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Conserved domains on  [gi|20072378|gb|AAH26645|]
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Efcab4a protein, partial [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 67-223 1.36e-09

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 1.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378  67 LEEVLMRASACLEAAAREREGLEQALRRRESEHEREVRGLYEELEQ--QLGEQRHRRQSQNLPREEQRGHLELELQTREQ 144
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20072378 145 ELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRNMQKE 223
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 67-223 1.36e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 1.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378  67 LEEVLMRASACLEAAAREREGLEQALRRRESEHEREVRGLYEELEQ--QLGEQRHRRQSQNLPREEQRGHLELELQTREQ 144
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20072378 145 ELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRNMQKE 223
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 67-221 3.10e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 3.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378     67 LEEVLMRASACLEAAAREREGLEQALRRRESEHEREVRGLYEELEQQlgeQRHRRQSQNLprEEQRGHLELELQTREQEL 146
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL---ARLEAEVEQL--EERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378    147 ERAGLRQRELEQQLQARAAE--QLEAQAQhiQLQRAYEAIRAQLDQAQEQLSRLEGEA---QGRQEQTQRDVVAVSRNMQ 221
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEieELEAQIE--QLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLE 841
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 135-218 9.79e-04

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.71  E-value: 9.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378   135 LELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQlsRLEGEAQGRQEQTQRDVV 214
Cdd:PRK11448  147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEK--AAETSQERKQKRKEITDQ 224


                  ....
gi 20072378   215 AVSR 218
Cdd:PRK11448  225 AAKR 228
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 135-219 6.45e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 37.79  E-value: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378   135 LELELQTREQELERAGL---RQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLE-----GEAQGRQ 206
Cdd:pfam00529  63 AEAQLAKAQAQVARLQAeldRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapiGGISRES 142

                          90
                  ....*....|...
gi 20072378   207 EQTQRDVVAVSRN 219
Cdd:pfam00529 143 LVTAGALVAQAQA 155
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 67-223 1.36e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 1.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378  67 LEEVLMRASACLEAAAREREGLEQALRRRESEHEREVRGLYEELEQ--QLGEQRHRRQSQNLPREEQRGHLELELQTREQ 144
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20072378 145 ELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRNMQKE 223
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 62-265 1.79e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 1.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378  62 ELLGSLEEVLMRASACLEAAAREREGLEQALRRRESEHEREVRGLYEELEQ--QLGEQRHRRQSQNLPREEQRGHLELEL 139
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEEL 325

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378 140 QTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRN 219
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 20072378 220 MQKEKLSLLRQLELLRELNLRLRDERDACETKLLGSSHRKALAIAH 265
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 57-224 2.37e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 2.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378  57 QRERPELLGSLEEVLMRASACLEAAAREREGLEQALRRRESEHEREVRGLYEELEQQLGEQRHRRQSQNlpreeQRGHLE 136
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA-----QLEELE 406

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378 137 LELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAV 216
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486


                ....*...
gi 20072378 217 SRNMQKEK 224
Cdd:COG1196 487 AEAAARLL 494
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 62-247 5.33e-08

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: 5.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378  62 ELLGSLEEVLMRASACLEAAAREREGLEQALRRRESEHEREVRGlyEELEQQLGEQRHRRQSQNLPREEQRGHLELELQT 141
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL--EEELEELEEELEELEEELEEAEEELEEAEAELAE 362

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378 142 REQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRNMQ 221
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442

                       170       180
                ....*....|....*....|....*.
gi 20072378 222 KEKLSLLRQLELLRELNLRLRDERDA 247
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAEL 468
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 107-264 4.71e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 4.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378 107 YEELEQQLGEQRHRRQSQnlprEEQRGHLELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRA 186
Cdd:COG1196 234 LRELEAELEELEAELEEL----EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20072378 187 QLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRNMQKEKLSLLRQLELLRELNLRLRDERDACETKLLGSSHRKALAIA 264
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
73-219 2.43e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378   73 RASACLEAAAREREGLEQALRRRESEHEREVRGLyEELEQQLGEQRHRRQSQNLPR----EEQRGHLELELQTREQELER 148
Cdd:COG4913  285 FAQRRLELLEAELEELRAELARLEAELERLEARL-DALREELDELEAQIRGNGGDRleqlEREIERLERELEERERRRAR 363

