NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|109287753|dbj|BAE96297|]
View 

bHLH-HALZ myc like protein [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
bHLH_AtILR3_like cd11446
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein IAA-leucine ...
97-172 2.39e-40

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein IAA-leucine resistant 3 (ILR3) and similar proteins; ILR3, also termed AtbHLH105, or EN 133, is a bHLH transcription factor that plays a role in resistance to amide-linked indole-3-acetic acid (IAA) conjugates such as IAA-Leu and IAA-Phe. It may regulate gene expression in response to metal homeostasis changes.


:

Pssm-ID: 381452 [Multi-domain]  Cd Length: 76  Bit Score: 134.00  E-value: 2.39e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109287753  97 KACREKVRRDKLNERFLELGAVLEPGKTPKMDKSSILNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELR 172
Cdd:cd11446    1 KACREKLRRDKLNERFMELSNVLEPGRPPKTDKATILGDAIRMLKQLRGEVQKLKEENSSLQEESKELKAEKNELR 76
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
138-228 2.95e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 138 RVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNARPSfvPHPPVIPASAFTAPQGqa 217
Cdd:COG4942  178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA--AAAERTPAAGFAALKG-- 253
                         90
                 ....*....|.
gi 109287753 218 agqKLMMPVIG 228
Cdd:COG4942  254 ---KLPWPVSG 261
 
Name Accession Description Interval E-value
bHLH_AtILR3_like cd11446
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein IAA-leucine ...
97-172 2.39e-40

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein IAA-leucine resistant 3 (ILR3) and similar proteins; ILR3, also termed AtbHLH105, or EN 133, is a bHLH transcription factor that plays a role in resistance to amide-linked indole-3-acetic acid (IAA) conjugates such as IAA-Leu and IAA-Phe. It may regulate gene expression in response to metal homeostasis changes.


Pssm-ID: 381452 [Multi-domain]  Cd Length: 76  Bit Score: 134.00  E-value: 2.39e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109287753  97 KACREKVRRDKLNERFLELGAVLEPGKTPKMDKSSILNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELR 172
Cdd:cd11446    1 KACREKLRRDKLNERFMELSNVLEPGRPPKTDKATILGDAIRMLKQLRGEVQKLKEENSSLQEESKELKAEKNELR 76
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
136-195 1.72e-09

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 53.05  E-value: 1.72e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 136 AIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:COG3074   16 AVDTIELLQMEVEELKEKNEELEQENEELQSENEELQSENEQLKTENAEWQERIRSLLGK 75
HLH smart00353
helix loop helix domain;
100-149 8.06e-09

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 50.68  E-value: 8.06e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 109287753   100 REKVRRDKLNERFLELGAVLEPG-KTPKMDKSSILNDAIRVMAELRSEAQK 149
Cdd:smart00353   3 RERRRRRKINEAFDELRSLLPTLpKNKKLSKAEILRLAIEYIKSLQEELQK 53
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
142-193 5.77e-07

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.02  E-value: 5.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 109287753  142 ELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLN 193
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
HLH pfam00010
Helix-loop-helix DNA-binding domain;
93-144 2.02e-06

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 43.99  E-value: 2.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 109287753   93 RPSSKACREKVRRDKLNERFLELGAVLePGKTP--KMDKSSILNDAIRVMAELR 144
Cdd:pfam00010   1 RREAHNERERRRRDRINDAFDELRELL-PTLPPdkKLSKAEILRLAIEYIKHLQ 53
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
138-228 2.95e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 138 RVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNARPSfvPHPPVIPASAFTAPQGqa 217
Cdd:COG4942  178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA--AAAERTPAAGFAALKG-- 253
                         90
                 ....*....|.
gi 109287753 218 agqKLMMPVIG 228
Cdd:COG4942  254 ---KLPWPVSG 261
DUF4140 pfam13600
N-terminal domain of unknown function (DUF4140); This family is often found at the N-terminus ...
158-192 8.78e-06

N-terminal domain of unknown function (DUF4140); This family is often found at the N-terminus of its member proteins, with DUF4139, pfam13598, at the C-terminus.


Pssm-ID: 463931 [Multi-domain]  Cd Length: 99  Bit Score: 43.36  E-value: 8.78e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 109287753  158 QEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFL 192
Cdd:pfam13600  65 DPELKALRAELEELEDELARLEDELAALEARLAFL 99
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
96-194 1.32e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753  96 SKACREKVRRDKLNERFLELGAVLEPGKTpkmdKSSILNDAIRVMAELRSEAQKLK-ESNESLQEKIKELKAEKNELRDE 174
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEE----RHELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEE 406
                         90       100
                 ....*....|....*....|
gi 109287753 175 KQKLKAEKESLEQQIKFLNA 194
Cdd:PRK03918 407 ISKITARIGELKKEIKELKK 426
 
Name Accession Description Interval E-value
bHLH_AtILR3_like cd11446
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein IAA-leucine ...
97-172 2.39e-40

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein IAA-leucine resistant 3 (ILR3) and similar proteins; ILR3, also termed AtbHLH105, or EN 133, is a bHLH transcription factor that plays a role in resistance to amide-linked indole-3-acetic acid (IAA) conjugates such as IAA-Leu and IAA-Phe. It may regulate gene expression in response to metal homeostasis changes.


Pssm-ID: 381452 [Multi-domain]  Cd Length: 76  Bit Score: 134.00  E-value: 2.39e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109287753  97 KACREKVRRDKLNERFLELGAVLEPGKTPKMDKSSILNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELR 172
Cdd:cd11446    1 KACREKLRRDKLNERFMELSNVLEPGRPPKTDKATILGDAIRMLKQLRGEVQKLKEENSSLQEESKELKAEKNELR 76
bHLH_AtbHLH_like cd11393
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana genes coding transcription ...
100-150 4.03e-11

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana genes coding transcription factors and similar proteins; bHLH proteins are the second largest class of plant transcription factors that regulate transcription of genes that are involve in many essential physiological and developmental process. bHLH proteins are transcriptional regulators that are found in organisms from yeast to humans. The Arabidopsis bHLH proteins that have been characterized so far have roles in regulation of fruit dehiscence, cell development (carpel, anther and epidermal), phytochrome signaling, flavonoid biosynthesis, hormone signaling and stress responses.


Pssm-ID: 381399 [Multi-domain]  Cd Length: 53  Bit Score: 56.81  E-value: 4.03e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 109287753 100 REKVRRDKLNERFLELGAVLEPGKtpKMDKSSILNDAIRVMAELRSEAQKL 150
Cdd:cd11393    4 AERKRREKINERIRALRSLVPNGG--KTDKASILDEAIEYIKFLQEQVKVL 52
bHLH_AtAIB_like cd11449
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein ABA-INDUCIBLE ...
101-167 2.52e-10

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein ABA-INDUCIBLE bHLH-TYPE (AIB) and similar proteins; The family includes several bHLH transcription factors from Arabidopsis thaliana, such as AIB and MYC proteins (MYC2, MYC3 and MYC4). AIB, also termed AtbHLH17, or EN 35, is a transcription activator that regulates positively abscisic acid (ABA) response. MYC2, also termed protein jasmonate insensitive 1, or R-homologous Arabidopsis protein 1 (RAP-1), or AtbHLH6, or EN 38, or Z-box binding factor 1 protein, is a transcriptional activator involved in abscisic acid (ABA), jasmonic acid (JA), and light signaling pathways. MYC3, also termed protein altered tryptophan regulation 2, or AtbHLH5, or transcription factor ATR2, or EN 36, is a transcription factor involved in tryptophan, jasmonic acid (JA) and other stress-responsive gene regulation. MYC4, also termed AtbHLH4, or EN 37, is a transcription factor involved in jasmonic acid (JA) gene regulation. MYC2, together with MYC3 and MYC4, controls additively subsets of JA-dependent responses.


Pssm-ID: 381455 [Multi-domain]  Cd Length: 78  Bit Score: 55.48  E-value: 2.52e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109287753 101 EKVRRDKLNERFLELGAVLEpgKTPKMDKSSILNDAIRVMAELRSEAQKLKESNESLQEKIKELKAE 167
Cdd:cd11449   13 ERQRREKLNQRFYALRAVVP--NVSKMDKASLLGDAISYINELKSKVQDMETEKKEMKRQESEKKTE 77
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
136-195 1.72e-09

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 53.05  E-value: 1.72e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 136 AIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:COG3074   16 AVDTIELLQMEVEELKEKNEELEQENEELQSENEELQSENEQLKTENAEWQERIRSLLGK 75
bHLH_AtNAI1_like cd11452
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein NAI1 and similar ...
101-182 2.14e-09

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein NAI1 and similar proteins; NAI1, also termed AtbHLH20, or EN 27, is a bHLH transcription activator that regulates the expression of at least NAI2, PYK10 and PBP1. It is required for and mediates the formation of endoplasmic reticulum bodies (ER bodies). It plays a role in the symbiotic interactions with the endophytes of the Sebacinaceae fungus family, such as Piriformospora indica and Sebacina.


