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Conserved domains on  [gi|503010706|ref|WP_013245682|]
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septation ring formation regulator EzrA [Lacticaseibacillus paracasei]

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
19-566 0e+00

septation ring formation regulator EzrA; Provisional


:

Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 552.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  19 WWLQHYFQTRIKNLDAQVEAIDVGALSSQIRSIEQLKLTGDSLATFSKWERAFDQLNDDDLADLQKILLDLEDQAKRFRF 98
Cdd:PRK04778  21 LILRKRNYKRIDELEERKQELENLPVNDELEKVKKLNLTGQSEEKFEEWRQKWDEIVTNSLPDIEEQLFEAEELNDKFRF 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  99 DHAQKIAKVLEAKIDTARQQYDLISQALQDIRHDEADNRSKMLQLRDDYQVSRKTILAKSFVFGDAQPALEQQLQQLAEL 178
Cdd:PRK04778 101 RKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEE 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 179 FQKIDQINNDGDHQAAKSEIKQLSDEMAALRCQVKELPPLVNEQVNEFPAQINEIEHGYRQLTTAHYVFTD-DIPGMVED 257
Cdd:PRK04778 181 FSQFVELTESGDYVEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHLDHlDIEKEIQD 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 258 VNEKMADANTALKSLDVDATEAANSEIEAEIDKMYAIMEKEMQARKRVDAAAPDLRQFIDHALRQNRELQTELDHLNQSY 337
Cdd:PRK04778 261 LKEQIDENLALLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSY 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 338 TLNHNEIKIAKDLKTQLDSIDANYIKDTDAIEAGKAVYSDVIERFDATKDELTAIEKQQVQINQAVAGLKKGEIVANKQA 417
Cdd:PRK04778 341 TLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKL 420
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 418 ENFELDMRNIKHEILRHHLPGLPQDYVSQVKHVTAEIEQLNHDLDQVKINMDAIAKFLIKIASDIDALKKATSALIDAAG 497
Cdd:PRK04778 421 ERYRNKLHEIKRYLEKSNLPGLPEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENAT 500
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503010706 498 LTEELMQYANRYKTTVKPVAEAVHQATESYMQFDYKQAADTLATALEQTEAGSYKKVEDAYLARKKASL 566
Cdd:PRK04778 501 LTEQLIQYANRYRSDNEEVAEALNEAERLFREYDYKAALEIIATALEKVEPGVTKRIEDSYEKEKETIR 569
 
Name Accession Description Interval E-value
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
19-566 0e+00

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 552.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  19 WWLQHYFQTRIKNLDAQVEAIDVGALSSQIRSIEQLKLTGDSLATFSKWERAFDQLNDDDLADLQKILLDLEDQAKRFRF 98
Cdd:PRK04778  21 LILRKRNYKRIDELEERKQELENLPVNDELEKVKKLNLTGQSEEKFEEWRQKWDEIVTNSLPDIEEQLFEAEELNDKFRF 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  99 DHAQKIAKVLEAKIDTARQQYDLISQALQDIRHDEADNRSKMLQLRDDYQVSRKTILAKSFVFGDAQPALEQQLQQLAEL 178
Cdd:PRK04778 101 RKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEE 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 179 FQKIDQINNDGDHQAAKSEIKQLSDEMAALRCQVKELPPLVNEQVNEFPAQINEIEHGYRQLTTAHYVFTD-DIPGMVED 257
Cdd:PRK04778 181 FSQFVELTESGDYVEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHLDHlDIEKEIQD 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 258 VNEKMADANTALKSLDVDATEAANSEIEAEIDKMYAIMEKEMQARKRVDAAAPDLRQFIDHALRQNRELQTELDHLNQSY 337
Cdd:PRK04778 261 LKEQIDENLALLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSY 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 338 TLNHNEIKIAKDLKTQLDSIDANYIKDTDAIEAGKAVYSDVIERFDATKDELTAIEKQQVQINQAVAGLKKGEIVANKQA 417
Cdd:PRK04778 341 TLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKL 420
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 418 ENFELDMRNIKHEILRHHLPGLPQDYVSQVKHVTAEIEQLNHDLDQVKINMDAIAKFLIKIASDIDALKKATSALIDAAG 497
Cdd:PRK04778 421 ERYRNKLHEIKRYLEKSNLPGLPEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENAT 500
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503010706 498 LTEELMQYANRYKTTVKPVAEAVHQATESYMQFDYKQAADTLATALEQTEAGSYKKVEDAYLARKKASL 566
Cdd:PRK04778 501 LTEQLIQYANRYRSDNEEVAEALNEAERLFREYDYKAALEIIATALEKVEPGVTKRIEDSYEKEKETIR 569
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
19-565 2.81e-163

