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Conserved domains on  [gi|577645388|gb|EUI56827|]
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septation ring formation regulator EzrA [Staphylococcus aureus M1184]

Protein Classification

septation ring formation regulator EzrA( domain architecture ID 11480297)

septation ring formation regulator EzrA is a negative regulator of FtsZ ring formation; it modulates the frequency and position of FtsZ ring formation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
18-564 0e+00

septation ring formation regulator EzrA; Provisional


:

Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 583.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  18 GVLFYLRSNKRQIIEKAIERKNEIETLPFDQNLAQLSKLNLKGETKTKYDAMKKDNVESTNKYLAPVEEKIHNAEALLDK 97
Cdd:PRK04778  18 LAGLILRKRNYKRIDELEERKQELENLPVNDELEKVKKLNLTGQSEEKFEEWRQKWDEIVTNSLPDIEEQLFEAEELNDK 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  98 FSFNASQSEIDDANELMDSYEQSYQQQLEDVNEIIALYKDNDELYDKCKVDYREMKRDVLANRHQFGEAASLLETEIEKF 177
Cdd:PRK04778  98 FRFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENL 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 178 EPRLEQYEVLKADGNYVQAHNHIAALNEQMKQLRSYMEEIPELIRETQKELPGQFQDLKYGCRDLKVEGYDLDHVKVDST 257
Cdd:PRK04778 178 EEEFSQFVELTESGDYVEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHLDHLDIEKE 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 258 LQSLKTELSFVEPLISRLELEEANDKLANINDKLDDMYDLIEHEVKAKNDVEETKDIITDNLFKAKDMNYTLQTEIEYVR 337
Cdd:PRK04778 258 IQDLKEQIDENLALLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVK 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 338 ENYYINESDAQSVRQFENEIQSLISVYDDILKEMSKSAVRYSEVQDNLQYLEDHVTVINDKQEKLQNHLIQLREDEAEAE 417
Cdd:PRK04778 338 QSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAR 417
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 418 DNLLRVQSKKEEVYRRLLASNLTSVPERFIIMKNEIDHEVRDVNEQFSERPIHVKQLKDKVSKIVIQMNTFEDEANDVLV 497
Cdd:PRK04778 418 EKLERYRNKLHEIKRYLEKSNLPGLPEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVE 497
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577645388 498 NAVYAEKLIQYGNRYRKDYSNVDKSLNEAERLFKNNRYKRAIEIAEQALESVEPGVTKHIEEEVIKQ 564
Cdd:PRK04778 498 NATLTEQLIQYANRYRSDNEEVAEALNEAERLFREYDYKAALEIIATALEKVEPGVTKRIEDSYEKE 564
 
Name Accession Description Interval E-value
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
18-564 0e+00

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 583.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  18 GVLFYLRSNKRQIIEKAIERKNEIETLPFDQNLAQLSKLNLKGETKTKYDAMKKDNVESTNKYLAPVEEKIHNAEALLDK 97
Cdd:PRK04778  18 LAGLILRKRNYKRIDELEERKQELENLPVNDELEKVKKLNLTGQSEEKFEEWRQKWDEIVTNSLPDIEEQLFEAEELNDK 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  98 FSFNASQSEIDDANELMDSYEQSYQQQLEDVNEIIALYKDNDELYDKCKVDYREMKRDVLANRHQFGEAASLLETEIEKF 177
Cdd:PRK04778  98 FRFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENL 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 178 EPRLEQYEVLKADGNYVQAHNHIAALNEQMKQLRSYMEEIPELIRETQKELPGQFQDLKYGCRDLKVEGYDLDHVKVDST 257
Cdd:PRK04778 178 EEEFSQFVELTESGDYVEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHLDHLDIEKE 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 258 LQSLKTELSFVEPLISRLELEEANDKLANINDKLDDMYDLIEHEVKAKNDVEETKDIITDNLFKAKDMNYTLQTEIEYVR 337
Cdd:PRK04778 258 IQDLKEQIDENLALLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVK 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 338 ENYYINESDAQSVRQFENEIQSLISVYDDILKEMSKSAVRYSEVQDNLQYLEDHVTVINDKQEKLQNHLIQLREDEAEAE 417
Cdd:PRK04778 338 QSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAR 417
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 418 DNLLRVQSKKEEVYRRLLASNLTSVPERFIIMKNEIDHEVRDVNEQFSERPIHVKQLKDKVSKIVIQMNTFEDEANDVLV 497
Cdd:PRK04778 418 EKLERYRNKLHEIKRYLEKSNLPGLPEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVE 497
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577645388 498 NAVYAEKLIQYGNRYRKDYSNVDKSLNEAERLFKNNRYKRAIEIAEQALESVEPGVTKHIEEEVIKQ 564
Cdd:PRK04778 498 NATLTEQLIQYANRYRSDNEEVAEALNEAERLFREYDYKAALEIIATALEKVEPGVTKRIEDSYEKE 564
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
18-564 7.01e-175

Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443574 [Multi-domain]  Cd Length: 567  Bit Score: 506.30  E-value: 7.01e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  18 GVLFYLRSNKRQIIEKAIERKNEIETLPFDQNLAQLSKLNLKGETKTKYDAMKKDNVESTNKYLAPVEEKIHNAEALLDK 97
Cdd:COG4477   17 GAGYIMRKKHYKEIDRLEERKLEIMNRPVLDELSKVKKLNLSGQTEEKFEEWRQKWDEIVTKQLPEIEELLFDAEEAADK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  98 FSFNASQSEIDDANELMDSYEQSYQQQLEDVNEIIALYKDNDELYDKCKVDYREMKRDVLANRHQFGEAASLLETEIEKF 177
Cdd:COG4477   97 FRFKKAKKALDEIEQLLDEIEEEIEEILEELEELLESEEKNREEIEELKEKYRELRKTLLAHRHSFGPAAEELEKQLEEL 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 178 EPRLEQYEVLKADGNYVQAHNHIAALNEQMKQLRSYMEEIPELIRETQKELPGQFQDLKYGCRDLKVEGYDLDHVKVDST 257
Cdd:COG4477  177 EPEFEEFEELTESGDYLEAREILEQLEEELNALEELMEEIPPLLKELQTELPDQLEELKSGYREMKEQGYVLEHLNIEKE 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 258 LQSLKTELSFVEPLISRLELEEANDKLANINDKLDDMYDLIEHEVKAKNDVEETKDIITDNLFKAKDMNYTLQTEIEYVR 337
Cdd:COG4477  257 IEQLEEQLKEALELLEELDLDEAEEELEEIEEEIDELYDLLEKEVEAKKYVDKNQEELEEYLEHLKEQNRELKEEIDRVQ 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 338 ENYYINESDAQSVRQFENEIQSLISVYDDILKEMSKSAVRYSEVQDNLQYLEDHVTVINDKQEKLQNHLIQLREDEAEAE 417
Cdd:COG4477  337 QSYRLNENELEKVRNLEKQIEELEKRYDEIDERIEEEKVAYSELQEELEEIEEQLEEIEEEQEEFSEKLKSLRKDELEAR 416
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 418 DNLLRVQSKKEEVYRRLLASNLTSVPERFIIMKNEIDHEVRDVNEQFSERPIHVKQLKDKVSKIVIQMNTFEDEANDVLV 497
Cdd:COG4477  417 EKLDELKKKLREIKRRLEKSNLPGLPEEYLEMFEEASDEIEELSEELNEVPLNMDEVNRLLEEAEEDIETLEEKTEELVE 496
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577645388 498 NAVYAEKLIQYGNRYRKDYSNVDKSLNEAERLFKNNRYKRAIEIAEQALESVEPGVTKHIEEEVIKQ 564
Cdd:COG4477  497 NATLTERLIQYANRYRSDNPEVAAALTEAERLFREYDYEKALEIAATALEKVEPGALKRIEESYKEE 563
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
21-561 2.81e-162

