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Conserved domains on  [gi|497538983|ref|WP_009853181|]
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CHAP domain-containing protein [Streptococcus gallolyticus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3942 COG3942
Surface antigen [Cell wall/membrane/envelope biogenesis];
350-459 1.43e-31

Surface antigen [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 443142 [Multi-domain]  Cd Length: 129  Bit Score: 117.40  E-value: 1.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 350 NTYPVGQCTWGV----KSLASWVGNNWGNANQWIASAQAAGHSVGTTPQVGAVAVW-PYDGGGYGHVAYVTAVQSSTSIQ 424
Cdd:COG3942   19 NGYPYGQCTWYAawrrAQLGGPIGSGWGNANNWADNARAAGYTVGSTPKVGAVAVFtPGVAGPYGHVAVVESVNSDGSIL 98

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 497538983 425 VMEANYAGNSSIgNYRgwfdpTSSTWGGGTVYYIY 459
Cdd:COG3942   99 VSEMNWGGPGIY-STR-----TISAGNASSYGFIH 127
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1-215 1.97e-23

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: 101.38  E-value: 1.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   1 MKKRILSAVLVSGVTLGTAAATVNA----DDYDTQIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQ 76
Cdd:COG4942    1 MRKLLLLALLLALAAAAQADAAAEAeaelEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  77 LEAESQKLSEEIQALSSKIVARNESLKKQARSAQKTNtATSYINTILNSKSISDAINRVAAVREVVSANEKMLEQQEADK 156
Cdd:COG4942   81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLG-RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 497538983 157 AAIEQKQAENQEAINTVAANKATIEQNQAALATQQAELEAAQLNLSAQLATAEDEKASL 215
Cdd:COG4942  160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
 
Name Accession Description Interval E-value
COG3942 COG3942
Surface antigen [Cell wall/membrane/envelope biogenesis];
350-459 1.43e-31

Surface antigen [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443142 [Multi-domain]  Cd Length: 129  Bit Score: 117.40  E-value: 1.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 350 NTYPVGQCTWGV----KSLASWVGNNWGNANQWIASAQAAGHSVGTTPQVGAVAVW-PYDGGGYGHVAYVTAVQSSTSIQ 424
Cdd:COG3942   19 NGYPYGQCTWYAawrrAQLGGPIGSGWGNANNWADNARAAGYTVGSTPKVGAVAVFtPGVAGPYGHVAVVESVNSDGSIL 98

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 497538983 425 VMEANYAGNSSIgNYRgwfdpTSSTWGGGTVYYIY 459
Cdd:COG3942   99 VSEMNWGGPGIY-STR-----TISAGNASSYGFIH 127
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1-215 1.97e-23

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: 101.38  E-value: 1.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   1 MKKRILSAVLVSGVTLGTAAATVNA----DDYDTQIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQ 76
Cdd:COG4942    1 MRKLLLLALLLALAAAAQADAAAEAeaelEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  77 LEAESQKLSEEIQALSSKIVARNESLKKQARSAQKTNtATSYINTILNSKSISDAINRVAAVREVVSANEKMLEQQEADK 156
Cdd:COG4942   81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLG-RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 497538983 157 AAIEQKQAENQEAINTVAANKATIEQNQAALATQQAELEAAQLNLSAQLATAEDEKASL 215
Cdd:COG4942  160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
 350-429 5.92e-20

CHAP domain; This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine.


Pssm-ID: 461605 [Multi-domain]  Cd Length: 83  Bit Score: 84.01  E-value: 5.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  350 NTYPVGQCTWGVKSLASWVGNNWGNANQWIASAQAAGHSVGTTPQVGAVAVWPYDGGG--YGHVAYVTAVqSSTSIQVME 427
Cdd:pfam05257   3 NGYPWGQCTWFVYWRVAQLGIYLGNAGDWADAAAGAYKVGSTTPKVGDIVVFDPGGGGasYGHVAIVEKV-NDGSITVSE 81


                  ..
gi 497538983  428 AN 429
Cdd:pfam05257  82 QN 83
PRK08581 PRK08581
amidase domain-containing protein;
352-440 4.31e-11

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 65.19  E-value: 4.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 352 YPVGQCTWGV----KSLASWVGNNWGNANQWIASAQAAGHSVGTTPQVGAVAVWPYDGGG----YGHVAYVTAVQSSTSI 423
Cdd:PRK08581 508 YPHGQCTWYVynrmKQFGTSISGDLGDAHNWNNRAQARGYQVSHTPKRHAAVVFEAGQAGadqhYGHVAFVEKVNSDGSI 587

                         90
                 ....*....|....*..
gi 497538983 424 QVMEANYAGNSSIgNYR 440
Cdd:PRK08581 588 VISESNVKGLGII-SYR 603
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-216 5.41e-10

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: 62.00  E-value: 5.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983    25 ADDYDTQIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVARNESLKK 104
Cdd:TIGR02168  721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   105 ---------------QARSAQKTNTATSYINTI-LNSKSISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQE 168
Cdd:TIGR02168  801 lrealdelraeltllNEEAANLRERLESLERRIaATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 497538983   169 AINTVAANKATIEQNQAALATQQAELEAAQLNLSAQLATAEDEKASLV 216
Cdd:TIGR02168  881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
15-209 9.71e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.19  E-value: 9.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  15 TLGTAAATVnaDDYD---TQIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQL-------EAESQKL 84
Cdd:PRK02224 235 TRDEADEVL--EEHEerrEELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaeagldDADAEAV 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  85 SEEIQALSSKIVARNESLKKQARSAQ-KTNTATSYintilnSKSISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQ 163
Cdd:PRK02224 313 EARREELEDRDEELRDRLEECRVAAQaHNEEAESL------REDADDLEERAEELREEAAELESELEEAREAVEDRREEI 386

