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Conserved domains on  [gi|2462505362|ref|XP_054190728|]
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spindle assembly abnormal protein 6 homolog isoform X2 [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000095)

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_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2-283 1.01e-15

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 80.49  E-value: 1.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362    2 QSLDDATKQLDFTRKTLAEKKQELDKLRNEwashtaaltnkhSQELTNEKEKALQAQVQYQQQHEQQKKDLEIL------ 75
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKE------------LEELEEELEQLRKELEELSRQISALRKDLARLeaeveq 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   76 HQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQT 155
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  156 KVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK 235
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2462505362  236 lkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQL 283
Cdd:TIGR02168  905 -------ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2-283 1.01e-15

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: 80.49  E-value: 1.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362    2 QSLDDATKQLDFTRKTLAEKKQELDKLRNEwashtaaltnkhSQELTNEKEKALQAQVQYQQQHEQQKKDLEIL------ 75
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKE------------LEELEEELEQLRKELEELSRQISALRKDLARLeaeveq 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   76 HQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQT 155
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  156 KVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK 235
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2462505362  236 lkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQL 283
Cdd:TIGR02168  905 -------ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
15-315 6.32e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.67  E-value: 6.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  15 RKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILhQQNIHQLQNRLSELEAAN 94
Cdd:COG1196   219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAEL 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  95 KDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRT 174
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 175 KEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEK 254
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462505362 255 LQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNE-KLITWLNKELNENQ 315
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGL 519
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
82-305 2.10e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  82 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQR---TKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVA 158
Cdd:PRK03918  190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 159 VLEQEIKDKDQLVLRTKE------AFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLqgdlKTLMG 232
Cdd:PRK03918  270 ELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL----EELKK 345
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462505362 233 KLKlkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLIT 305
Cdd:PRK03918  346 KLK-------ELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
83-303 8.77e-07

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 51.43  E-value: 8.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  83 LQNRLSELEAANKDLterkykgdstIRELKAKLSGVEEELQRTKQEVLSLRRENSTLdvechekEKHVNQLQTKVAVLEQ 162
Cdd:pfam07888  32 LQNRLEECLQERAEL----------LQAQEAANRQREKEKERYKRDREQWERQRREL-------ESRVAELKEELRQSRE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 163 EIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTI 242
Cdd:pfam07888  95 KHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERK 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462505362 243 QQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 303
Cdd:pfam07888 175 QLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
TOP4c cd00187
DNA Topoisomerase, subtype IIA; domain A'; bacterial DNA topoisomerase IV (C subunit, ParC), ...
193-313 3.06e-03

DNA Topoisomerase, subtype IIA; domain A'; bacterial DNA topoisomerase IV (C subunit, ParC), bacterial DNA gyrases (A subunit, GyrA),mammalian DNA toposiomerases II. DNA topoisomerases are essential enzymes that regulate the conformational changes in DNA topology by catalysing the concerted breakage and rejoining of DNA strands during normal cellular growth.


Pssm-ID: 238111 [Multi-domain]  Cd Length: 445  Bit Score: 39.86  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 193 EKNQVQLGKLEATIKSLSAeLLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKElqdvgqslrik 272
Cdd:cd00187   341 GKAEARLHILEGLLKAILN-IDEVINLIRSSDEAKKALIEELEKLGFSEIQADAILDMRLRRLTKLERE----------- 408
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462505362 273 eqevcKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 313
Cdd:cd00187   409 -----KLLKELKELEAEIEDLEKILASEERPKDLWKEELDE 444
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2-283 1.01e-15

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: 80.49  E-value: 1.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362    2 QSLDDATKQLDFTRKTLAEKKQELDKLRNEwashtaaltnkhSQELTNEKEKALQAQVQYQQQHEQQKKDLEIL------ 75
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKE------------LEELEEELEQLRKELEELSRQISALRKDLARLeaeveq 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   76 HQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQT 155
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  156 KVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK 235
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2462505362  236 lkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQL 283
Cdd:TIGR02168  905 -------ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
15-315 6.32e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.67  E-value: 6.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  15 RKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILhQQNIHQLQNRLSELEAAN 94
Cdd:COG1196   219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAEL 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  95 KDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRT 174
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 175 KEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEK 254
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462505362 255 LQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNE-KLITWLNKELNENQ 315
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGL 519
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
76-315 2.72e-12

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: 69.32  E-value: 2.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   76 HQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQT 155
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  156 KVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEEN-------GEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLK 228
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEElesleaeLEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  229 TLMGKLK-LKNTVTI---QQEKLLAEKEEKLQK-EQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 303
Cdd:TIGR02168  397 SLNNEIErLEARLERledRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
                          250
                   ....*....|..
gi 2462505362  304 ITWLNKELNENQ 315
Cdd:TIGR02168  477 LDAAERELAQLQ 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
69-321 5.59e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.42  E-value: 5.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  69 KKDLEIL-HQQNIHQLQNRLSELEAANKDLTERKykgdSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKE 147
Cdd:COG1196   219 KEELKELeAELLLLKLRELEAELEELEAELEELE----AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 148 KHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDL 227
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 228 KTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWL 307
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
                         250
                  ....*....|....
gi 2462505362 308 NKELNENQLVRKQD 321
Cdd:COG1196   455 EEEEEALLELLAEL 468
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
7-303 9.34e-12

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: 67.77  E-value: 9.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362    7 ATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKHSQELT-----NEKEKALQAQVQYQQQHEQQKKDLEilhqQNIH 81
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEElrlevSELEEEIEELQKELYALANEISRLE----QQKQ 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   82 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVEC-------HEKEKHVNQLQ 154
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELeelesrlEELEEQLETLR 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  155 TKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLgkLEATIKSLSAELLKANEIIKKLQGDLKTLMGKL 234
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELEELQEELERLEEAL 463
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462505362  235 KlkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQevckLQEQLEatvKKLEESKQLLKNNEKL 303
Cdd:TIGR02168  464 E-------ELREELEEAEQALDAAERELAQLQARLDSLER----LQENLE---GFSEGVKALLKNQSGL 518
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
4-313 1.66e-10

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: 63.55  E-value: 1.66e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362    4 LDDATKQLDFTRKTLAEKKQELDKL---RNEWASHTAALTNKHSQELT---NEKEKALQAQVQYQQQHEQQKKDLEILHQ 77
Cdd:TIGR02169  179 LEEVEENIERLDLIIDEKRQQLERLrreREKAERYQALLKEKREYEGYellKEKEALERQKEAIERQLASLEEELEKLTE 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   78 QnIHQLQNRLSELEAANKDLTER-KYKGDSTIRELKAKLSGVEEELQRT-------KQEVLSLRRENSTLDVECHEKEKH 149
Cdd:TIGR02169  259 E-ISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLersiaekERELEDAEERLAKLEAEIDKLLAE 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  150 VNQLQTKvavLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLeatiKSLSAELLKANEIIKKLQGDLKT 229
Cdd:TIGR02169  338 IEELERE---IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL----KDYREKLEKLKREINELKRELDR 410
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  230 LMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNK 309
Cdd:TIGR02169  411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490

                   ....
gi 2462505362  310 ELNE 313
Cdd:TIGR02169  491 ELAE 494
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2-304 1.69e-10

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: 63.55  E-value: 1.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362    2 QSLDDATKQLDFTRKTLAEKKQELDKLrnewashtaaltNKHSQELTNEKEKALqaqvqyqqqheqqKKDLEILHQQnIH 81
Cdd:TIGR02169  251 EELEKLTEEISELEKRLEEIEQLLEEL------------NKKIKDLGEEEQLRV-------------KEKIGELEAE-IA 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   82 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLE 161
Cdd:TIGR02169  305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  162 QEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVT 241
Cdd:TIGR02169  385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462505362  242 IQQEKLLAEKEEKLQKEQKELQDVGQSLrikeqevcklqEQLEATVKKLEESKQLLKNNEKLI 304
Cdd:TIGR02169  465 SKYEQELYDLKEEYDRVEKELSKLQREL-----------AEAEAQARASEERVRGGRAVEEVL 516
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
125-313 1.86e-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: 63.54  E-value: 1.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  125 TKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEA 204
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  205 TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLE 284
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
                          170       180
                   ....*....|....*....|....*....
gi 2462505362  285 ATVKKLEESKQLLKNNEKLITWLNKELNE 313
Cdd:TIGR02168  835 ATERRLEDLEEQIEELSEDIESLAAEIEE 863
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
4-263 3.74e-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: 3.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   4 LDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQaqvqyqqqheqqkkdleilhQQNIHQL 83
Cdd:COG1196   255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL--------------------EERRREL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  84 QNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQE 163
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 164 IKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQ 243
Cdd:COG1196   395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
                         250       260
                  ....*....|....*....|
gi 2462505362 244 QEKLLAEKEEKLQKEQKELQ 263
Cdd:COG1196   475 LEAALAELLEELAEAAARLL 494
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
69-294 8.37e-10

