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Conserved domains on  [gi|1485845428|ref|WP_119875826|]
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peptidoglycan hydrolase PcsB [Streptococcus respiraculi]

Protein Classification

CHAP domain-containing protein( domain architecture ID 11467527)

cysteine, histidine-dependent amidohydrolase/peptidase (CHAP) domain-containing protein may function as an amidase involved in the cleavage of peptidoglycan, such as Streptococcus pneumoniae PcsB

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];
273-394 1.67e-34

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


:

Pssm-ID: 443142 [Multi-domain]  Cd Length: 129  Bit Score: 123.95  E-value: 1.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 273 SVSAPQPKITYDSNNTYPWGQCTWGV----KTLAPWVGNYWGNAGQWLYSAQAAGFSIGSTPKVGAVAVWN---NTYWGH 345
Cdd:COG3942     5 SLGDGYPPNVVDPWNGYPYGQCTWYAawrrAQLGGPIGSGWGNANNWADNARAAGYTVGSTPKVGAVAVFTpgvAGPYGH 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1485845428 346 VAVVTAVNGNQ-IQVMEANYGGDG-YNADPRGIGNyrgwfvpTGVTGYIYP 394
Cdd:COG3942    85 VAVVESVNSDGsILVSEMNWGGPGiYSTRTISAGN-------ASSYGFIHP 128
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 31-394 3.60e-33

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


:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 127.64  E-value: 3.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  31 DSKIAAQDNKIKEIASQQATAQAQVDAVQAQVDSIVAEQTSLTAENERLEAETQALSAEIEKLAGDIVSRDEALKKQARS 110
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 111 AQTDGSATSYINTILDSKSIVDALSRVNAMREIVAANNRMLGQQKADKEAIEEKQKSNQEAINTLIANLRKLDEDAKVLE 190
Cdd:COG3883    95 LYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 191 ARQAELKVAQLNLAAEKATAEDEKQALIEEKAAAQAAAQAAAAAQAAYQAQQAAAAQAAVSQSQQPVVSNVVSNPSSDTS 270
Cdd:COG3883   175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 271 GPSVSAPQPKITYDSNNTYPWGQCTWGVkTLAPWVGNYWGNAGQWLYSAQAAGFSIGSTPKVGAVAVWNNTYWGHVAVVT 350
Cdd:COG3883   255 AGAAAGSAGAAGAAAGAAGAGAAAASAA-GGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGG 333

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1485845428 351 AVNGNQIQVMEANYGGDGYNADPRGIGNYRGWFVPTGVTGYIYP 394
Cdd:COG3883   334 SGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGGGVGLSVGGGYVG 377
 
Name Accession Description Interval E-value
COG3942 COG3942
Surface antigen [Cell wall/membrane/envelope biogenesis];
273-394 1.67e-34

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


Pssm-ID: 443142 [Multi-domain]  Cd Length: 129  Bit Score: 123.95  E-value: 1.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 273 SVSAPQPKITYDSNNTYPWGQCTWGV----KTLAPWVGNYWGNAGQWLYSAQAAGFSIGSTPKVGAVAVWN---NTYWGH 345
Cdd:COG3942     5 SLGDGYPPNVVDPWNGYPYGQCTWYAawrrAQLGGPIGSGWGNANNWADNARAAGYTVGSTPKVGAVAVFTpgvAGPYGH 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1485845428 346 VAVVTAVNGNQ-IQVMEANYGGDG-YNADPRGIGNyrgwfvpTGVTGYIYP 394
Cdd:COG3942    85 VAVVESVNSDGsILVSEMNWGGPGiYSTRTISAGN-------ASSYGFIHP 128
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 31-394 3.60e-33

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 127.64  E-value: 3.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  31 DSKIAAQDNKIKEIASQQATAQAQVDAVQAQVDSIVAEQTSLTAENERLEAETQALSAEIEKLAGDIVSRDEALKKQARS 110
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 111 AQTDGSATSYINTILDSKSIVDALSRVNAMREIVAANNRMLGQQKADKEAIEEKQKSNQEAINTLIANLRKLDEDAKVLE 190
Cdd:COG3883    95 LYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 191 ARQAELKVAQLNLAAEKATAEDEKQALIEEKAAAQAAAQAAAAAQAAYQAQQAAAAQAAVSQSQQPVVSNVVSNPSSDTS 270
Cdd:COG3883   175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 271 GPSVSAPQPKITYDSNNTYPWGQCTWGVkTLAPWVGNYWGNAGQWLYSAQAAGFSIGSTPKVGAVAVWNNTYWGHVAVVT 350
Cdd:COG3883   255 AGAAAGSAGAAGAAAGAAGAGAAAASAA-GGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGG 333