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 497538983 164 AENQEAINTVAANKATIEQNQAALATQQAELEAAQLNLSAQLATAE 209
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE 432
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 39-95 1.70e-04

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: 39.94  E-value: 1.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 497538983   39 ISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKI 95
Cdd:pfam06005  13 IQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGLLGKL 69
bZIP_ATF2 cd14687
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ...
 58-97 8.86e-04

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: 37.51  E-value: 8.86e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 497538983  58 EQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVA 97
Cdd:cd14687   22 QWVQQLEEKVRKLESENKALKAEVDKLREEVLDLKNLLLA 61
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
 39-148 8.48e-03

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 38.92  E-value: 8.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   39 ISNLTSEQ-AAAQSQVDALQ-EQVTSLQSQQDELEAQNaqleaesQKLSEEIQALSSKIVARNESLKKQARSAQKTNTAT 116
Cdd:NF033875  190 LGNVSSKDlAAKEKEVDQLQkEQAKKIAQQAAELKAKN-------EKIAKENAEIAAKNKAEKERYEKEVAEYNKHKNEN 262

                          90       100       110
                  ....*....|....*....|....*....|..
gi 497538983  117 SYINTILNSKSISDainrvaavREVVSANEKM 148
Cdd:NF033875  263 GYVNEAISKNLVFD--------QSVVTKDTKI 286
 
Name Accession Description Interval E-value
COG3942 COG3942
Surface antigen [Cell wall/membrane/envelope biogenesis];
350-459 1.43e-31

Surface antigen [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443142 [Multi-domain]  Cd Length: 129  Bit Score: 117.40  E-value: 1.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 350 NTYPVGQCTWGV----KSLASWVGNNWGNANQWIASAQAAGHSVGTTPQVGAVAVW-PYDGGGYGHVAYVTAVQSSTSIQ 424
Cdd:COG3942   19 NGYPYGQCTWYAawrrAQLGGPIGSGWGNANNWADNARAAGYTVGSTPKVGAVAVFtPGVAGPYGHVAVVESVNSDGSIL 98

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 497538983 425 VMEANYAGNSSIgNYRgwfdpTSSTWGGGTVYYIY 459
Cdd:COG3942   99 VSEMNWGGPGIY-STR-----TISAGNASSYGFIH 127
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1-215 1.97e-23

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: 101.38  E-value: 1.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   1 MKKRILSAVLVSGVTLGTAAATVNA----DDYDTQIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQ 76
Cdd:COG4942    1 MRKLLLLALLLALAAAAQADAAAEAeaelEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  77 LEAESQKLSEEIQALSSKIVARNESLKKQARSAQKTNtATSYINTILNSKSISDAINRVAAVREVVSANEKMLEQQEADK 156
Cdd:COG4942   81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLG-RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 497538983 157 AAIEQKQAENQEAINTVAANKATIEQNQAALATQQAELEAAQLNLSAQLATAEDEKASL 215
Cdd:COG4942  160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 29-215 1.31e-21

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 96.05  E-value: 1.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  29 DTQIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVARNESLKKQARS 108
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 109 AQKTNTATSYINTILNSKSISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQEAINTVAANKATIEQNQAALA 188
Cdd:COG3883   95 LYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174

                        170       180
                 ....*....|....*....|....*..
gi 497538983 189 TQQAELEAAQLNLSAQLATAEDEKASL 215
Cdd:COG3883  175 AQQAEQEALLAQLSAEEAAAEAQLAEL 201
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
 350-429 5.92e-20

CHAP domain; This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine.


Pssm-ID: 461605 [Multi-domain]  Cd Length: 83  Bit Score: 84.01  E-value: 5.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  350 NTYPVGQCTWGVKSLASWVGNNWGNANQWIASAQAAGHSVGTTPQVGAVAVWPYDGGG--YGHVAYVTAVqSSTSIQVME 427
Cdd:pfam05257   3 NGYPWGQCTWFVYWRVAQLGIYLGNAGDWADAAAGAYKVGSTTPKVGDIVVFDPGGGGasYGHVAIVEKV-NDGSITVSE 81


                  ..
gi 497538983  428 AN 429
Cdd:pfam05257  82 QN 83
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 20-215 3.31e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.89  E-value: 3.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  20 AATVNADDYDTQIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVARN 99
Cdd:COG1196  236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 100 ESLKKQARSAQKTNTAtsyinTILNSKSISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQEAINTVAANKAT 179
Cdd:COG1196  316 ERLEELEEELAELEEE-----LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 497538983 180 IEQNQAALATQQAELEAAQLNLSAQLATAEDEKASL 215
Cdd:COG1196  391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 29-215 3.01e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 3.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  29 DTQIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVARNESLKKQARS 108
Cdd:COG1196  280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 109 AQKTNTAtsyintilnsksISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQEAINTVAANKATIEQNQAALA 188
Cdd:COG1196  360 LAEAEEA------------LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427

