTstTGSILNLNLDRSKAEMDLKELSESVQQ-QSAPVPLISPKRQIRSRFQLNLDKTIESCKAQLGIN 265
Cdd:pfam12064  74 APGT--PKQEKTPT--TGSILNLNLDRSKAEMDLKELSETVQQqQGATVVLTSPKRQIRSRFQLNLDKTIESCKAQLGID 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1386806265 266 EISEDVYTAVEHSDSEDSEKSESSDSEYVSDEEQKPKNEPEDPEDK 311
Cdd:pfam12064 150 EISVDVYKGVEHSDSEDSDKSDSSDSEYASDEEQKPKNSQDDASDK 195
PWWP_PRKCBP1 cd20160
PWWP domain found in protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; ...
 3-51 4.97e-21

PWWP domain found in protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; PRKCBP1, also called cutaneous T-cell lymphoma-associated antigen se14-3 (CTCL-associated antigen se14-3), Rack7, or zinc finger MYND domain-containing protein 8 (ZMYND8), is a novel receptor for activated C-kinase (RACK)-like protein that may play an important role in the activation and regulation of PKC-beta I, and the PKC signaling cascade. It also has been identified as a formin homology-2-domain containing protein 1 (FHOD1)-binding protein that may be involved in FHOD1-regulated actin polymerization and transcription. Moreover, PRKCBP1 may function as a REST co-repressor 2 (RCOR2) interacting factor. They form a RCOR2/ZMYND8 complex which might be involved in the regulation of neural differentiation. PRKCBP1 contains a plant homeodomain (PHD) finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438988  Cd Length: 91  Bit Score: 88.39  E-value: 4.97e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1386806265   3 AWVPVNNCYLMSKEIPFSVKKTKSIFNSAMQEMEVYVENIRRKFGVFNY 51
Cdd:cd20160    43 AWVPVKDCYLYSKEPPTSVKKKKSGLDEAMEELEIHIEKLREKFGKFNY 91
PWWP_BS69-like cd05841
PWWP domain found in protein BS69, protein kinase C-binding protein 1 (PRKCBP1) and similar ...
 2-44 2.09e-10

PWWP domain found in protein BS69, protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; Protein BS69, also called zinc finger MYND domain-containing protein 11 (ZMYND11 or ZMY11), is a ubiquitously expressed nuclear protein acting as a transcriptional co-repressor in association with various transcription factors. It was originally identified as an adenovirus 5 E1A-binding protein that inhibits E1A transactivation, as well as c-Myb transcription. BS69 is a multi-domain protein, containing bromo, plant homeodomain (PHD), proline-tryptophan-tryptophan-proline (PWWP), and MYeloid translocation protein 8, Nervy and DEAF-1 (MYND) domains. The specific role of the PWWP domain within BS69 is not clearly identified, but BS69 functions in chromatin remodeling, consistent with other PWWP-containing proteins. PRKCBP1, also called cutaneous T-cell lymphoma-associated antigen se14-3 (CTCL-associated antigen se14-3), Rack7, or zinc finger MYND domain-containing protein 8 (ZMYND8), is a novel receptor for activated C-kinase (RACK)-like protein that may play an important role in the activation and regulation of PKC-beta I, and the PKC signaling cascade. It also has been identified as a formin homology-2-domain containing protein 1 (FHOD1)-binding protein that may be involved in FHOD1-regulated actin polymerization and transcription. Moreover, PRKCBP1 may function as a REST co-repressor 2 (RCOR2) interacting factor. They form a RCOR2/ZMYND8 complex which might be involved in the regulation of neural differentiation. PRKCBP1 contains a PHD finger, a bromodomain, and a PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438966  Cd Length: 89  Bit Score: 57.79  E-value: 2.09e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1386806265   2 TAWVPVNNCYLMSKEIP-----FSVKKTKSIFNSAMQEMEVYVENIRR 44
Cdd:cd05841    42 RAWLPSKNVTLHTREIVstlpdSSESKDKRTLKKAIKELERHIALLRQ 89
zf-MYND pfam01753
MYND finger;
729-763 9.24e-09

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 51.65  E-value: 9.24e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1386806265 729 CANCKKEA--IFYC--CWNTSYCDYPCQQAHWPEHMKSC 763
Cdd:pfam01753   1 CAVCGKEAlkLLRCsrCKSVYYCSKECQKADWPYHKKEC 39
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 658-725 9.20e-05

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: 43.62  E-value: 9.20e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386806265 658 IAEIRRLRIEIEKLQWLHQQELAEMKH-----------NLELTMAEMRQSLEQERDRLIAEVKKQLELEKQQAVDETKK 725
Cdd:COG0711    40 LAEAERAKEEAEAALAEYEEKLAEARAeaaeiiaearkEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRA 118
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 656-725 4.81e-04

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: 40.88  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806265 656 STIAEIRRLRIEIEKLQWLHQQELAE-----------MKHNLELTMAEMRQSLEQERDRLIAEVKKQLELEKQQAVDETK 724
Cdd:cd06503    37 ESLEEAEKAKEEAEELLAEYEEKLAEaraeaqeiieeARKEAEKIKEEILAEAKEEAERILEQAKAEIEQEKEKALAELR 116


                  .
gi 1386806265 725 K 725
Cdd:cd06503   117 K 117
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 657-726 1.09e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 40.53  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806265 657 TIAEIRRLRIEIEKLQWLHQQELAEMKH-----------NLELTMAEMRQSLEQERDRLIAEVKKQLELEKQQAVDETKK 725
Cdd:PRK05759   43 GLAAAERAKKELELAQAKYEAQLAEARAeaaeiieqakkRAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRK 122


                  .
gi 1386806265 726 K 726
Cdd:PRK05759  123 Q 123
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 350-454 7.93e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 39.60  E-value: 7.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386806265 350 DPTPAKDKASPEPEKDFVEKAKPSPHPTKDKLKGKDETDSPTVHLGLDSDSESElvidlGEdPSGREGRKNkKDPKVPS- 428
Cdd:PHA03264  265 EPPPAPSGGSPAPPGDDRPEAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAG-----GE-PKPGPPRPA-PDADRPEg 337

                          90       100
                  ....*....|....*....|....*..
gi 1386806265 429 -PKQDAIGKPPPSSTSAGnqSPPETPV 454
Cdd:PHA03264  338 wPSLEAITFPPPTPATPA--VPRARPV 362
 
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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