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1485845428 351 AVNGNQIQVMEANYGGDGYNADPRGIGNYRGWFVPTGVTGYIYP 394
Cdd:COG3883   334 SGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGGGVGLSVGGGYVG 377
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
 286-363 7.31e-22

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: 88.63  E-value: 7.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 286 NNTYPWGQCTWGVKTLAPWVGNYWGNAGQWLYSAQAAGFSIGSTPKVGAVAVWN----NTYWGHVAVVTAVNGNQIQVME 361
Cdd:pfam05257   2 GNGYPWGQCTWFVYWRVAQLGIYLGNAGDWADAAAGAYKVGSTTPKVGDIVVFDpgggGASYGHVAIVEKVNDGSITVSE 81


                  ..
gi 1485845428 362 AN 363
Cdd:pfam05257  82 QN 83
PRK08581 PRK08581
amidase domain-containing protein;
263-368 1.43e-12

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 69.05  E-value: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 263 SNPSSDTSGPSVSAPQPKITYDSNNTYPWGQCTWGV----KTLAPWVGNYWGNAGQWLYSAQAAGFSIGSTPKVGAVAVW 338
Cdd:PRK08581  482 YESSIKDYDDSSSEFKPFREYSGSSPYPHGQCTWYVynrmKQFGTSISGDLGDAHNWNNRAQARGYQVSHTPKRHAAVVF 561

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1485845428 339 N------NTYWGHVAVVTAVNG-NQIQVMEANYGGDG 368
Cdd:PRK08581  562 EagqagaDQHYGHVAFVEKVNSdGSIVISESNVKGLG 598
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 31-217 2.17e-06

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: 50.06  E-value: 2.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428   31 DSKIAAQDNKIKEIASQQATAQAQVDAVQAQVDSIVAEQTSLTAENERLEAETQALSAEIEKLAGDIvsrdEALKKQARS 110
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK----QILRERLAN 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  111 AQTDGSATSYINTILDSKSIVDAlsrvnamrEIVAANNRMLGQQKADKEAIEEKQKSNQEAINTLIANLRKLDEDAKVLE 190
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELA--------EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385

                          170       180
                   ....*....|....*....|....*..
gi 1485845428  191 ARQAELKVAQLNLAAEKATAEDEKQAL 217
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERL 412
DivIC pfam04977
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and ...
 67-110 5.36e-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: 37.97  E-value: 5.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1485845428  67 AEQTSLTAENERLEAETQALSAEIEKLAGDivsrDEALKKQARS 110
Cdd:pfam04977  13 QEIAQLQAEIAKLKQENEELEAEIKDLKSD----PDYIEERARS 52
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-214 8.06e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 8.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  33 KIAAQDNKIKEIASQQATAQAQVDAVQAQV---DSIVAEQTSLTAENERLEAETQALSA---EIEKLAGDIVSRDEALKK 106
Cdd:PRK03918  201 ELEEVLREINEISSELPELREELEKLEKEVkelEELKEEIEELEKELESLEGSKRKLEEkirELEERIEELKKEIEELEE 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 107 QA-RSAQTDGSATSYI------NTILDSKS-IVDALSRVNAMREIVAANNRMLGQQKADKEAIEEKQKSNQEAINTLIAN 178
Cdd:PRK03918  281 KVkELKELKEKAEEYIklsefyEEYLDELReIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1485845428 179 LRKLdEDAKVLEARQAELKVAQLNLAAEKATAEDEK 214
Cdd:PRK03918  361 HELY-EEAKAKKEELERLKKRLTGLTPEKLEKELEE 395
 
Name Accession Description Interval E-value
COG3942 COG3942
Surface antigen [Cell wall/membrane/envelope biogenesis];
273-394 1.67e-34