                        170       180
                 ....*....|....*....|....*..
gi 497538983 189 TQQAELEAAQLNLSAQLATAEDEKASL 215
Cdd:COG1196  428 EALAELEEEEEEEEEALEEAAEEEAEL 454
PRK08581 PRK08581
amidase domain-containing protein;
352-440 4.31e-11

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 65.19  E-value: 4.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 352 YPVGQCTWGV----KSLASWVGNNWGNANQWIASAQAAGHSVGTTPQVGAVAVWPYDGGG----YGHVAYVTAVQSSTSI 423
Cdd:PRK08581 508 YPHGQCTWYVynrmKQFGTSISGDLGDAHNWNNRAQARGYQVSHTPKRHAAVVFEAGQAGadqhYGHVAFVEKVNSDGSI 587

                         90
                 ....*....|....*..
gi 497538983 424 QVMEANYAGNSSIgNYR 440
Cdd:PRK08581 588 VISESNVKGLGII-SYR 603
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 31-215 4.01e-10

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: 59.94  E-value: 4.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  31 QIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIvARNESLKKQARSAq 110
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-KKYEEQLGNVRNN- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 111 ktntatsyintilnsksisdainrvaavREVvSANEKMLEQQEADKAAIEQKQAENQEAIntvAANKATIEQNQAALATQ 190
Cdd:COG1579   89 ----------------------------KEY-EALQKEIESLKRRISDLEDEILELMERI---EELEEELAELEAELAEL 136

                        170       180
                 ....*....|....*....|....*
gi 497538983 191 QAELEAAQLNLSAQLATAEDEKASL 215
Cdd:COG1579  137 EAELEEKKAELDEELAELEAELEEL 161
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-216 5.41e-10

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: 62.00  E-value: 5.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983    25 ADDYDTQIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVARNESLKK 104
Cdd:TIGR02168  721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   105 ---------------QARSAQKTNTATSYINTI-LNSKSISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQE 168
Cdd:TIGR02168  801 lrealdelraeltllNEEAANLRERLESLERRIaATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 497538983   169 AINTVAANKATIEQNQAALATQQAELEAAQLNLSAQLATAEDEKASLV 216
Cdd:TIGR02168  881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-215 2.23e-09

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: 60.07  E-value: 2.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983    26 DDYDTQIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVARNESLK-- 103
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnl 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   104 ---KQARSAQKTNTATSYINTILNSKSISDAINRVAAVREvvsANEKMLEQQEADKAAIEQKQAENQEAINTVAANKATI 180
Cdd:TIGR02168  315 erqLEELEAQLEELESKLDELAEELAELEEKLEELKEELE---SLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 497538983   181 EQNQAALATQQAELEAAQLNLSAQLATAEDEKASL 215
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 45-215 7.78e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 7.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  45 EQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVARNESLK-KQARSAQktntatsyintil 123
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeAQAEEYE------------- 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 124 nsksisdAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQEAIntvAANKATIEQNQAALATQQAELEAAQLNLSA 203
Cdd:COG1196  293 -------LLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL---EELEEELEELEEELEEAEEELEEAEAELAE 362

                        170
                 ....*....|..
gi 497538983 204 QLATAEDEKASL 215
Cdd:COG1196  363 AEEALLEAEAEL 374
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 31-215 2.71e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  31 QIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQ-----NAQLEAE---SQKLSEEIQALSSKIVARNESL 102
Cdd:COG1196  303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEleeaeEELEEAEaelAEAEEALLEAEAELAEAEEELE 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 103 KKQARSAQKTNTATSYINTILN-SKSISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQEAINTVAANKATIE 181
Cdd:COG1196  383 ELAEELLEALRAAAELAAQLEElEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462

                        170       180       190
                 ....*....|....*....|....*....|....
gi 497538983 182 QNQAALATQQAELEAAQLNLSAQLATAEDEKASL 215
Cdd:COG1196  463 ELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
30-211 2.78e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.46  E-value: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   30 TQIAAQDAVISNLTSEQAaaQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKI----VARNESLKKQ 105
Cdd:COG4913   269 ERLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgngGDRLEQLERE 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  106 ARSAQKTntatsyINTIlnSKSISDAINRVAAVREVVSANEKMLE--QQEAD--KAAIEQKQAENQEAINTVAANKATIE 181
Cdd:COG4913   347 IERLERE------LEER--ERRRARLEALLAALGLPLPASAEEFAalRAEAAalLEALEEELEALEEALAEAEAALRDLR 418

                         170       180       190
                  ....*....|....*....|....*....|
gi 497538983  182 QNQAALATQQAELEAAQLNLSAQLATAEDE 211
Cdd:COG4913   419 RELRELEAEIASLERRKSNIPARLLALRDA 448
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-216 4.26e-07

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: 52.75  E-value: 4.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983    26 DDYDTQIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQ-------NAQLEAESQKLSEEIQALSSKivaR 98
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerLANLERQLEELEAQLEELESK---L 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983    99 NESLKKQARSAQKTNTATSyintilNSKSISDAINRVAAVREV----VSANEKMLEQQEADKAAIEQKQAENQeaiNTVA 174
Cdd:TIGR02168  333 DELAEELAELEEKLEELKE------ELESLEAELEELEAELEElesrLEELEEQLETLRSKVAQLELQIASLN---NEIE 403