Pssm-ID: 381458 [Multi-domain]  Cd Length: 75  Bit Score: 52.85  E-value: 2.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 101 EKVRRDKLNERFLELGAVLePGkTPKMDKSSILNDAIRVMaelrseaqklkesnESLQEKIKELKAEKNELRDEKQKLKA 180
Cdd:cd11452   10 ERKRREKLSQRFIALSALV-PG-LKKMDKASVLGDAIKHI--------------KQLQERVKELEEEKKEKRLMSVVIVK 73

                 ..
gi 109287753 181 EK 182
Cdd:cd11452   74 KS 75
bHLH_SF cd00083
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
101-145 4.55e-09

basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators that are found in organisms from yeast to humans. Members of the bHLH superfamily have two highly conserved and functionally distinct regions. The basic part is at the amino end of the bHLH that may bind DNA to a consensus hexanucleotide sequence known as the E box (CANNTG). Different families of bHLH proteins recognize different E-box consensus sequences. At the carboxyl-terminal end of the region is the HLH region that interacts with other proteins to form homo- and heterodimers. bHLH proteins function as a diverse set of regulatory factors because they recognize different DNA sequences and dimerize with different proteins. The bHLH proteins can be divided to cell-type specific and widely expressed proteins. The cell-type specific members of bHLH superfamily are involved in cell-fate determination and act in neurogenesis, cardiogenesis, myogenesis, and hematopoiesis.


Pssm-ID: 381392 [Multi-domain]  Cd Length: 46  Bit Score: 50.98  E-value: 4.55e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 109287753 101 EKVRRDKLNERFLELGAVL-EPGKTPKMDKSSILNDAIRVMAELRS 145
Cdd:cd00083    1 ERRRRDKINDAFEELKRLLpELPDSKKLSKASILQKAVEYIRELQS 46
HLH smart00353
helix loop helix domain;
100-149 8.06e-09

helix loop helix domain;


Pssm-ID: 197674 [Multi-domain]  Cd Length: 53  Bit Score: 50.68  E-value: 8.06e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 109287753   100 REKVRRDKLNERFLELGAVLEPG-KTPKMDKSSILNDAIRVMAELRSEAQK 149
Cdd:smart00353   3 RERRRRRKINEAFDELRSLLPTLpKNKKLSKAEILRLAIEYIKSLQEELQK 53
bHLH_AtAMS_like cd11443
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein aborted microspores ...
101-159 1.10e-08

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein aborted microspores (AMS) and similar proteins; The family includes several bHLH transcription factors from Arabidopsis thaliana, such as AMS, ICE1 and SCREAM2. AMS, also termed AtbHLH21, or EN 48, plays a crucial role in tapetum development and it is required for male fertility and pollen differentiation. ICE1, also termed inducer of CBF expression 1, or AtbHLH116, or EN 45, or SCREAM, acts as a transcriptional activator that regulates the cold-induced transcription of CBF/DREB1 genes. It binds specifically to the MYC recognition sites (5'-CANNTG-3') found in the CBF3/DREB1A promoter. SCREAM2, also termed AtbHLH33, or EN 44, mediates stomatal differentiation in the epidermis probably by controlling successive roles of SPCH, MUTE, and FAMA.


Pssm-ID: 381449 [Multi-domain]  Cd Length: 72  Bit Score: 50.84  E-value: 1.10e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 109287753 101 EKVRRDKLNERFLELGAVLEpgKTPKMDKSSILNDAIRVMAELRSEAQKLKESNESLQE 159
Cdd:cd11443    7 ERRRRKKLNDRLYMLRSVVP--KITKMDRASILGDAIDYVKELLQEINELQDELEGLPE 63
bHLH_AtTT8_like cd11451
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein transparent testa 8 ...
96-162 1.52e-08

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein transparent testa 8 (TT8) and similar proteins; The family includes several bHLH transcription factors from Arabidopsis thaliana, such as TT8, EGL1, and GL3. TT8, also termed AtbHLH42, or EN 32, is involved in the control of flavonoid pigmentation and plays a key role in regulating leucoanthocyanidin reductase (BANYULS) and dihydroflavonol-4-reductase (DFR). EGL1, also termed AtbHLH2, or EN 30, or AtMYC146, or protein enhancer of GLABRA 3, is involved in epidermal cell fate specification and regulates negatively stomata formation but promotes trichome formation. GL3, also termed AtbHLH1, or AtMYC6, or protein shapeshifter, or EN 31, is involved in epidermal cell fate specification. It regulates negatively stomata formation, but, in association with TTG1 and MYB0/GL1, promotes trichome formation, branching and endoreplication.


Pssm-ID: 381457  Cd Length: 75  Bit Score: 50.50  E-value: 1.52e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109287753  96 SKACREKVRRDKLNERFLELGAVLePGKTpKMDKSSILNDAIRVMAELRSEAQKLKESNESLQEKIK 162
Cdd:cd11451    5 SHAMAERRRREKLNERFITLRSMV-PFVT-KMDKVSILGDAIEYLKQLQRRVEELESRRKSSDTETR 69
bHLHzip_MGA_like cd19682
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) ...
100-172 5.27e-08

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MAX gene-associated protein (MGA) family; The MGA family includes MGA, Schizosaccharomyces pombe ESC1 (spESC1) and similar proteins. MGA, also termed MAX dimerization protein 5 (MAD5), is a dual specificity T-box/ bHLHzip transcription factor that regulates the expression of both Max-network and T-box family target genes. It contains a Myc-like bHLHZip motif and requires heterodimerization with Max for binding to the preferred Myc-Max-binding site CACGTG. In addition to the bHLHZip domain, MGA harbors a second DNA-binding domain, the T-box or T-domain. It thus binds the preferred Brachyury-binding sequence and represses transcription of reporter genes containing promoter-proximal Brachyury-binding sites. spESC1 is a bHLHzip protein with homology to human MyoD and Myf-5 myogenic differentiation inducers. It is involved in the sexual differentiation process.


Pssm-ID: 381525 [Multi-domain]  Cd Length: 65  Bit Score: 48.81  E-value: 5.27e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109287753 100 REKVRRDKLNERFLELGAVLEPGKTPKMDKSSILNDAIRVMaelrseaqklkesnESLQEKIKELKAEKNELR 172
Cdd:cd19682    7 RERERRSELRELFDKLKQLLGLDSDEKASKLAVLTEAIEEI--------------QQLKREEDELQKEKARLT 65
bHLHzip_scCBP1 cd11398
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Saccharomyces cerevisiae ...
101-181 9.08e-08

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Saccharomyces cerevisiae centromere-binding protein 1 (CBP-1) and similar proteins; CBP-1, also termed centromere promoter factor 1 (CPF1), or centromere-binding factor 1 (CBF1), is a bHLHzip protein that is required for chromosome stability and methionine prototrophy. It binds as a homodimer to the centromere DNA elements I (CDEI, GTCACATG) region of the centromere that is required for optimal centromere function.


Pssm-ID: 381404 [Multi-domain]  Cd Length: 89  Bit Score: 48.49  E-value: 9.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 101 EKVRRDKLNERFLELGAVLePGKTPKMDKSSILNDAIRVMaelrseaQKLKESNESLQEKIKELKAEKNELRDEKQKLKA 180
Cdd:cd11398   15 ERRRRENINEGINELAALV-PGNAREKNKGAILARAVEYI-------QELQETEAKNIEKWTLEKLLTDQAIAELAALNE 86

                 .
gi 109287753 181 E 181
Cdd:cd11398   87 K 87
bHLH_AtFIT_like cd11450
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana Fe-deficiency induced ...
101-164 1.49e-07

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana Fe-deficiency induced transcription factor 1 (FIT) and similar proteins; The family includes bHLH transcription factors from Arabidopsis thaliana, such as FIT and DYT1. FIT, also termed FER-like iron deficiency-induced transcription factor, or FER-like regulator of iron uptake, or AtbHLH29, or EN 43, is a bHLH transcription factor that is required for the iron deficiency response in plant. It regulates FRO2 at the level of mRNA accumulation and IRT1 at the level of protein accumulation. DYT1, also termed AtbHLH22, or protein dysfunctional tapetum 1, or EN 49, is a bHLH transcription factor involved in the control of tapetum development. It is required for male fertility and pollen differentiation, especially during callose deposition.