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: 473.19  E-value: 2.81e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388   21 FYLRSNKRQIIEKAIERKNEIETLPFDQNLAQLSKLNLKGETKTKYDAMKKDNVESTNKYLAPVEEKIHNAEALLDKFSF 100
Cdd:pfam06160   2 LLLRKKIYKEIDELEERKNELMNLPVQEELSKVKKLNLTGETQEKFEEWRKKWDDIVTKSLPDIEELLFEAEELNDKYRF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  101 NASQSEIDDANELMDSYEQSYQQQLEDVNEIIALYKDNDELYDKCKVDYREMKRDVLANRHQFGEAASLLETEIEKFEPR 180
Cdd:pfam06160  82 KKAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  181 LEQYEVLKADGNYVQAHNHIAALNEQMKQLRSYMEEIPELIRETQKELPGQFQDLKYGCRDLKVEGYDLDHVKVDSTLQS 260
Cdd:pfam06160 162 FSQFEELTESGDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALEHLNVDKEIQQ 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  261 LKTELSFVEPLISRLELEEANDKLANINDKLDDMYDLIEHEVKAKNDVEETKDIITDNLFKAKDMNYTLQTEIEYVRENY 340
Cdd:pfam06160 242 LEEQLEENLALLENLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSY 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  341 YINESDAQSVRQFENEIQSLISVYDDILKEMSKSAVRYSEVQDNLQYLEDHVTVINDKQEKLQNHLIQLREDEAEAEDNL 420
Cdd:pfam06160 322 TLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKL 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  421 LRVQSKKEEVYRRLLASNLTSVPERFIIMKNEIDHEVRDVNEQFSERPIHVKQLKDKVSKIVIQMNTFEDEANDVLVNAV 500
Cdd:pfam06160 402 DEFKLELREIKRLVEKSNLPGLPESYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDDVDTLYEKTEELIDNAT 481
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577645388  501 YAEKLIQYGNRYRKDYSNVDKSLNEAERLFKNNRYKRAIEIAEQALESVEPGVTKHIEEEV 561
Cdd:pfam06160 482 LAEQLIQYANRYRSSNPEVAEALTEAELLFRNYDYEKALEIAATALEKVEPGAYERIEDSY 542
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
194-467 1.88e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388   194 VQAHNHIAALNEQMKQLRSYMEEIPELIRETQKELPG---QFQDLKYGCRDLKVEGYDL--DHVKVDSTLQSLKTELSFV 268
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAElrkELEELEEELEQLRKELEELsrQISALRKDLARLEAEVEQL 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388   269 EPLISRL--ELEEANDKLANINDKLDDMYDLIEHEVKAKNDVEETKDIITDNLFKAKDMNYTLQTEIEYVRENYYINESD 346
Cdd:TIGR02168  746 EERIAQLskELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388   347 AQSVRQFENEIQSLISVYDDILKEMSKSAVRYSEVQDNLQY----LEDHVTVINDKQEKLQNHLIQLREDEAEAEDNLLR 422
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEElieeLESELEALLNERASLEEALALLRSELEELSEELRE 905
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 577645388   423 VQSKKEEVYRRLLASN--LTSVPERFIIMKNEIDHevrdVNEQFSER 467
Cdd:TIGR02168  906 LESKRSELRRELEELRekLAQLELRLEGLEVRIDN----LQERLSEE 948
 
Name Accession Description Interval E-value
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
18-564 0e+00

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 583.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  18 GVLFYLRSNKRQIIEKAIERKNEIETLPFDQNLAQLSKLNLKGETKTKYDAMKKDNVESTNKYLAPVEEKIHNAEALLDK 97
Cdd:PRK04778  18 LAGLILRKRNYKRIDELEERKQELENLPVNDELEKVKKLNLTGQSEEKFEEWRQKWDEIVTNSLPDIEEQLFEAEELNDK 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  98 FSFNASQSEIDDANELMDSYEQSYQQQLEDVNEIIALYKDNDELYDKCKVDYREMKRDVLANRHQFGEAASLLETEIEKF 177
Cdd:PRK04778  98 FRFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENL 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 178 EPRLEQYEVLKADGNYVQAHNHIAALNEQMKQLRSYMEEIPELIRETQKELPGQFQDLKYGCRDLKVEGYDLDHVKVDST 257
Cdd:PRK04778 178 EEEFSQFVELTESGDYVEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHLDHLDIEKE 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 258 LQSLKTELSFVEPLISRLELEEANDKLANINDKLDDMYDLIEHEVKAKNDVEETKDIITDNLFKAKDMNYTLQTEIEYVR 337
Cdd:PRK04778 258 IQDLKEQIDENLALLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVK 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 338 ENYYINESDAQSVRQFENEIQSLISVYDDILKEMSKSAVRYSEVQDNLQYLEDHVTVINDKQEKLQNHLIQLREDEAEAE 417
Cdd:PRK04778 338 QSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAR 417
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 418 DNLLRVQSKKEEVYRRLLASNLTSVPERFIIMKNEIDHEVRDVNEQFSERPIHVKQLKDKVSKIVIQMNTFEDEANDVLV 497
Cdd:PRK04778 418 EKLERYRNKLHEIKRYLEKSNLPGLPEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVE 497
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577645388 498 NAVYAEKLIQYGNRYRKDYSNVDKSLNEAERLFKNNRYKRAIEIAEQALESVEPGVTKHIEEEVIKQ 564
Cdd:PRK04778 498 NATLTEQLIQYANRYRSDNEEVAEALNEAERLFREYDYKAALEIIATALEKVEPGVTKRIEDSYEKE 564
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
18-564 7.01e-175

Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443574 [Multi-domain]  Cd Length: 567  Bit Score: 506.30  E-value: 7.01e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  18 GVLFYLRSNKRQIIEKAIERKNEIETLPFDQNLAQLSKLNLKGETKTKYDAMKKDNVESTNKYLAPVEEKIHNAEALLDK 97
Cdd:COG4477   17 GAGYIMRKKHYKEIDRLEERKLEIMNRPVLDELSKVKKLNLSGQTEEKFEEWRQKWDEIVTKQLPEIEELLFDAEEAADK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  98 FSFNASQSEIDDANELMDSYEQSYQQQLEDVNEIIALYKDNDELYDKCKVDYREMKRDVLANRHQFGEAASLLETEIEKF 177
Cdd:COG4477   97 FRFKKAKKALDEIEQLLDEIEEEIEEILEELEELLESEEKNREEIEELKEKYRELRKTLLAHRHSFGPAAEELEKQLEEL 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 178 EPRLEQYEVLKADGNYVQAHNHIAALNEQMKQLRSYMEEIPELIRETQKELPGQFQDLKYGCRDLKVEGYDLDHVKVDST 257
Cdd:COG4477  177 EPEFEEFEELTESGDYLEAREILEQLEEELNALEELMEEIPPLLKELQTELPDQLEELKSGYREMKEQGYVLEHLNIEKE 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 258 LQSLKTELSFVEPLISRLELEEANDKLANINDKLDDMYDLIEHEVKAKNDVEETKDIITDNLFKAKDMNYTLQTEIEYVR 337
Cdd:COG4477  257 IEQLEEQLKEALELLEELDLDEAEEELEEIEEEIDELYDLLEKEVEAKKYVDKNQEELEEYLEHLKEQNRELKEEIDRVQ 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 338 ENYYINESDAQSVRQFENEIQSLISVYDDILKEMSKSAVRYSEVQDNLQYLEDHVTVINDKQEKLQNHLIQLREDEAEAE 417
Cdd:COG4477  337 QSYRLNENELEKVRNLEKQIEELEKRYDEIDERIEEEKVAYSELQEELEEIEEQLEEIEEEQEEFSEKLKSLRKDELEAR 416
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388 418 DNLLRVQSKKEEVYRRLLASNLTSVPERFIIMKNEIDHEVRDVNEQFSERPIHVKQLKDKVSKIVIQMNTFEDEANDVLV 497
Cdd:COG4477  417 EKLDELKKKLREIKRRLEKSNLPGLPEEYLEMFEEASDEIEELSEELNEVPLNMDEVNRLLEEAEEDIETLEEKTEELVE 496
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577645388 498 NAVYAEKLIQYGNRYRKDYSNVDKSLNEAERLFKNNRYKRAIEIAEQALESVEPGVTKHIEEEVIKQ 564
Cdd:COG4477  497 NATLTERLIQYANRYRSDNPEVAAALTEAERLFREYDYEKALEIAATALEKVEPGALKRIEESYKEE 563
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
21-561 2.81e-162