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


Pssm-ID: 443574 [Multi-domain]  Cd Length: 567  Bit Score: 476.64  E-value: 2.81e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  19 WWLQHYFQTRIKNLDAQVEAIDVGALSSQIRSIEQLKLTGDSLATFSKWERAFDQLNDDDLADLQKILLDLEDQAKRFRF 98
Cdd:COG4477   20 YIMRKKHYKEIDRLEERKLEIMNRPVLDELSKVKKLNLSGQTEEKFEEWRQKWDEIVTKQLPEIEELLFDAEEAADKFRF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  99 DHAQKIAKVLEAKIDTARQQYDLISQALQDIRHDEADNRSKMLQLRDDYQVSRKTILAKSFVFGDAQPALEQQLQQLAEL 178
Cdd:COG4477  100 KKAKKALDEIEQLLDEIEEEIEEILEELEELLESEEKNREEIEELKEKYRELRKTLLAHRHSFGPAAEELEKQLEELEPE 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 179 FQKIDQINNDGDHQAAKSEIKQLSDEMAALRCQVKELPPLVNEQVNEFPAQINEIEHGYRQLTTAHYVFTD-DIPGMVED 257
Cdd:COG4477  180 FEEFEELTESGDYLEAREILEQLEEELNALEELMEEIPPLLKELQTELPDQLEELKSGYREMKEQGYVLEHlNIEKEIEQ 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 258 VNEKMADANTALKSLDVDATEAANSEIEAEIDKMYAIMEKEMQARKRVDAAAPDLRQFIDHALRQNRELQTELDHLNQSY 337
Cdd:COG4477  260 LEEQLKEALELLEELDLDEAEEELEEIEEEIDELYDLLEKEVEAKKYVDKNQEELEEYLEHLKEQNRELKEEIDRVQQSY 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 338 TLNHNEIKIAKDLKTQLDSIDANYIKDTDAIEAGKAVYSDVIERFDATKDELTAIEKQQVQINQAVAGLKKGEIVANKQA 417
Cdd:COG4477  340 RLNENELEKVRNLEKQIEELEKRYDEIDERIEEEKVAYSELQEELEEIEEQLEEIEEEQEEFSEKLKSLRKDELEAREKL 419
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 418 ENFELDMRNIKHEILRHHLPGLPQDYVSQVKHVTAEIEQLNHDLDQVKINMDAIAKFLIKIASDIDALKKATSALIDAAG 497
Cdd:COG4477  420 DELKKKLREIKRRLEKSNLPGLPEEYLEMFEEASDEIEELSEELNEVPLNMDEVNRLLEEAEEDIETLEEKTEELVENAT 499
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503010706 498 LTEELMQYANRYKTTVKPVAEAVHQATESYMQFDYKQAADTLATALEQTEAGSYKKVEDAYLARKKAS 565
Cdd:COG4477  500 LTERLIQYANRYRSDNPEVAAALTEAERLFREYDYEKALEIAATALEKVEPGALKRIEESYKEEKETS 567
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
20-558 8.07e-143