Pssm-ID: 381456 [Multi-domain]  Cd Length: 76  Bit Score: 47.90  E-value: 1.49e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109287753 101 EKVRRDKLNERFLELGAVLePGKTpKMDKSSILNDAIRVMAELRSEAQKLKESNESLQEKIKEL 164
Cdd:cd11450   11 ERNRRQKLNQRLFALRSVV-PNIT-KMDKASIIKDAISYIQELQYQEKKLEAEIRELESRPPST 72
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
133-196 3.78e-07

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 49.91  E-value: 3.78e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109287753 133 LNDAIRvmaELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNARP 196
Cdd:COG1340   48 LNAQVK---ELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAG 108
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
142-193 5.77e-07

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.02  E-value: 5.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 109287753  142 ELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLN 193
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
HLH pfam00010
Helix-loop-helix DNA-binding domain;
93-144 2.02e-06

Helix-loop-helix DNA-binding domain;


Pssm-ID: 459628 [Multi-domain]  Cd Length: 53  Bit Score: 43.99  E-value: 2.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 109287753   93 RPSSKACREKVRRDKLNERFLELGAVLePGKTP--KMDKSSILNDAIRVMAELR 144
Cdd:pfam00010   1 RREAHNERERRRRDRINDAFDELRELL-PTLPPdkKLSKAEILRLAIEYIKHLQ 53
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
100-194 2.03e-06

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 2.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753   100 REKVRRDKLNERFLELGAVLEpgktpkmdkssilnDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLK 179
Cdd:TIGR02169  347 EERKRRDKLTEEYAELKEELE--------------DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
                           90
                   ....*....|....*
gi 109287753   180 AEKESLEQQIKFLNA 194
Cdd:TIGR02169  413 EELQRLSEELADLNA 427
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
141-195 2.29e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.90  E-value: 2.29e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109287753 141 AELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:COG3883   26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
133-190 2.80e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 2.80e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 109287753 133 LNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIK 190
Cdd:COG4372   89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA 146
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
138-228 2.95e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 138 RVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNARPSfvPHPPVIPASAFTAPQGqa 217
Cdd:COG4942  178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA--AAAERTPAAGFAALKG-- 253
                         90
                 ....*....|.
gi 109287753 218 agqKLMMPVIG 228
Cdd:COG4942  254 ---KLPWPVSG 261
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
83-195 4.03e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 4.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753  83 NKRPRSESGTRPSSKACREKVRR-DKLNERFLELGAVLepgKTPKMDKSSILNDAIRVMAELRSEAQKLKESNESLQ--- 158
Cdd:COG4372   17 GLRPKTGILIAALSEQLRKALFElDKLQEELEQLREEL---EQAREELEQLEEELEQARSELEQLEEELEELNEQLQaaq 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 109287753 159 -------EKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:COG4372   94 aelaqaqEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ 137
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
141-195 4.87e-06

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 44.94  E-value: 4.87e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 109287753  141 AELRSEAQKLKESNESLQEKIKELKAE----KNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:pfam07926  53 AEDIKALQALREELNELKAEIAELKAEaesaKAELEESEESWEEQKKELEKELSELEKR 111
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
134-185 8.50e-06

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 42.64  E-value: 8.50e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 109287753  134 NDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESL 185
Cdd:pfam06005  14 QAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGL 65
DUF4140 pfam13600
N-terminal domain of unknown function (DUF4140); This family is often found at the N-terminus ...
158-192 8.78e-06

N-terminal domain of unknown function (DUF4140); This family is often found at the N-terminus of its member proteins, with DUF4139, pfam13598, at the C-terminus.


Pssm-ID: 463931 [Multi-domain]  Cd Length: 99  Bit Score: 43.36  E-value: 8.78e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 109287753  158 QEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFL 192
Cdd:pfam13600  65 DPELKALRAELEELEDELARLEDELAALEARLAFL 99
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
148-195 1.28e-05

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 42.25  E-value: 1.28e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 109287753  148 QKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:pfam06005  21 ALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGLLGK 68
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
102-195 1.47e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753  102 KVRRDKLNERFLELGAVLEpgktpkMDKSSI-LNDAIRVMAELRSEAQKLKESN---ESLQEKIKELKAEKNELRDEKQK 177
Cdd:COG4913   637 EAELDALQERREALQRLAE------YSWDEIdVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDE 710
                          90
                  ....*....|....*...
gi 109287753  178 LKAEKESLEQQIKFLNAR 195
Cdd:COG4913   711 LKGEIGRLEKELEQAEEE 728
bHLH_AtMYC1_like cd18918
basic Helix-Loop-Helix (bHLH) domain found in Arabidopsis thaliana MYC1 and similar proteins; ...
101-151 2.17e-05

basic Helix-Loop-Helix (bHLH) domain found in Arabidopsis thaliana MYC1 and similar proteins; MYC1, also termed AtbHLH12, or EN 58, acts as a transcription activator, when associated with MYB75/PAP1 or MYB90/PAP2.


Pssm-ID: 381488 [Multi-domain]  Cd Length: 70  Bit Score: 41.55  E-value: 2.17e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 109287753 101 EKVRRDKLNERFLELGAVLePGKTpKMDKSSILNDAIRVMAELRSEAQKLK 151
Cdd:cd18918    5 ERERREKLNEKFSDLRNLI-PNPT-KNDRASILSDAIKYINELQRTVEELK 53
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
100-194 2.60e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 100 REKVRRDKLNERfleLGAVLEPGKTPKMD---KSSILNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQ 176
Cdd:COG4942   98 ELEAQKEELAEL---LRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
                         90
                 ....*....|....*...
gi 109287753 177 KLKAEKESLEQQIKFLNA 194
Cdd:COG4942  175 ELEALLAELEEERAALEA 192
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
142-187 2.75e-05

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 41.50  E-value: 2.75e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 109287753 142 ELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQ 187
Cdd:COG3074    8 ELEAKVQQAVDTIELLQMEVEELKEKNEELEQENEELQSENEELQS 53
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
139-188 2.81e-05

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 41.10  E-value: 2.81e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 109287753  139 VMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQ 188
Cdd:pfam06005   5 LLEQLETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQE 54
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
132-188 3.19e-05

Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.


Pssm-ID: 460827 [Multi-domain]  Cd Length: 383  Bit Score: 44.46  E-value: 3.19e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 109287753  132 ILNDAIRVMAELRSEAQK-LKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQ 188
Cdd:pfam03148  22 LRQESRRLRNETDAKTKWdQYDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEE 79
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
140-195 4.13e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 4.13e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 109287753 140 MAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:COG4372  103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
140-195 5.48e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 5.48e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 109287753 140 MAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:COG4942  152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
140-194 5.57e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 5.57e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109287753 140 MAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNA 194
Cdd:COG4372  117 LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
106-190 6.22e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.86  E-value: 6.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753  106 DKLNERFLELGAVLEPGKTPKMDKSSILNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESL 185
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK 410

                  ....*
gi 109287753  186 EQQIK 190
Cdd:TIGR04523 411 DEQIK 415
bHLHzip_SREBP cd11394
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
101-159 6.72e-05

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein (SREBP) family; The SREBP family includes SREBP1 and SREBP2, which are bHLHzip transcriptional activator of genes encoding proteins essential for cholesterol biosynthesis/uptake and fatty acid biosynthesis. SREBP1 and SREBP2 are principally found in the liver and in adipocytes and made up of an N-terminal transcription factor portion (composed of an activation domain, a bHLHzip domain, and a nuclear localization signal), a hydrophobic region containing two membrane spanning regions, and a C-terminal regulatory segment. They recognize a symmetric sterol regulatory element (TCACNCCAC) instead of E-box.