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 497538983   175 ANKATIEQNQAALATQQAELEAAQLNL--------SAQLATAEDEKASLV 216
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLKKLeeaelkelQAELEELEEELEELQ 453
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
15-209 9.71e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.19  E-value: 9.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  15 TLGTAAATVnaDDYD---TQIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQL-------EAESQKL 84
Cdd:PRK02224 235 TRDEADEVL--EEHEerrEELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaeagldDADAEAV 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  85 SEEIQALSSKIVARNESLKKQARSAQ-KTNTATSYintilnSKSISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQ 163
Cdd:PRK02224 313 EARREELEDRDEELRDRLEECRVAAQaHNEEAESL------REDADDLEERAEELREEAAELESELEEAREAVEDRREEI 386

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 497538983 164 AENQEAINTVAANKATIEQNQAALATQQAELEAAQLNLSAQLATAE 209
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 19-227 9.76e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 9.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  19 AAATVNADDYDTQIAAQDAVISNLTSEQAAAQSQVDALQEQvtsLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVAR 98
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE---LEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  99 NESLKKQARSAQKTNTATSYINTILN--SKSISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQEAINTVAAN 176
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLErlERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497538983 177 KATIEQNQAALATQQAELEAAQLNLSAQLATAEDEKA---------------------SLVAQKEAAEQAAA 227
Cdd:COG1196  469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflegvkaalllaglrglagavAVLIGVEAAYEAAL 540
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 14-215 3.15e-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: 49.68  E-value: 3.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983    14 VTLGTAAATVNADDYDTQIAAQdAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQ---- 89
Cdd:TIGR02169  272 QLLEELNKKIKDLGEEEQLRVK-EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEeerk 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983    90 ---ALSSKIVARNESLKKQARSAQKTNT--ATSYINTILNSKSISDAINRVAAVR--------EVVSANEKmLEQQEADK 156
Cdd:TIGR02169  351 rrdKLTEEYAELKEELEDLRAELEEVDKefAETRDELKDYREKLEKLKREINELKreldrlqeELQRLSEE-LADLNAAI 429

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 497538983   157 AAIEQKQAENQEAINTVAANKATIEQNQAALATQQAELEAAQLNLSAQLATAEDEKASL 215
Cdd:TIGR02169  430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
71-197 1.38e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   71 EAQNAQLEAESQKLSEEIQALSSKIVARNESLKKQARSAQKTNTATSYINTILNSKSISDAINRVAAVREVVSANEKMLE 150
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLA 688

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 497538983  151 QQEADKAAIEQKQAENQEAINTVAANKATIEQNQAALATQQAELEAA 197
Cdd:COG4913   689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
26-215 3.30e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   26 DDYDTQIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQ--SQQDELEAQNAQLEAESQKLSEEIQAL--SSKIVARnes 101
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLdaSSDDLAA--- 689

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  102 LKKQARSAQktntatsyintilnsKSISDAINRVAAVREVVSANEKmleQQEADKAAIEQKQAENQEAINTVAANKATIE 181
Cdd:COG4913   690 LEEQLEELE---------------AELEELEEELDELKGEIGRLEK---ELEQAEEELDELQDRLEAAEDLARLELRALL 751

                         170       180       190
                  ....*....|....*....|....*....|....
gi 497538983  182 QNQAALATQQAELEAAQLNLSAQLATAEDEKASL 215
Cdd:COG4913   752 EERFAAALGDAVERELRENLEERIDALRARLNRA 785
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 51-225 3.42e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  51 SQVDALQEQV------TSLQSQQDELEAQ-----NAQLEAESQKLSEEIQALSSKIvarnESLKKQARSAQKtntatsyi 119
Cdd:COG1196  200 RQLEPLERQAekaeryRELKEELKELEAEllllkLRELEAELEELEAELEELEAEL----EELEAELAELEA-------- 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 120 ntilnsksisdainRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQEAINTVAANKATIEQNQAALATQQAELEAAQL 199
Cdd:COG1196  268 --------------ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333

                        170       180
                 ....*....|....*....|....*.
gi 497538983 200 NLSAQLATAEDEKASLVAQKEAAEQA 225
Cdd:COG1196  334 ELEEELEELEEELEEAEEELEEAEAE 359
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
39-199 3.63e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 3.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  39 ISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVARNESLKKQARSAQKTNTATSY 118
Cdd:COG4372   89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 119 INTILNSKSISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQEAINTVAANKATIEQNQAALATQQAELEAAQ 198
Cdd:COG4372  169 LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248


                 .
gi 497538983 199 L 199
Cdd:COG4372  249 E 249
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 59-216 4.39e-05

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: 46.21  E-value: 4.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983    59 QVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVARNESLKKqarsaqktntatsyINTILNSKSiSDAINRVAAV 138
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE--------------LNKKIKDLG-EEEQLRVKEK 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   139 REVVSANEKMLEQQEADKAAiEQKQAENQEAINTVAANK--ATIEQNQAALATQQAELEAaqlnLSAQLATAEDEKASLV 216
Cdd:TIGR02169  296 IGELEAEIASLERSIAEKER-ELEDAEERLAKLEAEIDKllAEIEELEREIEEERKRRDK----LTEEYAELKEELEDLR 370
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 41-216 6.55e-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: 45.40  E-value: 6.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   41 NLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVARNESLKKqarsaqktntatsyIN 120
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK--------------DD 551

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  121 TILNSKSIsdainrvaavREVVSANEKMLEQQEADKAAIEQKQAENQEAINTVAANKATIEQnqaalatQQAELEAAQLN 200
Cdd:TIGR04523 552 FELKKENL----------EKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK-------EIEEKEKKISS 614