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20072378  149 AGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRN 219
Cdd:COG4913  364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 67-221 3.10e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 3.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378     67 LEEVLMRASACLEAAAREREGLEQALRRRESEHEREVRGLYEELEQQlgeQRHRRQSQNLprEEQRGHLELELQTREQEL 146
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL---ARLEAEVEQL--EERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378    147 ERAGLRQRELEQQLQARAAE--QLEAQAQhiQLQRAYEAIRAQLDQAQEQLSRLEGEA---QGRQEQTQRDVVAVSRNMQ 221
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEieELEAQIE--QLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAATERRLE 841
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
108-210 4.85e-05

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 44.27  E-value: 4.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378 108 EELEQQLGEQRHRRQSQ--NLPREEQRGHLELELQTREQELERAGLRQRELEQQLQAR---AAEQLEAQAQHIQLQRAYE 182
Cdd:COG1566  79 TDLQAALAQAEAQLAAAeaQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYqalYKKGAVSQQELDEARAALD 158

                        90       100
                ....*....|....*....|....*...
gi 20072378 183 AIRAQLDQAQEQLSRLEGEAQGRQEQTQ 210
Cdd:COG1566 159 AAQAQLEAAQAQLAQAQAGLREEEELAA 186
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 62-208 6.88e-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: 44.29  E-value: 6.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378     62 ELLGSLEEVLMRasacLEAAAREREGLEQALRRRESeherevrgLYEELEQQLGEQRHRRQSQNLPREEQRGHLELELQT 141
Cdd:TIGR02169  798 AELSKLEEEVSR----IEARLREIEQKLNRLTLEKE--------YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20072378    142 REQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQ 208
Cdd:TIGR02169  866 LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-208 7.02e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 7.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378  78 LEAAAREREGLEQALRRRESEHEREVRGLyEELEQQLGEQRHRRQSQNLpREEQRGHLELELQTREQELERAGLRQRELE 157
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERR 311

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 20072378 158 QQLQARAAEqleAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQ 208
Cdd:COG1196 312 RELEERLEE---LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-245 7.67e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 7.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378  66 SLEEVLMRASACLEAAAREREGLEQALRRRESEHEREVRGLYEELEQQLGEQRHRRQSQNLPREEQRGHLELELQTREQE 145
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378 146 LERAGLRQRELE-----QQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRNM 220
Cdd:COG1196 386 EELLEALRAAAElaaqlEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465

                       170       180
                ....*....|....*....|....*
gi 20072378 221 QKEKLSLLRQLELLRELNLRLRDER 245
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAA 490
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 106-252 8.16e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 8.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378 106 LYEELEQQLGE--------QRHRRQSQNLpREEQRGHLELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQL 177
Cdd:COG1196 194 ILGELERQLEPlerqaekaERYRELKEEL-KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20072378 178 QRAYEAIRAQLDQAQEQLSRLEGEAQgRQEQTQRDVVAVSRNMQKEKLSLLRQLELLRELNLRLRDERDACETKL 252
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
78-215 1.61e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378   78 LEAAAREREGLEQALRRRESEHEREvrglyEELEQQLGEQRHRRQSQNLPREEQRGHLELELQTREQELERAGLRQ---- 153
Cdd:COG4913  612 LAALEAELAELEEELAEAEERLEAL-----EAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAssdd 686

