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Conserved domains on  [gi|485745457|ref|WP_001371952|]
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MULTISPECIES: hypothetical protein [Enterobacterales]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

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]; ...
 137-355 1.87e-10

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: 62.65  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 137 DSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHEL 216
Cdd:COG1196  274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 217 SLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCAEL 296
Cdd:COG1196  354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 485745457 297 KSALSGKEGDLVAVNAELTELHKLNESLSADLKKVTLVSQGYEAEVAEQSSELKTLQSK 355
Cdd:COG1196  434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 137-355 1.87e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 137 DSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHEL 216
Cdd:COG1196  274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 217 SLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCAEL 296
Cdd:COG1196  354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 485745457 297 KSALSGKEGDLVAVNAELTELHKLNESLSADLKKVTLVSQGYEAEVAEQSSELKTLQSK 355
Cdd:COG1196  434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 140-352 9.42e-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: 60.84  E-value: 9.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   140 KKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSLA 219
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   220 QQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNaglsrqcDQLSQTVSDTKAERDRFEQELIAAQNLCAELKSA 299
Cdd:TIGR02168  858 AAEIEELEELIEELESELEALLNERASLEEALALLRSEL-------EELSEELRELESKRSELRRELEELREKLAQLELR 930

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 485745457   300 LSGKEGDLVAVNAELTELHKLN-ESLSADLKKVTLVSQGYEAEVAEQSSELKTL 352
Cdd:TIGR02168  931 LEGLEVRIDNLQERLSEEYSLTlEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 140-306 1.67e-04

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 44.05  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457  140 KKAEARSMQLEEEVTQLLQRLEQSATDM---DELKLEN------QALQGrlEIRDSTV--KELETRLNV----------- 197
Cdd:NF012221 1565 ERAEADRQRLEQEKQQQLAAISGSQSQLestDQNALETngqaqrDAILE--ESRAVTKelTTLAQGLDAldsqatyages 1642

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457  198 --------AEAELETCHHQLDSTRH----ELSLAQQSNDSLSQQL--AERKTEIAGHLEYQKKLNEEINTQRSDNAGLSR 263
Cdd:NF012221 1643 gdqwrnpfAGGLLDRVQEQLDDAKKisgkQLADAKQRHVDNQQKVkdAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKR 1722

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 485745457  264 QCDQLSQTVSDTKAERD----------RFEQELIAAQNLCAELKSALSG---KEGD 306
Cdd:NF012221 1723 KDDALAKQNEAQQAESDanaaandaqsRGEQDASAAENKANQAQADAKGakqDESD 1778
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 133-362 3.30e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.18  E-value: 3.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   133 AIQSDSVKKAEARSMQLEEEVTQLLQRLEQSATDMDE----LKLENQALQGRLEI------------------RDSTVKE 190
Cdd:pfam15921  249 ALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEkassARSQANSIQSQLEIiqeqarnqnsmymrqlsdLESTVSQ 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   191 LETRLNVA----EAELETCHHQLDSTRHELSLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDN-------A 259
Cdd:pfam15921  329 LRSELREAkrmyEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNkrlwdrdT 408

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   260 GLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCA----ELKSALSGKEGDLVAVNAELTELHKLNESLSADLKKVTLVS 335
Cdd:pfam15921  409 GNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQgqmeRQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKK 488

                          250       260
                   ....*....|....*....|....*..
gi 485745457   336 QGYEAEVAEQSSELKTLQSKVMKLEAT 362
Cdd:pfam15921  489 MTLESSERTVSDLTASLQEKERAIEAT 515
PLN02939 PLN02939
transferase, transferring glycosyl groups
 134-373 7.31e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 41.81  E-value: 7.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 134 IQSDSVKKAEARSMQLEEEVtQLLQRLE-----------QSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAE- 201
Cdd:PLN02939 115 QQTNSKDGEQLSDFQLEDLV-GMIQNAEknilllnqarlQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEk 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 202 --LETCHHQLDSTRHELSlaqqsndslsqqlaerkTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAEr 279
Cdd:PLN02939 194 ihVEILEEQLEKLRNELL-----------------IRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAET- 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 280 drfEQELIAAQNLCAELKSALSGKEGDLVAVNAELTELHKLN--------ESLSADLKKVTLVSQGYeAEVAEQSSELKt 351
Cdd:PLN02939 256 ---EERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQydcwwekvENLQDLLDRATNQVEKA-ALVLDQNQDLR- 330