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


Pssm-ID: 443142 [Multi-domain]  Cd Length: 129  Bit Score: 123.95  E-value: 1.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 273 SVSAPQPKITYDSNNTYPWGQCTWGV----KTLAPWVGNYWGNAGQWLYSAQAAGFSIGSTPKVGAVAVWN---NTYWGH 345
Cdd:COG3942     5 SLGDGYPPNVVDPWNGYPYGQCTWYAawrrAQLGGPIGSGWGNANNWADNARAAGYTVGSTPKVGAVAVFTpgvAGPYGH 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1485845428 346 VAVVTAVNGNQ-IQVMEANYGGDG-YNADPRGIGNyrgwfvpTGVTGYIYP 394
Cdd:COG3942    85 VAVVESVNSDGsILVSEMNWGGPGiYSTRTISAGN-------ASSYGFIHP 128
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 31-394 3.60e-33

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 127.64  E-value: 3.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  31 DSKIAAQDNKIKEIASQQATAQAQVDAVQAQVDSIVAEQTSLTAENERLEAETQALSAEIEKLAGDIVSRDEALKKQARS 110
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 111 AQTDGSATSYINTILDSKSIVDALSRVNAMREIVAANNRMLGQQKADKEAIEEKQKSNQEAINTLIANLRKLDEDAKVLE 190
Cdd:COG3883    95 LYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 191 ARQAELKVAQLNLAAEKATAEDEKQALIEEKAAAQAAAQAAAAAQAAYQAQQAAAAQAAVSQSQQPVVSNVVSNPSSDTS 270
Cdd:COG3883   175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 271 GPSVSAPQPKITYDSNNTYPWGQCTWGVkTLAPWVGNYWGNAGQWLYSAQAAGFSIGSTPKVGAVAVWNNTYWGHVAVVT 350
Cdd:COG3883   255 AGAAAGSAGAAGAAAGAAGAGAAAASAA-GGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGG 333

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1485845428 351 AVNGNQIQVMEANYGGDGYNADPRGIGNYRGWFVPTGVTGYIYP 394
Cdd:COG3883   334 SGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGGGVGLSVGGGYVG 377
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
 286-363 7.31e-22

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: 88.63  E-value: 7.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 286 NNTYPWGQCTWGVKTLAPWVGNYWGNAGQWLYSAQAAGFSIGSTPKVGAVAVWN----NTYWGHVAVVTAVNGNQIQVME 361
Cdd:pfam05257   2 GNGYPWGQCTWFVYWRVAQLGIYLGNAGDWADAAAGAYKVGSTTPKVGDIVVFDpgggGASYGHVAIVEKVNDGSITVSE 81


                  ..
gi 1485845428 362 AN 363
Cdd:pfam05257  82 QN 83
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1-220 8.48e-19

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: 87.13  E-value: 8.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428   1 MKKKILASLLVSTIALTTVGNVLDVKAD--DTDSKIAAQDNKIKEIASQQATAQAQVDAVQAQVDSIVAEQTSLTAENER 78
Cdd:COG4942     1 MRKLLLLALLLALAAAAQADAAAEAEAEleQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  79 LEAETQALSAEIEKLAGDIVSRDEALKKQARSAQTDGSAtSYINTILDSKSIVDALSRVNAMREIVAANNRMLGQQKADK 158
Cdd:COG4942    81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1485845428 159 EAIEEKQKSNQEAINTLIANLRKLDEDAKVLEARQAELKVAQLNLAAEKATAEDEKQALIEE 220
Cdd:COG4942   160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
PRK08581 PRK08581
amidase domain-containing protein;
263-368 1.43e-12

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 69.05  E-value: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 263 SNPSSDTSGPSVSAPQPKITYDSNNTYPWGQCTWGV----KTLAPWVGNYWGNAGQWLYSAQAAGFSIGSTPKVGAVAVW 338
Cdd:PRK08581  482 YESSIKDYDDSSSEFKPFREYSGSSPYPHGQCTWYVynrmKQFGTSISGDLGDAHNWNNRAQARGYQVSHTPKRHAAVVF 561