Pssm-ID: 381400 [Multi-domain]  Cd Length: 73  Bit Score: 40.33  E-value: 6.72e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 109287753 101 EKVRRDKLNERFLELgAVLEPGKTPKMDKSSILNDAIRVMAELRSEAQKLKESNESLQE 159
Cdd:cd11394   14 EKRYRSSINDRIIEL-KDLVVGPDAKMNKSAVLRKAIDYIRYLQKVNQKLKQENMALKK 71
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
131-195 9.22e-05

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: 43.51  E-value: 9.22e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109287753   131 SILNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:TIGR02168  246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
bHLH-PAS_CLOCK_like cd11441
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output ...
101-137 9.30e-05

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output cycles protein kaput (CLOCK) and similar proteins; The family includes CLOCK, neuronal PAS domain-containing protein 2 (NPAS2) and non-mammalian circadian clock protein PASD1. CLOCK, also termed Class E basic helix-loop-helix protein 8 (bHLHe8), is a transcriptional activator which forms a core component of the circadian clock. NPAS2, also termed neuronal PAS2, or basic-helix-loop-helix-PAS protein MOP4, or Class E basic helix-loop-helix protein 9 (bHLHe9), or member of PAS protein 4, or PAS domain-containing protein 4, is a transcriptional activator which forms a core component of the circadian clock. PASD1 is evolutionarily related to Circadian locomotor output cycles protein kaput (CLOCK)and functions as a suppressor of the biological clock that drives the daily circadian rhythms of cells throughout the body.


Pssm-ID: 381447  Cd Length: 54  Bit Score: 39.26  E-value: 9.30e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 109287753 101 EKVRRDKLNERFLELGAVLePGKTPKMDKSSILNDAI 137
Cdd:cd11441    8 EKKRRDQFNVLINELASML-PGRGRKMDKSTVLKKTI 43
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
133-190 9.42e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 9.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 109287753 133 LNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIK 190
Cdd:COG3883   25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
141-202 1.15e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 1.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109287753  141 AELRSEAQKLKESnesLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNARPSFVPHP 202
Cdd:COG4913   383 AALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
bZIP_Fos_like cd14699
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a ...
140-172 1.18e-04

Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of Fos proteins (c-Fos, FosB, Fos-related antigen 1 (Fra-1), and Fra-2), Activating Transcription Factor-3 (ATF-3), and similar proteins. Fos proteins are members of the activator protein-1 (AP-1) complex, which is mainly composed of bZIP dimers of the Jun and Fos families, and to a lesser extent, ATF and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. ATF3 is induced by various stress signals such as cytokines, genotoxic agents, or physiological stresses. It is implicated in cancer and host defense against pathogens. It negatively regulates the transcription of pro-inflammatory cytokines and is critical in preventing acute inflammatory syndromes. ATF3 dimerizes with Jun and other ATF proteins; the heterodimers function either as activators or repressors depending on the promoter context. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269847 [Multi-domain]  Cd Length: 59  Bit Score: 39.17  E-value: 1.18e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 109287753 140 MAELRSEAQKLKESNESLQEKIKELKAEKNELR 172
Cdd:cd14699   24 MEELQAEVEQLEDENEKLQSEIANLRSEKEQLE 56
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
141-195 1.23e-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: 43.12  E-value: 1.23e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 109287753   141 AELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
bHLH-PAS_CLOCK cd19734
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output ...
96-137 1.27e-04

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain found in Circadian locomotor output cycles protein kaput (CLOCK) and similar proteins; CLOCK, also termed Class E basic helix-loop-helix protein 8 (bHLHe8), is a bHLH-PAS transcriptional activator which forms a core component of the circadian clock. It forms heterodimers with another bHLH-PAS protein, Brain-Muscle-Arnt-Like (also known as BMAL or ARNT3 or mop3), which regulates circadian rhythm. BMAL1-CLOCK heterodimer complex activates transcription from E-box (CANNTG) elements found in the promoter of circadian responsive genes.


Pssm-ID: 381577  Cd Length: 61  Bit Score: 39.23  E-value: 1.27e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 109287753  96 SKACREKVRRDKLNERFLELGAVLePGKTPKMDKSSILNDAI 137
Cdd:cd19734   10 SRNKSEKKRRDQFNVLIKELGSML-PGNARKMDKSTVLQKSI 50
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
96-194 1.32e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753  96 SKACREKVRRDKLNERFLELGAVLEPGKTpkmdKSSILNDAIRVMAELRSEAQKLK-ESNESLQEKIKELKAEKNELRDE 174
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEE----RHELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEE 406
                         90       100
                 ....*....|....*....|
gi 109287753 175 KQKLKAEKESLEQQIKFLNA 194
Cdd:PRK03918 407 ISKITARIGELKKEIKELKK 426
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
140-187 1.39e-04

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 42.51  E-value: 1.39e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 109287753 140 MAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQ 187
Cdd:PRK03992   3 LEALEERNSELEEQIRQLELKLRDLEAENEKLERELERLKSELEKLKS 50
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
133-190 1.51e-04

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 41.15  E-value: 1.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109287753  133 LNDAIRV----MAELRSEAQKLKESNESLQEKI-----KELKAEKNeLRDEKQKLKAEKESLE------QQIK 190
Cdd:pfam11559  57 LNETIRTleaeIERLQSKIERLKTQLEDLERELallqaKERQLEKK-LKTLEQKLKNEKEELQrlknalQQIK 128
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
140-195 1.76e-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: 42.74  E-value: 1.76e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 109287753   140 MAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
bHLHzip_Mlx_like cd11404
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family; Mlx, ...
100-166 2.33e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family; Mlx, also termed Class D basic helix-loop-helix protein 13 (bHLHd13), or Max-like bHLHZip protein, or protein BigMax, or transcription factor-like protein 4, is a Max-like bHLHZip transcription regulator that interacts with the Max network of transcription factors. It forms a sequence-specific DNA-binding protein complex with some member of Mad family (Mad1 and Mad4) and Mondo family but not the Myc family and bind the E-box DNA to control transcription. The family also includes Saccharomyces cerevisiae INO4, which is a bHLH transcriptional activator of phospholipid synthetic genes (such as INO1, CHO1/PSS, CHO2/PEM1, OPI3/PEM2, etc.). It is required for de-repression of phospholipid biosynthetic gene expression in response to inositol deprivation in yeast.


Pssm-ID: 381410 [Multi-domain]  Cd Length: 70  Bit Score: 38.44  E-value: 2.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109287753 100 REKVRRDKLNERFLELGAVLePG-KTPKMDKSSILNDAIRVMaelrseaQKLKESNESLQEKIKELKA 166
Cdd:cd11404    9 SEKKRRELIKKGYDELCALV-PGlDPQKRTKADILQKAADWI-------QELKEENEKLEEQLDELKE 68
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
141-195 2.57e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 2.57e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109287753 141 AELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:COG3883   19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE 73
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
133-190 2.62e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 2.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109287753 133 LNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKN-------ELRDEKQKLKAEKESLEQQIK 190
Cdd:COG1340   10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDelnaqvkELREEAQELREKRDELNEKVK 74
FtsB COG2919
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
137-175 2.87e-04

Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442163 [Multi-domain]  Cd Length: 96  Bit Score: 39.09  E-value: 2.87e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 109287753 137 IRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEK 175
Cdd:COG2919   28 LLAYRELRQEIAELEAENAKLKARNAELEAEVADLKDGP 66
bHLH_AtAIG1_like cd11455
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein AIG1 and similar ...
87-160 2.87e-04

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein AIG1 and similar proteins; AIG1, also termed AtbHLH32, or EN 54, or protein target of MOOPTEROS 5, is a transcription factor required for MONOPTEROS-dependent root initiation in embryo.


Pssm-ID: 381461  Cd Length: 80  Bit Score: 38.43  E-value: 2.87e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109287753  87 RSESGTRPSSKAcrEKVRRDKLNERFLELGAVLePGKTpKMDKSSILNDAIRVMAELRSEAQKLKESNESLQEK 160
Cdd:cd11455    3 KALAASKSHSEA--ERRRRERINSHLATLRTLL-PNLS-KTDKASLLAEVVQHVKELKRQAAEITTPPDVPTED 72
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
101-186 3.04e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.84  E-value: 3.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 101 EKVRRD--KLNERFLELGAVLEPGKTPKMDKSSIlndairVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKL 178
Cdd:PRK05771  46 RKLRSLltKLSEALDKLRSYLPKLNPLREEKKKV------SVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKEL 119

                 ....*...
gi 109287753 179 KAEKESLE 186
Cdd:PRK05771 120 EQEIERLE 127
bHLHzip_MITF_like cd11397
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the microphthalmia-associated ...
101-155 3.11e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the microphthalmia-associated transcription factor family (MITF) family; The MITF (also known as microphthalmia-TFE, or MiT) family is a small family that contain a basic helix loop helix domain associated with a leucine zipper (bHLHZip). The MITF family comprises four genes in mammals (MITF, TFE3, TFEB, and TFEC); each gene has different functions. MITF is involved in neural crest melanocytes development as well as the pigmented retinal epithelium. TFEB is required for vascularization of the mouse placenta. TFE3 is involved in B cell function. TFEC regulates gene expression in macrophages. The MITF family can form homodimers or heterodimers with each other but not with other bHLH or bHLHzip proteins.