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: 61.62  E-value: 8.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   69 KKDLEILHQ------QNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVE 142
Cdd:TIGR02169  687 KRELSSLQSelrrieNRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  143 CHEKEKHVNQLQTKVAVLEQEIKDkdqlvlrtkEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKK 222
Cdd:TIGR02169  767 IEELEEDLHKLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462505362  223 LQGDLKTLMGKlklKNTVTIQQEKL---LAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESK 294
Cdd:TIGR02169  838 LQEQRIDLKEQ---IKSIEKEIENLngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
82-295 1.24e-08

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 57.33  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  82 QLQNRLSELEAANKDLTERkykgdstIRELKAKLSGVEEELQRTKQE--VLSLRRENSTLdvechekEKHVNQLQTKVAV 159
Cdd:COG3206   165 NLELRREEARKALEFLEEQ-------LPELRKELEEAEAALEEFRQKngLVDLSEEAKLL-------LQQLSELESQLAE 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 160 LEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQV--QLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-- 235
Cdd:COG3206   231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLraQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqe 310
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462505362 236 -------LKNTVTI--QQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQ 295
Cdd:COG3206   311 aqrilasLEAELEAlqAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
106-311 2.32e-08

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: 55.93  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 106 STIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQK 185
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 186 VVLEENGEK---NQVQLGKLEATIKSLSAE----LLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKE 258
Cdd:COG4942   100 EAQKEELAEllrALYRLGRQPPLALLLSPEdfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462505362 259 QKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKEL 311
Cdd:COG4942   180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
77-297 3.35e-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: 56.22  E-value: 3.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   77 QQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTK 156
Cdd:TIGR02168  690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  157 VAVLEQEIKdkdqlvlrtkEAFDTIQEqkvvLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKL 236
Cdd:TIGR02168  770 LEEAEEELA----------EAEAEIEE----LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462505362  237 K---NTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLL 297
Cdd:TIGR02168  836 TerrLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
77-311 5.49e-08

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: 54.77  E-value: 5.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  77 QQNIHQLQNRLSELEAANKDLTERkykgdstIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTK 156
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKE-------LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 157 VAVLEQEIKDKDQLvlrtkeafdtIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKL 236
Cdd:COG4942    92 IAELRAELEAQKEE----------LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462505362 237 KNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKEL 311
Cdd:COG4942   162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
105-344 1.04e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.07  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 105 DSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDK-DQLVLRTKEAFdtiqe 183
Cdd:COG3883    22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERrEELGERARALY----- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 184 qkvvleengeKNQVQLGKLEATIKSLS-AELLKANEIIKKLQGDLKTLMGKLKlkntvtiQQEKLLAEKEEKLQKEQKEL 262
Cdd:COG3883    97 ----------RSGGSVSYLDVLLGSESfSDFLDRLSALSKIADADADLLEELK-------ADKAELEAKKAELEAKLAEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 263 QDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQDVLGPSTTPPAHSSSNTIRSGI 342
Cdd:COG3883   160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239

                  ..
gi 2462505362 343 SP 344
Cdd:COG3883   240 AA 241
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
108-311 1.51e-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: 54.30  E-value: 1.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  108 IRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDK-------DQLVLRTKEAFDT 180
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELeedlsslEQEIENVKSELKE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  181 IQEQKVVLEENGEKNQVQLGKLEAT-----IKSLSAELLKANEIIKKLQGDLKTLMGKLklkntvtiqqeKLLAEKEEKL 255
Cdd:TIGR02169  763 LEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKL-----------NRLTLEKEYL 831
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462505362  256 QKEQKELQDVGQSLRIKEQEVCKLQEQLEAtvkKLEESKQLLKNNEKLITWLNKEL 311
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIENLNG---KKEELEEELEELEAALRDLESRL 884
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
82-305 2.10e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  82 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQR---TKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVA 158
Cdd:PRK03918  190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 159 VLEQEIKDKDQLVLRTKE------AFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLqgdlKTLMG 232
Cdd:PRK03918  270 ELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL----EELKK 345
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462505362 233 KLKlkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLIT 305
Cdd:PRK03918  346 KLK-------ELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
105-308 4.72e-07

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: 50.69  E-value: 4.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 105 DSTIRELKAKLSGVEEELQRTKQEVLSLRREnstldveCHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ 184
Cdd:COG1579    16 DSELDRLEHRLKELPAELAELEDELAALEAR-------LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 185 KVVleengEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgklklkntvtiqqEKLLAEKEEKLQKEQKELQD 264
Cdd:COG1579    89 KEY-----EALQKEIESLKRRISDLEDEILELMERIEELEEELAEL--------------EAELAELEAELEEKKAELDE 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2462505362 265 VGQSLRIKEQEvckLQEQLEATVKKLEEskQLLKNNEKLITWLN 308
Cdd:COG1579   150 ELAELEAELEE---LEAEREELAAKIPP--ELLALYERIRKRKN 188
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
20-321 6.98e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 6.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  20 EKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDleilhqqnIHQLQNRLSELEAA------ 93
Cdd:PRK03918  369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE--------IKELKKAIEELKKAkgkcpv 440
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  94 -NKDLTERKYKGdsTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQT--KVAVLEQEIKDKDQL 170
Cdd:PRK03918  441 cGRELTEEHRKE--LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLKKYNLE 518
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 171 VLRTKEafdtiqeqkvvleENGEKNQVQLGKLEATIKSLSAELLKANEIIKKL----------QGDLKTLMGKLKLKNTV 240
Cdd:PRK03918  519 ELEKKA-------------EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLaelekkldelEEELAELLKELEELGFE 585
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 241 TIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 320
Cdd:PRK03918  586 SVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR 665

                  .
gi 2462505362 321 D 321
Cdd:PRK03918  666 E 666
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
83-303 8.77e-07

