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Conserved domains on  [gi|891582120|ref|XP_013022054|]
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PWWP domain-containing protein [Schizosaccharomyces cryophilus OY26]

Protein Classification

PWWP_ScIOC4-like domain-containing protein( domain architecture ID 10146972)

PWWP_ScIOC4-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PWWP_ScIOC4-like cd05840
PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...
 148-238 3.52e-33

PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar proteins; ScIOC4 functions as a component of the ISW1B complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW1B complex acts within coding regions to control the amount of RNA polymerase II released into productive elongation and to coordinate elongation with termination and pre-mRNA processing. The family also includes Schizosaccharomyces pombe PWWP domain-containing proteins 1 and 2 (SpPDP1 and SpPDP2). SpPDP1 associates with Set9 to regulate its chromatin localization and methyltransferase activity towards H4K20. Members of this family contain a PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


:

Pssm-ID: 438965  Cd Length: 94  Bit Score: 122.03  E-value: 3.52e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891582120 148 GMRVLTKLAGFPWWPSMIITEDKMTSVAL---KSKPKRAENYYPVIFFPNKEYLWASPDALCPLTEDAISEFLEKPKPKT 224
Cdd:cd05840    1 GDLVLAKVKGYPPWPAMVLPEELLPKNVLkakKRKPKSKKTVYPVQFFPDNEYYWVSPSSLKPLTKEEIDKFLSKSKRKN 80

                         90
                 ....*....|....
gi 891582120 225 AGLIKAYKVAQATK 238
Cdd:cd05840   81 KDLIEAYEVALEPP 94
PTZ00341 super family cl31759
Ring-infected erythrocyte surface antigen; Provisional
 1-120 1.76e-03

Ring-infected erythrocyte surface antigen; Provisional


The actual alignment was detected with superfamily member PTZ00341:

Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 41.31  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891582120    1 MEASSEKRQEEKAAPVEDTKEALTPVSGENPEESETKEVEDAQKES--ENDHEPQEDVEAKLEEAPEqENGASSDKQEST 78
Cdd:PTZ00341 1015 IEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENieEYDEENVEEIEENIEENIE-ENVEENVEENVE 1093

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 891582120   79 VTEEEPKENGATATEEDSktlENKQEESSPESNEDQSTEKQE 120
Cdd:PTZ00341 1094 EIEENVEENVEENAEENA---EENAEENAEEYDDENPEEHNE 1132
 
Name Accession Description Interval E-value
PWWP_ScIOC4-like cd05840
PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...
 148-238 3.52e-33

PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar proteins; ScIOC4 functions as a component of the ISW1B complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW1B complex acts within coding regions to control the amount of RNA polymerase II released into productive elongation and to coordinate elongation with termination and pre-mRNA processing. The family also includes Schizosaccharomyces pombe PWWP domain-containing proteins 1 and 2 (SpPDP1 and SpPDP2). SpPDP1 associates with Set9 to regulate its chromatin localization and methyltransferase activity towards H4K20. Members of this family contain a PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438965  Cd Length: 94  Bit Score: 122.03  E-value: 3.52e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891582120 148 GMRVLTKLAGFPWWPSMIITEDKMTSVAL---KSKPKRAENYYPVIFFPNKEYLWASPDALCPLTEDAISEFLEKPKPKT 224
Cdd:cd05840    1 GDLVLAKVKGYPPWPAMVLPEELLPKNVLkakKRKPKSKKTVYPVQFFPDNEYYWVSPSSLKPLTKEEIDKFLSKSKRKN 80

                         90
                 ....*....|....
gi 891582120 225 AGLIKAYKVAQATK 238
Cdd:cd05840   81 KDLIEAYEVALEPP 94
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 145-209 1.58e-20

domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 85.47  E-value: 1.58e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 891582120   145 YKSGMRVLTKLAGFPWWPSMIITEdKMTSVALKsKPKRAENYYPVIFFPNKEYLWASPDALCPLT 209
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISP-KMTPDNIM-KRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 148-236 3.41e-19

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyzes all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organizing higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 82.47  E-value: 3.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891582120  148 GMRVLTKLAGFPWWPSMIItEDKMTSVALKsKPKRAENYYPVIFFPNKEYLWASPDALCPLTEDAISEFLEKPKPKTAG- 226
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVV-DPEELPENVL-KPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEYLKKKKKKKKKk 78

                          90
                  ....*....|.
gi 891582120  227 -LIKAYKVAQA 236
Cdd:pfam00855  79 aFKKALEEAEE 89
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 1-120 1.76e-03

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 41.31  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891582120    1 MEASSEKRQEEKAAPVEDTKEALTPVSGENPEESETKEVEDAQKES--ENDHEPQEDVEAKLEEAPEqENGASSDKQEST 78
Cdd:PTZ00341 1015 IEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENieEYDEENVEEIEENIEENIE-ENVEENVEENVE 1093