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: 423.50  E-value: 8.07e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   20 WLQHYFQTRIKNLDAQVEAIDVGALSSQIRSIEQLKLTGDSLATFSKWERAFDQLNDDDLADLQKILLDLEDQAKRFRFD 99
Cdd:pfam06160   3 LLRKKIYKEIDELEERKNELMNLPVQEELSKVKKLNLTGETQEKFEEWRKKWDDIVTKSLPDIEELLFEAEELNDKYRFK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  100 HAQKIAKVLEAKIDTARQQYDLISQALQDIRHDEADNRSKMLQLRDDYQVSRKTILAKSFVFGDAQPALEQQLQQLAELF 179
Cdd:pfam06160  83 KAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  180 QKIDQINNDGDHQAAKSEIKQLSDEMAALRCQVKELPPLVNEQVNEFPAQINEIEHGYRQLTTAHYVFTD-DIPGMVEDV 258
Cdd:pfam06160 163 SQFEELTESGDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALEHlNVDKEIQQL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  259 NEKMADANTALKSLDVDATEAANSEIEAEIDKMYAIMEKEMQARKRVDAAAPDLRQFIDHALRQNRELQTELDHLNQSYT 338
Cdd:pfam06160 243 EEQLEENLALLENLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYT 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  339 LNHNEIKIAKDLKTQLDSIDANYIKDTDAIEAGKAVYSDVIERFDATKDELTAIEKQQVQINQAVAGLKKGEIVANKQAE 418
Cdd:pfam06160 323 LNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLD 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  419 NFELDMRNIKHEILRHHLPGLPQDYVSQVKHVTAEIEQLNHDLDQVKINMDAIAKFLIKIASDIDALKKATSALIDAAGL 498
Cdd:pfam06160 403 EFKLELREIKRLVEKSNLPGLPESYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDDVDTLYEKTEELIDNATL 482
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  499 TEELMQYANRYKTTVKPVAEAVHQATESYMQFDYKQAADTLATALEQTEAGSYKKVEDAY 558
Cdd:pfam06160 483 AEQLIQYANRYRSSNPEVAEALTEAELLFRNYDYEKALEIAATALEKVEPGAYERIEDSY 542
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
108-406 4.52e-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: 4.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   108 LEAKIDTARQQYDLISQALQDIRHDEADNRSKMLQLRDDYQVSRKTILAKSFVFGDAQPALEQQLQQLAELFQKIDQINN 187
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   188 DGDHQAAKSE-----IKQLSDEMAALRCQVKELpplvNEQVNEFPAQINEIEHGYRQLTTAHyvftDDIPGMVEDVNEKM 262
Cdd:TIGR02168  776 ELAEAEAEIEeleaqIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLERRI----AATERRLEDLEEQI 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   263 ADANTALKSL--DVDATEAANSEIEAEIDKMYAIMEKEMQARKRVDAAAPDLRQFIDHALRQNRELQTELDHLNQSY--- 337
Cdd:TIGR02168  848 EELSEDIESLaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLaql 927
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   338 ---------TLNHNEIKIAKDLKTQLDSIDANYIKDTDAIEAGKA--------------VYSDVIERFDATKDELTAIEK 394
Cdd:TIGR02168  928 elrleglevRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRrlkrlenkikelgpVNLAAIEEYEELKERYDFLTA 1007
                          330
                   ....*....|..
gi 503010706   395 QQVQINQAVAGL 406
Cdd:TIGR02168 1008 QKEDLTEAKETL 1019
 
Name Accession Description Interval E-value
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
19-566 0e+00

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 552.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  19 WWLQHYFQTRIKNLDAQVEAIDVGALSSQIRSIEQLKLTGDSLATFSKWERAFDQLNDDDLADLQKILLDLEDQAKRFRF 98
Cdd:PRK04778  21 LILRKRNYKRIDELEERKQELENLPVNDELEKVKKLNLTGQSEEKFEEWRQKWDEIVTNSLPDIEEQLFEAEELNDKFRF 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  99 DHAQKIAKVLEAKIDTARQQYDLISQALQDIRHDEADNRSKMLQLRDDYQVSRKTILAKSFVFGDAQPALEQQLQQLAEL 178
Cdd:PRK04778 101 RKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEE 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 179 FQKIDQINNDGDHQAAKSEIKQLSDEMAALRCQVKELPPLVNEQVNEFPAQINEIEHGYRQLTTAHYVFTD-DIPGMVED 257
Cdd:PRK04778 181 FSQFVELTESGDYVEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHLDHlDIEKEIQD 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 258 VNEKMADANTALKSLDVDATEAANSEIEAEIDKMYAIMEKEMQARKRVDAAAPDLRQFIDHALRQNRELQTELDHLNQSY 337
Cdd:PRK04778 261 LKEQIDENLALLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSY 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 338 TLNHNEIKIAKDLKTQLDSIDANYIKDTDAIEAGKAVYSDVIERFDATKDELTAIEKQQVQINQAVAGLKKGEIVANKQA 417
Cdd:PRK04778 341 TLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKL 420
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 418 ENFELDMRNIKHEILRHHLPGLPQDYVSQVKHVTAEIEQLNHDLDQVKINMDAIAKFLIKIASDIDALKKATSALIDAAG 497
Cdd:PRK04778 421 ERYRNKLHEIKRYLEKSNLPGLPEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENAT 500
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503010706 498 LTEELMQYANRYKTTVKPVAEAVHQATESYMQFDYKQAADTLATALEQTEAGSYKKVEDAYLARKKASL 566
Cdd:PRK04778 501 LTEQLIQYANRYRSDNEEVAEALNEAERLFREYDYKAALEIIATALEKVEPGVTKRIEDSYEKEKETIR 569
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
19-565 2.81e-163