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 51.43  E-value: 8.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  83 LQNRLSELEAANKDLterkykgdstIRELKAKLSGVEEELQRTKQEVLSLRRENSTLdvechekEKHVNQLQTKVAVLEQ 162
Cdd:pfam07888  32 LQNRLEECLQERAEL----------LQAQEAANRQREKEKERYKRDREQWERQRREL-------ESRVAELKEELRQSRE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 163 EIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTI 242
Cdd:pfam07888  95 KHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERK 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462505362 243 QQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 303
Cdd:pfam07888 175 QLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
119-320 1.13e-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: 51.22  E-value: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  119 EEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDkdqlvlrtkeafdtIQEQKVVLEENGEKNQVQ 198
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE--------------IEKEIEQLEQEEEKLKER 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  199 LGKLEATIKSLSAELLKANEIIKKLqgdlktlmgklklkntvtiqqEKLLAEKEEKLQKEQKELQDVGQSLRikeqevck 278
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKEL---------------------EARIEELEEDLHKLEEALNDLEARLS-------- 789
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2462505362  279 lQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 320
Cdd:TIGR02169  790 -HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
18-231 2.16e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 2.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   18 LAEKKQELDKLRNEWASHTAALtnkhsQELTNEKEKALQAQVQYQQQHEQQKKDLEIL-HQQNIHQLQNRLSELEAANKD 96
Cdd:COG4913    612 LAALEAELAELEEELAEAEERL-----EALEAELDALQERREALQRLAEYSWDEIDVAsAEREIAELEAELERLDASSDD 686
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   97 LterkykgdstiRELKAKLSGVEEELQRTKQEvlslrrenstldvechekekhVNQLQTKVAVLEQEIKDKDQLVLRTKE 176
Cdd:COG4913    687 L-----------AALEEQLEELEAELEELEEE---------------------LDELKGEIGRLEKELEQAEEELDELQD 734
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462505362  177 AFDTIQE-QKVVLEENGEK--NQVQLGKLEATI-KSLSAELLKANEIIKKLQGDLKTLM 231
Cdd:COG4913    735 RLEAAEDlARLELRALLEErfAAALGDAVERELrENLEERIDALRARLNRAEEELERAM 793
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
154-302 7.44e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 7.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 154 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLK----- 228
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGerara 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 229 ---------------------TLMGKLKLKNTVTIQQEKLLAE---KEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLE 284
Cdd:COG3883    95 lyrsggsvsyldvllgsesfsDFLDRLSALSKIADADADLLEElkaDKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
                         170
                  ....*....|....*...
gi 2462505362 285 ATVKKLEESKQLLKNNEK 302
Cdd:COG3883   175 AQQAEQEALLAQLSAEEA 192
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
80-316 8.08e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 8.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  80 IHQLQNRLSELEAANKDL---TERKYKGDSTIRELKAKLSGVEEELQRTKQEV-LSLRRENSTLDV---ECHEKEKHVNQ 152
Cdd:PRK02224  281 VRDLRERLEELEEERDDLlaeAGLDDADAEAVEARREELEDRDEELRDRLEECrVAAQAHNEEAESlreDADDLEERAEE 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 153 LQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMG 232
Cdd:PRK02224  361 LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARE 440
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 233 KLKlkntvtiQQEKLLA---------------------EKEEKLQKEQKELQDvgqsLRIKEQEVCKLQEQLEATVK--- 288
Cdd:PRK02224  441 RVE-------EAEALLEagkcpecgqpvegsphvetieEDRERVEELEAELED----LEEEVEEVEERLERAEDLVEaed 509
                         250       260
                  ....*....|....*....|....*...
gi 2462505362 289 KLEESKQLLKNNEKLITWLNKELNENQL 316
Cdd:PRK02224  510 RIERLEERREDLEELIAERRETIEEKRE 537
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
2-302 8.15e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.48  E-value: 8.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   2 QSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEilhqqnih 81
Cdd:TIGR04523 253 TQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLE-------- 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  82 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENStldvechEKEKHVNQLQTKVAVLE 161
Cdd:TIGR04523 325 EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ-------SYKQEIKNLESQINDLE 397
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 162 QEIKDKDQlvlrtkeafdtiqeQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVT 241
Cdd:TIGR04523 398 SKIQNQEK--------------LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462505362 242 IQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQ---LEATVKKLEESKQLLKNNEK 302
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEkkeLEEKVKDLTKKISSLKEKIE 527
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-213 1.04e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   2 QSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKdleilhQQNIH 81
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA------EAELA 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  82 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLE 161
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462505362 162 QEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAEL 213
Cdd:COG1196   456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
72-315 1.14e-05

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: 48.19  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   72 LEILHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEElqrtkqevlsLRRENSTLDVECHEKEKHVN 151
Cdd:pfam15921  258 IELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ----------ARNQNSMYMRQLSDLESTVS 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  152 QLQTKVAVLEQEIKDK-----DQLVLRTKEAFDTIQEQKVVLEENGEKNQvQLGKLEATIKSLSAELLKANEIIKKL--- 223
Cdd:pfam15921  328 QLRSELREAKRMYEDKieeleKQLVLANSELTEARTERDQFSQESGNLDD-QLQKLLADLHKREKELSLEKEQNKRLwdr 406
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  224 -QGDLKT---LMGKLKLKNTVTIQQEKLL----AEKEEKLQKEQKELQDVGQSLrikeQEVCKLQEQLEAT-------VK 288
Cdd:pfam15921  407 dTGNSITidhLRRELDDRNMEVQRLEALLkamkSECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTkemlrkvVE 482
                          250       260
                   ....*....|....*....|....*..
gi 2462505362  289 KLEESKQLLKNNEKLITWLNKELNENQ 315
Cdd:pfam15921  483 ELTAKKMTLESSERTVSDLTASLQEKE 509
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
108-321 1.19e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 108 IRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVV 187
Cdd:COG4372    47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 188 LEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQ 267
Cdd:COG4372   127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462505362 268 SLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQD 321
Cdd:COG4372   207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
PRK12704 PRK12704
phosphodiesterase; Provisional
181-292 1.33e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 181 IQEQKVVLEENGEKNQVQLGKLEAtiKSLSAE-LLKANEIIKKLQ----GDLKTLMGKLKLKNTVTIQQEKLLAEKEEKL 255
Cdd:PRK12704   28 IAEAKIKEAEEEAKRILEEAKKEA--EAIKKEaLLEAKEEIHKLRnefeKELRERRNELQKLEKRLLQKEENLDRKLELL 105
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462505362 256 QKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEE 292
Cdd:PRK12704  106 EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
PRK12704 PRK12704
phosphodiesterase; Provisional
93-260 1.52e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  93 ANKDLTERKYKGDSTIRELKAKLSGVEEE-LQRTKQEVLSLRREnstLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLV 171
Cdd:PRK12704   29 AEAKIKEAEEEAKRILEEAKKEAEAIKKEaLLEAKEEIHKLRNE---FEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 172 LRTKEAFDTiqeqkvvLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGD------LKTLMGKLKLKNTVTIQQe 245
Cdd:PRK12704  106 EKREEELEK-------KEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeakeilLEKVEEEARHEAAVLIKE- 177
                         170
                  ....*....|....*
gi 2462505362 246 kllAEKEEKLQKEQK 260
Cdd:PRK12704  178 ---IEEEAKEEADKK 189
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
120-307 1.52e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 120 EELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLvlrtKEAFDTIQEQKVvLEENGEKNQVQL 199
Cdd:COG4717    74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL----LQLLPLYQELEA-LEAELAELPERL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 200 GKLEA---TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQeklLAEKEEKLQKEQKELQdvgQSLRIKEQEV 276
Cdd:COG4717   149 EELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAELE---EELEEAQEEL 222
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462505362 277 CKLQEQLEATVKKLEESKQLLKNNEKLITWL 307
Cdd:COG4717   223 EELEEELEQLENELEAAALEERLKEARLLLL 253
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
22-323 2.98e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.55  E-value: 2.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  22 KQELDKLRNEWASHTAALTNKHSQ--ELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQnIHQLQNRLSEL-----EAAN 94
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQlnQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ-LNQLKSEISDLnnqkeQDWN 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  95 KDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQ----L 170
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQeiknL 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 171 VLRTKEAFDTIQEQKVV---LEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKL 247
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLnqqKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 248 LAEKEEKLQKEQKELQDVGQSLRIKEQE--------------VCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 313
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKElkklneekkeleekVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
                         330
                  ....*....|
gi 2462505362 314 NQLVRKQDVL 323
Cdd:TIGR04523 550 DDFELKKENL 559
CAGE1 pfam15066
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...
72-305 3.76e-05

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.


Pssm-ID: 464481  Cd Length: 528  Bit Score: 45.98  E-value: 3.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  72 LEILHQQNiHQLQNRLSELEAANKDLTERkykgdstIRELKAKLsgveeelqrTKQEVLslrrenstLDVechekekhVN 151
Cdd:pfam15066 320 LQKLKHTN-RKQQMQIQDLQCSNLYLEKK-------VKELQMKI---------TKQQVF--------VDI--------IN 366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 152 QLQTKVavlEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENgeKNQVQLGKLEATIKSLSAELLKANEIikKLQGDLKTLM 231
Cdd:pfam15066 367 KLKENV---EELIEDKYNVILEKNDINKTLQNLQEILANT--QKHLQESRKEKETLQLELKKIKVNYV--HLQERYITEM 439
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 232 GKLKLKNTVTIQQEKLLAEKEE---KLQKEQKELQDVGQSL--------RIKEQEVCKLQEQLEATVKK-LEESKQLLKN 299
Cdd:pfam15066 440 QQKNKSVSQCLEMDKTLSKKEEeveRLQQLKGELEKATTSAldllkrekETREQEFLSLQEEFQKHEKEnLEERQKLKSR 519