                        250       260
                 ....*....|....*....|..
gi 485745457 352 lqSKVMKLEATLEAEKTISESL 373
Cdd:PLN02939 331 --DKVDKLEASLKEANVSKFSS 350
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 137-355 1.87e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 137 DSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHEL 216
Cdd:COG1196  274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 217 SLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCAEL 296
Cdd:COG1196  354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 485745457 297 KSALSGKEGDLVAVNAELTELHKLNESLSADLKKVTLVSQGYEAEVAEQSSELKTLQSK 355
Cdd:COG1196  434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 125-380 2.14e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 125 WHYRRSYTAIQSDSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELET 204
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 205 CHHQLDSTRHELSLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQ 284
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 285 ELIAAQNLCAELKSALSGKEGDLVAVNAELTELHKLNESLSADLKKVTLVSQGYEAEVAEQSSELKTLQSKVMKLEATLE 364
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473

                        250
                 ....*....|....*.
gi 485745457 365 AEKTISESLKGTIDTL 380
Cdd:COG1196  474 LLEAALAELLEELAEA 489
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 140-352 9.42e-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: 60.84  E-value: 9.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   140 KKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSLA 219
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   220 QQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNaglsrqcDQLSQTVSDTKAERDRFEQELIAAQNLCAELKSA 299
Cdd:TIGR02168  858 AAEIEELEELIEELESELEALLNERASLEEALALLRSEL-------EELSEELRELESKRSELRRELEELREKLAQLELR 930

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 485745457   300 LSGKEGDLVAVNAELTELHKLN-ESLSADLKKVTLVSQGYEAEVAEQSSELKTL 352
Cdd:TIGR02168  931 LEGLEVRIDNLQERLSEEYSLTlEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 135-372 5.24e-09

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: 57.47  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 135 QSDSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETchhqldstrh 214
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE---------- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 215 elslAQQSNDSLSQQLAERKTEIAGHLEYQKKLNE----EINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQ 290
Cdd:COG4942   88 ----LEKEIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 291 NLCAELKSALSGKEGDLVAVNAELTELHKLNESLSADLKKVTLVSQGYEAEVAEQSSELKTLQSKVMKLEATLEAEKTIS 370
Cdd:COG4942  164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243


                 ..
gi 485745457 371 ES 372
Cdd:COG4942  244 PA 245
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 149-369 2.94e-08

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: 55.83  E-value: 2.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   149 LEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSLAQQSNDSLSQ 228
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   229 QLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQnlCAELKSALSGKEGDLV 308
Cdd:TIGR02168  380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELE 457

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 485745457   309 AVNAELtelhklnESLSADLKKVTLVSQGYEAEVAEQSSELKTLQSKVMKLEATLEAEKTI 369
Cdd:TIGR02168  458 RLEEAL-------EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 175-380 1.13e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 175 QALQGRLEIRDstvkeletrLNVAEAELETCHHQLDSTRHELSLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQ 254
Cdd:COG1196  216 RELKEELKELE---------AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 255 RSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCAELKSALSGKEGDLVAVNAELTELHKLNESLSADLKKVTLV 334
Cdd:COG1196  287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 485745457 335 SQGYEAEVAEQSSELKTLQSKVMKLEATLEAEKTISESLKGTIDTL 380
Cdd:COG1196  367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 137-380 1.93e-07