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1485845428 339 N------NTYWGHVAVVTAVNG-NQIQVMEANYGGDG 368
Cdd:PRK08581  562 EagqagaDQHYGHVAFVEKVNSdGSIVISESNVKGLG 598
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-220 1.06e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  26 KADDTDSKIAAQDNKIKEIASQQATAQAQVDAVQAQVDSIVAEQTSLTAENERLEAETQALSAEIEKLAGDIVSRDEALK 105
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 106 -KQARSAQTDGSATSYINTI-LDSKSIVDALSRVNAMREIVAANNRMLGQQKADKEAIEEKQKSNQEAINTLIANLRKLD 183
Cdd:COG1196   313 eLEERLEELEEELAELEEELeELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1485845428 184 EDAKVLEARQAELKVAQLNLAAEKATAEDEKQALIEE 220
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
77-221 7.08e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 7.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428   77 ERLEAETQALSAEIEKLAGDIVSRDEALKKQARSAQTDGSATSYINTILDSKSIVDALSRVNAMREIVAANNRMLGQQKA 156
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEE 692

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1485845428  157 DKEAIEEKQKSNQEAINTLIANLRKLDEDakvLEARQAELKVAQLNLAAEKATAEDEKQALIEEK 221
Cdd:COG4913    693 QLEELEAELEELEEELDELKGEIGRLEKE---LEQAEEELDELQDRLEAAEDLARLELRALLEER 754
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 22-221 1.42e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  22 VLDVKADDTDSKIAAQDNKIKEIASQQATAQAQVDAVQAQVDSIVAEQTSLTAENERLEAETQALSAEIEKLAGDIVSRD 101
Cdd:COG1196   257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 102 EALKKQARSAQtdgsatsyintildsksivDALSRVNAMREIVAANNRMLGQQKADKEAIEEKQKSNQEAINTLIANLRK 181
Cdd:COG1196   337 EELEELEEELE-------------------EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1485845428 182 LDEDAKVLEARQAELKVAQLNLAAEKATAEDEKQALIEEK 221
Cdd:COG1196   398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 60-220 3.87e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 3.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  60 AQVDSIVAEQTSLTAENERLEAETQALSAEIEKLAGDIvsrdEALKKQARSAQTDGSATsyintildSKSIVDALSRVNA 139
Cdd:COG1196   232 LKLRELEAELEELEAELEELEAELEELEAELAELEAEL----EELRLELEELELELEEA--------QAEEYELLAELAR 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 140 MREIVAANNRMLGQQKADKEAIEEKQKSNQEAINTLIANLRKLDEDAKVLEARQAELKVAQLNLAAEKATAEDEKQALIE 219
Cdd:COG1196   300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379


                  .
gi 1485845428 220 E 220
Cdd:COG1196   380 E 380
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 31-217 2.17e-06

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: 50.06  E-value: 2.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428   31 DSKIAAQDNKIKEIASQQATAQAQVDAVQAQVDSIVAEQTSLTAENERLEAETQALSAEIEKLAGDIvsrdEALKKQARS 110
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK----QILRERLAN 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  111 AQTDGSATSYINTILDSKSIVDAlsrvnamrEIVAANNRMLGQQKADKEAIEEKQKSNQEAINTLIANLRKLDEDAKVLE 190
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELA--------EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385

                          170       180
                   ....*....|....*....|....*..
gi 1485845428  191 ARQAELKVAQLNLAAEKATAEDEKQAL 217
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERL 412
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 56-230 4.18e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 4.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  56 DAVQAQVDSIVAEQTSLTAENERLEAETQALSAEIEKLAGDIvsrdEALKKQARSAQtdgsatsyintildsKSIVDALS 135
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL----EELELELEEAQ---------------AEEYELLA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 136 RVNAMREIVAANNRMLGQQKADKEAIEEKQKSNQEAINTLIANLRKLDEDAKVLEARQAELKVAQLNLAAEKATAEDEKQ 215
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                         170
                  ....*....|....*
gi 1485845428 216 ALIEEkaaAQAAAQA 230
Cdd:COG1196   376 EAEEE---LEELAEE 387
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 58-220 2.85e-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: 2.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428   58 VQAQVDSIVAEQTSLTAENERLEAETQALSAEI---EKLAGDIVSRDEALKKQARSAQtdgsatsyiNTILDSKSIVDAL 134
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDELSQELsdaSRKIGEIEKEIEQLEQEEEKLK---------ERLEELEEDLSSL 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  135 SR-VNAMREIVAANNRMLGQQKADKEAIEE-----KQKSNQEAINTLIANLRKLDEDAKVLEARQAELKVAQLNLAAEKA 208
Cdd:TIGR02169  750 EQeIENVKSELKELEARIEELEEDLHKLEEalndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829