                  ....*.
gi 2462505362 300 NEKLIT 305
Cdd:pfam15066 520 LEKLVA 525
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
16-261 3.89e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.91  E-value: 3.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  16 KTLAEKKQELDKLRNEwashtAALTNKHSQELTNEKEKALqaqvqyqqqheqqkKDLEILhQQNIHQLQNRLSELEAANK 95
Cdd:COG4942    20 DAAAEAEAELEQLQQE-----IAELEKELAALKKEEKALL--------------KQLAAL-ERRIAALARRIRALEQELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  96 DLTERkykgdstIRELKAKLSGVEEELQRTKQE----VLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLV 171
Cdd:COG4942    80 ALEAE-------LAELEKEIAELRAELEAQKEElaelLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 172 LRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKntvtIQQEKLLAEK 251
Cdd:COG4942   153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL----QQEAEELEAL 228
                         250
                  ....*....|
gi 2462505362 252 EEKLQKEQKE 261
Cdd:COG4942   229 IARLEAEAAA 238
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
45-309 4.49e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 46.32  E-value: 4.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   45 QELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQNIHQlQNRLSELEAANKDLTerkykgdSTIRELKAKLSGVEEELQR 124
Cdd:pfam01576    4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEE-KNALQEQLQAETELC-------AEAEEMRARLAARKQELEE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  125 TKQEvlslrrenstLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEA 204
Cdd:pfam01576   76 ILHE----------LESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLED 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  205 TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLE 284
Cdd:pfam01576  146 QNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA 225
                          250       260
                   ....*....|....*....|....*.
gi 2462505362  285 ATVKKLEESK-QLLKNNEKLITWLNK 309
Cdd:pfam01576  226 ELQAQIAELRaQLAKKEEELQAALAR 251
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
71-321 4.54e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.17  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  71 DLEILHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDvechEKEKHV 150
Cdd:TIGR04523  61 KNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLE----KQKKEN 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 151 NQLQTKVAVleqEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKAN---EIIKKLQGDL 227
Cdd:TIGR04523 137 KKNIDKFLT---EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKN 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 228 KTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWL 307
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL 293
                         250
                  ....*....|....
gi 2462505362 308 NKELNENQLVRKQD 321
Cdd:TIGR04523 294 KSEISDLNNQKEQD 307
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
72-318 4.96e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.07  E-value: 4.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  72 LEILHQQNIHQLQNrLSELEAANKDLTERKYKGD-----STIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEK 146
Cdd:PRK05771   22 LEALHELGVVHIED-LKEELSNERLRKLRSLLTKlsealDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 147 EkhVNQLQTKVAVLEQEIKDKDQLVLRTK--EAFDTiqeqKVVLEENGEKNQVQLGKLEATIKS-LSAELLKANEIIKKl 223
Cdd:PRK05771  101 E--IKELEEEISELENEIKELEQEIERLEpwGNFDL----DLSLLLGFKYVSVFVGTVPEDKLEeLKLESDVENVEYIS- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 224 qgdlktlmgKLKLKNTVTIQQEKLLAEK-EEKLQK---EQKELQDVG---QSLRIKEQEVCKLQEQLEATVKKLEESKQl 296
Cdd:PRK05771  174 ---------TDKGYVYVVVVVLKELSDEvEEELKKlgfERLELEEEGtpsELIREIKEELEEIEKERESLLEELKELAK- 243
                         250       260
                  ....*....|....*....|..
gi 2462505362 297 lKNNEKLITWlnKELNENQLVR 318
Cdd:PRK05771  244 -KYLEELLAL--YEYLEIELER 262
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
78-294 5.03e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 5.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   78 QNIHQLQNRLSELEAANKDLTERKYKgdstiRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEkhVNQLQTKV 157
Cdd:COG4913    225 EAADALVEHFDDLERAHEALEDAREQ-----IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAEL 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  158 AVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQ-LGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgKLKL 236
Cdd:COG4913    298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAAL--GLPL 375
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  237 KNTVTI--QQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESK 294
Cdd:COG4913    376 PASAEEfaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
37-289 5.82e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 5.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  37 AALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLeilhQQNIHQLQNRLSELEAANKDLTERkykgdstIRELKAKLS 116
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARR-------IRALEQELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 117 GVEEELQRTKQEVLSLRREnstLDVECHEKEKHVNQLQTkvavleQEIKDKDQLVLRTKEAFDTIQEQKvVLEENGEKNQ 196
Cdd:COG4942    80 ALEAELAELEKEIAELRAE---LEAQKEELAELLRALYR------LGRQPPLALLLSPEDFLDAVRRLQ-YLKYLAPARR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 197 VQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEV 276
Cdd:COG4942   150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
                         250
                  ....*....|...
gi 2462505362 277 CKLQEQLEATVKK 289
Cdd:COG4942   230 ARLEAEAAAAAER 242
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2-217 6.82e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.14  E-value: 6.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   2 QSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALtnkhsqeltNEKEKALQAQVQYQQQHEQQKKDLEILHQQNIH 81
Cdd:COG4942    62 RRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---------EAQKEELAELLRALYRLGRQPPLALLLSPEDFL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  82 QLQNRLSELEAANKDLTERkykgdstIRELKAKLsgveEELQRTKQEVLSLRRenstldvechEKEKHVNQLQTKVAVLE 161
Cdd:COG4942   133 DAVRRLQYLKYLAPARREQ-------AEELRADL----AELAALRAELEAERA----------ELEALLAELEEERAALE 191
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462505362 162 QEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKAN 217
Cdd:COG4942   192 ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
19-317 8.71e-05

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: 45.49  E-value: 8.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   19 AEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKAlqaqVQYQQQHEQQKKDLEILHQQNIHQ---LQNRLSELEAA-- 93
Cdd:pfam15921  252 SESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKA----SSARSQANSIQSQLEIIQEQARNQnsmYMRQLSDLESTvs 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   94 --NKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLD-------VECHEKEKHVN--QLQTK------ 156
Cdd:pfam15921  328 qlRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDdqlqkllADLHKREKELSleKEQNKrlwdrd 407
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  157 ------VAVLEQEIKDKDQLVLRTKEAFDTIQ-EQKVVLEENGEKNQVQLGKLEaTIKSLSAELLKANEIIKKLQGDLKT 229
Cdd:pfam15921  408 tgnsitIDHLRRELDDRNMEVQRLEALLKAMKsECQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTA 486
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  230 LMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQ---EQLEATVKKLEESKQLLKNNEKLITW 306
Cdd:pfam15921  487 KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKnegDHLRNVQTECEALKLQMAEKDKVIEI 566
                          330
                   ....*....|..
gi 2462505362  307 LNKEL-NENQLV 317
Cdd:pfam15921  567 LRQQIeNMTQLV 578
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
145-320 8.88e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 8.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 145 EKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQ 224
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 225 GDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLI 304
Cdd:COG4942   104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
                         170
                  ....*....|....*.
gi 2462505362 305 TWLNKELNENQLVRKQ 320
Cdd:COG4942   184 EEERAALEALKAERQK 199
PTZ00121 PTZ00121
MAEBL; Provisional
5-350 9.35e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 9.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362    5 DDATKQLDFTRKtlAEKKQELDKLRN-EWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEilhqQNIHQL 83
Cdd:PTZ00121  1506 AEAKKKADEAKK--AEEAKKADEAKKaEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE----EDKNMA 1579
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   84 QNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEElQRTKQEvlSLRREnstldvecHEKEKHVNQLQTKVavlEQE 163
Cdd:PTZ00121  1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAE--ELKKA--------EEEKKKVEQLKKKE---AEE 1645
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  164 IKDKDQLvlRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQ 243
Cdd:PTZ00121  1646 KKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  244 QEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKqllKNNEKLItwlNKELNENQLVRKQDVl 323
Cdd:PTZ00121  1724 AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR---KEKEAVI---EEELDEEDEKRRMEV- 1796
                          330       340
                   ....*....|....*....|....*..
gi 2462505362  324 gPSTTPPAHSSSNTIRSGISPNLNVVD 350
Cdd:PTZ00121  1797 -DKKIKDIFDNFANIIEGGKEGNLVIN 1822
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
77-281 1.37e-04