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: 473.19  E-value: 2.81e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388   21 FYLRSNKRQIIEKAIERKNEIETLPFDQNLAQLSKLNLKGETKTKYDAMKKDNVESTNKYLAPVEEKIHNAEALLDKFSF 100
Cdd:pfam06160   2 LLLRKKIYKEIDELEERKNELMNLPVQEELSKVKKLNLTGETQEKFEEWRKKWDDIVTKSLPDIEELLFEAEELNDKYRF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  101 NASQSEIDDANELMDSYEQSYQQQLEDVNEIIALYKDNDELYDKCKVDYREMKRDVLANRHQFGEAASLLETEIEKFEPR 180
Cdd:pfam06160  82 KKAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  181 LEQYEVLKADGNYVQAHNHIAALNEQMKQLRSYMEEIPELIRETQKELPGQFQDLKYGCRDLKVEGYDLDHVKVDSTLQS 260
Cdd:pfam06160 162 FSQFEELTESGDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALEHLNVDKEIQQ 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  261 LKTELSFVEPLISRLELEEANDKLANINDKLDDMYDLIEHEVKAKNDVEETKDIITDNLFKAKDMNYTLQTEIEYVRENY 340
Cdd:pfam06160 242 LEEQLEENLALLENLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSY 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  341 YINESDAQSVRQFENEIQSLISVYDDILKEMSKSAVRYSEVQDNLQYLEDHVTVINDKQEKLQNHLIQLREDEAEAEDNL 420
Cdd:pfam06160 322 TLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKL 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388  421 LRVQSKKEEVYRRLLASNLTSVPERFIIMKNEIDHEVRDVNEQFSERPIHVKQLKDKVSKIVIQMNTFEDEANDVLVNAV 500
Cdd:pfam06160 402 DEFKLELREIKRLVEKSNLPGLPESYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDDVDTLYEKTEELIDNAT 481
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577645388  501 YAEKLIQYGNRYRKDYSNVDKSLNEAERLFKNNRYKRAIEIAEQALESVEPGVTKHIEEEV 561
Cdd:pfam06160 482 LAEQLIQYANRYRSSNPEVAEALTEAELLFRNYDYEKALEIAATALEKVEPGAYERIEDSY 542
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
194-467 1.88e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388   194 VQAHNHIAALNEQMKQLRSYMEEIPELIRETQKELPG---QFQDLKYGCRDLKVEGYDL--DHVKVDSTLQSLKTELSFV 268
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAElrkELEELEEELEQLRKELEELsrQISALRKDLARLEAEVEQL 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388   269 EPLISRL--ELEEANDKLANINDKLDDMYDLIEHEVKAKNDVEETKDIITDNLFKAKDMNYTLQTEIEYVRENYYINESD 346
Cdd:TIGR02168  746 EERIAQLskELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388   347 AQSVRQFENEIQSLISVYDDILKEMSKSAVRYSEVQDNLQY----LEDHVTVINDKQEKLQNHLIQLREDEAEAEDNLLR 422
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEElieeLESELEALLNERASLEEALALLRSELEELSEELRE 905
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 577645388   423 VQSKKEEVYRRLLASN--LTSVPERFIIMKNEIDHevrdVNEQFSER 467
Cdd:TIGR02168  906 LESKRSELRRELEELRekLAQLELRLEGLEVRIDN----LQERLSEE 948
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
24-292 3.17e-03

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: 40.44  E-value: 3.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388    24 RSNKRQIIEKAIERKNEIetlpfdqnLAQL-SKLNLKGETKTKYDAMKKDNvestNKYLAPVEEKIHNAEALLDKFSFNA 102
Cdd:TIGR02169  721 IEKEIEQLEQEEEKLKER--------LEELeEDLSSLEQEIENVKSELKEL----EARIEELEEDLHKLEEALNDLEARL 788
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388   103 SQSEIDDANELMDSYEQSYQQQLEDVNEIIALYKDND---ELYDKCKVDYREMKRDVLANRHQFGEAASLLETEIEKFEP 179
Cdd:TIGR02169  789 SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTlekEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE 868
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388   180 RLE--QYEVLKADGNYVQAHNHIAALNEQMKQLRSYMEEIP---ELIRETQKELPGQFQDLKY--------GCRDLKVEG 246
Cdd:TIGR02169  869 ELEelEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiEKKRKRLSELKAKLEALEEelseiedpKGEDEEIPE 948
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 577645388   247 YDLDHVKVDSTLQSLKTELSFVEPLISRL--ELEEANDKLANINDKLD 292
Cdd:TIGR02169  949 EELSLEDVQAELQRVEEEIRALEPVNMLAiqEYEEVLKRLDELKEKRA 996
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
34-317 5.08e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 5.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388    34 AIERKNEIETLPFDQNLAQLSKLNLKGETKTKYDAM--KKDNVESTNKYLAPVEEKIHNAEALLDKFSFNASQ--SEIDD 109
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELeeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQleERIAQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388   110 ANELMDSYEQSYQQQLEDVNEIIALYKDNDELYDKCKVDYREMKRDVLANRHQFGEA---ASLLETEIEKFEPRLEQYEV 186
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeLTLLNEEAANLRERLESLER 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577645388   187 LKADG--NYVQAHNHIAALNEQMKQLRSYMEEIPELIRETQKELPG---QFQDLKYGCRDLKVEGYDLDHV--KVDSTLQ 259
Cdd:TIGR02168  832 RIAATerRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSELEELSEElrELESKRS 911
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577645388   260 SLKTELSFVEPLIS--RLELEEANDKLANINDKL-----DDMYDLIEHEVKAKNDVEETKDIITD 317
Cdd:TIGR02168  912 ELRRELEELREKLAqlELRLEGLEVRIDNLQERLseeysLTLEEAEALENKIEDDEEEARRRLKR 976
 
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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