                          170
                   ....*....|..
gi 1485845428  209 TAEDEKQALIEE 220
Cdd:TIGR02169  830 YLEKEIQELQEQ 841
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 32-217 4.93e-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: 45.44  E-value: 4.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428   32 SKIAAQDNKIKEIASQQATAQAQVDAVQAQVDSIVAEQTSLTAENERLEAETQALSAEIEKLAGDIVSRDEALKKQARSA 111
Cdd:TIGR02169  709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL 788

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  112 qtdgsATSYINTILDSKSIVDA-LSRVNA-MREI-VAANNRMLGQQKADKE---------AIEEKQKSNQEAINTLIANL 179
Cdd:TIGR02169  789 -----SHSRIPEIQAELSKLEEeVSRIEArLREIeQKLNRLTLEKEYLEKEiqelqeqriDLKEQIKSIEKEIENLNGKK 863

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1485845428  180 RKLDEDAKVLEARQAELKVAQLNLAAEKATAEDEKQAL 217
Cdd:TIGR02169  864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
55-206 7.73e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 7.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428   55 VDAVQAQVDSIVAEQTSLTAENERLEAETQALSAEIEKLAGDIVSRD----EALKKQARSAQTDgsatsyINTILDSKSI 130
Cdd:COG4913    290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgdrlEQLEREIERLERE------LEERERRRAR 363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  131 VDALSR-----VNAMREIVAANNRMLgqqKADKEAIEEKQKSNQEAINTLIANLRKLDEDAKVLEARQAELKVAQLNLAA 205
Cdd:COG4913    364 LEALLAalglpLPASAEEFAALRAEA---AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA 440


                   .
gi 1485845428  206 E 206
Cdd:COG4913    441 R 441
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 33-221 1.09e-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: 43.37  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  33 KIAAQDNKIKEIASQQATAQAQVDAVQAQVDSIVAEQTSLTAENERLEAETQALSAEIEKLagdivsrdEALKKQARSAQ 112
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV--------EARIKKYEEQL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 113 tdgsatsyiNTILDSKSIVDALSRVNAM-REIVAANNRMLGQQkadkEAIEEKQKsnqeaintlianlrKLDEDAKVLEA 191
Cdd:COG1579    83 ---------GNVRNNKEYEALQKEIESLkRRISDLEDEILELM----ERIEELEE--------------ELAELEAELAE 135

                         170       180       190
                  ....*....|....*....|....*....|
gi 1485845428 192 RQAELKVAQLNLAAEKATAEDEKQALIEEK 221
Cdd:COG1579   136 LEAELEEKKAELDEELAELEAELEELEAER 165
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 29-219 1.78e-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: 43.89  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428   29 DTDSKIAAQDNKIKEIASQQATAQAQVDAVQAQVDSIVAEQTSLTAENERLEAETQALSAEieklAGDIVSRDEALKKQA 108
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE----AANLRERLESLERRI 833

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  109 RSAQtdgsatsyintildsKSIVDALSRVNAMREIVAANNRMLGQQKADKEAIEEK-------QKSNQEAINTLIANLRK 181
Cdd:TIGR02168  834 AATE---------------RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEleallneRASLEEALALLRSELEE 898

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1485845428  182 LDEDAKVLEARQAELKvAQLNLAAEKATAEDEKQALIE 219
Cdd:TIGR02168  899 LSEELRELESKRSELR-RELEELREKLAQLELRLEGLE 935
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
28-221 2.37e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 2.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  28 DDTDSKIAAQDNKIKEIASQQATAQAQVDAVQAQVDSIVAEQTSLTAENERLEAETQALSAEIEKLAGDIVSRDEALKKQ 107
Cdd:COG4372    76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 108 ARSAQTDGSATSYINTILDSKSIVDALSRVNAMREivAANNRMLGQQKADkeaiEEKQKSNQEAINTLIANLRKLDEDAK 187
Cdd:COG4372   156 EEQLESLQEELAALEQELQALSEAEAEQALDELLK--EANRNAEKEEELA----EAEKLIESLPRELAEELLEAKDSLEA 229