                         170
                  ....*....|....*.
gi 497538983  201 LSAQLATAEDEKASLV 216
Cdd:TIGR04523 615 LEKELEKAKKENEKLS 630
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
37-214 6.84e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 6.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  37 AVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVARNESLKKQarsaqktntat 116
Cdd:COG4372   24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA----------- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 117 syintilnSKSISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQEAINTVAANKATIEQNQAALATQQAELEA 196
Cdd:COG4372   93 --------QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164

                        170
                 ....*....|....*...
gi 497538983 197 AQLNLSAQLATAEDEKAS 214
Cdd:COG4372  165 ELAALEQELQALSEAEAE 182
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
49-212 1.32e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   49 AQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSsKIVARNESLKKqARSAQKTntatsyintilnsksI 128
Cdd:COG4913   608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEID-VASAERE---------------I 670

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  129 SDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQEAINTVAANKATIEQNQAALATQQAELEAAQLNLSAQLATA 208
Cdd:COG4913   671 AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750


                  ....
gi 497538983  209 EDEK 212
Cdd:COG4913   751 LEER 754
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
45-215 1.52e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  45 EQAAAQSQVDALQEQVTS---LQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVARNESLKKQARSAQKTNTATSYINT 121
Cdd:COG4717   72 ELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 122 ILNSKSISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAenQEAINTVAANKATIEQNQAALATQQAELEAAQlnl 201
Cdd:COG4717  152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL--QDLAEELEELQQRLAELEEELEEAQEELEELE--- 226

                        170
                 ....*....|....
gi 497538983 202 sAQLATAEDEKASL 215
Cdd:COG4717  227 -EELEQLENELEAA 239
46 PHA02562
endonuclease subunit; Provisional
 30-216 1.54e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 44.23  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  30 TQIAAQDAVISNLTSEQAAAqsqVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSS----------KIVARN 99
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKNGEN---IARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAalnklntaaaKIKSKI 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 100 ESLKKQARSAQKTNTATSYintilnSKSISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQEAINTVAANKAT 179
Cdd:PHA02562 272 EQFQKVIKMYEKGGVCPTC------TQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNK 345

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 497538983 180 IEQNQAALATQQAE---LEAAQLNLSAQLATAEDEKASLV 216
Cdd:PHA02562 346 ISTNKQSLITLVDKakkVKAAIEELQAEFVDNAEELAKLQ 385
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 39-95 1.70e-04

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: 39.94  E-value: 1.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 497538983   39 ISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKI 95
Cdd:pfam06005  13 IQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGLLGKL 69
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
39-210 1.96e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  39 ISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVARNESLKKQARSAQKTNTATSY 118
Cdd:COG3206  207 LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARY 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 119 INtilNSKSISDAINRVAAVREVVSAN-EKMLEQQEADKAAIEQKQAENQEAINTVAANKATIEQNQAALATQQAELEAA 197
Cdd:COG3206  287 TP---NHPDVIALRAQIAALRAQLQQEaQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVA 363

                        170
                 ....*....|...
gi 497538983 198 QLNLSAQLATAED 210
Cdd:COG3206  364 RELYESLLQRLEE 376
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
17-205 2.01e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  17 GTAAATVNADDYDTQIAAQDAVISNLTSEQAAAQSQVDALQEQV-------------TSLQSQQDELEAQNAQLEAESQK 83
Cdd:COG3206  206 GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalpellqsPVIQQLRAQLAELEAELAELSAR 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  84 LSEE---IQALSSKIVARNESLKKQARsaqktntatsyintilnsKSISDAINRVAAVREVVSANEKMLEQQEADKAAIE 160
Cdd:COG3206  286 YTPNhpdVIALRAQIAALRAQLQQEAQ------------------RILASLEAELEALQAREASLQAQLAQLEARLAELP 347

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 497538983 161 QKQAENQEAINTVAANKATIEQNQAALatQQAELEAAQLNLSAQL 205
Cdd:COG3206  348 ELEAELRRLEREVEVARELYESLLQRL--EEARLAEALTVGNVRV 390
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 39-208 4.92e-04

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: 42.57  E-value: 4.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   39 ISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVARNESLKKQARSAQKTNtatsy 118
Cdd:pfam07888 138 IKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQ----- 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  119 intilnsKSISDAINRVAAVREVVSANEKMLEQQEA--DKAAIEQKQAEN-QEAINTVAANKatiEQNQAALatQQAELE 195
Cdd:pfam07888 213 -------DTITTLTQKLTTAHRKEAENEALLEELRSlqERLNASERKVEGlGEELSSMAAQR---DRTQAEL--HQARLQ 280

                         170
                  ....*....|...
gi 497538983  196 AAQLNLsaQLATA 208
Cdd:pfam07888 281 AAQLTL--QLADA 291
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
24-94 7.78e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 7.78e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497538983   24 NADDYDTQIAA----QDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSK 94
Cdd:COG4913   360 RRARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
bZIP_ATF2 cd14687
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ...
 58-97 8.86e-04

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: 37.51  E-value: 8.86e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 497538983  58 EQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVA 97
Cdd:cd14687   22 QWVQQLEEKVRKLESENKALKAEVDKLREEVLDLKNLLLA 61
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 26-215 9.15e-04

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: 41.98  E-value: 9.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983    26 DDYDTQIAAQDAVISNLTSEQAA-----AQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQK-------LSEEIQALss 93
Cdd:TIGR02169  761 KELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltlekeyLEKEIQEL-- 838