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 44.03  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  77 QQNIHQLQNRLSELEAANkDLTERKYKGDST---IRELKAKLSGVEEELQRTKQEVLSLRREnstLDVECHEKEKHVNQL 153
Cdd:pfam15905 121 SASVASLEKQLLELTRVN-ELLKAKFSEDGTqkkMSSLSMELMKLRNKLEAKMKEVMAKQEG---MEGKLQVTQKNLEHS 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 154 QTKVAVLEQEIKDKDQLVLRTK----EAFDTIQEQKVVLEEnGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKT 229
Cdd:pfam15905 197 KGKVAQLEEKLVSTEKEKIEEKseteKLLEYITELSCVSEQ-VEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSK 275
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462505362 230 LMGKLKLK-NTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQE 281
Cdd:pfam15905 276 QIKDLNEKcKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
76-315 1.41e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.34  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  76 HQQNI--HQLQNRLSELEAAN-KDLTERKYKGDSTIRELKAKLSGVEEELQR-----TKQEVLSLRRENSTLDVECHEKE 147
Cdd:pfam17380 280 HQKAVseRQQQEKFEKMEQERlRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaiyAEQERMAMERERELERIRQEERK 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 148 KHVNQL-QTKVAVLEQEIKDKDQLVL-------RTKEAFDTIQEQKVVLEENGEKNQVQLGKLEatikSLSAELLKANEI 219
Cdd:pfam17380 360 RELERIrQEEIAMEISRMRELERLQMerqqkneRVRQELEAARKVKILEEERQRKIQQQKVEME----QIRAEQEEARQR 435
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 220 -IKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQdvgqslriKEQEVCKLQEQLEATV--KKLEESKQL 296
Cdd:pfam17380 436 eVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE--------KEKRDRKRAEEQRRKIleKELEERKQA 507
                         250
                  ....*....|....*....
gi 2462505362 297 LKNNEKLITWLNKELNENQ 315
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQ 526
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
23-323 1.64e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  23 QELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILHQ---QNIHQLQNRLSELEAANKDLTE 99
Cdd:COG4717    74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyQELEALEAELAELPERLEELEE 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 100 RKykgdSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTldvechEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFD 179
Cdd:COG4717   154 RL----EELRELEEELEELEAELAELQEELEELLEQLSL------ATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 180 TIQEQKVVLEENGEKNQV--QLGKLEATIKSLSAeLLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQK 257
Cdd:COG4717   224 ELEEELEQLENELEAAALeeRLKEARLLLLIAAA-LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462505362 258 EQKELQDVGQSLRIKEQEVCKL-----------QEQLEATVKKLEESKQLLKNNEKlitwLNKELNENQLVRKQDVL 323
Cdd:COG4717   303 EAEELQALPALEELEEEELEELlaalglppdlsPEELLELLDRIEELQELLREAEE----LEEELQLEELEQEIAAL 375
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
35-320 1.69e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  35 HTAALTNKHSQELTN-EKEKALQAQVQYQQQHEQQKKDLEILHQQNI-------HQLQNRLSELEAANKDLTERKYKGDS 106
Cdd:PRK03918  449 HRKELLEEYTAELKRiEKELKEIEEKERKLRKELRELEKVLKKESELiklkelaEQLKELEEKLKKYNLEELEKKAEEYE 528
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 107 TIRE----LKAKLSGVEEELQRTKQevlsLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFdtiq 182
Cdd:PRK03918  529 KLKEklikLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPF---- 600
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 183 EQKVVLEENGEKnqvQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKlkntvtiQQEKLLAEKE-EKLQKEQKE 261
Cdd:PRK03918  601 YNEYLELKDAEK---ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE-------ELEKKYSEEEyEELREEYLE 670
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462505362 262 LQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 320
Cdd:PRK03918  671 LSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
46 PHA02562
endonuclease subunit; Provisional
71-312 1.75e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 44.23  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  71 DLEILH-QQNIHQLQNRLSELEAANKDLTERKykgdstirelKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKH 149
Cdd:PHA02562  187 DMKIDHiQQQIKTYNKNIEEQRKKNGENIARK----------QNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAA 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 150 VNQLQTKVAVLEQEIK--DKDQLVLRT-------KEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEII 220
Cdd:PHA02562  257 LNKLNTAAAKIKSKIEqfQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQS 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 221 KKLQgDLKTLMGKLKlkntvtiQQEKLLAEKEEKLQKEQKELQDvgqSLRIKEQEVCKLQEQLEATVKKLEESKQ----- 295
Cdd:PHA02562  337 KKLL-ELKNKISTNK-------QSLITLVDKAKKVKAAIEELQA---EFVDNAEELAKLQDELDKIVKTKSELVKekyhr 405
                         250       260
                  ....*....|....*....|....*....
gi 2462505362 296 -----LLKNN-------EKLITWLNKELN 312
Cdd:PHA02562  406 givtdLLKDSgikasiiKKYIPYFNKQIN 434
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
70-302 2.21e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 43.67  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  70 KDLEILHQQN---IHQLQNRLSELEaanKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQevlslrrENSTLDVEchEK 146
Cdd:PRK04778  129 QELLESEEKNreeVEQLKDLYRELR---KSLLANRFSFGPALDELEKQLENLEEEFSQFVE-------LTESGDYV--EA 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 147 EKHVNQLQTKVAVLEQEIKDKDQLVLRT-----------KEAFDTIQEQKVVLEENGEKNQV-----QLGKLEATIKSLs 210
Cdd:PRK04778  197 REILDQLEEELAALEQIMEEIPELLKELqtelpdqlqelKAGYRELVEEGYHLDHLDIEKEIqdlkeQIDENLALLEEL- 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 211 aELLKANEIIKKLQGDLKTLMGKL----KLKNTVTIQQEKL---LAEKEEKLQKEQKELQDVGQSLRIKEQEVCK---LQ 280
Cdd:PRK04778  276 -DLDEAEEKNEEIQERIDQLYDILerevKARKYVEKNSDTLpdfLEHAKEQNKELKEEIDRVKQSYTLNESELESvrqLE 354
                         250       260
                  ....*....|....*....|..
gi 2462505362 281 EQLEATVKKLEESKQLLKNNEK 302
Cdd:PRK04778  355 KQLESLEKQYDEITERIAEQEI 376
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
77-314 2.59e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  77 QQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTK 156
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 157 VAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKL 236
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 237 KNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSL---------RIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWL 307
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELkkenlekeiDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601