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20072378  154 -RELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVA 215
Cdd:COG4913  687 lAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
35-212 4.85e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 4.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378   35 EKLGVARVLGEQWAVRTLWVGLQRERPELLGSLEEvLMRASACLEAAAREREGLEQALrrreseherevrglyEELEQQL 114
Cdd:COG4913  645 ERREALQRLAEYSWDEIDVASAEREIAELEAELER-LDASSDDLAALEEQLEELEAEL---------------EELEEEL 708

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378  115 GEQRHRRQSqnlpreeqrghLELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQ 194
Cdd:COG4913  709 DELKGEIGR-----------LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDA 777

                        170
                 ....*....|....*...
gi 20072378  195 LSRLEGEAQGRQEQTQRD 212
Cdd:COG4913  778 LRARLNRAEEELERAMRA 795
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 56-212 9.45e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 9.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378  56 LQRERPELLGSLEEVLMRASACLEAAAREREGLEQALRrreseherevrglyeeLEQQLGEQRHRRQSQNLPREEQRGHL 135
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE----------------RLERLEEELEELEEALAELEEEEEEE 440

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20072378 136 ELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRD 212
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 135-218 9.79e-04

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.71  E-value: 9.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378   135 LELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQlsRLEGEAQGRQEQTQRDVV 214
Cdd:PRK11448  147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEK--AAETSQERKQKRKEITDQ 224


                  ....
gi 20072378   215 AVSR 218
Cdd:PRK11448  225 AAKR 228
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 112-224 1.01e-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: 40.81  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378    112 QQLGEQRHRRQSQNLPREEQRGHLELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQA 191
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314

                           90       100       110
                   ....*....|....*....|....*....|...
gi 20072378    192 QEQLSRLegEAQGRQEQTQRDVVAVSRNMQKEK 224
Cdd:TIGR02168  315 ERQLEEL--EAQLEELESKLDELAEELAELEEK 345
PTZ00121 PTZ00121
MAEBL; Provisional
 57-247 1.05e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378    57 QRERPELLGSLEEVLMRASAcLEAAAREREGLEQALRRRESEHEREVRGLYEELEQQLGEQRHRRQSQNLPREEQRGHLE 136
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEE-AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378   137 LELQTREQELERAGLRQRELEQQLQARAAEQleAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAV 216
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEEA--KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748

                         170       180       190
                  ....*....|....*....|....*....|.
gi 20072378   217 SRNMQKEKLSLLRQLELLRELNLRLRDERDA 247
Cdd:PTZ00121 1749 AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
138-199 1.15e-03

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 40.03  E-value: 1.15e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20072378 138 ELQTREQELERAGLRQRELEQQLQArAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLE 199
Cdd:COG1566 149 ELDEARAALDAAQAQLEAAQAQLAQ-AQAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
64-218 1.63e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 1.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378  64 LGSLEEVLMRASACLEAAAREREGLEQALRRRESEHEREVR-GLYEELEQQLGEQRHRRQS------------------- 123
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQsPVIQQLRAQLAELEAELAElsarytpnhpdvialraqi 300

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378 124 ----QNLPREEQRGHLELELQTREQELERAGLRQREleQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAqeqLSRLE 199
Cdd:COG3206 301 aalrAQLQQEAQRILASLEAELEALQAREASLQAQL--AQLEARLAELPELEAELRRLEREVEVARELYESL---LQRLE 375

                       170
                ....*....|....*....
gi 20072378 200 gEAQGRQEQTQRDVVAVSR 218
Cdd:COG3206 376 -EARLAEALTVGNVRVIDP 393
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 128-221 2.12e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 2.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378 128 REEQRGHLELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQE 207
Cdd:COG4942  25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104

                        90
                ....*....|....
gi 20072378 208 QTQRDVVAVSRNMQ 221
Cdd:COG4942 105 ELAELLRALYRLGR 118
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 135-199 2.16e-03