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1485845428 188 VLEARQAELKVAQLNLAAEKATAEDEKQALIEEK 221
Cdd:COG4372   230 KLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
DivIC pfam04977
Septum formation initiator; DivIC from B. subtilis is necessary for both vegetative and ...
 67-110 5.36e-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: 37.97  E-value: 5.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1485845428  67 AEQTSLTAENERLEAETQALSAEIEKLAGDivsrDEALKKQARS 110
Cdd:pfam04977  13 QEIAQLQAEIAKLKQENEELEAEIKDLKSD----PDYIEERARS 52
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
33-214 8.06e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 8.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  33 KIAAQDNKIKEIASQQATAQAQVDAVQAQV---DSIVAEQTSLTAENERLEAETQALSA---EIEKLAGDIVSRDEALKK 106
Cdd:PRK03918  201 ELEEVLREINEISSELPELREELEKLEKEVkelEELKEEIEELEKELESLEGSKRKLEEkirELEERIEELKKEIEELEE 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 107 QA-RSAQTDGSATSYI------NTILDSKS-IVDALSRVNAMREIVAANNRMLGQQKADKEAIEEKQKSNQEAINTLIAN 178
Cdd:PRK03918  281 KVkELKELKEKAEEYIklsefyEEYLDELReIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1485845428 179 LRKLdEDAKVLEARQAELKVAQLNLAAEKATAEDEK 214
Cdd:PRK03918  361 HELY-EEAKAKKEELERLKKRLTGLTPEKLEKELEE 395
FtsB COG2919
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
61-110 8.40e-04

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


Pssm-ID: 442163 [Multi-domain]  Cd Length: 96  Bit Score: 38.32  E-value: 8.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1485845428  61 QVDSIVAEQTSLTAENERLEAETQALSAEIEKLAgdivSRDEALKKQARS 110
Cdd:COG2919    30 AYRELRQEIAELEAENAKLKARNAELEAEVADLK----DGPDYIEERARE 75
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 136-220 1.43e-03

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: 38.36  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 136 RVNAMREIVAANNRMLgQQKADKEAIEEKQKSNQEAINTLIANLRKLDEDAKVLEARQAELKVAQLNLAAEKATAEDEKQ 215
Cdd:pfam20492   1 REEAEREKQELEERLK-QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKE 79


                  ....*
gi 1485845428 216 ALIEE 220
Cdd:pfam20492  80 QLEAE 84
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
55-220 3.63e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  55 VDAVQAQVDSIVAEQTSLTAENERLEAETQALSAEIEKLAGDIVSRDEALkkQARSAQTDGSATSYINTILDSKSIVDAL 134
Cdd:COG4372    40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL--QAAQAELAQAQEELESLQEEAEELQEEL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 135 SRVNAMREIVAANNRmlgQQKADKEAIEEKQKSNQEAINTLIANLRKLDEDAKVLEARQAELKVAQLNLAAEKATAEDEK 214
Cdd:COG4372   118 EELQKERQDLEQQRK---QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANR 194


                  ....*.
gi 1485845428 215 QALIEE 220
Cdd:COG4372   195 NAEKEE 200
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 59-220 5.22e-03

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: 39.27  E-value: 5.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428   59 QAQVDSIVAEQTSLTAENERLEAETQALSAEIEKLAGDIVSRDEALKkQARSAQTDGSATS-YINTILDSKSIvdALSRV 137
Cdd:TIGR02168  224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE-ELRLEVSELEEEIeELQKELYALAN--EISRL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  138 NAMREIVAANNRMLGQQKADKEA-IEEKQKSNQEAINTLIANLRKLDEDAKVLEARQAELKVAQlNLAAEKATAEDEKQA 216
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE-AELEELESRLEELEE 379


                   ....
gi 1485845428  217 LIEE 220
Cdd:TIGR02168  380 QLET 383
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
59-220 6.06e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 6.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428  59 QAQVDSIVAEQTSLTAENERLEAETQALSAEIEKLAGDIVSRDEALKKQARSAQ-TDGSATSYintildSKSIVDALSRV 137
Cdd:PRK02224  285 RERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQaHNEEAESL------REDADDLEERA 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485845428 138 NAMREivaannrmlgqqkaDKEAIEEKQKSNQEAINTLIANLRKLDEDAKVLEARQAELKVAQLNLAAEKATAEDEKQAL 217
Cdd:PRK02224  359 EELRE--------------EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424


                  ...
gi 1485845428 218 IEE 220
Cdd:PRK02224  425 RER 427
 
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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