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


Pssm-ID: 443574 [Multi-domain]  Cd Length: 567  Bit Score: 476.64  E-value: 2.81e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  19 WWLQHYFQTRIKNLDAQVEAIDVGALSSQIRSIEQLKLTGDSLATFSKWERAFDQLNDDDLADLQKILLDLEDQAKRFRF 98
Cdd:COG4477   20 YIMRKKHYKEIDRLEERKLEIMNRPVLDELSKVKKLNLSGQTEEKFEEWRQKWDEIVTKQLPEIEELLFDAEEAADKFRF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  99 DHAQKIAKVLEAKIDTARQQYDLISQALQDIRHDEADNRSKMLQLRDDYQVSRKTILAKSFVFGDAQPALEQQLQQLAEL 178
Cdd:COG4477  100 KKAKKALDEIEQLLDEIEEEIEEILEELEELLESEEKNREEIEELKEKYRELRKTLLAHRHSFGPAAEELEKQLEELEPE 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 179 FQKIDQINNDGDHQAAKSEIKQLSDEMAALRCQVKELPPLVNEQVNEFPAQINEIEHGYRQLTTAHYVFTD-DIPGMVED 257
Cdd:COG4477  180 FEEFEELTESGDYLEAREILEQLEEELNALEELMEEIPPLLKELQTELPDQLEELKSGYREMKEQGYVLEHlNIEKEIEQ 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 258 VNEKMADANTALKSLDVDATEAANSEIEAEIDKMYAIMEKEMQARKRVDAAAPDLRQFIDHALRQNRELQTELDHLNQSY 337
Cdd:COG4477  260 LEEQLKEALELLEELDLDEAEEELEEIEEEIDELYDLLEKEVEAKKYVDKNQEELEEYLEHLKEQNRELKEEIDRVQQSY 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 338 TLNHNEIKIAKDLKTQLDSIDANYIKDTDAIEAGKAVYSDVIERFDATKDELTAIEKQQVQINQAVAGLKKGEIVANKQA 417
Cdd:COG4477  340 RLNENELEKVRNLEKQIEELEKRYDEIDERIEEEKVAYSELQEELEEIEEQLEEIEEEQEEFSEKLKSLRKDELEAREKL 419
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 418 ENFELDMRNIKHEILRHHLPGLPQDYVSQVKHVTAEIEQLNHDLDQVKINMDAIAKFLIKIASDIDALKKATSALIDAAG 497
Cdd:COG4477  420 DELKKKLREIKRRLEKSNLPGLPEEYLEMFEEASDEIEELSEELNEVPLNMDEVNRLLEEAEEDIETLEEKTEELVENAT 499
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503010706 498 LTEELMQYANRYKTTVKPVAEAVHQATESYMQFDYKQAADTLATALEQTEAGSYKKVEDAYLARKKAS 565
Cdd:COG4477  500 LTERLIQYANRYRSDNPEVAAALTEAERLFREYDYEKALEIAATALEKVEPGALKRIEESYKEEKETS 567
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
20-558 8.07e-143