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 891582120   79 VTEEEPKENGATATEEDSktlENKQEESSPESNEDQSTEKQE 120
Cdd:PTZ00341 1094 EIEENVEENVEENAEENA---EENAEENAEEYDDENPEEHNE 1132
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 29-122 2.90e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 40.75  E-value: 2.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891582120    29 ENPEESETKEVEDAQKESENDHEPQEDVEAKLEEAPEQEngASSDKQESTVTEEEPKENGATATEEDSKTLENKQEESSP 108
Cdd:TIGR00927  798 EGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQE--LNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEE 875

                           90
                   ....*....|....
gi 891582120   109 ESNEDQSTEKQESE 122
Cdd:TIGR00927  876 EEEEEEEEEEEEEE 889
 
Name Accession Description Interval E-value
PWWP_ScIOC4-like cd05840
PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...
 148-238 3.52e-33

PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar proteins; ScIOC4 functions as a component of the ISW1B complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW1B complex acts within coding regions to control the amount of RNA polymerase II released into productive elongation and to coordinate elongation with termination and pre-mRNA processing. The family also includes Schizosaccharomyces pombe PWWP domain-containing proteins 1 and 2 (SpPDP1 and SpPDP2). SpPDP1 associates with Set9 to regulate its chromatin localization and methyltransferase activity towards H4K20. Members of this family contain a PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438965  Cd Length: 94  Bit Score: 122.03  E-value: 3.52e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891582120 148 GMRVLTKLAGFPWWPSMIITEDKMTSVAL---KSKPKRAENYYPVIFFPNKEYLWASPDALCPLTEDAISEFLEKPKPKT 224
Cdd:cd05840    1 GDLVLAKVKGYPPWPAMVLPEELLPKNVLkakKRKPKSKKTVYPVQFFPDNEYYWVSPSSLKPLTKEEIDKFLSKSKRKN 80

                         90
                 ....*....|....
gi 891582120 225 AGLIKAYKVAQATK 238
Cdd:cd05840   81 KDLIEAYEVALEPP 94
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 145-209 1.58e-20

domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 85.47  E-value: 1.58e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 891582120   145 YKSGMRVLTKLAGFPWWPSMIITEdKMTSVALKsKPKRAENYYPVIFFPNKEYLWASPDALCPLT 209
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISP-KMTPDNIM-KRKSDENLYPVLFFGDKDTAWIPSSKLFPLT 63
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 148-236 3.41e-19

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyzes all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organizing higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 82.47  E-value: 3.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891582120  148 GMRVLTKLAGFPWWPSMIItEDKMTSVALKsKPKRAENYYPVIFFPNKEYLWASPDALCPLTEDAISEFLEKPKPKTAG- 226
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVV-DPEELPENVL-KPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEYLKKKKKKKKKk 78

                          90
                  ....*....|.
gi 891582120  227 -LIKAYKVAQA 236
Cdd:pfam00855  79 aFKKALEEAEE 89
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 148-236 6.95e-14

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.


Pssm-ID: 438958 [Multi-domain]  Cd Length: 86  Bit Score: 67.14  E-value: 6.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891582120 148 GMRVLTKLAGFPWWPSMIITEDkmtSVALKSKPKRAENYYPVIFFPNKEYLWASPDALCPLTEDAIsEFLEKPKPKTAGL 227
Cdd:cd05162    1 GDLVWAKLKGYPWWPARVVDPE---ELPEEVGKKKKKGGVLVQFFGDNDYAWVKSKNIKPFEEGFK-KEFKKKKKKSKKF 76


                 ....*....
gi 891582120 228 IKAYKVAQA 236
Cdd:cd05162   77 KKAVEEAEE 85
PWWP_HRP cd05834
PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The ...
 145-223 3.09e-06

PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The HRP family includes hepatoma-derived growth factor (HDGF), and HDGF-related proteins (HRPs). HDGF, also called high mobility group protein 1-like 2 (HMG-1L2), is a heparin-binding protein that acts as a transcriptional repressor with mitogenic activity for fibroblasts. It is a prognostic factor in several types of cancer. HDGFL1 is also called PWWP domain-containing protein 1 (PWWP1). Its biological function remains unclear. HDGFL2, also called HDGF-related protein 2 (HRP-2), or hepatoma-derived growth factor 2 (HDGF-2), is involved in cellular growth control, through the regulation of cyclin D1 expression. HDGFL3, also called HDGF-related protein 3 (HRP-3), enhances DNA synthesis and may play a role in cell proliferation. The family also includes PC4 and SFRS1-interacting protein (PSIP) and similar proteins. PSIP, also called CLL-associated antigen KW-7, dense fine speckles 70 kDa protein (DFS 70), lens epithelium-derived growth factor (LEDGF), or transcriptional coactivator p75/p52, acts as a transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Members of the HRP family contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438959 [Multi-domain]  Cd Length: 82  Bit Score: 45.24  E-value: 3.09e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 891582120 145 YKSGMRVLTKLAGFPWWPSMIiteDKMTSVALKSKPKraenyYPVIFFPNKEYLWASPDALCPLTEDAisEFLEKPKPK 223
Cdd:cd05834    1 FKPGDLVFAKVKGYPPWPARI---DEIPEGAKIPKNK-----YPVFFYGTHETAFLKPKDLFPYEENK--EKYGKPRKR 69
PWWP_BRPF cd05839
PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family; The BRPF ...
 145-212 1.02e-04

PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family; The BRPF family of proteins includes BRPF1, BRD1/BRPF2, and BRPF3. They are scaffold proteins that form monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complexes with other regulatory subunits, such as inhibitor of growth 5 (ING5) and Esa1-associated factor 6 ortholog (EAF6). BRPF proteins have multiple domains, including a plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, C2HC5HC2H, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The PHD finger binds to lysine 4 of histone H3 (K4H3), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties.


Pssm-ID: 438964  Cd Length: 106  Bit Score: 41.87  E-value: 1.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 891582120 145 YKSGMRVLTKLAGFPWWPSMIITEDKMTS--------VALKSKPKRAENYYPVIFFPNKE-YLWASPDALCPLTEDA 212
Cdd:cd05839    1 LEPGDLVWAKCRGYPWYPAEIVDPKDPKEgngvpipvPPDRVLKKSNEKLYLVLFFDAKRtWGWLPRNKLRPLGVDE 77
PWWP_HDGFL3 cd20150
PWWP domain found in Hepatoma-derived growth factor-related protein 3 (HDGFL3); HDGFL3, also ...
 144-210 1.45e-04

PWWP domain found in Hepatoma-derived growth factor-related protein 3 (HDGFL3); HDGFL3, also called HDGF-related protein 3 (HRP-3), is the only hepatoma-derived growth factor (HDGF)-related protein (HRP) family member whose expression is almost restricted to the nervous tissue. It enhances DNA synthesis and may play a role in cell proliferation. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438978 [Multi-domain]  Cd Length: 93  Bit Score: 40.82  E-value: 1.45e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 891582120 144 EYKSGMRVLTKLAGFPWWPSMIiteDKMTSVALKSkpkrAENYYPVIFFPNKEYLWASPDALCPLTE 210
Cdd:cd20150    5 EYKAGDLVFAKMKGYPHWPARI---DELPEGAVKP----PANKYPIFFFGTHETAFLGPKDLFPYKE 64
PWWP_HULK cd20147
PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family ...
 151-226 3.36e-04

PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family includes HUA2-like proteins 1-3 (HULK1-3), which are probable transcription factors that act with partial redundancy with each other. They may play diverse and essential roles in the control of plant development, physiology and flowering time. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438975 [Multi-domain]  Cd Length: 92  Bit Score: 39.78  E-value: 3.36e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 891582120 151 VLTKLAGFPWWPSMIitedkmtSVALKSKPKRAENYYPVIFFPNKEYLWASPDALCPLTEDAISEFLEKPKPKTAG 226
Cdd:cd20147    4 VLAKVKGFPAWPAQV-------SEPEDWGSAPDPKKVFVHFFGTQQIGFCNPGELSEFTEEIKQSLLARTLKKKKG 72
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 145-223 5.27e-04

PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called 3-hydroxyisobutyrate dehydrogenase-like protein, cytokine-like nuclear factor N-PAC, nuclear protein NP60, or nuclear protein of 60 kDa, is a putative oxidoreductase that is recruited on chromatin and promotes KDM1B demethylase activity. It recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3). GLYR1 enhances the activity of MAP2K4 and MAP2K6 kinases to phosphorylate p38-alpha. In addition to the PWWP domain, GLYR1 also contains an AT-hook and a C-terminal NAD-binding domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438961 [Multi-domain]  Cd Length: 86  Bit Score: 39.12  E-value: 5.27e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 891582120 145 YKSGMRVLTKLAGFPWWPSMIITEDKmtsvALKSKPKRAENYYpVIFFPNKEYLWASPDALCPLTEDAiSEFLEKPKPK 223
Cdd:cd05836    1 FKIGDLVWAKMKGFPPWPGKIVNPPP----DLKKPPRKKKMHC-VYFFGSENYAWIEDENIKPYEEFK-EEMLKSKKSA 73
PWWP_HDGF cd20148
PWWP domain found in Hepatoma-derived growth factor (HDGF); HDGF, also called high mobility ...
 145-210 1.43e-03