                  ....*..
gi 2462505362 308 NKELNEN 314
Cdd:TIGR04523 602 IKEIEEK 608
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
95-303 3.06e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  95 KDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRT 174
Cdd:PRK03918  182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 175 KEAFDTIQEQKVVLEEngeknqvqLGKLEATIKSLSaELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEK 254
Cdd:PRK03918  262 RELEERIEELKKEIEE--------LEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2462505362 255 LQKEQKELQDvgqsLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 303
Cdd:PRK03918  333 LEEKEERLEE----LKKKLKELEKRLEELEERHELYEEAKAKKEELERL 377
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
105-303 3.12e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 105 DSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ 184
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 185 KVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-LKNTVTIQQEKLLAEKEEKLQKEQKELQ 263
Cdd:COG4372   110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEsLQEELAALEQELQALSEAEAEQALDELL 189
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462505362 264 DVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 303
Cdd:COG4372   190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
86-313 3.54e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  86 RLSELEAANKDLTErkykgdsTIRELKAKLSGVEEELQRTkQEVLSLRRENSTldvECHEKEKHVNQLQTKVAVLEQEIK 165
Cdd:PRK03918  156 GLDDYENAYKNLGE-------VIKEIKRRIERLEKFIKRT-ENIEELIKEKEK---ELEEVLREINEISSELPELREELE 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 166 DKDQLVLR---TKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQgdlktlmgKLKLKNTVTI 242
Cdd:PRK03918  225 KLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK--------ELKEKAEEYI 296
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462505362 243 QQEKLLAEKEEKLQKEQKELQDVgqslrikEQEVCKLQEQLeatvKKLEESKQLLKNNEKLITWLNKELNE 313
Cdd:PRK03918  297 KLSEFYEEYLDELREIEKRLSRL-------EEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEE 356
PRK12704 PRK12704
phosphodiesterase; Provisional
194-313 4.64e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 194 KNQVQLGKLEATIKSLSAELLKANEIIKKLqgdlKTLMGK---LKLKNtvtiQQEKLLAEKEEKLQKEQKELQDVGQSLR 270
Cdd:PRK12704   28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKE----ALLEAKeeiHKLRN----EFEKELRERRNELQKLEKRLLQKEENLD 99
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462505362 271 IKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 313
Cdd:PRK12704  100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
9-199 4.81e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   9 KQLDFTRKTLAEKKQELDKLRNE----WASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDL--------EILH 76
Cdd:COG3206   182 EQLPELRKELEEAEAALEEFRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalpELLQ 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  77 QQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVL-SLRRENSTLDVECHEKEKHVNQLQT 155
Cdd:COG3206   262 SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEA 341
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2462505362 156 KVAVL---EQEIKDKDQLVLRTKEAFDTIQE--QKVVLEENGEKNQVQL 199
Cdd:COG3206   342 RLAELpelEAELRRLEREVEVARELYESLLQrlEEARLAEALTVGNVRV 390
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
86-330 5.29e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 42.61  E-value: 5.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  86 RLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRR-ENSTLDVECHEKEKHVnqlQTKVAVLEQEI 164
Cdd:PRK05771   80 SVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPwGNFDLDLSLLLGFKYV---SVFVGTVPEDK 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 165 KDKDQLVLrtkeafdtiqEQKVVLEENGEKNQVQLgkLEATIKSLSAELlkaNEIIKKLQGDlktlmgKLKLKNTVTIQQ 244
Cdd:PRK05771  157 LEELKLES----------DVENVEYISTDKGYVYV--VVVVLKELSDEV---EEELKKLGFE------RLELEEEGTPSE 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 245 ekLLAEKEEKLQKEQKELQDVGQSLR----IKEQEVCKLQEQLEATVKKLEESKQLL--------------KNNEKLITW 306
Cdd:PRK05771  216 --LIREIKEELEEIEKERESLLEELKelakKYLEELLALYEYLEIELERAEALSKFLktdktfaiegwvpeDRVKKLKEL 293
                         250       260
                  ....*....|....*....|....
gi 2462505362 307 LNKELNENQLVRKQDVLGPSTTPP 330
Cdd:PRK05771  294 IDKATGGSAYVEFVEPDEEEEEVP 317
PRK11281 PRK11281
mechanosensitive channel MscK;
77-319 5.41e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.59  E-value: 5.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   77 QQNIHQLQNRLSELEAANKDLTErkykgdstireLKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKhVNQLQTK 156
Cdd:PRK11281    62 QQDLEQTLALLDKIDRQKEETEQ-----------LKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLS-LRQLESR 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  157 VAVLEQEIKDkdqlvlrTKEAFDTIQEQKVVLEENGEK-------NQVQLGKLEATIKSLSAELLKAN-EIIKKLQGDLK 228
Cdd:PRK11281   130 LAQTLDQLQN-------AQNDLAEYNSQLVSLQTQPERaqaalyaNSQRLQQIRNLLKGGKVGGKALRpSQRVLLQAEQA 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  229 TLMGKLK-----LKNTVTIQ-----QEKLLAEKEEKLQKEQKELQDVGQSLRIK--EQEVCKLQEQLEAT-------VKK 289
Cdd:PRK11281   203 LLNAQNDlqrksLEGNTQLQdllqkQRDYLTARIQRLEHQLQLLQEAINSKRLTlsEKTVQEAQSQDEAAriqanplVAQ 282
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2462505362  290 -----LEESKQLLKNNEKLitwlnkelneNQLVRK 319
Cdd:PRK11281   283 eleinLQLSQRLLKATEKL----------NTLTQQ 307
PTZ00121 PTZ00121
MAEBL; Provisional
5-317 5.54e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 5.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362    5 DDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKhSQELTNEKEKAlQAQVQYQQQHEQQKKDLEILHQQNIHQLQ 84
Cdd:PTZ00121  1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK-ADEAKKKAEEA-KKKADEAKKAAEAKKKADEAKKAEEAKKA 1524
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   85 NRLSELEAANKDLTERKYKGDSTIREL-KAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQE 163
Cdd:PTZ00121  1525 DEAKKAEEAKKADEAKKAEEKKKADELkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  164 IKDKDQLVLRTKEAfdTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQ 243
Cdd:PTZ00121  1605 KKMKAEEAKKAEEA--KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462505362  244 QEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCK---LQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLV 317
Cdd:PTZ00121  1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
80-298 6.20e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 42.13  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  80 IHQLQN----RLSELEAANKDLTERKYKGDSTirelkaklsGVEEELQRTKQEVLSLRRENSTLDVEchEKEKHVNQLQT 155
Cdd:PRK04778  221 LKELQTelpdQLQELKAGYRELVEEGYHLDHL---------DIEKEIQDLKEQIDENLALLEELDLD--EAEEKNEEIQE 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 156 KV----AVLEQEIKDK---DQLVLRTKEAFDTIQEQKVVLEEN----GEKNQVQLGKLEaTIKSLSAELlkaNEIIKKLQ 224
Cdd:PRK04778  290 RIdqlyDILEREVKARkyvEKNSDTLPDFLEHAKEQNKELKEEidrvKQSYTLNESELE-SVRQLEKQL---ESLEKQYD 365
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462505362 225 GDLKTLMGKLKLKNTVTIQQEKLLAEKEEkLQKEQKELQDVGQSLRIKEQEVcklQEQLEATVKKLEESKQLLK 298
Cdd:PRK04778  366 EITERIAEQEIAYSELQEELEEILKQLEE-IEKEQEKLSEMLQGLRKDELEA---REKLERYRNKLHEIKRYLE 435
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
77-319 8.37e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 42.27  E-value: 8.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   77 QQNIHQLQNRLSELEAANKDLTERKYKgdsTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTK 156
Cdd:pfam02463  182 TENLAELIIDLEELKLQELKLKEQAKK---ALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  157 VAVLEQEIKDKDQLVLRTKEAFDTIQE-QKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMG--- 232
Cdd:pfam02463  259 EIEKEEEKLAQVLKENKEEEKEKKLQEeELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEeie 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  233 -KLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDvgqsLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKEL 311
Cdd:pfam02463  339 eLEKELKELEIKREAEEEEEEELEKLQEKLEQL----EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELA 414

                   ....*...
gi 2462505362  312 NENQLVRK 319
Cdd:pfam02463  415 RQLEDLLK 422
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
14-320 1.16e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.50  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   14 TRKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQNIHQLQNRLSELEAA 93
Cdd:pfam02463  665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   94 NKDLTERKYKGDSTIRELKAKLSgvEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLR 173
Cdd:pfam02463  745 IDEEEEEEEKSRLKKEEKEEEKS--ELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQL 822
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  174 TKEAFDTIQEQKVVLEENGEKN-QVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNtvTIQQEKLLAEKE 252
Cdd:pfam02463  823 LIEQEEKIKEEELEELALELKEeQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDEL--ESKEEKEKEEKK 900
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462505362  253 EKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 320
Cdd:pfam02463  901 ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLA 968
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
101-322 1.33e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 101 KYKgdSTIRELKAKLSGVEEELQRtkqevLSLRREnstldvechEKEKHVNQL--QTKVA----VLEQEIKDKDQLVLRT 174
Cdd:COG1196   169 KYK--ERKEEAERKLEATEENLER-----LEDILG---------ELERQLEPLerQAEKAeryrELKEELKELEAELLLL 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 175 KeaFDTIQEQKVVLEEngeknqvQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEK 254
Cdd:COG1196   233 K--LRELEAELEELEA-------ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462505362 255 LQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQDV 322
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
82-303 1.34e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 40.66  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  82 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDV---ECHEKEKHVNQL----Q 154
Cdd:COG1340    47 ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKaggSIDKLRKEIERLewrqQ 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 155 TKVAVLEQEIkdkdQLVLRTKEAFDTIQEQKVVLEENGEKN---------QVQLGKLEATIKSLSAELLKANEIIKKLQG 225
Cdd:COG1340   127 TEVLSPEEEK----ELVEKIKELEKELEKAKKALEKNEKLKelraelkelRKEAEEIHKKIKELAEEAQELHEEMIELYK 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 226 DLKTLMGKL-KLKNTVTIQQEKL--LAEKEEKLQKEQKELQDVGQSLRIKEQEVcKLQEQLEATVKKLEESKQLLKNNEK 302
Cdd:COG1340   203 EADELRKEAdELHKEIVEAQEKAdeLHEEIIELQKELRELRKELKKLRKKQRAL-KREKEKEELEEKAEEIFEKLKKGEK 281