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: 423.50  E-value: 8.07e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   20 WLQHYFQTRIKNLDAQVEAIDVGALSSQIRSIEQLKLTGDSLATFSKWERAFDQLNDDDLADLQKILLDLEDQAKRFRFD 99
Cdd:pfam06160   3 LLRKKIYKEIDELEERKNELMNLPVQEELSKVKKLNLTGETQEKFEEWRKKWDDIVTKSLPDIEELLFEAEELNDKYRFK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  100 HAQKIAKVLEAKIDTARQQYDLISQALQDIRHDEADNRSKMLQLRDDYQVSRKTILAKSFVFGDAQPALEQQLQQLAELF 179
Cdd:pfam06160  83 KAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  180 QKIDQINNDGDHQAAKSEIKQLSDEMAALRCQVKELPPLVNEQVNEFPAQINEIEHGYRQLTTAHYVFTD-DIPGMVEDV 258
Cdd:pfam06160 163 SQFEELTESGDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALEHlNVDKEIQQL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  259 NEKMADANTALKSLDVDATEAANSEIEAEIDKMYAIMEKEMQARKRVDAAAPDLRQFIDHALRQNRELQTELDHLNQSYT 338
Cdd:pfam06160 243 EEQLEENLALLENLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYT 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  339 LNHNEIKIAKDLKTQLDSIDANYIKDTDAIEAGKAVYSDVIERFDATKDELTAIEKQQVQINQAVAGLKKGEIVANKQAE 418
Cdd:pfam06160 323 LNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLD 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  419 NFELDMRNIKHEILRHHLPGLPQDYVSQVKHVTAEIEQLNHDLDQVKINMDAIAKFLIKIASDIDALKKATSALIDAAGL 498
Cdd:pfam06160 403 EFKLELREIKRLVEKSNLPGLPESYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDDVDTLYEKTEELIDNATL 482
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  499 TEELMQYANRYKTTVKPVAEAVHQATESYMQFDYKQAADTLATALEQTEAGSYKKVEDAY 558
Cdd:pfam06160 483 AEQLIQYANRYRSSNPEVAEALTEAELLFRNYDYEKALEIAATALEKVEPGAYERIEDSY 542
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
108-406 4.52e-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: 4.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   108 LEAKIDTARQQYDLISQALQDIRHDEADNRSKMLQLRDDYQVSRKTILAKSFVFGDAQPALEQQLQQLAELFQKIDQINN 187
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   188 DGDHQAAKSE-----IKQLSDEMAALRCQVKELpplvNEQVNEFPAQINEIEHGYRQLTTAHyvftDDIPGMVEDVNEKM 262
Cdd:TIGR02168  776 ELAEAEAEIEeleaqIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLERRI----AATERRLEDLEEQI 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   263 ADANTALKSL--DVDATEAANSEIEAEIDKMYAIMEKEMQARKRVDAAAPDLRQFIDHALRQNRELQTELDHLNQSY--- 337
Cdd:TIGR02168  848 EELSEDIESLaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLaql 927
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   338 ---------TLNHNEIKIAKDLKTQLDSIDANYIKDTDAIEAGKA--------------VYSDVIERFDATKDELTAIEK 394
Cdd:TIGR02168  928 elrleglevRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRrlkrlenkikelgpVNLAAIEEYEELKERYDFLTA 1007
                          330
                   ....*....|..
gi 503010706   395 QQVQINQAVAGL 406
Cdd:TIGR02168 1008 QKEDLTEAKETL 1019
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
102-395 2.25e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 2.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   102 QKIAKvLEAKIDTARQQYDLISQALQDIRH--------------DEADNRSKMLQLRDDYQVSRKTILAKSFVFGDAQPA 167
Cdd:TIGR02168  677 REIEE-LEEKIEELEEKIAELEKALAELRKeleeleeeleqlrkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   168 LEQQLQQLAELFQKIDQINNDGDHQAAKSE-----IKQLSDEMAALRCQVKELpplvNEQVNEFPAQINEIEHGYRQLTT 242
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEeleaqIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLER 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   243 AHyvftDDIPGMVEDVNEKMADANTALKSL--DVDATEAANSEIEAEIDKMYAIMEKEMQARKRVDAAAPDLRQFIDHAL 320
Cdd:TIGR02168  832 RI----AATERRLEDLEEQIEELSEDIESLaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503010706   321 RQNRELQTELDHLNQSY-TLNHNEIKIAKDLKTQLDSIDANYIKDTDAIEagkAVYSDVIERFDATKDELTAIEKQ 395
Cdd:TIGR02168  908 SKRSELRRELEELREKLaQLELRLEGLEVRIDNLQERLSEEYSLTLEEAE---ALENKIEDDEEEARRRLKRLENK 980
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
28-322 2.98e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 2.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   28 RIKNLDAQVEAI--DVGALSSQIRSIE-QLKLTGDSLATFSKWERAFDQlnDDDLADLQKILLDLEDQAKRFR-----FD 99
Cdd:COG4913   611 KLAALEAELAELeeELAEAEERLEALEaELDALQERREALQRLAEYSWD--EIDVASAEREIAELEAELERLDassddLA 688
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  100 HAQKIAKVLEAKIDTARQQYDLISQALQDIRHDEADNRSKMLQLRDdyQVSRKTILAKSFVFGDAQPALEQQLQQlaELF 179
Cdd:COG4913   689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD--RLEAAEDLARLELRALLEERFAAALGD--AVE 764
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  180 QKIDQiNNDGDHQAAKSEIKQLSDEMAALRCQVKELPPLVNEQVNEFPAQINEIEHGYRQLTtahyvfTDDIPGMVEDVN 259
Cdd:COG4913   765 RELRE-NLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLE------EDGLPEYEERFK 837
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503010706  260 EKMADANTALKSLDVDATEAANSEIEAEIDKMYAIMEK---------EMQARKRVDAAAPDLRQFIDHALRQ 322
Cdd:COG4913   838 ELLNENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRipfgpgrylRLEARPRPDPEVREFRQELRAVTSG 909
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
28-244 2.84e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706    28 RIKNLDAQVEAID--VGALSSQIRSIE-QLKLTGDSLATFskweRAFDQLNDDDLADLQKILLDL---------EDQAKR 95
Cdd:TIGR02168  233 RLEELREELEELQeeLKEAEEELEELTaELQELEEKLEEL----RLEVSELEEEIEELQKELYALaneisrleqQKQILR 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706    96 FRFDHAQKIAKVLEAKIDTARQQYDLISQALQDIRHDEADNRSKMLQLRDDYQVSRKTILAKSFVFGDAQPALEQQLQQL 175
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   176 AELFQKIDQINNdgDHQAAKSEIKQLSDEMAALRCQVKEL-PPLVNEQVNEFPAQINEIEHGYRQLTTAH 244
Cdd:TIGR02168  389 AQLELQIASLNN--EIERLEARLERLEDRRERLQQEIEELlKKLEEAELKELQAELEELEEELEELQEEL 456
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
74-393 4.64e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 4.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706  74 LNDDDLADLQKILLDLEDQAKRFRFDHAQKIAKVLEAKIDTARQQYDLISQALQDIRHDEADNRSKMLQLRDDYQVSRKT 153
Cdd:COG1196  231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 154 ILAKSFVFGDAQPALEQQLQQLAELFQKIDQINNdgDHQAAKSEIKQLSDEMAALRCQVKELpplvNEQVNEFPAQINEI 233
Cdd:COG1196  311 RRELEERLEELEEELAELEEELEELEEELEELEE--ELEEAEEELEEAEAELAEAEEALLEA----EAELAEAEEELEEL 384
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 234 EHGYRQLTTAHYVFTDDIPG---MVEDVNEKMADANTALKSLDVDATEAANSEIEAEIDKmyaimEKEMQARKRVDAAAP 310
Cdd:COG1196  385 AEELLEALRAAAELAAQLEEleeAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL-----EEAAEEEAELEEEEE 459
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706 311 DLRQFIDHALRQNRELQTELDHLNQSYTLNHNEIKIAKDLKTQLDSiDANYIKDTDAIEAGKAVYSDVIERFDATKDELT 390
Cdd:COG1196  460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG-FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA 538