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983    94 kiVARNESLKKQARSAQKTntatsyintilnsksISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQEAIntv 173
Cdd:TIGR02169  839 --QEQRIDLKEQIKSIEKE---------------IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL--- 898

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 497538983   174 aaNKATIEQNQAALATQQAELEAAQLNlsAQLATAEDEKASL 215
Cdd:TIGR02169  899 --RELERKIEELEAQIEKKRKRLSELK--AKLEALEEELSEI 936
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
23-108 1.05e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   23 VNADDYDTQIAAQDAVISNLTSEQ---AAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVARN 99
Cdd:COG4913   661 IDVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740


                  ....*....
gi 497538983  100 ESLKKQARS 108
Cdd:COG4913   741 DLARLELRA 749
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 24-95 1.21e-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: 40.29  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  24 NADDYDT---QIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQ-----------QDELEAQNAQLEAESQKLSEEIQ 89
Cdd:COG1579   87 NNKEYEAlqkEIESLKRRISDLEDEILELMERIEELEEELAELEAElaeleaeleekKAELDEELAELEAELEELEAERE 166


                 ....*.
gi 497538983  90 ALSSKI 95
Cdd:COG1579  167 ELAAKI 172
FtsB COG2919
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
52-100 1.71e-03

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


Pssm-ID: 442163 [Multi-domain]  Cd Length: 96  Bit Score: 37.55  E-value: 1.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 497538983  52 QVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKivARNE 100
Cdd:COG2919   30 AYRELRQEIAELEAENAKLKARNAELEAEVADLKDGPDYIEER--AREE 76
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
31-198 2.34e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  31 QIAAQDAVISNLTSEQAAAQSQVDALQEQvtsLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVARNESLKKQARSAQ 110
Cdd:COG4372   32 QLRKALFELDKLQEELEQLREELEQAREE---LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 111 KTNTATSYINTIlnSKSISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQEAINTVAANKATIEQNQAALATQ 190
Cdd:COG4372  109 EAEELQEELEEL--QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186


                 ....*...
gi 497538983 191 QAELEAAQ 198
Cdd:COG4372  187 ELLKEANR 194
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
53-212 2.37e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  53 VDALQEQvtslQSQQDELEAQNAQLEAESQKLSEEIqalsskivARNESLKKQARSAQKTNTATSYINTILNSK--SISD 130
Cdd:PRK02224 467 VETIEED----RERVEELEAELEDLEEEVEEVEERL--------ERAEDLVEAEDRIERLEERREDLEELIAERreTIEE 534

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 131 AINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQEAINTV----AANKATIEQnQAALATQQAELEAAQLNLS---- 202
Cdd:PRK02224 535 KRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELnsklAELKERIES-LERIRTLLAAIADAEDEIErlre 613

                        170
                 ....*....|..
gi 497538983 203 --AQLATAEDEK 212
Cdd:PRK02224 614 krEALAELNDER 625
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 68-233 2.76e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  68 DELEAQNAQLEAES------QKLSEEIQALSSKI-VARNESLKKQARSAQKTntatsyintilnsksISDAINRVAAVRE 140
Cdd:COG1196  196 GELERQLEPLERQAekaeryRELKEELKELEAELlLLKLRELEAELEELEAE---------------LEELEAELEELEA 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 141 VVSANEKMLEQQEADKAAIEQKQAENQEAINTVAANKATIEQNQAALATQQAELEAAQLNLSAQLATAEDEKASLVAQKE 220
Cdd:COG1196  261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340

                        170
                 ....*....|...
gi 497538983 221 AAEQAAAEAAAAQ 233
Cdd:COG1196  341 ELEEELEEAEEEL 353
PRK11637 PRK11637
AmiB activator; Provisional
 31-211 3.04e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 39.68  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  31 QIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEaesQKLSEEIQALSSK--------IVARNESL 102
Cdd:PRK11637  76 QLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQE---RLLAAQLDAAFRQgehtglqlILSGEESQ 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 103 KKQARSAQktntaTSYINtilnsKSISDAINRVAAVREVVSANEKMLEQ-----------QEADKAAIEQKQAENQeaiN 171
Cdd:PRK11637 153 RGERILAY-----FGYLN-----QARQETIAELKQTREELAAQKAELEEkqsqqktllyeQQAQQQKLEQARNERK---K 219

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 497538983 172 TVAANKATIEQNQAALatqqAELEAAQLNLSAQLATAEDE 211
Cdd:PRK11637 220 TLTGLESSLQKDQQQL----SELRANESRLRDSIARAERE 255
bZIP_Fos_like cd14699
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a ...
 57-91 3.09e-03

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: 35.70  E-value: 3.09e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 497538983  57 QEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQAL 91
Cdd:cd14699   21 RELMEELQAEVEQLEDENEKLQSEIANLRSEKEQL 55
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 33-206 3.31e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 39.85  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  33 AAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAEsqklseeiQALSSKIVARNESLKKQARSAQKT 112
Cdd:PRK07994 369 EVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLP--------ETTSQLLAARQQLQRAQGATKAKK 440

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 113 NTATSYINTilnsKSISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQEAINTVAANKATIEQNQAALATQQA 192
Cdd:PRK07994 441 SEPAAASRA----RPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKALKKALEHEKTPELAAKL 516