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 39.16  E-value: 2.16e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20072378 135 LELELQTREQELERAGLRQRELEQQLQ---------ARAAEQLE-AQAQHIQLQRAYEAIRAQLDQAQEQLSRLE 199
Cdd:COG0845  59 LQAALAQAQAQLAAAQAQLELAKAELErykallkkgAVSQQELDqAKAALDQAQAALAAAQAALEQARANLAYTT 133
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
59-211 3.25e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 3.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378   59 ERPELLGSLEEV------LMRASACLEAAAREREGLEQALRRRESeherevrglYEELEQQLGEQRHRRQSQNLpreeQR 132
Cdd:COG4913  219 EEPDTFEAADALvehfddLERAHEALEDAREQIELLEPIRELAER---------YAAARERLAELEYLRAALRL----WF 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378  133 GHLELELQTREQELERAglrqrELEQQLQARAAEQLEAQAQHIQLQRAYEAIR----AQLDQAQEQLSRLEGEAQGRQEQ 208
Cdd:COG4913  286 AQRRLELLEAELEELRA-----ELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERR 360


                 ...
gi 20072378  209 TQR 211
Cdd:COG4913  361 RAR 363
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 138-211 3.49e-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: 38.88  E-value: 3.49e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20072378    138 ELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQR 211
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 62-223 4.00e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 4.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378  62 ELLGSLEEVLMRASACLEAAAREREGLEQALRRRESEHEREVR-GLYEELEQQLGEQRHRRQSQNLPREEQRGHLELELQ 140
Cdd:COG1196 606 SDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREvTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378 141 TREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQRDVVAVSRNM 220
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL 765


                ...
gi 20072378 221 QKE 223
Cdd:COG1196 766 ERE 768
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 107-211 5.75e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 38.39  E-value: 5.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378  107 YEELEQQLGEQR---------HRRQSQNLPREEQRGHLELELQTR----EQELERAGLRQRELEQQLQARAA--EQLEAQ 171
Cdd:COG3096  521 LAELEQRLRQQQnaerlleefCQRIGQQLDAAEELEELLAELEAQleelEEQAAEAVEQRSELRQQLEQLRAriKELAAR 600

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 20072378  172 AQH-IQLQRAYEAIRAQLDQA-----------QEQLSRLEGEAQGRQEQTQR 211
Cdd:COG3096  601 APAwLAAQDALERLREQSGEAladsqevtaamQQLLEREREATVERDELAAR 652
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 138-210 5.93e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 37.78  E-value: 5.93e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20072378   138 ELQTREQELERAGLRQRELEQQL-QARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLEGEAQGRQEQTQ 210
Cdd:TIGR04320 283 ALTSAQTAYAAAQAALATAQKELaNAQAQALQTAQNNLATAQAALANAEARLAKAKEALANLNADLAKKQAALD 356
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 135-219 6.45e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 37.79  E-value: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378   135 LELELQTREQELERAGL---RQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIRAQLDQAQEQLSRLE-----GEAQGRQ 206
Cdd:pfam00529  63 AEAQLAKAQAQVARLQAeldRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvlapiGGISRES 142

                          90
                  ....*....|...
gi 20072378   207 EQTQRDVVAVSRN 219
Cdd:pfam00529 143 LVTAGALVAQAQA 155
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 38-201 7.09e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.99  E-value: 7.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378  38 GVARVLGEQWAVRTLWVGLQRERPELLGSLEEVLMRASacLEAAAREREGLEQALRRRESEHEREVRglyEELEQQLGEQ 117
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT--LEGEGGSAGGSLTGGSRRELLAALLEA---EAELEELAER 687

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20072378 118 RHRRQSQNLPREEQRGHLELELQTREQELERAGLRQRELEQQLQARAAEQLEAQAQHIQLQRAYEAIR----AQLDQAQE 193
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEElpepPDLEELER 767


                ....*...
gi 20072378 194 QLSRLEGE 201
Cdd:COG1196 768 ELERLERE 775
 
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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