                  .
gi 2462505362 303 L 303
Cdd:COG1340   282 L 282
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
244-315 1.36e-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: 40.90  E-value: 1.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462505362 244 QEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQ 315
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
75-299 1.36e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.31  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   75 LHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEeelqRTKQEVLSLRREnstLDVECHEKEKHVNQLQ 154
Cdd:pfam01576  156 LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEE----KGRQELEKAKRK---LEGESTDLQEQIAELQ 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  155 TKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKL 234
Cdd:pfam01576  229 AQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEL 308
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462505362  235 KLKNTVTIQQEKLLAEKEEKLQKEQKELQDVG-------QSLRIKE-QEVCKLQEQLEATVK---KLEESKQLLKN 299
Cdd:pfam01576  309 EDTLDTTAAQQELRSKREQEVTELKKALEEETrsheaqlQEMRQKHtQALEELTEQLEQAKRnkaNLEKAKQALES 384
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-145 1.71e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362    2 QSLDDATKQLDFTRKTLAEKKQELDKLRNEWASH-TAALtnkhsQELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQ-- 78
Cdd:COG4913    302 AELARLEAELERLEARLDALREELDELEAQIRGNgGDRL-----EQLEREIERLERELEERERRRARLEALLAALGLPlp 376
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462505362   79 -NIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHE 145
Cdd:COG4913    377 aSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
108-304 2.40e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.48  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 108 IRELKAKLSGVEEELQRtkqEVLSLRRENSTLDVECHEKEkhvNQLQTKVAVLEQEIKDKDQLVLRTK---EAFDTIQEQ 184
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKE---NKMKDLTFLLEESRDKANQLEEKTKlqdENLKELIEK 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 185 KVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNT----VTIQQEKLLAEKEEKLQKEQK 260
Cdd:pfam05483 291 KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAahsfVVTEFEATTCSLEELLRTEQQ 370
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462505362 261 ELQDVGQSLRIKEQEVCKLQEQLEATVK-------KLEESKQLLKNNEKLI 304
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELEEMTKfknnkevELEELKKILAEDEKLL 421
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
198-313 2.68e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 198 QLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKL-----QKE----QKELQDVGQS 268
Cdd:COG1579    25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEyealQKEIESLKRR 104
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462505362 269 LRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 313
Cdd:COG1579   105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
PRK12705 PRK12705
hypothetical protein; Provisional
172-318 2.85e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.08  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 172 LRTKEAFDTIQEqkVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgklklkntvtIQQEKLLAEK 251
Cdd:PRK12705   30 RLAKEAERILQE--AQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERL-----------VQKEEQLDAR 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462505362 252 EEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEAtvkKLEESKQLLKN--NEKLITWLNKELNENQLVR 318
Cdd:PRK12705   97 AEKLDNLENQLEEREKALSARELELEELEKQLDN---ELYRVAGLTPEqaRKLLLKLLDAELEEEKAQR 162
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1-285 2.99e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   1 MQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAAL--TNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQ 78
Cdd:COG4372    37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELeqLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  79 nIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKE--KHVNQLQTK 156
Cdd:COG4372   117 -LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldELLKEANRN 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 157 VAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKL 236
Cdd:COG4372   196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2462505362 237 KNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEA 285
Cdd:COG4372   276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
TOP4c cd00187
DNA Topoisomerase, subtype IIA; domain A'; bacterial DNA topoisomerase IV (C subunit, ParC), ...
193-313 3.06e-03

DNA Topoisomerase, subtype IIA; domain A'; bacterial DNA topoisomerase IV (C subunit, ParC), bacterial DNA gyrases (A subunit, GyrA),mammalian DNA toposiomerases II. DNA topoisomerases are essential enzymes that regulate the conformational changes in DNA topology by catalysing the concerted breakage and rejoining of DNA strands during normal cellular growth.


Pssm-ID: 238111 [Multi-domain]  Cd Length: 445  Bit Score: 39.86  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 193 EKNQVQLGKLEATIKSLSAeLLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKElqdvgqslrik 272
Cdd:cd00187   341 GKAEARLHILEGLLKAILN-IDEVINLIRSSDEAKKALIEELEKLGFSEIQADAILDMRLRRLTKLERE----------- 408
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462505362 273 eqevcKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 313
Cdd:cd00187   409 -----KLLKELKELEAEIEDLEKILASEERPKDLWKEELDE 444
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
77-313 3.78e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.03  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   77 QQNIHQLQNRLSELEAANKDLTERKYKGDSTiRELKAKLSGVEEELQRTKQE--------------VLSLRRENSTLDVE 142
Cdd:TIGR00606  604 EQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQramlagatavysqfITQLTDENQSCCPV 682
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  143 CH-------EKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLK 215
Cdd:TIGR00606  683 CQrvfqteaELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQR 762
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  216 ANEIIKKLQGDLKTLMGKLKLKN------TVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKE--QEVCKLQEQLEATV 287
Cdd:TIGR00606  763 LKNDIEEQETLLGTIMPEEESAKvcltdvTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQvnQEKQEKQHELDTVV 842
                          250       260
                   ....*....|....*....|....*.
gi 2462505362  288 KKLEESKQLLKNNEKLITWLNKELNE 313
Cdd:TIGR00606  843 SKIELNRKLIQDQQEQIQHLKSKTNE 868
COG5022 COG5022
Myosin heavy chain [General function prediction only];
100-313 3.78e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 40.06  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  100 RKYKGD--STIRELKAKLsgVEEELQRTKQEVLSLRRENSTLD--VECHEKEKHVNQLQTKVAVLeqeikdkdQLVLRTK 175
Cdd:COG5022    809 RKEYRSylACIIKLQKTI--KREKKLRETEEVEFSLKAEVLIQkfGRSLKAKKRFSLLKKETIYL--------QSAQRVE 878
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  176 EAFDTIQEQKvvlEENGEKNQVqlgkleatiKSLSAELLK-ANEIIKKLQGDLktlMGKLKLKNTVTIQQEKLLAEKEEK 254
Cdd:COG5022    879 LAERQLQELK---IDVKSISSL---------KLVNLELESeIIELKKSLSSDL---IENLEFKTELIARLKKLLNNIDLE 943
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462505362  255 LQKE-QKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESK-QLLKNNEKLITWlNKELNE 313
Cdd:COG5022    944 EGPSiEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVrEGNKANSELKNF-KKELAE 1003
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
76-275 3.91e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   76 HQQNIHQLQNRLSELEAANKDLteRKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKH------ 149
Cdd:COG4913    260 LAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgngg 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  150 --VNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQ----LGKLEATIKSLSAELLKANEIIKKL 223
Cdd:COG4913    338 drLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaaalLEALEEELEALEEALAEAEAALRDL 417
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462505362  224 QGDLKTLMGKLKL----KNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQE 275
Cdd:COG4913    418 RRELRELEAEIASlerrKSNIPARLLALRDALAEALGLDEAELPFVGELIEVRPEE 473
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
192-323 4.22e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 4.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  192 GEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLL--AEKEEKLQKEQKELQDVGQSl 269
Cdd:COG4913    605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDAS- 683
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462505362  270 rikEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELN--ENQLVRKQDVL 323
Cdd:COG4913    684 ---SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEqaEEELDELQDRL 736
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
80-299 4.29e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 39.45  E-value: 4.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  80 IHQLQN----RLSELEAANKDLTERKYKGDSTirELKAKLSGVEEELQRTKQEVLSLRRENSTLDVEchEKEKHVNQLQt 155
Cdd:pfam06160 202 YEELKTelpdQLEELKEGYREMEEEGYALEHL--NVDKEIQQLEEQLEENLALLENLELDEAEEALE--EIEERIDQLY- 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 156 kvAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEK-NQVQL-----GKLEATIKSLSAELlkaNEIIKKLQGDLKT 229
Cdd:pfam06160 277 --DLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEElERVQQsytlnENELERVRGLEKQL---EELEKRYDEIVER 351
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 230 LMGKLKLKNTVTIQQEKLLAEKEEkLQKEQKELQDVGQSLRIKEQEVcklQEQLEATVKKLEESKQLLKN 299
Cdd:pfam06160 352 LEEKEVAYSELQEELEEILEQLEE-IEEEQEEFKESLQSLRKDELEA---REKLDEFKLELREIKRLVEK 417
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
45-302 4.39e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 39.70  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  45 QELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQNihqlQNRLSELEaankdltERKYKGDSTIRELKAKLSGVEEELQR 124
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKENKMKDLTFLLEES----RDKANQLE-------EKTKLQDENLKELIEKKDHLTKELED 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 125 TKQEVLSLRRENSTLDVECHEKEKHVNQL-QTKVAVLEQEIKDKDQLVLRTKEAFDTIqeqkVVLEENGEKNQVQLGKLE 203
Cdd:pfam05483 301 IKMSLQRSMSTQKALEEDLQIATKTICQLtEEKEAQMEELNKAKAAHSFVVTEFEATT----CSLEELLRTEQQRLEKNE 376
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 204 ATIKSLSAELLKANEIIKKlqgdlktlMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQL 283
Cdd:pfam05483 377 DQLKIITMELQKKSSELEE--------MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR 448
                         250
                  ....*....|....*....
gi 2462505362 284 EATVKKLEESKQLLKNNEK 302
Cdd:pfam05483 449 EKEIHDLEIQLTAIKTSEE 467
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
2-301 4.91e-03