                 ...
gi 503010706 391 AIE 393
Cdd:COG1196  539 ALE 541
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
56-393 8.76e-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: 39.28  E-value: 8.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706    56 LTGDSLATFSKWERAFDQLNDDDLADLQKILLDLEDqakrfRFDHAQKIAKVLEAKIDTARQQYDLISQALQDIRHDEAD 135
Cdd:TIGR02169  660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQS-----ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   136 NRSKMLQLRDDYQVSRKTILAKSfvfgDAQPALEQQLQQLAELFQKIDQINNDGDHQAAKSEIKQLSDEMAALRcqvkel 215
Cdd:TIGR02169  735 LKERLEELEEDLSSLEQEIENVK----SELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLE------ 804
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   216 pplvnEQVNEFPAQINEIEHGYRQLTTAHYVFTDDIPGMVEDVNEkmadantalksldvdaTEAANSEIEAEID------ 289
Cdd:TIGR02169  805 -----EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----------------LKEQIKSIEKEIEnlngkk 863
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503010706   290 -KMYAIMEKEMQARKRVDAAAPDLRQFIDHALRQNRELQTELDHLNQSY---TLNHNEIKIAKD-LKTQLDSIDANYIKD 364
Cdd:TIGR02169  864 eELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIekkRKRLSELKAKLEaLEEELSEIEDPKGED 943
                          330       340
                   ....*....|....*....|....*....
gi 503010706   365 TDaIEAGKAVYSDVIERFDATKDELTAIE 393
Cdd:TIGR02169  944 EE-IPEEELSLEDVQAELQRVEEEIRALE 971
 
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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