                        170       180
                 ....*....|....*....|....*..
gi 497538983 193 ELEA----------AQLNLS---AQLA 206
Cdd:PRK07994 517 AAEAierdpwaalvSQLGLPglvEQLA 543
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
30-210 3.35e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  30 TQIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIvarnESLKKQARSA 109
Cdd:COG4372   94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL----ESLQEELAAL 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 110 QKTNTATSYINTILNSKSISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQEAINTVAANKATIEQNQAALAT 189
Cdd:COG4372  170 EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249

                        170       180
                 ....*....|....*....|.
gi 497538983 190 QQAELEAAQLNLSAQLATAED 210
Cdd:COG4372  250 ELLEEVILKEIEELELAILVE 270
bZIP_Fos_like cd14699
Basic leucine zipper (bZIP) domain of the oncogene Fos (Fos)-like transcription factors: a ...
 46-86 3.44e-03

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: 35.70  E-value: 3.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 497538983  46 QAAA------QSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSE 86
Cdd:cd14699   11 VAAAkcrqrrRELMEELQAEVEQLEDENEKLQSEIANLRSEKEQLEE 57
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 49-171 3.60e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.81  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  49 AQSQVDALQEQV----TSLQSQQDELEAQNAQLEA---ESQKLSEEIQALSSKIVARNESLKKQARSA--QKTNTATSYI 119
Cdd:PRK00409 507 AKKLIGEDKEKLneliASLEELERELEQKAEEAEAllkEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqQAIKEAKKEA 586

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 497538983 120 NTILNSKSISDAINRVAAVREVVSANEKMLEQQEADKAAIEQKQAENQEAIN 171
Cdd:PRK00409 587 DEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
29-195 4.83e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  29 DTQIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVARNESLKKQARS 108
Cdd:COG4372   72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983 109 AQKTNTATSYINTILNSKSISDAINRVAAVREVV-----SANEKMLEQQEADKAAIEQKQAENQEAINTVAANKATIEQN 183
Cdd:COG4372  152 LKELEEQLESLQEELAALEQELQALSEAEAEQALdellkEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231

                        170
                 ....*....|..
gi 497538983 184 QAALATQQAELE 195
Cdd:COG4372  232 GLALSALLDALE 243
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
 50-95 5.21e-03

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


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 35.72  E-value: 5.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 497538983  50 QSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKI 95
Cdd:COG3074   31 KEKNEELEQENEELQSENEELQSENEQLKTENAEWQERIRSLLGKI 76
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 26-211 5.99e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.44  E-value: 5.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983    26 DDYDTQIAAQDAVISNLTSEQAAAQSQVDAL------------------QEQVTSLQSQQDELEAQNAQLEAESQKLSEE 87
Cdd:pfam12128  297 DQWKEKRDELNGELSAADAAVAKDRSELEALedqhgafldadietaaadQEQLPSWQSELENLEERLKALTGKHQDVTAK 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983    88 IQALSSKIVARNeslkKQARSAQKTNTATSYINTILNSKSISDAINRV---------AAVREVVSANEKMLEQQEADKAA 158
Cdd:pfam12128  377 YNRRRSKIKEQN----NRDIAGIKDKLAKIREARDRQLAVAEDDLQALeselreqleAGKLEFNEEEYRLKSRLGELKLR 452

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 497538983   159 IEQKQAENQEAINtVAANKATIEQNQAALATQQAELEAAQLNLsAQLATAEDE 211
Cdd:pfam12128  453 LNQATATPELLLQ-LENFDERIERAREEQEAANAEVERLQSEL-RQARKRRDQ 503
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 30-215 6.14e-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: 39.23  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   30 TQIAAQDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNA--------------QLEAESQKLSEEIQALSSKI 95
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSekqreleekqneieKLKKENQSYKQEIKNLESQI 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   96 VARNESLKKQARSAQ----KTNTATSYINTIL------------NSKSISDAINRVAAVREVVSANEKMLEQQEAD---- 155
Cdd:TIGR04523 394 NDLESKIQNQEKLNQqkdeQIKKLQQEKELLEkeierlketiikNNSEIKDLTNQDSVKELIIKNLDNTRESLETQlkvl 473

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497538983  156 -------KAAIEQKQAE----NQEaINTVAANKATIEQNQAALATQQAELEAAQLNLSAQLATAEDEKASL 215
Cdd:TIGR04523 474 srsinkiKQNLEQKQKElkskEKE-LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
PRK11281 PRK11281
mechanosensitive channel MscK;
1-196 6.32e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.12  E-value: 6.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983    1 MKKRILSAVLVSGVTLGTAAATVNADDYDTQIAAQ---DAV--ISNLTSEQAAAQSQVDALQEQVTSLQSQQ---DELEA 72
Cdd:PRK11281    8 VFRAFIAFLFLLLCLSSAFARAASNGDLPTEADVQaqlDALnkQKLLEAEDKLVQQDLEQTLALLDKIDRQKeetEQLKQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   73 QNAQLEAESQKLSEEIQALSSKIVA------RNESLKK-QARSAQKTNtatsyintilnskSISDAINRVAAVREVVSAN 145
Cdd:PRK11281   88 QLAQAPAKLRQAQAELEALKDDNDEetretlSTLSLRQlESRLAQTLD-------------QLQNAQNDLAEYNSQLVSL 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 497538983  146 EKMLEQ-QEADKAAIEQKQAENQEAINTVAANKATIEQNQAALATQQAELEA 196
Cdd:PRK11281  155 QTQPERaQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNA 206
bZIP_CNC cd14698
Basic leucine zipper (bZIP) domain of Cap'n'Collar (CNC) transcription factors: a DNA-binding ...
 48-92 6.90e-03