Pssm-ID: 381403  Cd Length: 69  Bit Score: 38.04  E-value: 3.11e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 109287753 101 EKVRRDKLNERFLELGAVLEPGKTPKM--DKSSILNDAIRVMAELRSEAQKLKESNE 155
Cdd:cd11397   13 ERRRRFNINDRIKELGTLLPKSNDPDMrwNKGTILKASVDYIRKLQKEQERLRQLEE 69
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
91-195 3.25e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753  91 GTRPSSKACREKVRRDKLNERFLELGAVLepgktpkmdkSSILNDAIRVMAELRSEA----QKLKESNESLQEKIKELKA 166
Cdd:COG4372    1 GDRLGEKVGKARLSLFGLRPKTGILIAAL----------SEQLRKALFELDKLQEELeqlrEELEQAREELEQLEEELEQ 70
                         90       100
                 ....*....|....*....|....*....
gi 109287753 167 EKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:COG4372   71 ARSELEQLEEELEELNEQLQAAQAELAQA 99
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
97-190 3.31e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 3.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753  97 KACREKVRRDKLNERFLELGAVLEpGKTPKMDKSSILNDAIRVMAELRSEAQKLKESNE---SLQEKIKELKAEKNELRD 173
Cdd:COG4717  389 AALEQAEEYQELKEELEELEEQLE-ELLGELEELLEALDEEELEEELEELEEELEELEEeleELREELAELEAELEQLEE 467
                         90
                 ....*....|....*....
gi 109287753 174 EK--QKLKAEKESLEQQIK 190
Cdd:COG4717  468 DGelAELLQELEELKAELR 486
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
104-195 3.46e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 3.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 104 RRDKLNERFLELGAVLEPGKTPKMDKSSILNDAIRVMAELRSEAQKLKESNE----SLQEKIKELKAEKNELRDEKQKLK 179
Cdd:COG4717  140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeelqDLAEELEELQQRLAELEEELEEAQ 219
                         90
                 ....*....|....*.
gi 109287753 180 AEKESLEQQIKFLNAR 195
Cdd:COG4717  220 EELEELEEELEQLENE 235
bHLHzip_SREBP2 cd18922
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
91-158 3.47e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein 2 (SREBP2) and similar proteins; SREBP2, also termed Class D basic helix-loop-helix protein 2 (bHLHd2), or sterol regulatory element-binding transcription factor 2 (SREBF2), is a member of a family of bHLHzip transcription factors that recognize sterol regulatory element 1 (SRE-1). It acts as a transcription activator of cholesterol biosynthesis.


Pssm-ID: 381492 [Multi-domain]  Cd Length: 77  Bit Score: 38.40  E-value: 3.47e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109287753  91 GTRPSSKACREKVRRDKLNERFLELGAVLEpGKTPKMDKSSILNDAIRVMAELRSEAQKLKESNESLQ 158
Cdd:cd18922    4 GERRTTHNIIEKRYRSSINDKIIELKDLVM-GTDAKMHKSGVLRKAIDYIKYLQQVNHKLRQENMALK 70
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
140-195 3.50e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 3.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 109287753 140 MAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:COG1579   19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
131-190 3.50e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 3.50e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109287753 131 SILNDAIR-VMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIK 190
Cdd:COG1579  106 SDLEDEILeLMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
141-189 3.50e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 3.50e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 109287753 141 AELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQI 189
Cdd:COG1579  124 EELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
DUF5082 pfam16888
Domain of unknown function (DUF5082); This entry contains proteins that are uncharacterized.
140-189 3.67e-04

Domain of unknown function (DUF5082); This entry contains proteins that are uncharacterized.


Pssm-ID: 407125 [Multi-domain]  Cd Length: 122  Bit Score: 39.21  E-value: 3.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 109287753  140 MAELRSEAQklkesneSLQEKIKELKAEKNELRDEKQKLKAEKESLEQQI 189
Cdd:pfam16888  12 IAQLRSEIA-------ALEEKIERLKEAKTKLDAEKESLHDKKTKLQGPL 54
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
140-190 3.99e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.05  E-value: 3.99e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 109287753 140 MAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIK 190
Cdd:COG1340  197 MIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
140-190 4.05e-04

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 38.32  E-value: 4.05e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 109287753 140 MAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIK 190
Cdd:cd22887   13 LAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEKLR 63
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
145-195 4.47e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 4.47e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 109287753 145 SEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR 70
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
142-193 4.49e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 4.49e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 109287753  142 ELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLN 193
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
141-225 4.54e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 4.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 141 AELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNARPSFVPHPPVIPASAFTAPQGQAAGQ 220
Cdd:COG3883  150 AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229

                 ....*
gi 109287753 221 KLMMP 225
Cdd:COG3883  230 AAAAA 234
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
105-192 4.65e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 4.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 105 RDKLNERFLELGavlepgkTPKMDKSSILNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKES 184
Cdd:COG4717   48 LERLEKEADELF-------KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK 120

                 ....*...
gi 109287753 185 LEQQIKFL 192
Cdd:COG4717  121 LEKLLQLL 128
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
131-195 5.25e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 5.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109287753 131 SILNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:COG3883  133 DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQ 197
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
142-194 5.72e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 5.72e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 109287753  142 ELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNA 194
Cdd:TIGR04523 572 ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
106-191 6.20e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753  106 DKLNERFLELGAVLEPGKTPKMDKSSILNDA---IRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEK 182
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIknkLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI 241

                  ....*....
gi 109287753  183 ESLEQQIKF 191
Cdd:TIGR04523 242 NEKTTEISN 250
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
133-188 6.31e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.97  E-value: 6.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 109287753 133 LNDAIRVMAELRseaQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQ 188
Cdd:PRK00409 518 LNELIASLEELE---RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE 570
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
133-189 6.36e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 38.75  E-value: 6.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 109287753  133 LNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQI 189
Cdd:pfam20492  29 LEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAEL 85
BRE1 pfam08647
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a ...
142-194 7.14e-04

BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a transcriptional activator through direct activator interactions.


Pssm-ID: 462547 [Multi-domain]  Cd Length: 95  Bit Score: 37.95  E-value: 7.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 109287753  142 ELRSEAQKLKESNESLQEKIKELKAEKNElrdEKQKLKA---EKESLEQQIKFLNA 194
Cdd:pfam08647  14 ELSEQLDKKVKDLTILEEKKLRLEAEKAK---ADQKYFAamrSKDALENENKKLNT 66
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
140-190 7.47e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 7.47e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 109287753 140 MAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIK 190
Cdd:COG1340    3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK 53
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
102-195 7.69e-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: 40.43  E-value: 7.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753   102 KVRRDKLNERFLELGAVLEPGKTPKMDKSSILNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAE 181
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
                           90
                   ....*....|....
gi 109287753   182 KESLEQQIKFLNAR 195
Cdd:TIGR02168  388 VAQLELQIASLNNE 401
bZIP_Fos_like cd14699
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a ...
148-186 7.72e-04

Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of Fos proteins (c-Fos, FosB, Fos-related antigen 1 (Fra-1), and Fra-2), Activating Transcription Factor-3 (ATF-3), and similar proteins. Fos proteins are members of the activator protein-1 (AP-1) complex, which is mainly composed of bZIP dimers of the Jun and Fos families, and to a lesser extent, ATF and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. ATF3 is induced by various stress signals such as cytokines, genotoxic agents, or physiological stresses. It is implicated in cancer and host defense against pathogens. It negatively regulates the transcription of pro-inflammatory cytokines and is critical in preventing acute inflammatory syndromes. ATF3 dimerizes with Jun and other ATF proteins; the heterodimers function either as activators or repressors depending on the promoter context. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269847 [Multi-domain]  Cd Length: 59  Bit Score: 36.85  E-value: 7.72e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 109287753 148 QKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLE 186
Cdd:cd14699   18 QRRRELMEELQAEVEQLEDENEKLQSEIANLRSEKEQLE 56
FtsB COG2919
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
160-199 7.86e-04

Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442163 [Multi-domain]  Cd Length: 96  Bit Score: 37.94  E-value: 7.86e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 109287753 160 KIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNARPSFV 199
Cdd:COG2919   30 AYRELRQEIAELEAENAKLKARNAELEAEVADLKDGPDYI 69
bHLHzip_SREBP1 cd18921
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
101-163 8.34e-04

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein 1 (SREBP1) and similar proteins; SREBP1, also termed Class D basic helix-loop-helix protein 1 (bHLHd1), or sterol regulatory element-binding transcription factor 1 (SREBF1), is a member of a family of bHLHzip transcription factors that recognize sterol regulatory element 1 (SRE-1). It acts as a transcriptional activator required for lipid homeostasis. It may control transcription of the low-density lipoprotein receptor gene as well as the fatty acid. SREBP1 has dual sequence specificity binding to both an E-box motif (5'-ATCACGTGA-3') and to SRE-1 (5'-ATCACCCCAC-3').