PWWP domain found in Hepatoma-derived growth factor (HDGF); HDGF, also called high mobility group protein 1-like 2 (HMG-1L2), is a heparin-binding protein that acts as a transcriptional repressor with mitogenic activity for fibroblasts. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438976 [Multi-domain]  Cd Length: 87  Bit Score: 38.08  E-value: 1.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 891582120 145 YKSGMRVLTKLAGFPWWPSMIiteDKMTSVALKSkpkrAENYYPVIFFPNKEYLWASPDALCPLTE 210
Cdd:cd20148    1 YKCGDLVFAKMKGYPHWPARI---DEMPEAAVKS----TANKYQVFFFGTHETAFLGPKDLFPYEE 59
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 1-120 1.76e-03

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 41.31  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891582120    1 MEASSEKRQEEKAAPVEDTKEALTPVSGENPEESETKEVEDAQKES--ENDHEPQEDVEAKLEEAPEqENGASSDKQEST 78
Cdd:PTZ00341 1015 IEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEENieEYDEENVEEIEENIEENIE-ENVEENVEENVE 1093

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 891582120   79 VTEEEPKENGATATEEDSktlENKQEESSPESNEDQSTEKQE 120
Cdd:PTZ00341 1094 EIEENVEENVEENAEENA---EENAEENAEEYDDENPEEHNE 1132
PWWP_HDGFL2 cd20149
PWWP domain found in Hepatoma-derived growth factor-related protein 2 (HDGFL2); HDGFL2, also ...
 145-207 2.03e-03

PWWP domain found in Hepatoma-derived growth factor-related protein 2 (HDGFL2); HDGFL2, also called HDGF-related protein 2 (HRP-2), or Hepatoma-derived growth factor 2 (HDGF-2), is involved in cellular growth control, through the regulation of cyclin D1 expression. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438977 [Multi-domain]  Cd Length: 84  Bit Score: 37.57  E-value: 2.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 891582120 145 YKSGMRVLTKLAGFPWWPSMIiteDKMTSVALKSKPkraeNYYPVIFFPNKEYLWASPDALCP 207
Cdd:cd20149    1 FKPGDLVFAKMKGYPHWPARI---DDIADGAVKPPP----NKYPIFFFGTHETAFLGPKDLFP 56
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 29-122 2.90e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 40.75  E-value: 2.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891582120    29 ENPEESETKEVEDAQKESENDHEPQEDVEAKLEEAPEQEngASSDKQESTVTEEEPKENGATATEEDSKTLENKQEESSP 108
Cdd:TIGR00927  798 EGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQE--LNAENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEE 875

                           90
                   ....*....|....
gi 891582120   109 ESNEDQSTEKQESE 122
Cdd:TIGR00927  876 EEEEEEEEEEEEEE 889
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 3-144 3.85e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 40.36  E-value: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891582120     3 ASSEKRQEEKAAPVEDTKEAltpvSGENPEESETKEVEDAQKESENDHEPQEDVEAKLE-------EAPEQENGASSDKQ 75
Cdd:TIGR00927  636 AEAEHTGERTGEEGERPTEA----EGENGEESGGEAEQEGETETKGENESEGEIPAERKgeqegegEIEAKEADHKGETE 711

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 891582120    76 ESTVTEEEPKENGATATEEDSKTLENKQEESSPESNEDQSTEKQESEGTAKSAAKNAAKQKSGEKQNVE 144
Cdd:TIGR00927  712 AEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDE 780
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 1-113 5.72e-03

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 39.77  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891582120    1 MEASSEKRQEEKAAPVEDTKEALTPVSGENPEESETKEVED--AQKESENDHEPQEDVEAKLEEAPEQENGASSDKQEST 78
Cdd:PTZ00341 1019 VEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEENIEEniEEYDEENVEEIEENIEENIEENVEENVEENVEEIEEN 1098

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 891582120   79 VtEEEPKENGATATEEDS-KTLENKQEESSPESNED 113
Cdd:PTZ00341 1099 V-EENVEENAEENAEENAeENAEEYDDENPEEHNEE 1133
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 9-117 9.99e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 38.81  E-value: 9.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891582120   9 QEEKAAPVEDTKEALTPVSGENPEESETKEVEDAQKESENDHEPQEDVEAKLEEAPEQENGA---SSDKQESTVTEEEPK 85
Cdd:PRK13108 320 PGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQVADRDGESTPAVEETSEADIEREQPGDLAGqapAAHQVDAEAASAAPE 399

                         90       100       110
                 ....*....|....*....|....*....|..
gi 891582120  86 ENGATATEEDSKTLENKQEESSPESNEDQSTE 117
Cdd:PRK13108 400 EPAALASEAHDETEPEVPEKAAPIPDPAKPDE 431
 
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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