Basic leucine zipper (bZIP) domain of Cap'n'Collar (CNC) transcription factors: a DNA-binding and dimerization domain; CNC proteins form a subfamily of Basic leucine zipper (bZIP) transcription factors that are defined by a conserved 43-amino acid region (called the CNC domain) located N-terminal to the bZIP DNA-binding domain. This subfamily includes Drosophila Cnc and four vertebrate counterparts, NFE2 (nuclear factor, erythroid-derived 2), NFE2-like 1 or NFE2-related factor 1 (NFE2L1 or Nrf1), NFE2L2 (or Nrf2), and NFE2L3 (or Nrf3). It also includes BACH1 and BACH2, which contain an additional BTB domain (Broad complex###Tramtrack###Bric-a-brac domain, also known as the POZ [poxvirus and zinc finger] domain). CNC proteins function during development and/or contribute in maintaining homeostasis during stress responses. In flies, Cnc functions both in development and in stress responses. In vertebrates, several CNC proteins encoded by distinct genes show varying functions and expression patterns. NFE2 is required for the proper development of platelets while the three Nrfs function in stress responses. Nrf2, the most extensively studied member of this subfamily, acts as a xenobiotic-activated receptor that regulates the adaptive response to oxidants and electrophiles. BACH1 forms heterodimers with small Mafs such as MafK to function as a repressor of heme oxygenase-1 (HO-1) gene (Hmox-1) enhancers. BACH2 is a B-cell specific transcription factor that plays a critical role in oxidative stress-mediated apoptosis. 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: 269846 [Multi-domain]  Cd Length: 68  Bit Score: 35.31  E-value: 6.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 497538983  48 AAQS-------QVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALS 92
Cdd:cd14698   17 AAQNcrkrkldQISTLEDEVDELKEEKEKLLKERDELEAETREMKDKYSQLY 68
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
 39-148 8.48e-03

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 38.92  E-value: 8.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   39 ISNLTSEQ-AAAQSQVDALQ-EQVTSLQSQQDELEAQNaqleaesQKLSEEIQALSSKIVARNESLKKQARSAQKTNTAT 116
Cdd:NF033875  190 LGNVSSKDlAAKEKEVDQLQkEQAKKIAQQAAELKAKN-------EKIAKENAEIAAKNKAEKERYEKEVAEYNKHKNEN 262

                          90       100       110
                  ....*....|....*....|....*....|..
gi 497538983  117 SYINTILNSKSISDainrvaavREVVSANEKM 148
Cdd:NF033875  263 GYVNEAISKNLVFD--------QSVVTKDTKI 286
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 47-210 8.65e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 38.52  E-value: 8.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983   47 AAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSK----IVAR------NESLK-KQARSAQKTNTA 115
Cdd:pfam05622 179 NALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEkerlIIERdtlretNEELRcAQLQQAELSQAD 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  116 TSyintilnSKSISDAINRVAAvrEVVSAN--EKMLEQQEADKAAIEQKQAENQEAINTVA-----ANKATIE-QNQAAL 187
Cdd:pfam05622 259 AL-------LSPSSDPGDNLAA--EIMPAEirEKLIRLQHENKMLRLGQEGSYRERLTELQqlledANRRKNElETQNRL 329

                         170       180
                  ....*....|....*....|....*...
gi 497538983  188 ATQ-----QAELEAAQLNLSAQLATAED 210
Cdd:pfam05622 330 ANQrilelQQQVEELQKALQEQGSKAED 357
PRK13729 PRK13729
conjugal transfer pilus assembly protein TraB; Provisional
 35-97 8.71e-03

conjugal transfer pilus assembly protein TraB; Provisional


Pssm-ID: 184281 [Multi-domain]  Cd Length: 475  Bit Score: 38.27  E-value: 8.71e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497538983  35 QDAVISNLTSEQAAAQSQVDALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIVA 97
Cdd:PRK13729  67 RQHATTEMQVTAAQMQKQYEEIRRELDVLNKQRGDDQRRIEKLGQDNAALAEQVKALGANPVT 129
DUF724 pfam05266
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ...
 55-109 8.82e-03

Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.


Pssm-ID: 428400 [Multi-domain]  Cd Length: 188  Bit Score: 37.25  E-value: 8.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 497538983   55 ALQEQVTSLQSQQDELEAQNAQLEAESQKLSEEIQALSSKIV--ARNESLKKQARSA 109
Cdd:pfam05266  99 SLKDRQTKLLEELKKLEKKIAEEESEKRKLEEEIDELEKKILelERQLALAKEKKEA 155
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 29-115 9.03e-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: 35.62  E-value: 9.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497538983  29 DTQIAAQDAVISNLTSEQAAAQSQVDALQEQV----TSLQSQQDELEA---QNAQLEAESQKLSEEIQALsskiVARneS 101
Cdd:cd22887    3 ESELQELEKRLAELEAELASLEEEIKDLEEELkeknKANEILNDELIAlqiENNLLEEKLRKLQEENDEL----VER--W 76

                         90
                 ....*....|....
gi 497538983 102 LKKQARSAQKTNTA 115
Cdd:cd22887   77 MAKKQQEADKMNEA 90
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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