Pssm-ID: 381491  Cd Length: 75  Bit Score: 37.18  E-value: 8.34e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109287753 101 EKVRRDKLNERFLELGAvLEPGKTPKMDKSSILNDAIRVMAELRSEAQKLKESNESLQEKIKE 163
Cdd:cd18921   14 EKRYRSSINDKIIELKD-LVVGTEAKLNKSAVLRKAIDYIRFLQQSNQKLKQENMALKMAVQK 75
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
136-195 8.48e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 8.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109287753  136 AIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKA--------EKESLEQQIKFLNAR 195
Cdd:COG4913   286 AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAqirgnggdRLEQLEREIERLERE 353
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
134-193 9.22e-04

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 37.93  E-value: 9.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753  134 NDAIRVMAELRseAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLN 193
Cdd:pfam13863  57 NDAKRRRALKK--AEEETKLKKEKEKEIKKLTAQIEELKSEISKLEEKLEEYKPYEDFLE 114
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
140-195 9.35e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 9.35e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 109287753 140 MAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:COG4372  124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
DivIC pfam04977
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and ...
148-190 9.69e-04

Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and sporulation septum formation. These proteins are mainly composed of an amino terminal coiled-coil.


Pssm-ID: 428231 [Multi-domain]  Cd Length: 69  Bit Score: 36.81  E-value: 9.69e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 109287753  148 QKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIK 190
Cdd:pfam04977   9 YQLKQEIAQLQAEIAKLKQENEELEAEIKDLKSDPDYIEERAR 51
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
141-190 1.08e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 1.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 109287753 141 AELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIK 190
Cdd:COG1579   13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK 62
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
145-193 1.09e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 1.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 109287753  145 SEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLN 193
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
134-190 1.12e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 1.12e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 109287753 134 NDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIK 190
Cdd:COG3883  132 ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
bZIP_ATF2 cd14687
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ...
148-189 1.13e-03

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar proteins: a DNA-binding and dimerization domain; ATF-2 is a sequence-specific DNA-binding protein that belongs to the Basic leucine zipper (bZIP) family of transcription factors. In response to stress, it activates a variety of genes including cyclin A, cyclin D, and c-Jun. ATF-2 also plays a role in the DNA damage response that is independent of its transcriptional activity. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269835 [Multi-domain]  Cd Length: 61  Bit Score: 36.35  E-value: 1.13e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 109287753 148 QKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQI 189
Cdd:cd14687   18 QRKKQWVQQLEEKVRKLESENKALKAEVDKLREEVLDLKNLL 59
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
138-189 1.15e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 1.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 109287753 138 RVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQI 189
Cdd:COG3883  126 KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
128-193 1.30e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.62  E-value: 1.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109287753  128 DKSSILNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLN 193
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEN 558
bHLHzip_TFE3 cd18928
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor E3 (TFE3) and ...
101-161 1.31e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor E3 (TFE3) and similar proteins; TFE3, also termed Class E basic helix-loop-helix protein 33 (bHLHe33), is a bHLHzip transcription factor that is involved in B cell function. It specifically recognizes and binds E-box sequences (5'-CANNTG-3'). Its efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFEB or MITF.


Pssm-ID: 381498 [Multi-domain]  Cd Length: 91  Bit Score: 36.95  E-value: 1.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109287753 101 EKVRRDKLNERFLELGAVLEPGKTPKM--DKSSILNDAIRVMAELRSEAQ----------KLKESNESLQEKI 161
Cdd:cd18928   19 ERRRRFNINDRIKELGTLIPKSTDPEMrwNKGTILKASVDYIRKLQKEQQrskeiemrqrKLEQANRSLQLRI 91
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
128-190 1.33e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 1.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109287753 128 DKSSILNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIK 190
Cdd:COG3883   27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
bHLH_AtBIM_like cd11453
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana BES1-interacting Myc-like ...
92-157 1.38e-03

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana BES1-interacting Myc-like proteins (BIMs) and similar proteins; The family includes Arabidopsis thaliana BIM1 and its homologs (BIM2 and BIM3), which are bHLH transcription factors that interact with BES1 to regulate transcription of Brassinosteroid (BR)-induced gene. BR regulates many growth and developmental processes such as cell elongation, vascular development, senescence stress responses, and photomorphogenesis. BIM1 heterodimerize with BES1 and bind to E-box sequences present in many BR-induced promoters to regulated BR-induced genes.


Pssm-ID: 381459  Cd Length: 77  Bit Score: 36.68  E-value: 1.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109287753  92 TRPSSKACREKVRRDKLNERFlELGAVLEPGKTPKMDKSSILNDAIRVMAELRSEAQKLKESNESL 157
Cdd:cd11453    2 TPRSKHSATEQRRRSKINERL-QALRDLIPHSDQKRDKASFLLEVIEYIQALQEKVAKLEEQVQGW 66
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
130-192 1.42e-03

Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.


Pssm-ID: 460827 [Multi-domain]  Cd Length: 383  Bit Score: 39.45  E-value: 1.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109287753  130 SSILNDAIRvmaELRSEAQKLkesNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFL 192
Cdd:pfam03148 228 DSILEQTAN---DLRAQADAV---NFALRKRIEETEDAKNKLEWQLKKTLQEIAELEKNIEAL 284
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
133-193 1.53e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.62  E-value: 1.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109287753  133 LNDAIrvmAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLN 193
Cdd:TIGR04523 340 LNEQI---SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE 397
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
138-192 1.57e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.49  E-value: 1.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 109287753  138 RVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFL 192
Cdd:pfam07888  80 SRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL 134
DivIC pfam04977
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and ...
155-199 1.77e-03

Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and sporulation septum formation. These proteins are mainly composed of an amino terminal coiled-coil.


Pssm-ID: 428231 [Multi-domain]  Cd Length: 69  Bit Score: 36.04  E-value: 1.77e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 109287753  155 ESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNARPSFV 199
Cdd:pfam04977   2 KNGLLTYYQLKQEIAQLQAEIAKLKQENEELEAEIKDLKSDPDYI 46
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
133-195 1.96e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 1.96e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109287753 133 LNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:COG1196  283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
FtsB COG2919
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
148-195 2.47e-03

Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442163 [Multi-domain]  Cd Length: 96  Bit Score: 36.40  E-value: 2.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 109287753 148 QKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQikflnAR 195
Cdd:COG2919   32 RELRQEIAELEAENAKLKARNAELEAEVADLKDGPDYIEER-----AR 74
PRK12705 PRK12705
hypothetical protein; Provisional
93-195 2.54e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 38.92  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753  93 RPSSKACREKVRRDKLNERFLElGAVLEPGKTPKMDKSSILNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELR 172
Cdd:PRK12705  30 RLAKEAERILQEAQKEAEEKLE-AALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLE 108
                         90       100
                 ....*....|....*....|...
gi 109287753 173 DEKQKLKAEKESLEQQIKFLNAR 195
Cdd:PRK12705 109 EREKALSARELELEELEKQLDNE 131
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
128-192 2.64e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.04  E-value: 2.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 128 DKSSILNDAIRVMAELRSEAQKLKESnesLQEKIKELKAEKNELRDE-----KQKLKAEKESLEQQIKFL 192
Cdd:PRK00409 527 ELERELEQKAEEAEALLKEAEKLKEE---LEEKKEKLQEEEDKLLEEaekeaQQAIKEAKKEADEIIKEL 593
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
142-193 2.78e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.85  E-value: 2.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 109287753  142 ELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLN 193
Cdd:TIGR04523 600 DLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
120-188 2.80e-03

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).