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: 39.72  E-value: 4.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362    2 QSLDDATKQLDFTRKTLAEKKQELDKLRNEwashtAALTNKHSQELTNEKE---KALQAQVQYQQQHEQQKKDLEILHQQ 78
Cdd:pfam15921  496 RTVSDLTASLQEKERAIEATNAEITKLRSR-----VDLKLQELQHLKNEGDhlrNVQTECEALKLQMAEKDKVIEILRQQ 570
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   79 --NIHQLQNR--------LSELEAANKDLTER----------KYKGDSTIRELKAKLSGVEeelqrtkqevlslrrenst 138
Cdd:pfam15921  571 ieNMTQLVGQhgrtagamQVEKAQLEKEINDRrlelqefkilKDKKDAKIRELEARVSDLE------------------- 631
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  139 ldvecHEKEKHVNQLQTKVAVLEQEIKDKDQL---VLRTKEAFDTIQEQKVVLEEN----GEKNQVQLGKLEATIKSLSA 211
Cdd:pfam15921  632 -----LEKVKLVNAGSERLRAVKDIKQERDQLlneVKTSRNELNSLSEDYEVLKRNfrnkSEEMETTTNKLKMQLKSAQS 706
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  212 ELLKANEIIKKLQGD----LKTLMGKLK-----------LKNTVTIQQEKLL-AEKEEKLQKEQKelQDVGQSLRIKEQE 275
Cdd:pfam15921  707 ELEQTRNTLKSMEGSdghaMKVAMGMQKqitakrgqidaLQSKIQFLEEAMTnANKEKHFLKEEK--NKLSQELSTVATE 784
                          330       340
                   ....*....|....*....|....*.
gi 2462505362  276 VCKLQEQLEATVKKLEESKQLLKNNE 301
Cdd:pfam15921  785 KNKMAGELEVLRSQERRLKEKVANME 810
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
2-222 6.09e-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: 38.37  E-value: 6.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   2 QSLDDATKQLDFTRKTLaekKQELDKLRNEWASHTAALTNKhsqeltnekekalqaqvqyqqqheqqkkdleilhQQNIH 81
Cdd:COG1579    13 QELDSELDRLEHRLKEL---PAELAELEDELAALEARLEAA----------------------------------KTELE 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  82 QLQNRLSELEAANKDLTERkykgdstIRELKAKLSGV--EEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAV 159
Cdd:COG1579    56 DLEKEIKRLELEIEEVEAR-------IKKYEEQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAE 128
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462505362 160 LEQEIKDKDQLVLRTKEAFDTIQEQkvvLEENGEKNQVQLGKLEATIkslSAELLKANEIIKK 222
Cdd:COG1579   129 LEAELAELEAELEEKKAELDEELAE---LEAELEELEAEREELAAKI---PPELLALYERIRK 185
PRK11281 PRK11281
mechanosensitive channel MscK;
77-316 6.86e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.12  E-value: 6.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362   77 QQNIHQLQNRLSELEAANKDLTErkykgdSTIRELKAKLSGVEE--ELQRTK-------QEVLSLRRENSTLdvecheke 147
Cdd:PRK11281   169 SQRLQQIRNLLKGGKVGGKALRP------SQRVLLQAEQALLNAqnDLQRKSlegntqlQDLLQKQRDYLTA-------- 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  148 kHVNQLQTKVAVLEQEIKDKdqlvlRTKEAFDTIQEQkVVLEENGEKNQVQLGKLEATI-KSLSAELLKANEiikklqgD 226
Cdd:PRK11281   235 -RIQRLEHQLQLLQEAINSK-----RLTLSEKTVQEA-QSQDEAARIQANPLVAQELEInLQLSQRLLKATE-------K 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  227 LKTLMGK-LKLKNTV--TIQQEKLLAEKEEKLQ----------KEQ------KELQDVGQS---LRIKEQEVCKLQEQL- 283
Cdd:PRK11281   301 LNTLTQQnLRVKNWLdrLTQSERNIKEQISVLKgslllsrilyQQQqalpsaDLIEGLADRiadLRLEQFEINQQRDALf 380
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2462505362  284 --EATVKKLEES-------------KQLLKNNEKLITWLNKELNeNQL 316
Cdd:PRK11281   381 qpDAYIDKLEAGhksevtdevrdalLQLLDERRELLDQLNKQLN-NQL 427
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
72-297 8.61e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 38.65  E-value: 8.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  72 LEILHQQNIHQLQNRLSELEAANKDLterkykgdstiRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVN 151
Cdd:pfam10174 452 IERLKEQREREDRERLEELESLKKEN-----------KDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLK 520
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 152 QLqtkvavlEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQvqlgkleaTIKSLSAELLKANEIIKKLQGDLKTLM 231
Cdd:pfam10174 521 SL-------EIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEIND--------RIRLLEQEVARYKEESGKAQAEVERLL 585
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 232 GKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEV--------------------CKLQEQLEATVKKLE 291
Cdd:pfam10174 586 GILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMkkkgaqlleearrrednladNSQQLQLEELMGALE 665

                  ....*.
gi 2462505362 292 ESKQLL 297
Cdd:pfam10174 666 KTRQEL 671
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
209-315 8.74e-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: 38.21  E-value: 8.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 209 LSAELLKANEIIKKLQGDLKTLmgklklkntvtiQQEklLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVK 288
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQL------------QQE--IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ 76
                          90       100
                  ....*....|....*....|....*..
gi 2462505362 289 KLEESKQLLKNNEKLITWLNKELNENQ 315
Cdd:COG4942    77 ELAALEAELAELEKEIAELRAELEAQK 103
PRK01156 PRK01156
chromosome segregation protein; Provisional
69-313 9.72e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 38.73  E-value: 9.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362  69 KKDLEILHQQNIHQLQNRLSELEAANKDLTERKYKgDSTIRELKAKLSGVEEELQRTKQEVLSLRREN--------STLD 140
Cdd:PRK01156  503 KKRKEYLESEEINKSINEYNKIESARADLEDIKIK-INELKDKHDKYEEIKNRYKSLKLEDLDSKRTSwlnalaviSLID 581
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 141 VEC-----HEKEKHVNQLQTKVAVLEQEIKD----KDQLVLRTKEAFDTIQEQKVVLEENgeknQVQLGKLEATIKSLSA 211
Cdd:PRK01156  582 IETnrsrsNEIKKQLNDLESRLQEIEIGFPDdksyIDKSIREIENEANNLNNKYNEIQEN----KILIEKLRGKIDNYKK 657
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505362 212 ELLKANEIIKKlqgdlktlmgklklKNTVTIQqeklLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLE 291
Cdd:PRK01156  658 QIAEIDSIIPD--------------LKEITSR----INDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIN 719
                         250       260
                  ....*....|....*....|....
gi 2462505362 292 ESKQLLKNNEKLITWLN--KELNE 313
Cdd:PRK01156  720 DINETLESMKKIKKAIGdlKRLRE 743
 
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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