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: 53.15  E-value: 1.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   137 DSVKKAEARSMQLEEEVTQLLQRLEqsatDMDELKLENQALQGRLeiRDSTVKELETRLNVAEAELETCHHQLDSTRHEL 216
Cdd:TIGR02169  180 EEVEENIERLDLIIDEKRQQLERLR----REREKAERYQALLKEK--REYEGYELLKEKEALERQKEAIERQLASLEEEL 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   217 slaqqsnDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNA-GLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCAE 295
Cdd:TIGR02169  254 -------EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   296 LKSALSGKEGDLVAVNAELTELHKLNESLSADLKKVTLVSQGYEAEVAEQSSELKTLQSKVMKLEATLEAEKTISESLKG 375
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406


                   ....*
gi 485745457   376 TIDTL 380
Cdd:TIGR02169  407 ELDRL 411
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 133-360 2.18e-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: 53.14  E-value: 2.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   133 AIQSDSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEirdsTVKELETRLNVAEAELETCHHQLDST 212
Cdd:TIGR02168  694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----QLEERIAQLSKELTELEAEIEELEER 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   213 RHELSLAQQSNDSLSQQLAERkteiaghleyQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNL 292
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELEAQ----------IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 485745457   293 CAELKSALSGKEGDLVAVNAELTELHKLNESLSADLKKVTLVSQGYEAEVAEQSSELKTLQSKVMKLE 360
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 138-350 2.24e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 2.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 138 SVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELS 217
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 218 LAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCAELK 297
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 485745457 298 SALSGKEGDLVAVNAELTELHKLNESLSADLKKVTLVSQGYEAEVAEQSSELK 350
Cdd:COG1196  456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 104-374 1.85e-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: 1.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   104 RYLDIPDEVKVALGDIiSYITWHYRRSYTAIQSDSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEI 183
Cdd:TIGR02168  214 RYKELKAELRELELAL-LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   184 RDSTVKELETRLNVAEAELETCHHQLDSTRHELSLAQQSNDSLSQQLAERKTEIAG---------------HLEYQ---- 244
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeelesleaeleelEAELEeles 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   245 --KKLNEEINTQRSDNAGLSRQCDQ-------LSQTVSDTKAERDRFEQELiaAQNLCAELKSALSGKEGDLVAVNAELT 315
Cdd:TIGR02168  373 rlEELEEQLETLRSKVAQLELQIASlnneierLEARLERLEDRRERLQQEI--EELLKKLEEAELKELQAELEELEEELE 450

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 485745457   316 ELHKLNESLSADLKKVTLVSQGYEAEVAEQSSELKTLQSKVMKLEATLEAEKTISESLK 374
Cdd:TIGR02168  451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 134-380 4.09e-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: 49.28  E-value: 4.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   134 IQSDSVKKAEARSMQLEE-EVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDST 212
Cdd:TIGR02168  207 RQAEKAERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   213 RHELSLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNL 292
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   293 CAELKSALSGKEGDLVAVNAELTELHKLNESLSADL----KKVTLVSQGYEAEVAEQSSELKTLQSKVMK-LEATLEAEK 367
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIerleARLERLEDRRERLQQEIEELLKKLEEAELKeLQAELEELE 446

                          250
                   ....*....|...
gi 485745457   368 TISESLKGTIDTL 380
Cdd:TIGR02168  447 EELEELQEELERL 459
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
126-295 4.29e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 4.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457  126 HYRRSYTAIQSDSVKKAEArsmqLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAeletc 205
Cdd:COG4913   596 RRIRSRYVLGFDNRAKLAA----LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA----- 666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457  206 HHQLDSTRHELSLAQQSNDSLsQQLAERkteiaghleyQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQE 285
Cdd:COG4913   667 EREIAELEAELERLDASSDDL-AALEEQ----------LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735

                         170
                  ....*....|
gi 485745457  286 LIAAQNLCAE 295
Cdd:COG4913   736 LEAAEDLARL 745
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
127-370 4.46e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.86  E-value: 4.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 127 YRRSYTAIQSDSVKKAEArsmQLEEEVTQLLQRLEQSATDMDELKLENQ--ALQGRLEIRDSTVKELETRLNVAEAELET 204
Cdd:COG3206  161 YLEQNLELRREEARKALE---FLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAE 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 205 chhqldstrhelslAQQSNDSLSQQLAERKTEIAGHLEyqkklNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQ 284
Cdd:COG3206  238 --------------AEARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA 298

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 285 ELIAA-QNLCAELKSALSGKEGDLVAVNAELTELHKLNESLSADLKKVTLVSQGY-----EAEVAEQSseLKTLQSKVMk 358
Cdd:COG3206  299 QIAALrAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELrrlerEVEVAREL--YESLLQRLE- 375

                        250
                 ....*....|..
gi 485745457 359 lEATLEAEKTIS 370
Cdd:COG3206  376 -EARLAEALTVG 386
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 177-380 7.50e-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: 48.13  E-value: 7.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   177 LQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRS 256
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   257 DNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCAELKSALSGKEGDLVAVNAE---------------------LT 315
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerleslerriaaterrLE 841

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485745457   316 ELHKLNESLSADLKKVTLVSQGYEAEVAEQSSELKTLQSKVMKLEATLEAEKTISESLKGTIDTL 380
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 141-365 9.14e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 9.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   141 KAEARSMQLEEEVTQLLQRLEQSA---------------TDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETC 205
Cdd:TIGR02169  255 KLTEEISELEKRLEEIEQLLEELNkkikdlgeeeqlrvkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   206 HHQLDSTRHELSLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQE 285
Cdd:TIGR02169  335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   286 LIAAQNLCAELKSALSGKEGDLVAVNAELTELH--------KLnESLSADLKKVTLVSQGYEAEVAEQSSELKTLQSKVM 357
Cdd:TIGR02169  415 LQRLSEELADLNAAIAGIEAKINELEEEKEDKAleikkqewKL-EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493


                   ....*...
gi 485745457   358 KLEATLEA 365
Cdd:TIGR02169  494 EAEAQARA 501
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 78-352 9.38e-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: 47.76  E-value: 9.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457    78 VGGSFARSqemfAEYQKYVKEVPEEARYLDIPDEVKVALGDIISYITWHYRRSYTAIQ-----SDSVKKAEARSMQLEEE 152
Cdd:TIGR02169  656 TGGSRAPR----GGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQelsdaSRKIGEIEKEIEQLEQE 731

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   153 VTQLLQRLEQSATDMDEL-------KLENQALQGRLEIRDSTVKELETRLNVAEAELEtcHHQLDSTRHELSLAQQSNDS 225
Cdd:TIGR02169  732 EEKLKERLEELEEDLSSLeqeienvKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSR 809

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   226 LSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCAELKSALSGKEG 305
Cdd:TIGR02169  810 IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 485745457   306 DLVAVNAELTELHKLNESLSADLKKVTLVSQGYEAEVAEQSSELKTL 352
Cdd:TIGR02169  890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 141-331 4.83e-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: 45.83  E-value: 4.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   141 KAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSLAQ 220
Cdd:TIGR02169  333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   221 QSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCAELKSAL 300
Cdd:TIGR02169  413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492

                          170       180       190
                   ....*....|....*....|....*....|.
gi 485745457   301 SGKEGDLVAVNAELTELHKLNESLSADLKKV 331
Cdd:TIGR02169  493 AEAEAQARASEERVRGGRAVEEVLKASIQGV 523
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 83-283 9.08e-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: 44.67  E-value: 9.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457    83 ARSQEMFAEYQKYVKEVPEEARYLDIPDEVKVALGDIISYITWHYRRSYTAIQSDSVKKAEARsmqleEEVTQLLQRLEQ 162
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR-----DELKDYREKLEK 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   163 SATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSLAQQSNDSLSQQLAERKTEIAGHLE 242
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE 476

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 485745457   243 YQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFE 283
Cdd:TIGR02169  477 EYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLK 517
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 137-354 1.33e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 137 DSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHEL 216
Cdd:COG3883   16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 217 SLAQQSNDSLSQQL-AERKTEIAGHLEYQKKL----NEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQN 291
Cdd:COG3883   96 YRSGGSVSYLDVLLgSESFSDFLDRLSALSKIadadADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 485745457 292 LCAELKSALSGKEGDLVAVNAELTELHKLNESLSADLKKVTLVSQGYEAEVAEQSSELKTLQS 354
Cdd:COG3883  176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
155-378 1.40e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457  155 QLLQRLEQSATDMDELKLENQALQGRLEIRDstVKELETRLNVAEAELETChhqldstRHELSLAQQSNDSLSQQLAERK 234
Cdd:COG4913   252 ELLEPIRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEEL-------RAELARLEAELERLEARLDALR 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457  235 TEIaghleyqkklnEEINTQRSDNAGlsRQCDQLSQTVSDTKAERDRFEQELIAAQNLCAELKSALSGKEGDLVAVNAEL 314
Cdd:COG4913   323 EEL-----------DELEAQIRGNGG--DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 485745457  315 TELhklNESLSADlkkvtlvsqgyEAEVAEQSSELKTLQSKVMKLEATLEAEKTISESLKGTID 378
Cdd:COG4913   390 AAL---LEALEEE-----------LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 140-306 1.67e-04

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 44.05  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457  140 KKAEARSMQLEEEVTQLLQRLEQSATDM---DELKLEN------QALQGrlEIRDSTV--KELETRLNV----------- 197
Cdd:NF012221 1565 ERAEADRQRLEQEKQQQLAAISGSQSQLestDQNALETngqaqrDAILE--ESRAVTKelTTLAQGLDAldsqatyages 1642

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457  198 --------AEAELETCHHQLDSTRH----ELSLAQQSNDSLSQQL--AERKTEIAGHLEYQKKLNEEINTQRSDNAGLSR 263
Cdd:NF012221 1643 gdqwrnpfAGGLLDRVQEQLDDAKKisgkQLADAKQRHVDNQQKVkdAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKR 1722

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 485745457  264 QCDQLSQTVSDTKAERD----------RFEQELIAAQNLCAELKSALSG---KEGD 306
Cdd:NF012221 1723 KDDALAKQNEAQQAESDanaaandaqsRGEQDASAAENKANQAQADAKGakqDESD 1778
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 142-288 1.93e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 142 AEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSLAQQ 221
Cdd:COG1196  377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 485745457 222 SNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIA 288
Cdd:COG1196  457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 133-362 3.30e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.18  E-value: 3.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   133 AIQSDSVKKAEARSMQLEEEVTQLLQRLEQSATDMDE----LKLENQALQGRLEI------------------RDSTVKE 190
Cdd:pfam15921  249 ALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEkassARSQANSIQSQLEIiqeqarnqnsmymrqlsdLESTVSQ 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   191 LETRLNVA----EAELETCHHQLDSTRHELSLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSDN-------A 259
Cdd:pfam15921  329 LRSELREAkrmyEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNkrlwdrdT 408

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   260 GLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCA----ELKSALSGKEGDLVAVNAELTELHKLNESLSADLKKVTLVS 335
Cdd:pfam15921  409 GNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQgqmeRQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKK 488

                          250       260
                   ....*....|....*....|....*..
gi 485745457   336 QGYEAEVAEQSSELKTLQSKVMKLEAT 362
Cdd:pfam15921  489 MTLESSERTVSDLTASLQEKERAIEAT 515
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 139-373 3.85e-04

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: 42.90  E-value: 3.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   139 VKKAEARSMQLEEEVTQLLQRLEQS-ATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAEletcHHQLDSTRHELS 217
Cdd:pfam12128  267 YKSDETLIASRQEERQETSAELNQLlRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQ----HGAFLDADIETA 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457   218 LAQQSN-DSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSdnAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCAEL 296
Cdd:pfam12128  343 AADQEQlPSWQSELENLEERLKALTGKHQDVTAKYNRRRS--KIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQAL 420

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 485745457   297 KSALSGKegdLVAVNAELTELHKLNESLSADLkKVTLVSQGYEAEVAEQsseLKTLQSKVMKLEATLEAEKTISESL 373
Cdd:pfam12128  421 ESELREQ---LEAGKLEFNEEEYRLKSRLGEL-KLRLNQATATPELLLQ---LENFDERIERAREEQEAANAEVERL 490
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
128-317 5.31e-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: 5.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457  128 RRSYTAIQSDSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELEtchh 207
Cdd:COG4913   258 RELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR---- 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457  208 QLDSTRHElSLAQQSnDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRsdnAGLSRQCDQLSQTVSDTKAERDRFEQELi 287
Cdd:COG4913   334 GNGGDRLE-QLEREI-ERLERELEERERRRARLEALLAALGLPLPASA---EEFAALRAEAAALLEALEEELEALEEAL- 407

                         170       180       190
                  ....*....|....*....|....*....|
gi 485745457  288 aaqnlcAELKSALSGKEGDLVAVNAELTEL 317
Cdd:COG4913   408 ------AEAEAALRDLRRELRELEAEIASL 431
PLN02939 PLN02939
transferase, transferring glycosyl groups
 134-373 7.31e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 41.81  E-value: 7.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 134 IQSDSVKKAEARSMQLEEEVtQLLQRLE-----------QSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAE- 201
Cdd:PLN02939 115 QQTNSKDGEQLSDFQLEDLV-GMIQNAEknilllnqarlQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEk 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 202 --LETCHHQLDSTRHELSlaqqsndslsqqlaerkTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAEr 279
Cdd:PLN02939 194 ihVEILEEQLEKLRNELL-----------------IRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAET- 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 280 drfEQELIAAQNLCAELKSALSGKEGDLVAVNAELTELHKLN--------ESLSADLKKVTLVSQGYeAEVAEQSSELKt 351
Cdd:PLN02939 256 ---EERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQydcwwekvENLQDLLDRATNQVEKA-ALVLDQNQDLR- 330

                        250       260
                 ....*....|....*....|..
gi 485745457 352 lqSKVMKLEATLEAEKTISESL 373
Cdd:PLN02939 331 --DKVDKLEASLKEANVSKFSS 350
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 180-366 1.05e-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: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 180 RLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSLAQQSNDSLSQQLAERKTEIAGHLEYQKKLNEEINTQRSdna 259
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN--- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 260 glSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCAELKSALSGKEGDLVAVNAELTELHKlneslsadlkkvtlvsqGYE 339
Cdd:COG1579   88 --NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA-----------------ELD 148

                        170       180
                 ....*....|....*....|....*..
gi 485745457 340 AEVAEQSSELKTLQSKVMKLEATLEAE 366
Cdd:COG1579  149 EELAELEAELEELEAEREELAAKIPPE 175
PRK09039 PRK09039
peptidoglycan -binding protein;
149-307 1.29e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.72  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 149 LEEEVTQLLQRLEQSATDMDELkleNQAL----QGRLEIRDStVKELETRLNVAEAELETCHHQLDSTRHELSLAQQSND 224
Cdd:PRK09039  44 LSREISGKDSALDRLNSQIAEL---ADLLslerQGNQDLQDS-VANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAG 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 225 SLSQQLAERKTEIAGHLEYQKKLNEEIntqrsdnAGLSRQCDQLsQTVSDTKAERDRFEQELIAAqnLCAELKSALSGKE 304
Cdd:PRK09039 120 ELAQELDSEKQVSARALAQVELLNQQI-------AALRRQLAAL-EAALDASEKRDRESQAKIAD--LGRRLNVALAQRV 189


                 ...
gi 485745457 305 GDL 307
Cdd:PRK09039 190 QEL 192
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
148-394 1.49e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 148 QLEEEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSLAQQSNDSLS 227
Cdd:COG4372   35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 228 QQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCAELKSALSGKEGDL 307
Cdd:COG4372  115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANR 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 308 VAVNAELTELHKLNESLSADLKKVTLVSQGYEAEVAEQSSELKTLQSKVMKLEATLEAEKTISESLKGTIDTLTGAMAGG 387
Cdd:COG4372  195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274


                 ....*..
gi 485745457 388 GTGKSKQ 394
Cdd:COG4372  275 EEELEIA 281
PRK11281 PRK11281
mechanosensitive channel MscK;
137-376 4.03e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.51  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457  137 DSVKKAEARSMQLEEEVTQLLQRLEQSATDMDELK-------------LENQALQGRLEIRDSTVKELETRLNVAEAELE 203
Cdd:PRK11281   73 DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKddndeetretlstLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLV 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457  204 TCHHQLDSTRHELSLAQQSNDSLSQQLAERKTE-IAGHLEYQKKLNEE---INTQ----RSDNAGLSRQCDQLSQTVSDT 275
Cdd:PRK11281  153 SLQTQPERAQAALYANSQRLQQIRNLLKGGKVGgKALRPSQRVLLQAEqalLNAQndlqRKSLEGNTQLQDLLQKQRDYL 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457  276 KAERDRFEQELIAAQNLCAELKSALSGKEGDlVAVNAELTELHKLNESLSADLKKVTLVSQgyeaEVAEQSSELKTL--Q 353
Cdd:PRK11281  233 TARIQRLEHQLQLLQEAINSKRLTLSEKTVQ-EAQSQDEAARIQANPLVAQELEINLQLSQ----RLLKATEKLNTLtqQ 307

                         250       260
                  ....*....|....*....|....*...
gi 485745457  354 SKVMK--LEATLEAEKTISE---SLKGT 376
Cdd:PRK11281  308 NLRVKnwLDRLTQSERNIKEqisVLKGS 335
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
151-372 7.21e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.48  E-value: 7.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 151 EEVTQLLQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELEtchhqLDSTRHELSLAQQSN-----DS 225
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG-----LDDADAEAVEARREEledrdEE 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 226 LSQQLAERKTEIAGHLEYQKKLNEEINTQRSDNAGLSRQCDQLSQTVSDTKAERDRFEQELIAAQNLCAELKSA------ 299
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgdapv 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457 300 -LSGKEGDLVAVNAELTELHKLNESLSADLKKV--------TLVSQG--------------------YEAEVAEQSSELK 350
Cdd:PRK02224 406 dLGNAEDFLEELREERDELREREAELEATLRTArerveeaeALLEAGkcpecgqpvegsphvetieeDRERVEELEAELE 485

                        250       260
                 ....*....|....*....|..
gi 485745457 351 TLQSKVMKLEATLEAEKTISES 372
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEA 507
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
142-264 9.18e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 9.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485745457  142 AEARSMQLEEEVTQL---LQRLEQSATDMDELKLENQALQGRLEIRDSTVKELETRLNVAEAELETCHHQLDSTRHELSL 218
Cdd:COG4913   659 DEIDVASAEREIAELeaeLERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 485745457  219 AQQSNDS-LSQQLAERKTEIAG---HLEYQKKLNEEINTQRSDNAGLSRQ 264
Cdd:COG4913   739 AEDLARLeLRALLEERFAAALGdavERELRENLEERIDALRARLNRAEEE 788
 
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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