Pssm-ID: 464620 [Multi-domain]  Cd Length: 276  Bit Score: 38.15  E-value: 2.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109287753  120 EPGKTPKMDKssiLNDAiRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQ 188
Cdd:pfam15294 112 FELNKPKLEP---LNEG-GGSALLHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKE 176
PRK12704 PRK12704
phosphodiesterase; Provisional
142-195 2.81e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.61  E-value: 2.81e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109287753 142 ELRSEAQK-LKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:PRK12704  68 KLRNEFEKeLRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
140-190 2.84e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 37.88  E-value: 2.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 109287753 140 MAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIK 190
Cdd:COG1842  100 AEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEK 150
bHLHzip_USF3 cd18910
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in basic helix-loop-helix ...
101-150 2.98e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in basic helix-loop-helix domain-containing protein USF3 and similar proteins; USF3, also termed upstream transcription factor 3, is a bHLHzip protein that is involved in the negative regulation of epithelial-mesenchymal transition, the process by which epithelial cells lose their polarity and adhesion properties to become mesenchymal cells with enhanced migration and invasive properties.


Pssm-ID: 381480  Cd Length: 65  Bit Score: 35.35  E-value: 2.98e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 109287753 101 EKVRRDKLNERFLELGAVLEPGKTPKMDKSSILNDAIRVMAELRSEAQKL 150
Cdd:cd18910   13 ERRRKDKINAGINKIGELLPDRDAKKQSKNMILEQAYKYIVELKKKNDKL 62
bHLH_AtIND_like cd11454
basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein INDEHISCENT (IND) ...
92-150 3.10e-03

basic helix-loop-helix (bHLH) domain found in Arabidopsis thaliana protein INDEHISCENT (IND) and similar proteins; The family includes several bHLH transcription factors from Arabidopsis thaliana, such as IND, HEC proteins (HEC1, HEC2 and HEC3) and UNE12. IND, also termed AtbHLH40, or EN 120, is a bHLH transcription regulator required for seed dispersal. It is involved in the differentiation of all three cell types required for fruit dehiscence. HEC1 (also termed AtbHLH88, or protein HECATE 1, or EN 118), HEC2 (also termed AtbHLH37, or protein HECATE 2, or EN 117) and HEC3 (also termed AtbHLH43, or protein HECATE 3, or EN 119) are required for the female reproductive tract development and fertility. Both IND and HEC proteins have been implicated in regulation of auxin signaling. They heterodimerize with SPATULA (SPT) bHLH transcription factor to regulate reproductive tract development in plant. UNE12, also termed AtbHLH59, or protein UNFERTILIZED EMBRYO SAC 12, or EN 93, is required for ovule fertilization.


Pssm-ID: 381460  Cd Length: 63  Bit Score: 35.06  E-value: 3.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 109287753  92 TRPSSKACREkvRRDKLNERFLELGAvLEPGKTpKMDKSSILNDAIRVMAELRSEAQKL 150
Cdd:cd11454    2 TDPQSVAARH--RRERISERIRILQR-LVPGGT-KMDTASMLDEAIHYVKFLQLQVKLL 56
bHLH_PAS cd11391
basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain family; bHLH-PAS domain has been found ...
93-133 3.18e-03

basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS) domain family; bHLH-PAS domain has been found in a large group of bHLH transcription regulators that are involved in gene expression responding to environmental change and controlling aspects of neural development, including proteins from aryl hydrocarbon receptor nuclear translocator (ARNT) family, hypoxia-inducible factor (HIF) family, aryl hydrocarbon receptor (AhR) family, neuronal PAS domain-containing protein (NPAS) family, Circadian locomotor output cycles protein kaput (CLOCK)-like family, and single-minded (SIM) family. bHLH-PAS transcriptional regulatory factors have a bHLH DNA-binding domain followed by two PAS domains and a C-terminal activation or repression domain. bHLH-PAS family members can be divided into class I and class II based on their dimerization partner. bHLH-PAS class I factors include AhR, HIF and SIM. The best characterized bHLH-PAS Class II protein is the ubiquitous ARNT. Some members of bHLH-PAS family act as transcriptional coactivators (such as NCoA) that lack the ability to dimerize and bind DNA.


Pssm-ID: 381397 [Multi-domain]  Cd Length: 55  Bit Score: 34.86  E-value: 3.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 109287753  93 RPSSKAcrEKVRRDKLNERFLELGAVL--EPGKTPKMDKSSIL 133
Cdd:cd11391    2 EKSREA--AKKRRDKENAEISELASLLplPPAVGSKLDKLSVL 42
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
140-190 3.28e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.07  E-value: 3.28e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 109287753   140 MAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQ----KLKAEKESLEQQIK 190
Cdd:smart00787 167 LELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPteldRAKEKLKKLLQEIM 221
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
148-181 3.32e-03

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269834 [Multi-domain]  Cd Length: 52  Bit Score: 34.83  E-value: 3.32e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 109287753 148 QKLKESNESLQEKIKELKAEKNELRDEKQKLKAE 181
Cdd:cd14686   17 ERKKERIEELEEEVEELEEENEELKAELEELRAE 50
bHLHzip_Myc cd11400
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Myc family; The Myc family is a ...
101-192 3.50e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Myc family; The Myc family is a member of the bHLHzip family of transcription factors that play important roles in the control of normal cell proliferation, growth, survival and differentiation. All Myc isoforms contain two independently functioning polypeptide chain regions: N-terminal transactivating residues and a C-terminal bHLHzip segment. The bHLHzip family of bHLH transcription factors are characterized by a highly conserved N-terminal basic region that may bind DNA at a consensus hexanucleotide sequence known as the E-box (CANNTG) followed by HLH and leucine zipper motifs that may interact with other proteins to form homo- and heterodimers. Myc heterodimerizes with Max enabling specific binding to E-box DNA sequences in the promoters of target genes. The Myc proto-oncoprotein family includes at least five different functional members: c-, N-, L-, S- and B-Myc (which is lacking the bHLH domain).


Pssm-ID: 381406 [Multi-domain]  Cd Length: 80  Bit Score: 35.60  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 101 EKVRRDKLNERFLEL----GAVLEPGKTPKMdksSILNDAIrvmaelrseaqklkesneslqEKIKELKAEKNELRDEKQ 176
Cdd:cd11400    9 ERQRRNDLKNSFEKLrdlvPELADNEKASKV---VILKKAT---------------------EYIKQLQQEEKKLEKEKD 64
                         90
                 ....*....|....*.
gi 109287753 177 KLKAEKESLEQQIKFL 192
Cdd:cd11400   65 KLKARNEQLRKKLERL 80
PRK08476 PRK08476
F0F1 ATP synthase subunit B'; Validated
108-190 3.73e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 181442 [Multi-domain]  Cd Length: 141  Bit Score: 36.59  E-value: 3.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 108 LNERFLELGAVLEPGKTPKMDKSSILNDAIRVMAELRSEAQKLKES--NESLQEKIKELKAEKNELRDE----KQKLKAE 181
Cdd:PRK08476  36 MDNRNASIKNDLEKVKTNSSDVSEIEHEIETILKNAREEANKIRQKaiAKAKEEAEKKIEAKKAELESKyeafAKQLANQ 115

                 ....*....
gi 109287753 182 KESLEQQIK 190
Cdd:PRK08476 116 KQELKEQLL 124
Prefoldin_alpha cd00584
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, ...
146-189 3.76e-03

Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467468 [Multi-domain]  Cd Length: 121  Bit Score: 36.44  E-value: 3.76e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 109287753 146 EAQKLKESNESLQEKIKELKAEKNELRDEKQKLKA-EKESLEQQI 189
Cdd:cd00584    4 QLQELREQIEALQEEIEQLEEEQAEIDEAKEALEElKKEGSEVLV 48
bZIP_ATF4 cd14692
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar ...
142-173 3.89e-03

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar proteins: a DNA-binding and dimerization domain; ATF-4 was also isolated and characterized as the cAMP-response element binding protein 2 (CREB2). It is a Basic leucine zipper (bZIP) transcription factor that has been reported to act as both an activator or repressor. It is a critical component in both the unfolded protein response (UPR) and amino acid response (AAR) pathways. Under certain stress conditions, ATF-4 transcription is increased; accumulation of ATF-4 induces the expression of genes involved in amino acid metabolism and transport, mitochondrial function, redox chemistry, and others that ensure protein synthesis and recovery from stress. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269840 [Multi-domain]  Cd Length: 63  Bit Score: 34.86  E-value: 3.89e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 109287753 142 ELRSEAQKLKESNESLQEKIKELKAEKNELRD 173
Cdd:cd14692   27 ELLSEEEELEDRNRELKDEVEELQREINYLKD 58
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
140-195 4.07e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.60  E-value: 4.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 140 MAELRSEAQKLKESNESLQEKIKELKAE----KNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:COG1579  105 ISDLEDEILELMERIEELEEELAELEAElaelEAELEEKKAELDEELAELEAELEELEAE 164
bZIP_Zip1 cd14705
Basic leucine zipper (bZIP) domain of Fungal Zip1-like transcription factors: a DNA-binding ...
148-185 4.29e-03

Basic leucine zipper (bZIP) domain of Fungal Zip1-like transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of fungal bZIP transcription factors including Schizosaccharomyces pombe Zip1, Saccharomyces cerevisiae Methionine-requiring protein 28 (Met28p), and Neurospora crassa cys-3, among others. Zip1 is required for the production of key proteins involved in sulfur metabolism and also plays a role in cadmium response. Met28p acts as a cofactor of Met4p, a transcriptional activator of the sulfur metabolic network; it stabilizes DNA:Met4 complexes. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269853 [Multi-domain]  Cd Length: 55  Bit Score: 34.43  E-value: 4.29e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 109287753 148 QKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESL 185
Cdd:cd14705   17 AKKKQREQELEEKLKELEERIKELERRLDELESENKFL 54
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
130-188 5.36e-03

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 37.03  E-value: 5.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 109287753  130 SSILNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQ 188
Cdd:pfam17078  58 SSMLNRKERRLKDLEDQLSELKNSYEELTESNKQLKKRLENSSASETTLEAELERLQIQ 116
DivIC pfam04977
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and ...
137-175 5.38e-03

Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and sporulation septum formation. These proteins are mainly composed of an amino terminal coiled-coil.


Pssm-ID: 428231 [Multi-domain]  Cd Length: 69  Bit Score: 34.89  E-value: 5.38e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 109287753  137 IRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEK 175
Cdd:pfam04977   5 LLTYYQLKQEIAQLQAEIAKLKQENEELEAEIKDLKSDP 43
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
133-192 5.44e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 37.82  E-value: 5.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109287753 133 LNDAIRVMAELRSEAQKLKESN--ESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFL 192
Cdd:COG4717  404 LEELEEQLEELLGELEELLEALdeEELEEELEELEEELEELEEELEELREELAELEAELEQL 465
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
136-190 5.56e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 37.11  E-value: 5.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109287753 136 AIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIK 190
Cdd:COG1842   89 ALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAK 143
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
104-188 5.86e-03

LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.


Pssm-ID: 462869 [Multi-domain]  Cd Length: 303  Bit Score: 37.37  E-value: 5.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753  104 RRDKLNErflELGAVLEPGKTPKMDKSSILNDAIRvmAELRSEAQKLKES--NESLQEKIKELKAEKNELRDEKQKLKAE 181
Cdd:pfam09738 174 QRDELIE---KHGLVIVPDENTNGEEENSPADAKR--ALVSVEAAEVLESagEGSLDVRLKKLADEKEELLDEVRKLKLQ 248

                  ....*..
gi 109287753  182 KESLEQQ 188
Cdd:pfam09738 249 LEEEKSK 255
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
149-193 6.04e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 35.23  E-value: 6.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 109287753 149 KLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLN 193
Cdd:cd22887    1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILN 45
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
130-195 6.11e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 37.53  E-value: 6.11e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109287753 130 SSILNDAI-RVMAELRSEAQKLKESNE----SLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:COG2433  379 EEALEELIeKELPEEEPEAEREKEHEEreltEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERE 449
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
133-195 6.36e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 37.74  E-value: 6.36e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109287753 133 LNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
141-192 6.74e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 37.53  E-value: 6.74e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 109287753 141 AELRSEAQKLKEsnesLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFL 192
Cdd:COG2433  406 RELTEEEEEIRR----LEEQVERLEAEVEELEAELEEKDERIERLERELSEA 453
bZIP_Fos cd14721
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos): a DNA-binding and dimerization ...
148-187 6.82e-03

Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos): a DNA-binding and dimerization domain; Fos proteins are members of the activator protein-1 (AP-1) complex, which is mainly composed of Basic leucine zipper (bZIP) dimers of the Jun and Fos families, and to a lesser extent, the activating transcription factor (ATF) and musculoaponeurotic fibrosarcoma (Maf) families. The broad combinatorial possibilities for various dimers determine binding specificity, affinity, and the spectrum of regulated genes. The AP-1 complex is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. There are four Fos proteins: c-Fos, FosB, Fos-related antigen 1 (Fra-1), and Fra-2. In addition, FosB also exists as smaller splice variants FosB2 and deltaFosB2. They all contain an N-terminal region and a bZIP domain. c-Fos and FosB also contain a C-terminal transactivation domain which is absent in Fra-1/2 and the smaller FosB variants. Fos proteins can only heterodimerize with Jun and other AP-1 proteins, but cannot homodimerize. Fos:Jun heterodimers are more stable and can bind DNA with more affinity that Jun:Jun homodimers. Fos proteins can enhance the trans-activating and transforming properties of Jun proteins. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269869 [Multi-domain]  Cd Length: 62  Bit Score: 34.26  E-value: 6.82e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 109287753 148 QKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQ 187
Cdd:cd14721   18 QRRVDLTNTLQAETEQLEDEKSSLQNEIANLQKQKEQLEF 57
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
133-195 7.23e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 37.05  E-value: 7.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109287753 133 LNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:COG4942   36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
46 PHA02562
endonuclease subunit; Provisional
105-212 7.25e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 37.30  E-value: 7.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 105 RDKLNERFLELGAVLEpgktpkMDKssILNDAIRvmaELRSEAQKLKESNESLQEKIK-------ELKAEKNELRDEKQ- 176
Cdd:PHA02562 152 RRKLVEDLLDISVLSE------MDK--LNKDKIR---ELNQQIQTLDMKIDHIQQQIKtynknieEQRKKNGENIARKQn 220
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 109287753 177 ---KLKAEKESLEQQIKFLNARPSFVPHPPVIPASAFTA 212
Cdd:PHA02562 221 kydELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNK 259
bHLHzip_USF_MITF cd11387
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in USF/MITF family; The USF (upstream ...
101-148 7.78e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in USF/MITF family; The USF (upstream stimulatory factor)/MITF (microphthalmia-associated transcription factor) family includes two bHLHzip transcription factor subfamilies. USFs are ubiquitously expressed and key regulators of a wide number of gene regulation networks, including the stress and immune responses, cell cycle and proliferation, lipid and glucid metabolism. USFs recruit chromatin remodeling enzymes and interact with co-activators and the members of the transcription pre-initiation complex. USFs interact with high affinity to E-box regulatory elements. The MITF (also known as microphthalmia-TFE, or MiT) subfamily comprises four genes in mammals (MITF, TFE3, TFEB, and TFEC); each gene has different functions. MITF is involved in neural crest melanocytes development as well as the pigmented retinal epithelium. TFEB is required for vascularization of the mouse placenta. TFE3 is involved in B cell function. TFEC regulates gene expression in macrophages. The MITF subfamily proteins can form homodimers or heterodimers with each other but not with other bHLH or bHLHzip proteins.


Pssm-ID: 381393 [Multi-domain]  Cd Length: 58  Bit Score: 34.15  E-value: 7.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 109287753 101 EKVRRDKLNERFLELGAVLEP----GKTPKMDKSSILNDAIRVMAELRSEAQ 148
Cdd:cd11387    6 ERRRRDNINEKIQELGSLVPPsrleTKDLKPNKGSILSKAVEYIRELQNQNQ 57
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
77-194 8.33e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 37.46  E-value: 8.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753    77 GKEQPTNKRPRSESGTRPSSKACREKVR-RDKLNERFLELGAVLEpgktpkmDKSSILNDA----IRVMAELRSEAQKLK 151
Cdd:pfam01576  399 AKQDSEHKRKKLEGQLQELQARLSESERqRAELAEKLSKLQSELE-------SVSSLLNEAegknIKLSKDVSSLESQLQ 471
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 109287753   152 ESNESLQE----------KIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNA 194
Cdd:pfam01576  472 DTQELLQEetrqklnlstRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA 524
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
104-198 9.12e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 37.05  E-value: 9.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109287753 104 RRDKLNERFLELGAVLEPGKT--PKMDKSSILNDAIRVMAELRSEAQKLKESNESLQEKIKELKaeknELRDEKQKLKAE 181
Cdd:COG4717   96 ELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR----ELEEELEELEAE 171
                         90
                 ....*....|....*..
gi 109287753 182 KESLEQQIKFLNARPSF 198
Cdd:COG4717  172 LAELQEELEELLEQLSL 188
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
133-195 9.46e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 37.05  E-value: 9.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109287753 133 LNDAIRVMAELRSEAQKLKESNESLQEKIKELKAEKNELRDEKQKLKAEKESLEQQIKFLNAR 195
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH